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7NMI

Transactivation domain of p53 in complex with S100P, using annexin A2 as crystallization chaperone

Functional Information from GO Data
ChainGOidnamespacecontents
B0000287molecular_functionmagnesium ion binding
B0001525biological_processangiogenesis
B0001533cellular_componentcornified envelope
B0001765biological_processmembrane raft assembly
B0001786molecular_functionphosphatidylserine binding
B0001921biological_processpositive regulation of receptor recycling
B0002020molecular_functionprotease binding
B0002091biological_processnegative regulation of receptor internalization
B0003723molecular_functionRNA binding
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005544molecular_functioncalcium-dependent phospholipid binding
B0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
B0005576cellular_componentextracellular region
B0005604cellular_componentbasement membrane
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005765cellular_componentlysosomal membrane
B0005768cellular_componentendosome
B0005769cellular_componentearly endosome
B0005811cellular_componentlipid droplet
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005912cellular_componentadherens junction
B0006900biological_processvesicle budding from membrane
B0007155biological_processcell adhesion
B0007160biological_processcell-matrix adhesion
B0009986cellular_componentcell surface
B0010756biological_processpositive regulation of plasminogen activation
B0012506cellular_componentvesicle membrane
B0014823biological_processresponse to activity
B0016020cellular_componentmembrane
B0016323cellular_componentbasolateral plasma membrane
B0016363cellular_componentnuclear matrix
B0019834molecular_functionphospholipase A2 inhibitor activity
B0030199biological_processcollagen fibril organization
B0030324biological_processlung development
B0030496cellular_componentmidbody
B0031012cellular_componentextracellular matrix
B0031340biological_processpositive regulation of vesicle fusion
B0031528cellular_componentmicrovillus membrane
B0031902cellular_componentlate endosome membrane
B0031982cellular_componentvesicle
B0032804biological_processnegative regulation of low-density lipoprotein particle receptor catabolic process
B0034774cellular_componentsecretory granule lumen
B0035578cellular_componentazurophil granule lumen
B0035749cellular_componentmyelin sheath adaxonal region
B0036035biological_processosteoclast development
B0042383cellular_componentsarcolemma
B0042470cellular_componentmelanosome
B0042730biological_processfibrinolysis
B0042789biological_processmRNA transcription by RNA polymerase II
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0042995cellular_componentcell projection
B0043220cellular_componentSchmidt-Lanterman incisure
B0043542biological_processendothelial cell migration
B0044090biological_processpositive regulation of vacuole organization
B0044548molecular_functionS100 protein binding
B0045121cellular_componentmembrane raft
B0045296molecular_functioncadherin binding
B0045921biological_processpositive regulation of exocytosis
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0046872molecular_functionmetal ion binding
B0046914molecular_functiontransition metal ion binding
B0048306molecular_functioncalcium-dependent protein binding
B0050767biological_processregulation of neurogenesis
B0050819biological_processnegative regulation of coagulation
B0051051biological_processnegative regulation of transport
B0051240biological_processpositive regulation of multicellular organismal process
B0070062cellular_componentextracellular exosome
B0090575cellular_componentRNA polymerase II transcription regulator complex
B0098609biological_processcell-cell adhesion
B0098641molecular_functioncadherin binding involved in cell-cell adhesion
B0098797cellular_componentplasma membrane protein complex
B1904019biological_processepithelial cell apoptotic process
B1905581biological_processpositive regulation of low-density lipoprotein particle clearance
B1905602biological_processpositive regulation of receptor-mediated endocytosis involved in cholesterol transport
B1905686biological_processpositive regulation of plasma membrane repair
B1990665cellular_componentAnxA2-p11 complex
B1990667cellular_componentPCSK9-AnxA2 complex
Functional Information from PROSITE/UniProt
site_idPS00223
Number of Residues53
DetailsANNEXIN_1 Annexin repeat signature. GVdevtivniLtnRsneQrqDiafaYqrrtkkeLasaLksalsGhletvIlgL
ChainResidueDetails
BGLY222-LEU274
BGLY294-LEU346
BGLY379-LEU431
BGLY454-LEU506

site_idPS00303
Number of Residues22
DetailsS100_CABP S-100/ICaBP type calcium binding protein signature. LLkdLDangDaqvDFsEFivFV
ChainResidueDetails
BLEU57-VAL78
BLEU160-VAL181

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by CHEK2, CK1 and PLK3","evidences":[{"source":"PubMed","id":"10570149","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11447225","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11551930","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12810724","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20041275","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by CDK5 and CDK7","evidences":[{"source":"PubMed","id":"17591690","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9372954","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by MAPKAPK5","evidences":[{"source":"PubMed","id":"17254968","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by CDK5, DYRK2, HIPK2 and PKC/PRKCG","evidences":[{"source":"PubMed","id":"11740489","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11780126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16377624","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17349958","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17591690","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by TAF1 and GRK5","evidences":[{"source":"PubMed","id":"15053879","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20124405","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"21597459","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues71
DetailsRepeat: {"description":"Annexin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues71
DetailsRepeat: {"description":"Annexin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues72
DetailsRepeat: {"description":"Annexin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues71
DetailsRepeat: {"description":"Annexin 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P07356","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07356","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P07356","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
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_FI16
Number of Residues35
DetailsDomain: {"description":"EF-hand 1","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues35
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues8
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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