Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1HM6

X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001786	molecular_function	phosphatidylserine binding
A	0001891	cellular_component	phagocytic cup
A	0002250	biological_process	adaptive immune response
A	0002376	biological_process	immune system process
A	0002548	biological_process	monocyte chemotaxis
A	0002685	biological_process	regulation of leukocyte migration
A	0004859	molecular_function	phospholipase inhibitor activity
A	0005509	molecular_function	calcium ion binding
A	0005544	molecular_function	calcium-dependent phospholipid binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005768	cellular_component	endosome
A	0005769	cellular_component	early endosome
A	0005886	cellular_component	plasma membrane
A	0005929	cellular_component	cilium
A	0006909	biological_process	phagocytosis
A	0006954	biological_process	inflammatory response
A	0007165	biological_process	signal transduction
A	0007187	biological_process	G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger
A	0008360	biological_process	regulation of cell shape
A	0012506	cellular_component	vesicle membrane
A	0016020	cellular_component	membrane
A	0016323	cellular_component	basolateral plasma membrane
A	0016324	cellular_component	apical plasma membrane
A	0016328	cellular_component	lateral plasma membrane
A	0019834	molecular_function	phospholipase A2 inhibitor activity
A	0030036	biological_process	actin cytoskeleton organization
A	0030659	cellular_component	cytoplasmic vesicle membrane
A	0031410	cellular_component	cytoplasmic vesicle
A	0031514	cellular_component	motile cilium
A	0031901	cellular_component	early endosome membrane
A	0032652	biological_process	regulation of interleukin-1 production
A	0032743	biological_process	positive regulation of interleukin-2 production
A	0042102	biological_process	positive regulation of T cell proliferation
A	0042119	biological_process	neutrophil activation
A	0045087	biological_process	innate immune response
A	0045627	biological_process	positive regulation of T-helper 1 cell differentiation
A	0045629	biological_process	negative regulation of T-helper 2 cell differentiation
A	0045920	biological_process	negative regulation of exocytosis
A	0046872	molecular_function	metal ion binding
A	0046883	biological_process	regulation of hormone secretion
A	0050727	biological_process	regulation of inflammatory response
A	0070062	cellular_component	extracellular exosome
A	0071385	biological_process	cellular response to glucocorticoid stimulus
A	0071621	biological_process	granulocyte chemotaxis
A	0090303	biological_process	positive regulation of wound healing
B	0001786	molecular_function	phosphatidylserine binding
B	0001891	cellular_component	phagocytic cup
B	0002250	biological_process	adaptive immune response
B	0002376	biological_process	immune system process
B	0002548	biological_process	monocyte chemotaxis
B	0002685	biological_process	regulation of leukocyte migration
B	0004859	molecular_function	phospholipase inhibitor activity
B	0005509	molecular_function	calcium ion binding
B	0005544	molecular_function	calcium-dependent phospholipid binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005768	cellular_component	endosome
B	0005769	cellular_component	early endosome
B	0005886	cellular_component	plasma membrane
B	0005929	cellular_component	cilium
B	0006909	biological_process	phagocytosis
B	0006954	biological_process	inflammatory response
B	0007165	biological_process	signal transduction
B	0007187	biological_process	G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger
B	0008360	biological_process	regulation of cell shape
B	0012506	cellular_component	vesicle membrane
B	0016020	cellular_component	membrane
B	0016323	cellular_component	basolateral plasma membrane
B	0016324	cellular_component	apical plasma membrane
B	0016328	cellular_component	lateral plasma membrane
B	0019834	molecular_function	phospholipase A2 inhibitor activity
B	0030036	biological_process	actin cytoskeleton organization
B	0030659	cellular_component	cytoplasmic vesicle membrane
B	0031410	cellular_component	cytoplasmic vesicle
B	0031514	cellular_component	motile cilium
B	0031901	cellular_component	early endosome membrane
B	0032652	biological_process	regulation of interleukin-1 production
B	0032743	biological_process	positive regulation of interleukin-2 production
B	0042102	biological_process	positive regulation of T cell proliferation
B	0042119	biological_process	neutrophil activation
B	0045087	biological_process	innate immune response
B	0045627	biological_process	positive regulation of T-helper 1 cell differentiation
B	0045629	biological_process	negative regulation of T-helper 2 cell differentiation
B	0045920	biological_process	negative regulation of exocytosis
B	0046872	molecular_function	metal ion binding
B	0046883	biological_process	regulation of hormone secretion
B	0050727	biological_process	regulation of inflammatory response
B	0070062	cellular_component	extracellular exosome
B	0071385	biological_process	cellular response to glucocorticoid stimulus
B	0071621	biological_process	granulocyte chemotaxis
B	0090303	biological_process	positive regulation of wound healing

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 801

Chain	Residue
A	ARG124
A	LYS128
A	HOH1010
A	HOH1015
A	HOH1063

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 802

Chain	Residue
B	ARG234
B	ARG235
B	GLN238
B	HOH961

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 803

Chain	Residue
A	THR145
A	ARG147
A	HOH810
A	HOH879

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 804

Chain	Residue
A	ARG234
A	ARG235
A	GLN238
A	HOH887
A	HOH1053

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 805

Chain	Residue
A	ARG124
A	LYS128
A	GLY129
A	HOH1012
A	HOH1013
A	HOH1082

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 806

Chain	Residue
A	LYS81
A	GLN117
A	HOH872
A	HOH983
A	HOH985

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 807

Chain	Residue
A	ARG212
B	ARG213
B	THR216
B	HOH900

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 808

Chain	Residue
B	ARG124
B	LYS128
B	HOH1202

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 809

Chain	Residue
B	ARG124
B	LYS128
B	GLY129

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 800

Chain	Residue
B	THR145
B	ARG147
B	HOH827

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 811

Chain	Residue
A	ASN249
B	THR291
B	HIS293
B	LYS294
B	HOH1136

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 812

Chain	Residue
B	GLY174
B	ASP175
B	LYS257
B	HOH848
B	HOH990
B	HOH1144

Functional Information from PROSITE/UniProt

site_id	PS00223
Number of Residues	53
Details	ANNEXIN_1 Annexin repeat signature. GVdeatiieiLtkRtnaQrqQikaaYlqekgkpLdeaLkkaltGhleevAlaL

Chain	Residue	Details
A	GLY59-LEU111
A	GLY131-LEU183
A	GLY215-VAL267
A	GLY290-LEU342

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	Peptide: {"description":"Annexin Ac2-26","featureId":"PRO_0000454559","evidences":[{"source":"UniProtKB","id":"P04083","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	142
Details	Repeat: {"description":"Annexin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	142
Details	Repeat: {"description":"Annexin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	144
Details	Repeat: {"description":"Annexin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	142
Details	Repeat: {"description":"Annexin 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	44
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	52
Details	Binding site: {"evidences":[{"source":"PDB","id":"1MCX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Site: {"description":"Cleavage; by CTSG","evidences":[{"source":"UniProtKB","id":"P04083","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P04083","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by TRPM7","evidences":[{"source":"UniProtKB","id":"P04083","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine; by EGFR","evidences":[{"source":"PubMed","id":"3020049","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P04083","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04083","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P10107","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P04083","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Cross-link: {"description":"Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"UniProtKB","id":"P04083","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P04083","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"UniProtKB","id":"P10107","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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