Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6FTG

Subtomogram average of OST-containing ribosome-translocon complexes from canine rough microsomal membranes

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
3	0006486	biological_process	obsolete protein glycosylation
3	0008250	cellular_component	oligosaccharyltransferase complex
5	0004576	molecular_function	oligosaccharyl transferase activity
5	0004579	molecular_function	dolichyl-diphosphooligosaccharide-protein glycotransferase activity
5	0005789	cellular_component	endoplasmic reticulum membrane
5	0006486	biological_process	obsolete protein glycosylation
5	0008250	cellular_component	oligosaccharyltransferase complex
5	0016020	cellular_component	membrane
5	0016740	molecular_function	transferase activity
5	0016757	molecular_function	glycosyltransferase activity
5	0018279	biological_process	protein N-linked glycosylation via asparagine
5	0043686	biological_process	obsolete co-translational protein modification
5	0043687	biological_process	post-translational protein modification
5	0046872	molecular_function	metal ion binding
A	0002181	biological_process	cytoplasmic translation
A	0003723	molecular_function	RNA binding
A	0003735	molecular_function	structural constituent of ribosome
A	0005737	cellular_component	cytoplasm
A	0005840	cellular_component	ribosome
A	0006412	biological_process	translation
A	0015934	cellular_component	large ribosomal subunit
A	0019843	molecular_function	rRNA binding
A	0022625	cellular_component	cytosolic large ribosomal subunit
A	1990904	cellular_component	ribonucleoprotein complex
B	0003723	molecular_function	RNA binding
B	0003735	molecular_function	structural constituent of ribosome
B	0005730	cellular_component	nucleolus
B	0005737	cellular_component	cytoplasm
B	0005840	cellular_component	ribosome
B	0006412	biological_process	translation
B	0022625	cellular_component	cytosolic large ribosomal subunit
B	1990904	cellular_component	ribonucleoprotein complex
C	0003735	molecular_function	structural constituent of ribosome
C	0005840	cellular_component	ribosome
C	0006412	biological_process	translation
D	0000027	biological_process	ribosomal large subunit assembly
D	0003723	molecular_function	RNA binding
D	0003735	molecular_function	structural constituent of ribosome
D	0005730	cellular_component	nucleolus
D	0005737	cellular_component	cytoplasm
D	0005840	cellular_component	ribosome
D	0006412	biological_process	translation
D	0008097	molecular_function	5S rRNA binding
D	0019843	molecular_function	rRNA binding
D	0022625	cellular_component	cytosolic large ribosomal subunit
D	1990904	cellular_component	ribonucleoprotein complex
E	0003735	molecular_function	structural constituent of ribosome
E	0005840	cellular_component	ribosome
E	0006412	biological_process	translation
F	0000463	biological_process	maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
F	0003723	molecular_function	RNA binding
F	0003735	molecular_function	structural constituent of ribosome
F	0005737	cellular_component	cytoplasm
F	0005840	cellular_component	ribosome
F	0022625	cellular_component	cytosolic large ribosomal subunit
F	1990904	cellular_component	ribonucleoprotein complex
G	0003723	molecular_function	RNA binding
G	0042254	biological_process	ribosome biogenesis
G	1990904	cellular_component	ribonucleoprotein complex
H	0002181	biological_process	cytoplasmic translation
H	0003735	molecular_function	structural constituent of ribosome
H	0005737	cellular_component	cytoplasm
H	0005840	cellular_component	ribosome
H	0006412	biological_process	translation
H	0019843	molecular_function	rRNA binding
H	0022625	cellular_component	cytosolic large ribosomal subunit
H	1990904	cellular_component	ribonucleoprotein complex
I	0003735	molecular_function	structural constituent of ribosome
I	0005737	cellular_component	cytoplasm
I	0005840	cellular_component	ribosome
I	0006412	biological_process	translation
I	0022625	cellular_component	cytosolic large ribosomal subunit
I	1990904	cellular_component	ribonucleoprotein complex
J	0003723	molecular_function	RNA binding
J	0003735	molecular_function	structural constituent of ribosome
J	0005730	cellular_component	nucleolus
J	0005737	cellular_component	cytoplasm
J	0005840	cellular_component	ribosome
J	0006412	biological_process	translation
J	0019843	molecular_function	rRNA binding
J	1990904	cellular_component	ribonucleoprotein complex
L	0003735	molecular_function	structural constituent of ribosome
L	0005840	cellular_component	ribosome
L	0006412	biological_process	translation
M	0003723	molecular_function	RNA binding
M	0003735	molecular_function	structural constituent of ribosome
M	0005840	cellular_component	ribosome
M	0006412	biological_process	translation
N	0002181	biological_process	cytoplasmic translation
N	0003723	molecular_function	RNA binding
N	0003735	molecular_function	structural constituent of ribosome
N	0005737	cellular_component	cytoplasm
N	0005840	cellular_component	ribosome
N	0006412	biological_process	translation
N	0022625	cellular_component	cytosolic large ribosomal subunit
N	0022626	cellular_component	cytosolic ribosome
N	0044391	cellular_component	ribosomal subunit
N	1990904	cellular_component	ribonucleoprotein complex
O	0003735	molecular_function	structural constituent of ribosome
O	0005840	cellular_component	ribosome
O	0006412	biological_process	translation
O	0015934	cellular_component	large ribosomal subunit
P	0003735	molecular_function	structural constituent of ribosome
P	0005840	cellular_component	ribosome
P	0006412	biological_process	translation
P	0015934	cellular_component	large ribosomal subunit
Q	0003735	molecular_function	structural constituent of ribosome
Q	0005840	cellular_component	ribosome
Q	0006412	biological_process	translation
R	0003723	molecular_function	RNA binding
R	0003735	molecular_function	structural constituent of ribosome
R	0005840	cellular_component	ribosome
R	0006412	biological_process	translation
R	0022625	cellular_component	cytosolic large ribosomal subunit
S	0003735	molecular_function	structural constituent of ribosome
S	0005840	cellular_component	ribosome
S	0006412	biological_process	translation
T	0003735	molecular_function	structural constituent of ribosome
T	0005737	cellular_component	cytoplasm
T	0005783	cellular_component	endoplasmic reticulum
T	0005829	cellular_component	cytosol
T	0005840	cellular_component	ribosome
T	0006412	biological_process	translation
T	0022625	cellular_component	cytosolic large ribosomal subunit
T	1990904	cellular_component	ribonucleoprotein complex
U	0003735	molecular_function	structural constituent of ribosome
U	0005840	cellular_component	ribosome
U	0006412	biological_process	translation
V	0003735	molecular_function	structural constituent of ribosome
V	0005737	cellular_component	cytoplasm
V	0005840	cellular_component	ribosome
V	0006412	biological_process	translation
V	0015934	cellular_component	large ribosomal subunit
V	0022625	cellular_component	cytosolic large ribosomal subunit
V	0070180	molecular_function	large ribosomal subunit rRNA binding
V	1990904	cellular_component	ribonucleoprotein complex
W	0003735	molecular_function	structural constituent of ribosome
X	0003735	molecular_function	structural constituent of ribosome
X	0005840	cellular_component	ribosome
X	0006412	biological_process	translation
X	0019843	molecular_function	rRNA binding
Y	0003723	molecular_function	RNA binding
Y	0003735	molecular_function	structural constituent of ribosome
Y	0005737	cellular_component	cytoplasm
Y	0005840	cellular_component	ribosome
Y	0006412	biological_process	translation
Y	0015934	cellular_component	large ribosomal subunit
Y	1990904	cellular_component	ribonucleoprotein complex
Z	0003735	molecular_function	structural constituent of ribosome
Z	0005737	cellular_component	cytoplasm
Z	0005791	cellular_component	rough endoplasmic reticulum
Z	0005829	cellular_component	cytosol
Z	0005840	cellular_component	ribosome
Z	0006412	biological_process	translation
Z	0022625	cellular_component	cytosolic large ribosomal subunit
Z	0045202	cellular_component	synapse
Z	1990904	cellular_component	ribonucleoprotein complex
a	0003735	molecular_function	structural constituent of ribosome
a	0005737	cellular_component	cytoplasm
a	0005840	cellular_component	ribosome
a	0006412	biological_process	translation
a	0015934	cellular_component	large ribosomal subunit
a	0022625	cellular_component	cytosolic large ribosomal subunit
a	1990904	cellular_component	ribonucleoprotein complex
b	0003735	molecular_function	structural constituent of ribosome
b	0005840	cellular_component	ribosome
b	0006412	biological_process	translation
c	0003723	molecular_function	RNA binding
d	0003735	molecular_function	structural constituent of ribosome
d	0005840	cellular_component	ribosome
d	0006412	biological_process	translation
e	0003735	molecular_function	structural constituent of ribosome
e	0005737	cellular_component	cytoplasm
e	0005840	cellular_component	ribosome
e	0006412	biological_process	translation
e	0022625	cellular_component	cytosolic large ribosomal subunit
e	1990904	cellular_component	ribonucleoprotein complex
f	0000049	molecular_function	tRNA binding
f	0003723	molecular_function	RNA binding
f	0003735	molecular_function	structural constituent of ribosome
f	0005737	cellular_component	cytoplasm
f	0005840	cellular_component	ribosome
f	0006412	biological_process	translation
f	0022625	cellular_component	cytosolic large ribosomal subunit
f	0045202	cellular_component	synapse
f	1990904	cellular_component	ribonucleoprotein complex
g	0003735	molecular_function	structural constituent of ribosome
g	0005737	cellular_component	cytoplasm
g	0005783	cellular_component	endoplasmic reticulum
g	0005829	cellular_component	cytosol
g	0005840	cellular_component	ribosome
g	0006412	biological_process	translation
g	1990904	cellular_component	ribonucleoprotein complex
h	0000463	biological_process	maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
h	0003729	molecular_function	mRNA binding
h	0003735	molecular_function	structural constituent of ribosome
h	0005737	cellular_component	cytoplasm
h	0005840	cellular_component	ribosome
h	0006412	biological_process	translation
h	0015934	cellular_component	large ribosomal subunit
h	0022625	cellular_component	cytosolic large ribosomal subunit
h	1990904	cellular_component	ribonucleoprotein complex
i	0003735	molecular_function	structural constituent of ribosome
i	0005737	cellular_component	cytoplasm
i	0005829	cellular_component	cytosol
i	0005840	cellular_component	ribosome
i	0006412	biological_process	translation
i	1990904	cellular_component	ribonucleoprotein complex
j	0003735	molecular_function	structural constituent of ribosome
j	0005840	cellular_component	ribosome
j	0006412	biological_process	translation
k	0003735	molecular_function	structural constituent of ribosome
k	0005840	cellular_component	ribosome
k	0006412	biological_process	translation
l	0003735	molecular_function	structural constituent of ribosome
l	0005737	cellular_component	cytoplasm
l	0005840	cellular_component	ribosome
l	0006412	biological_process	translation
l	0022625	cellular_component	cytosolic large ribosomal subunit
l	1990904	cellular_component	ribonucleoprotein complex
m	0003735	molecular_function	structural constituent of ribosome
m	0005840	cellular_component	ribosome
m	0006412	biological_process	translation
n	0003735	molecular_function	structural constituent of ribosome
n	0005737	cellular_component	cytoplasm
n	0005840	cellular_component	ribosome
n	0006412	biological_process	translation
n	1990904	cellular_component	ribonucleoprotein complex
o	0003735	molecular_function	structural constituent of ribosome
o	0005840	cellular_component	ribosome
o	0006412	biological_process	translation
p	0003735	molecular_function	structural constituent of ribosome
p	0005737	cellular_component	cytoplasm
p	0005840	cellular_component	ribosome
p	0006412	biological_process	translation
p	0008270	molecular_function	zinc ion binding
p	0022625	cellular_component	cytosolic large ribosomal subunit
p	0046872	molecular_function	metal ion binding
p	0070180	molecular_function	large ribosomal subunit rRNA binding
p	1990904	cellular_component	ribonucleoprotein complex
r	0003735	molecular_function	structural constituent of ribosome
r	0005737	cellular_component	cytoplasm
r	0005840	cellular_component	ribosome
r	0006412	biological_process	translation
r	1990904	cellular_component	ribonucleoprotein complex
t	0003723	molecular_function	RNA binding
t	0003735	molecular_function	structural constituent of ribosome
t	0005737	cellular_component	cytoplasm
t	0005840	cellular_component	ribosome
t	0006412	biological_process	translation
t	0015934	cellular_component	large ribosomal subunit
t	0022625	cellular_component	cytosolic large ribosomal subunit
t	0070180	molecular_function	large ribosomal subunit rRNA binding
t	1990904	cellular_component	ribonucleoprotein complex
x	0005048	molecular_function	signal sequence binding
x	0005784	cellular_component	Sec61 translocon complex
x	0005789	cellular_component	endoplasmic reticulum membrane
x	0006613	biological_process	cotranslational protein targeting to membrane
x	0006616	biological_process	SRP-dependent cotranslational protein targeting to membrane, translocation
x	0008320	molecular_function	protein transmembrane transporter activity
x	0015031	biological_process	protein transport
x	0016020	cellular_component	membrane
x	0031204	biological_process	post-translational protein targeting to membrane, translocation
x	0039019	biological_process	pronephric nephron development
x	0043022	molecular_function	ribosome binding
x	0045047	biological_process	protein targeting to ER
x	0045048	biological_process	protein insertion into ER membrane
y	0005543	molecular_function	phospholipid binding
y	0005789	cellular_component	endoplasmic reticulum membrane
y	0006605	biological_process	protein targeting
y	0006886	biological_process	intracellular protein transport
y	0008320	molecular_function	protein transmembrane transporter activity
y	0015031	biological_process	protein transport
y	0016020	cellular_component	membrane
y	0022406	biological_process	membrane docking
y	0031204	biological_process	post-translational protein targeting to membrane, translocation
y	0043022	molecular_function	ribosome binding
y	0045047	biological_process	protein targeting to ER
y	0071261	cellular_component	Ssh1 translocon complex
z	0005784	cellular_component	Sec61 translocon complex
z	0006886	biological_process	intracellular protein transport

Functional Information from PROSITE/UniProt

site_id	PS00049
Number of Residues	27
Details	RIBOSOMAL_L14 Ribosomal protein L14 signature. AVVIrqrksyrrk.DGvflyFedNagVI

Chain	Residue	Details
V	ALA79-ILE105

site_id	PS00050
Number of Residues	16
Details	RIBOSOMAL_L23 Ribosomal protein L23 signature. KKAYVRLApdydaldV

Chain	Residue	Details
X	LYS134-VAL149

site_id	PS00051
Number of Residues	17
Details	RIBOSOMAL_L39E Ribosomal protein L39e signature. KTgnkIryNskrRHWRR

Chain	Residue	Details
l	LYS30-ARG46

site_id	PS00358
Number of Residues	17
Details	RIBOSOMAL_L5 Ribosomal protein L5 signature. LeqLTGQtpVfSkARyT

Chain	Residue	Details
J	LEU40-THR56

site_id	PS00359
Number of Residues	16
Details	RIBOSOMAL_L11 Ribosomal protein L11 signature. KeIlGTaqSVGcNVdG

Chain	Residue	Details
t	LYS130-GLY145

site_id	PS00464
Number of Residues	25
Details	RIBOSOMAL_L22 Ribosomal protein L22 signature. RrrTyRAhGRinpymsspCHIEMiL

Chain	Residue	Details
P	ARG126-LEU150

site_id	PS00467
Number of Residues	12
Details	RIBOSOMAL_L2 Ribosomal protein L2 signature. PrvRGVAmNPvE

Chain	Residue	Details
A	PRO197-GLU208

site_id	PS00474
Number of Residues	24
Details	RIBOSOMAL_L3 Ribosomal protein L3 signature. FgqdemiDviGvTkGKGykGvtsR

Chain	Residue	Details
B	PHE211-ARG234

site_id	PS00475
Number of Residues	32
Details	RIBOSOMAL_L15 Ribosomal protein L15 signature. KVLGkGkLpkqp.ViVkakfFSrrAeekIkgvG

Chain	Residue	Details
a	LYS110-GLY141

site_id	PS00526
Number of Residues	20
Details	RIBOSOMAL_L19E Ribosomal protein L19e signature. QKRLaSsvlrCGkkkVWLDP

Chain	Residue	Details
R	GLN7-PRO26

site_id	PS00579
Number of Residues	15
Details	RIBOSOMAL_L29 Ribosomal protein L29 signature. KLSKIRvVRKSIARV

Chain	Residue	Details
h	LYS43-VAL57

site_id	PS00580
Number of Residues	21
Details	RIBOSOMAL_L32E Ribosomal protein L32e signature. FiRhqsdRyvKIkrn..WRKprG

Chain	Residue	Details
e	PHE20-GLY40

site_id	PS00634
Number of Residues	33
Details	RIBOSOMAL_L30 Ribosomal protein L30 signature. VLqlLrLrQifNgTfvklnkasinMLriVepYI

Chain	Residue	Details
F	VAL110-ILE142

site_id	PS00687
Number of Residues	8
Details	ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GESSGKNV

Chain	Residue	Details
C	GLY15-VAL22

site_id	PS00700
Number of Residues	22
Details	RIBOSOMAL_L6_2 Ribosomal protein L6 signature 2. QattVknKdiRkFlDGIYVseK

Chain	Residue	Details
H	GLN163-LYS184

site_id	PS00709
Number of Residues	25
Details	RIBOSOMAL_L30E_1 Ribosomal protein L30e signature 1. SgkyvlGyKqtLKmiRqGkaKlVIL

Chain	Residue	Details
c	SER24-LEU48

site_id	PS00755
Number of Residues	20
Details	SECY_1 Protein secY signature 1. TLMeLGIsPIVtSGLIMQLL

Chain	Residue	Details
x	THR75-LEU94

site_id	PS00756
Number of Residues	19
Details	SECY_2 Protein secY signature 2. LLdElLQkgyGLGSGiSLF

Chain	Residue	Details
x	LEU164-PHE182

site_id	PS00783
Number of Residues	24
Details	RIBOSOMAL_L13 Ribosomal protein L13 signature. VRGMLPhktkrGQaaldrLkVFdG

Chain	Residue	Details
O	VAL84-GLY107

site_id	PS00939
Number of Residues	27
Details	RIBOSOMAL_L1E Ribosomal protein L1e signature. NttqKryAIcSALaASAlpalvmsKGH

Chain	Residue	Details
C	ASN116-HIS142

site_id	PS00993
Number of Residues	21
Details	RIBOSOMAL_L30E_2 Ribosomal protein L30e signature 2. ELGTacGKyyrvctLaIiDpG

Chain	Residue	Details
c	GLU80-GLY100

site_id	PS01067
Number of Residues	29
Details	SECE_SEC61G Protein secE/sec61-gamma signature. FvKDsIrlVkRctKPdrkEfqkiaMATAI

Chain	Residue	Details
y	PHE14-ILE42

site_id	PS01073
Number of Residues	18
Details	RIBOSOMAL_L24E Ribosomal protein L24e signature. FsGykIyPGhGrrYaRtD

Chain	Residue	Details
W	PHE8-ASP25

site_id	PS01077
Number of Residues	20
Details	RIBOSOMAL_L37E Ribosomal protein L37e signature. GTsSfGkRrnkt.HtlCrRCG

Chain	Residue	Details
j	GLY4-GLY23

site_id	PS01082
Number of Residues	18
Details	RIBOSOMAL_L7AE Ribosomal protein L7Ae signature. CrkmgVPYciLkGKarLG

Chain	Residue	Details
G	CYS174-GLY191

site_id	PS01104
Number of Residues	15
Details	RIBOSOMAL_L13E Ribosomal protein L13e signature. RaGRGFSLeELrvaG

Chain	Residue	Details
L	ARG71-GLY85

site_id	PS01105
Number of Residues	22
Details	RIBOSOMAL_L35AE Ribosomal protein L35Ae signature. GKVtRaHGnsGmVrAkFrsnLP

Chain	Residue	Details
f	GLY72-PRO93

site_id	PS01106
Number of Residues	18
Details	RIBOSOMAL_L18E Ribosomal protein L18e signature. KrLfmSRtnRPpLSLsRM

Chain	Residue	Details
Q	LYS49-MET66

site_id	PS01107
Number of Residues	12
Details	RIBOSOMAL_L27E Ribosomal protein L27e signature. GKNkWFFqkLRF

Chain	Residue	Details
Z	GLY125-PHE136

site_id	PS01108
Number of Residues	19
Details	RIBOSOMAL_L24 Ribosomal protein L24 signature. DDeVqVVrGhyKGqqiGkV

Chain	Residue	Details
Y	ASP52-VAL70

site_id	PS01144
Number of Residues	15
Details	RIBOSOMAL_L31E Ribosomal protein L31e signature. VRIDtrLNkAvWaKG

Chain	Residue	Details
d	VAL62-GLY76

site_id	PS01145
Number of Residues	14
Details	RIBOSOMAL_L34E Ribosomal protein L34e signature. TaSnKtrlsRTPGN

Chain	Residue	Details
g	THR15-ASN28

site_id	PS01170
Number of Residues	19
Details	RIBOSOMAL_L6E Ribosomal protein L6e signature. NrvPLRRthqkFVIATSt.K

Chain	Residue	Details
E	ASN178-LYS196

site_id	PS01171
Number of Residues	26
Details	RIBOSOMAL_L21E Ribosomal protein L21e signature. GDiVdikgmgtvqk.GmpHkcYhGkTG

Chain	Residue	Details
T	GLY37-GLY62

site_id	PS01172
Number of Residues	12
Details	RIBOSOMAL_L44E Ribosomal protein L44e signature. KtTKKivLRleC

Chain	Residue	Details
o	LYS61-CYS72

site_id	PS01190
Number of Residues	11
Details	RIBOSOMAL_L36E Ribosomal protein L36e signature. PYERRaMELLK

Chain	Residue	Details
i	PRO52-LYS62

site_id	PS01194
Number of Residues	24
Details	RIBOSOMAL_L15E Ribosomal protein L15e signature. DKARrLGYkAkqGYVIYRiRVrRG

Chain	Residue	Details
N	ASP46-GLY69

site_id	PS01257
Number of Residues	22
Details	RIBOSOMAL_L10E Ribosomal protein L10e signature. ADRlqtGMRgAFGKPqGtvARV

Chain	Residue	Details
I	ALA108-VAL129

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	159
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"(3S)-3-hydroxyhistidine","evidences":[{"source":"UniProtKB","id":"P62917","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P62917","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	64
Details	Compositional bias: {"description":"Basic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P39023","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P27659","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"UniProtKB","id":"P39023","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P27659","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P39023","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	6
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P39023","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P39023","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"source":"UniProtKB","id":"P39023","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	1
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P36578","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P36578","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q9D8E6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9D8E6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P36578","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P50878","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P36578","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	1
Details	Modified residue: {"description":"Citrulline","evidences":[{"source":"UniProtKB","id":"Q9D8E6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9D8E6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P36578","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"source":"UniProtKB","id":"P36578","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P46777","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P46777","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P47962","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P46777","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P46777","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P18124","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P14148","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P18124","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P62424","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62424","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P62424","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P62424","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI36
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P32969","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI37
Number of Residues	1
Details	Modified residue: {"description":"Citrulline","evidences":[{"source":"UniProtKB","id":"Q6ZWV3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI38
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P27635","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI39
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P27635","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI40
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62913","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI41
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62913","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI42
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P62913","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI43
Number of Residues	3
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P62913","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI44
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P62913","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI45
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P50914","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI46
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CR57","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI47
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P50914","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI48
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P50914","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI49
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P61314","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI50
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P61313","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI51
Number of Residues	1
Details	Lipidation: {"description":"N-myristoyl glycine","evidences":[{"source":"UniProtKB","id":"P61313","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI52
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P61313","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI53
Number of Residues	20
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI54
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P62829","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI55
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62829","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI56
Number of Residues	1
Details	Modified residue: {"description":"ADP-ribosyl glutamic acid","evidences":[{"source":"UniProtKB","id":"P83731","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI57
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P83731","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI58
Number of Residues	3
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P83731","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI59
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P83731","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI60
Number of Residues	1
Details	Modified residue: {"description":"Citrulline","evidences":[{"source":"UniProtKB","id":"P62751","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI61
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P62750","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI62
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62750","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI63
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P62751","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI64
Number of Residues	29
Details	Domain: {"description":"KOW","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI65
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P61353","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI66
Number of Residues	1
Details	Modified residue: {"description":"(3S)-3-hydroxyhistidine","evidences":[{"source":"UniProtKB","id":"P46776","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI67
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P46776","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI68
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P46776","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI69
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P47914","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI70
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P47914","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI71
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P47914","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI72
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62900","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI73
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62900","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI74
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P62899","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI75
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62911","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI76
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P62910","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI77
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P62910","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI78
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P18077","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI79
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"O55142","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI80
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P49207","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI81
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P49207","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI82
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9D1R9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI83
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P49207","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI84
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P42766","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI85
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P42766","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI86
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P42766","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI87
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9Y3U8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI88
Number of Residues	18
Details	Zinc finger: {"description":"C4-type","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI89
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29856316","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33296660","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6D90","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7A01","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI90
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P61927","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI91
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26245381","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3JAG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3JAH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI92
Number of Residues	21
Details	Zinc finger: {"description":"C4-type","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI93
Number of Residues	1
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"UniProtKB","id":"P46779","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI94
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P46779","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI95
Number of Residues	3
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P46779","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI96
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P30050","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI97
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P30050","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI98
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P30050","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI99
Number of Residues	3
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P30050","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI100
Number of Residues	223
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"36261528","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TM3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI101
Number of Residues	86
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"36261528","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TM3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI102
Number of Residues	85
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"36261528","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TM3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI103
Number of Residues	6
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"36261528","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TM3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI104
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P60059","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI105
Number of Residues	225
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"29519914","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI106
Number of Residues	39
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI107
Number of Residues	52
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI108
Number of Residues	27
Details	Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI109
Number of Residues	59
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P39007","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI110
Number of Residues	2
Details	Region: {"description":"Interacts with target acceptor peptide in protein substrate","evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI111
Number of Residues	2
Details	Motif: {"description":"DXD motif 1","evidences":[{"source":"UniProtKB","id":"Q5HTX9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI112
Number of Residues	2
Details	Motif: {"description":"DXD motif 2","evidences":[{"source":"UniProtKB","id":"P39007","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI113
Number of Residues	3
Details	Motif: {"description":"SVSE motif","evidences":[{"source":"UniProtKB","id":"Q5HTX9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI114
Number of Residues	4
Details	Motif: {"description":"WWDYG motif","evidences":[{"source":"UniProtKB","id":"P39007","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI115
Number of Residues	7
Details	Motif: {"description":"DK motif","evidences":[{"source":"UniProtKB","id":"P39007","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI116
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI117
Number of Residues	3
Details	Site: {"description":"Interacts with target acceptor peptide in protein substrate","evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI118
Number of Residues	1
Details	Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI119
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI120
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"UniProtKB","id":"P39007","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		Validation report (PDF)