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1AIN

CRYSTAL STRUCTURE OF HUMAN ANNEXIN I AT 2.5 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0001533cellular_componentcornified envelope
A0001780biological_processneutrophil homeostasis
A0001786molecular_functionphosphatidylserine binding
A0001891cellular_componentphagocytic cup
A0002250biological_processadaptive immune response
A0002376biological_processimmune system process
A0002548biological_processmonocyte chemotaxis
A0002685biological_processregulation of leukocyte migration
A0004859molecular_functionphospholipase inhibitor activity
A0005102molecular_functionsignaling receptor binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005543molecular_functionphospholipid binding
A0005544molecular_functioncalcium-dependent phospholipid binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005769cellular_componentearly endosome
A0005829cellular_componentcytosol
A0005884cellular_componentactin filament
A0005886cellular_componentplasma membrane
A0005912cellular_componentadherens junction
A0005925cellular_componentfocal adhesion
A0005929cellular_componentcilium
A0006909biological_processphagocytosis
A0006954biological_processinflammatory response
A0007165biological_processsignal transduction
A0007166biological_processcell surface receptor signaling pathway
A0007187biological_processG protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger
A0008289molecular_functionlipid binding
A0008360biological_processregulation of cell shape
A0009986cellular_componentcell surface
A0010008cellular_componentendosome membrane
A0012506cellular_componentvesicle membrane
A0014839biological_processmyoblast migration involved in skeletal muscle regeneration
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016324cellular_componentapical plasma membrane
A0016328cellular_componentlateral plasma membrane
A0018149biological_processpeptide cross-linking
A0019834molecular_functionphospholipase A2 inhibitor activity
A0030036biological_processactin cytoskeleton organization
A0030216biological_processkeratinocyte differentiation
A0030659cellular_componentcytoplasmic vesicle membrane
A0031012cellular_componentextracellular matrix
A0031340biological_processpositive regulation of vesicle fusion
A0031410cellular_componentcytoplasmic vesicle
A0031514cellular_componentmotile cilium
A0031901cellular_componentearly endosome membrane
A0031982cellular_componentvesicle
A0032652biological_processregulation of interleukin-1 production
A0032717biological_processnegative regulation of interleukin-8 production
A0032743biological_processpositive regulation of interleukin-2 production
A0033031biological_processpositive regulation of neutrophil apoptotic process
A0035924biological_processcellular response to vascular endothelial growth factor stimulus
A0042102biological_processpositive regulation of T cell proliferation
A0042119biological_processneutrophil activation
A0042127biological_processregulation of cell population proliferation
A0042383cellular_componentsarcolemma
A0042995cellular_componentcell projection
A0043066biological_processnegative regulation of apoptotic process
A0045087biological_processinnate immune response
A0045627biological_processpositive regulation of T-helper 1 cell differentiation
A0045629biological_processnegative regulation of T-helper 2 cell differentiation
A0045920biological_processnegative regulation of exocytosis
A0046632biological_processalpha-beta T cell differentiation
A0046872molecular_functionmetal ion binding
A0046883biological_processregulation of hormone secretion
A0048306molecular_functioncalcium-dependent protein binding
A0050482biological_processarachidonate secretion
A0050727biological_processregulation of inflammatory response
A0051051biological_processnegative regulation of transport
A0051240biological_processpositive regulation of multicellular organismal process
A0070062cellular_componentextracellular exosome
A0071385biological_processcellular response to glucocorticoid stimulus
A0071621biological_processgranulocyte chemotaxis
A0090050biological_processpositive regulation of cell migration involved in sprouting angiogenesis
A0090303biological_processpositive regulation of wound healing
A0097350biological_processneutrophil clearance
A0098609biological_processcell-cell adhesion
A0098641molecular_functioncadherin binding involved in cell-cell adhesion
A1900087biological_processpositive regulation of G1/S transition of mitotic cell cycle
Functional Information from PDB Data
site_idCA1
Number of Residues3
Details
ChainResidue
AGLY32
AVAL33
AGLU35

site_idCA2
Number of Residues3
Details
ChainResidue
ALYS70
ALEU73
AGLU78

site_idCA3
Number of Residues4
Details
ChainResidue
AASP144
AMET100
AGLY102
AGLY104

site_idCA4
Number of Residues4
Details
ChainResidue
AGLY183
AARG186
AGLY188
AGLU228

site_idCA5
Number of Residues4
Details
ChainResidue
AMET259
AGLY261
AGLY263
AGLU303

site_idCA6
Number of Residues3
Details
ChainResidue
ALEU301
ATHR304
AGLU309

Functional Information from PROSITE/UniProt
site_idPS00223
Number of Residues53
DetailsANNEXIN_1 Annexin repeat signature. GVdeatiidiLtkRnnaQrqQikaaYlqetgkpLdetLkkaltGhleevVlaL
ChainResidueDetails
AGLY32-LEU84
AGLY104-LEU156
AGLY188-ILE240
AGLY263-LEU315

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues71
DetailsRepeat: {"description":"Annexin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues71
DetailsRepeat: {"description":"Annexin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues72
DetailsRepeat: {"description":"Annexin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues71
DetailsRepeat: {"description":"Annexin 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues26
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P19619","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P10107","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25772364","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"UniProtKB","id":"P10107","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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