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4CYM

Complex of human VARP-ANKRD1 with Rab32-GppCp

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005769cellular_componentearly endosome
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005802cellular_componenttrans-Golgi network
A0005829cellular_componentcytosol
A0006886biological_processintracellular protein transport
A0007005biological_processmitochondrion organization
A0012505cellular_componentendomembrane system
A0016020cellular_componentmembrane
A0016192biological_processvesicle-mediated transport
A0016787molecular_functionhydrolase activity
A0019882biological_processantigen processing and presentation
A0030670cellular_componentphagocytic vesicle membrane
A0030742molecular_functionGTP-dependent protein binding
A0031090cellular_componentorganelle membrane
A0031410cellular_componentcytoplasmic vesicle
A0031905cellular_componentearly endosome lumen
A0031982cellular_componentvesicle
A0032438biological_processmelanosome organization
A0033162cellular_componentmelanosome membrane
A0035612molecular_functionAP-2 adaptor complex binding
A0035646biological_processendosome to melanosome transport
A0035650molecular_functionAP-1 adaptor complex binding
A0035651molecular_functionAP-3 adaptor complex binding
A0036461molecular_functionBLOC-2 complex binding
A0042470cellular_componentmelanosome
A0044233cellular_componentmitochondria-associated endoplasmic reticulum membrane contact site
A0045335cellular_componentphagocytic vesicle
A0072657biological_processprotein localization to membrane
A0090382biological_processphagosome maturation
A1903232biological_processmelanosome assembly
B0000166molecular_functionnucleotide binding
B0003924molecular_functionGTPase activity
B0003925molecular_functionG protein activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005739cellular_componentmitochondrion
B0005741cellular_componentmitochondrial outer membrane
B0005769cellular_componentearly endosome
B0005783cellular_componentendoplasmic reticulum
B0005794cellular_componentGolgi apparatus
B0005802cellular_componenttrans-Golgi network
B0005829cellular_componentcytosol
B0006886biological_processintracellular protein transport
B0007005biological_processmitochondrion organization
B0012505cellular_componentendomembrane system
B0016020cellular_componentmembrane
B0016192biological_processvesicle-mediated transport
B0016787molecular_functionhydrolase activity
B0019882biological_processantigen processing and presentation
B0030670cellular_componentphagocytic vesicle membrane
B0030742molecular_functionGTP-dependent protein binding
B0031090cellular_componentorganelle membrane
B0031410cellular_componentcytoplasmic vesicle
B0031905cellular_componentearly endosome lumen
B0031982cellular_componentvesicle
B0032438biological_processmelanosome organization
B0033162cellular_componentmelanosome membrane
B0035612molecular_functionAP-2 adaptor complex binding
B0035646biological_processendosome to melanosome transport
B0035650molecular_functionAP-1 adaptor complex binding
B0035651molecular_functionAP-3 adaptor complex binding
B0036461molecular_functionBLOC-2 complex binding
B0042470cellular_componentmelanosome
B0044233cellular_componentmitochondria-associated endoplasmic reticulum membrane contact site
B0045335cellular_componentphagocytic vesicle
B0072657biological_processprotein localization to membrane
B0090382biological_processphagosome maturation
B1903232biological_processmelanosome assembly
C0000166molecular_functionnucleotide binding
C0003924molecular_functionGTPase activity
C0003925molecular_functionG protein activity
C0005515molecular_functionprotein binding
C0005525molecular_functionGTP binding
C0005739cellular_componentmitochondrion
C0005741cellular_componentmitochondrial outer membrane
C0005769cellular_componentearly endosome
C0005783cellular_componentendoplasmic reticulum
C0005794cellular_componentGolgi apparatus
C0005802cellular_componenttrans-Golgi network
C0005829cellular_componentcytosol
C0006886biological_processintracellular protein transport
C0007005biological_processmitochondrion organization
C0012505cellular_componentendomembrane system
C0016020cellular_componentmembrane
C0016192biological_processvesicle-mediated transport
C0016787molecular_functionhydrolase activity
C0019882biological_processantigen processing and presentation
C0030670cellular_componentphagocytic vesicle membrane
C0030742molecular_functionGTP-dependent protein binding
C0031090cellular_componentorganelle membrane
C0031410cellular_componentcytoplasmic vesicle
C0031905cellular_componentearly endosome lumen
C0031982cellular_componentvesicle
C0032438biological_processmelanosome organization
C0033162cellular_componentmelanosome membrane
C0035612molecular_functionAP-2 adaptor complex binding
C0035646biological_processendosome to melanosome transport
C0035650molecular_functionAP-1 adaptor complex binding
C0035651molecular_functionAP-3 adaptor complex binding
C0036461molecular_functionBLOC-2 complex binding
C0042470cellular_componentmelanosome
C0044233cellular_componentmitochondria-associated endoplasmic reticulum membrane contact site
C0045335cellular_componentphagocytic vesicle
C0072657biological_processprotein localization to membrane
C0090382biological_processphagosome maturation
C1903232biological_processmelanosome assembly
Functional Information from PDB Data
site_idAC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE GCP A 1198
ChainResidue
ALEU34
AGLN52
ATYR54
AALA56
ATHR57
AGLY84
AASN143
ALYS144
AASP146
AGLN147
ASER174
AGLY35
AALA175
ALYS176
AMG1199
AHOH2003
AHOH2004
AHOH2012
AHOH2013
AVAL36
AGLY37
ALYS38
ATHR39
ASER40
APHE50
ASER51

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1199
ChainResidue
ATHR39
ATHR57
AGCP1198
AHOH2003
AHOH2004

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE GCP B 1198
ChainResidue
BLEU34
BGLY35
BVAL36
BGLY37
BLYS38
BTHR39
BSER40
BPHE50
BSER51
BGLN52
BTYR54
BALA56
BTHR57
BGLY84
BASN143
BLYS144
BASP146
BSER174
BALA175
BLYS176
BMG1199
BHOH2003
BHOH2004
BHOH2008

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 1199
ChainResidue
BTHR39
BTHR57
BGCP1198
BHOH2003
BHOH2004

site_idAC5
Number of Residues27
DetailsBINDING SITE FOR RESIDUE GCP C 1198
ChainResidue
CGLU33
CLEU34
CGLY35
CVAL36
CGLY37
CLYS38
CTHR39
CSER40
CPHE50
CSER51
CGLN52
CHIS53
CTYR54
CALA56
CTHR57
CGLY84
CASN143
CLYS144
CASP146
CGLN147
CSER174
CALA175
CLYS176
CMG1199
CHOH2003
CHOH2004
CHOH2006

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 1199
ChainResidue
CTHR39
CTHR57
CGCP1198
CHOH2003
CHOH2004

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues32
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGKTSIIKrYvhqlfsqhyratigvd..FALK
ChainResidueDetails
ALEU34-LYS65

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues57
DetailsRegion: {"description":"PKA-RII subunit binding domain"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues42
DetailsMotif: {"description":"Switch 1","evidences":[{"source":"PubMed","id":"24856514","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CYM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CZ2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues39
DetailsMotif: {"description":"Switch 2","evidences":[{"source":"PubMed","id":"24856514","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CYM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CZ2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues39
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24856514","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4CYM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CZ2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24856514","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CYM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CZ2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24856514","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CZ2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues87
DetailsRepeat: {"description":"ANK 2"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues87
DetailsRepeat: {"description":"ANK 3"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues96
DetailsRepeat: {"description":"ANK 4"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues87
DetailsRepeat: {"description":"ANK 5"}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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