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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7PCB

The PDZ domain of SNX27 fused with ANXA2

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0001533cellular_componentcornified envelope
A0001765biological_processmembrane raft assembly
A0001786molecular_functionphosphatidylserine binding
A0001921biological_processpositive regulation of receptor recycling
A0002020molecular_functionprotease binding
A0002091biological_processnegative regulation of receptor internalization
A0003723molecular_functionRNA binding
A0004859molecular_functionphospholipase inhibitor activity
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005544molecular_functioncalcium-dependent phospholipid binding
A0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
A0005576cellular_componentextracellular region
A0005604cellular_componentbasement membrane
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005768cellular_componentendosome
A0005769cellular_componentearly endosome
A0005811cellular_componentlipid droplet
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005912cellular_componentadherens junction
A0006900biological_processvesicle budding from membrane
A0007155biological_processcell adhesion
A0007160biological_processcell-matrix adhesion
A0008092molecular_functioncytoskeletal protein binding
A0009986cellular_componentcell surface
A0010756biological_processpositive regulation of plasminogen activation
A0012506cellular_componentvesicle membrane
A0014823biological_processresponse to activity
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016363cellular_componentnuclear matrix
A0019834molecular_functionphospholipase A2 inhibitor activity
A0030199biological_processcollagen fibril organization
A0030324biological_processlung development
A0030496cellular_componentmidbody
A0031012cellular_componentextracellular matrix
A0031340biological_processpositive regulation of vesicle fusion
A0031902cellular_componentlate endosome membrane
A0031982cellular_componentvesicle
A0032804biological_processnegative regulation of low-density lipoprotein particle receptor catabolic process
A0035578cellular_componentazurophil granule lumen
A0035749cellular_componentmyelin sheath adaxonal region
A0036035biological_processosteoclast development
A0042383cellular_componentsarcolemma
A0042470cellular_componentmelanosome
A0042730biological_processfibrinolysis
A0042789biological_processmRNA transcription by RNA polymerase II
A0042802molecular_functionidentical protein binding
A0043220cellular_componentSchmidt-Lanterman incisure
A0044090biological_processpositive regulation of vacuole organization
A0044548molecular_functionS100 protein binding
A0045121cellular_componentmembrane raft
A0045921biological_processpositive regulation of exocytosis
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0048306molecular_functioncalcium-dependent protein binding
A0050767biological_processregulation of neurogenesis
A0051051biological_processnegative regulation of transport
A0051240biological_processpositive regulation of multicellular organismal process
A0070062cellular_componentextracellular exosome
A0090575cellular_componentRNA polymerase II transcription regulator complex
A0098609biological_processcell-cell adhesion
A0098641molecular_functioncadherin binding involved in cell-cell adhesion
A0098797cellular_componentplasma membrane protein complex
A1904019biological_processepithelial cell apoptotic process
A1905581biological_processpositive regulation of low-density lipoprotein particle clearance
A1905602biological_processpositive regulation of receptor-mediated endocytosis involved in cholesterol transport
A1905686biological_processpositive regulation of plasma membrane repair
A1990665cellular_componentAnxA2-p11 complex
A1990667cellular_componentPCSK9-AnxA2 complex
Functional Information from PROSITE/UniProt
site_idPS00223
Number of Residues53
DetailsANNEXIN_1 Annexin repeat signature. GVdevtivniLtnRsneQrqDiafaYqrrtkkeLasaLksalsGhletvIlgL
ChainResidueDetails
AGLY165-LEU217
AGLY237-LEU289
AGLY322-LEU374
AGLY397-LEU449
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 Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"15302870","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28669632","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"28669632","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2946940","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P07356","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07356","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P07356","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues93
DetailsDomain: {"description":"PDZ","evidences":[{"source":"PROSITE-ProRule","id":"PRU00143","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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