Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

9FPZ

Human NatA-MAP2 80S ribosome complex

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
2	0004596	molecular_function	protein-N-terminal amino-acid acetyltransferase activity
2	0006474	biological_process	N-terminal protein amino acid acetylation
2	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
2	0031415	cellular_component	NatA complex
A	0003723	molecular_function	RNA binding
A	0004177	molecular_function	aminopeptidase activity
A	0004239	molecular_function	initiator methionyl aminopeptidase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006446	biological_process	regulation of translational initiation
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008235	molecular_function	metalloexopeptidase activity
A	0016485	biological_process	protein processing
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
A	0070006	molecular_function	metalloaminopeptidase activity
B	0001525	biological_process	angiogenesis
B	0003723	molecular_function	RNA binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005667	cellular_component	transcription regulator complex
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006351	biological_process	DNA-templated transcription
B	0010698	molecular_function	acetyltransferase activator activity
B	0016020	cellular_component	membrane
B	0016407	molecular_function	acetyltransferase activity
B	0016604	cellular_component	nuclear body
B	0030154	biological_process	cell differentiation
B	0031415	cellular_component	NatA complex
B	0043022	molecular_function	ribosome binding
B	0045893	biological_process	positive regulation of DNA-templated transcription
B	0050821	biological_process	protein stabilization
B	0051604	biological_process	protein maturation
LC	0002181	biological_process	cytoplasmic translation
LC	0003723	molecular_function	RNA binding
LC	0003735	molecular_function	structural constituent of ribosome
LC	0005515	molecular_function	protein binding
LC	0005634	cellular_component	nucleus
LC	0005730	cellular_component	nucleolus
LC	0005737	cellular_component	cytoplasm
LC	0005791	cellular_component	rough endoplasmic reticulum
LC	0005829	cellular_component	cytosol
LC	0005840	cellular_component	ribosome
LC	0005925	cellular_component	focal adhesion
LC	0006412	biological_process	translation
LC	0006941	biological_process	striated muscle contraction
LC	0007283	biological_process	spermatogenesis
LC	0016020	cellular_component	membrane
LC	0022625	cellular_component	cytosolic large ribosomal subunit
LC	0022626	cellular_component	cytosolic ribosome
LC	0070062	cellular_component	extracellular exosome
LC	1901740	biological_process	negative regulation of myoblast fusion
LC	1990904	cellular_component	ribonucleoprotein complex
LE	0002181	biological_process	cytoplasmic translation
LE	0003677	molecular_function	DNA binding
LE	0003723	molecular_function	RNA binding
LE	0003735	molecular_function	structural constituent of ribosome
LE	0005515	molecular_function	protein binding
LE	0005634	cellular_component	nucleus
LE	0005737	cellular_component	cytoplasm
LE	0005791	cellular_component	rough endoplasmic reticulum
LE	0005829	cellular_component	cytosol
LE	0005840	cellular_component	ribosome
LE	0005925	cellular_component	focal adhesion
LE	0006355	biological_process	regulation of DNA-templated transcription
LE	0006412	biological_process	translation
LE	0006941	biological_process	striated muscle contraction
LE	0007283	biological_process	spermatogenesis
LE	0014069	cellular_component	postsynaptic density
LE	0015934	cellular_component	large ribosomal subunit
LE	0016020	cellular_component	membrane
LE	0022625	cellular_component	cytosolic large ribosomal subunit
LE	0022626	cellular_component	cytosolic ribosome
LE	0036464	cellular_component	cytoplasmic ribonucleoprotein granule
LE	0045202	cellular_component	synapse
LE	0045296	molecular_function	cadherin binding
LE	1901740	biological_process	negative regulation of myoblast fusion
LE	1990904	cellular_component	ribonucleoprotein complex
Lh	0000463	biological_process	maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
Lh	0002181	biological_process	cytoplasmic translation
Lh	0003723	molecular_function	RNA binding
Lh	0003729	molecular_function	mRNA binding
Lh	0003735	molecular_function	structural constituent of ribosome
Lh	0005515	molecular_function	protein binding
Lh	0005730	cellular_component	nucleolus
Lh	0005737	cellular_component	cytoplasm
Lh	0005829	cellular_component	cytosol
Lh	0005840	cellular_component	ribosome
Lh	0006412	biological_process	translation
Lh	0006941	biological_process	striated muscle contraction
Lh	0007283	biological_process	spermatogenesis
Lh	0015934	cellular_component	large ribosomal subunit
Lh	0016020	cellular_component	membrane
Lh	0022625	cellular_component	cytosolic large ribosomal subunit
Lh	0022626	cellular_component	cytosolic ribosome
Lh	1901740	biological_process	negative regulation of myoblast fusion
Lh	1990904	cellular_component	ribonucleoprotein complex
Lk	0002181	biological_process	cytoplasmic translation
Lk	0003723	molecular_function	RNA binding
Lk	0003735	molecular_function	structural constituent of ribosome
Lk	0005515	molecular_function	protein binding
Lk	0005737	cellular_component	cytoplasm
Lk	0005783	cellular_component	endoplasmic reticulum
Lk	0005829	cellular_component	cytosol
Lk	0005840	cellular_component	ribosome
Lk	0005925	cellular_component	focal adhesion
Lk	0006412	biological_process	translation
Lk	0006941	biological_process	striated muscle contraction
Lk	0007283	biological_process	spermatogenesis
Lk	0014069	cellular_component	postsynaptic density
Lk	0022618	biological_process	protein-RNA complex assembly
Lk	0022625	cellular_component	cytosolic large ribosomal subunit
Lk	0022626	cellular_component	cytosolic ribosome
Lk	0033291	cellular_component	eukaryotic 80S initiation complex
Lk	0045202	cellular_component	synapse
Lk	1901740	biological_process	negative regulation of myoblast fusion
Lk	1990904	cellular_component	ribonucleoprotein complex
Lr	0002181	biological_process	cytoplasmic translation
Lr	0003723	molecular_function	RNA binding
Lr	0003735	molecular_function	structural constituent of ribosome
Lr	0005515	molecular_function	protein binding
Lr	0005737	cellular_component	cytoplasm
Lr	0005783	cellular_component	endoplasmic reticulum
Lr	0005829	cellular_component	cytosol
Lr	0005840	cellular_component	ribosome
Lr	0006412	biological_process	translation
Lr	0006941	biological_process	striated muscle contraction
Lr	0007283	biological_process	spermatogenesis
Lr	0016020	cellular_component	membrane
Lr	0022625	cellular_component	cytosolic large ribosomal subunit
Lr	0022626	cellular_component	cytosolic ribosome
Lr	0030425	cellular_component	dendrite
Lr	0036464	cellular_component	cytoplasmic ribonucleoprotein granule
Lr	0044297	cellular_component	cell body
Lr	0045202	cellular_component	synapse
Lr	0070062	cellular_component	extracellular exosome
Lr	1901740	biological_process	negative regulation of myoblast fusion
Lr	1990904	cellular_component	ribonucleoprotein complex
LR	0002181	biological_process	cytoplasmic translation
LR	0003723	molecular_function	RNA binding
LR	0003735	molecular_function	structural constituent of ribosome
LR	0005515	molecular_function	protein binding
LR	0005730	cellular_component	nucleolus
LR	0005737	cellular_component	cytoplasm
LR	0005829	cellular_component	cytosol
LR	0005840	cellular_component	ribosome
LR	0005925	cellular_component	focal adhesion
LR	0006412	biological_process	translation
LR	0006941	biological_process	striated muscle contraction
LR	0007283	biological_process	spermatogenesis
LR	0016020	cellular_component	membrane
LR	0022625	cellular_component	cytosolic large ribosomal subunit
LR	0022626	cellular_component	cytosolic ribosome
LR	0045202	cellular_component	synapse
LR	1901740	biological_process	negative regulation of myoblast fusion
LR	1990904	cellular_component	ribonucleoprotein complex
LX	0002181	biological_process	cytoplasmic translation
LX	0003723	molecular_function	RNA binding
LX	0003735	molecular_function	structural constituent of ribosome
LX	0005515	molecular_function	protein binding
LX	0005634	cellular_component	nucleus
LX	0005730	cellular_component	nucleolus
LX	0005737	cellular_component	cytoplasm
LX	0005829	cellular_component	cytosol
LX	0005840	cellular_component	ribosome
LX	0006412	biological_process	translation
LX	0006941	biological_process	striated muscle contraction
LX	0007283	biological_process	spermatogenesis
LX	0019843	molecular_function	rRNA binding
LX	0022625	cellular_component	cytosolic large ribosomal subunit
LX	0022626	cellular_component	cytosolic ribosome
LX	0045296	molecular_function	cadherin binding
LX	0070062	cellular_component	extracellular exosome
LX	1901740	biological_process	negative regulation of myoblast fusion
LX	1904841	molecular_function	TORC2 complex binding
LX	1990904	cellular_component	ribonucleoprotein complex
LY	0002181	biological_process	cytoplasmic translation
LY	0003723	molecular_function	RNA binding
LY	0003735	molecular_function	structural constituent of ribosome
LY	0005515	molecular_function	protein binding
LY	0005654	cellular_component	nucleoplasm
LY	0005730	cellular_component	nucleolus
LY	0005737	cellular_component	cytoplasm
LY	0005829	cellular_component	cytosol
LY	0005840	cellular_component	ribosome
LY	0006364	biological_process	rRNA processing
LY	0006412	biological_process	translation
LY	0015934	cellular_component	large ribosomal subunit
LY	0016020	cellular_component	membrane
LY	0022625	cellular_component	cytosolic large ribosomal subunit
LY	0022626	cellular_component	cytosolic ribosome
LY	0030330	biological_process	DNA damage response, signal transduction by p53 class mediator
LY	0034644	biological_process	cellular response to UV
LY	0042273	biological_process	ribosomal large subunit biogenesis
LY	0043517	biological_process	positive regulation of DNA damage response, signal transduction by p53 class mediator
LY	0045727	biological_process	positive regulation of translation
LY	0048027	molecular_function	mRNA 5'-UTR binding
LY	0070062	cellular_component	extracellular exosome
LY	0071480	biological_process	cellular response to gamma radiation
LY	1902167	biological_process	positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator
LY	1904803	biological_process	regulation of translation involved in cellular response to UV
LY	1990904	cellular_component	ribonucleoprotein complex

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
LX	LYS134-VAL149

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

Chain	Residue	Details
LR	GLN7-PRO26

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

Chain	Residue	Details
Lh	LYS43-VAL57

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

Chain	Residue	Details
LC	GLY15-VAL22

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

Chain	Residue	Details
LC	ASN116-HIS142

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

Chain	Residue	Details
LY	ASP52-VAL70

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

Chain	Residue	Details
LE	ASN182-LYS200

site_id	PS01202
Number of Residues	17
Details	MAP_2 Methionine aminopeptidase subfamily 2 signature. DIcKIDfGtHISGriiD

Chain	Residue	Details
A	ASP246-ASP262

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"27708256","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03175","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16540317","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03175","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14534293","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16134930","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16540317","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17350258","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17636946","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	33
Details	Repeat: {"description":"TPR 1"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	33
Details	Repeat: {"description":"TPR 2"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	36
Details	Repeat: {"description":"TPR 3"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	33
Details	Repeat: {"description":"TPR 4"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	33
Details	Repeat: {"description":"TPR 5"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	32
Details	Repeat: {"description":"TPR 6"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	33
Details	Repeat: {"description":"TPR 7"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	33
Details	Repeat: {"description":"TPR 8"}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	120
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	17
Details	Motif: {"description":"Bipartite nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	30
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	19
Details	Compositional bias: {"description":"Basic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	10
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
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_FI20
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9D8E6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P50878","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	1
Details	Modified residue: {"description":"Citrulline","evidences":[{"source":"UniProtKB","id":"Q9D8E6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
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_FI26
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

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 SUMO1); alternate","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P47911","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17924679","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	1
Details	Modified residue: {"description":"Citrulline","evidences":[{"source":"UniProtKB","id":"P62751","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI35
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_FI36
Number of Residues	3
Details	Modified residue: {"description":"Citrulline","evidences":[{"source":"UniProtKB","id":"P84099","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI37
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI38
Number of Residues	1
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"12962325","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Boldt K.","von Kriegsheim A.","Lilla S.","Lempens A.","Kolch W."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI39
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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