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5SZI

Structure of human Rab8a in complex with the bMERB domain of Mical-cL

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000166molecular_functionnucleotide binding
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005768cellular_componentendosome
A0005794cellular_componentGolgi apparatus
A0005813cellular_componentcentrosome
A0005814cellular_componentcentriole
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005929cellular_componentcilium
A0005930cellular_componentaxoneme
A0006887biological_processexocytosis
A0006904biological_processvesicle docking involved in exocytosis
A0006914biological_processautophagy
A0007030biological_processGolgi organization
A0007409biological_processaxonogenesis
A0008021cellular_componentsynaptic vesicle
A0010008cellular_componentendosome membrane
A0010506biological_processregulation of autophagy
A0015031biological_processprotein transport
A0016787molecular_functionhydrolase activity
A0019003molecular_functionGDP binding
A0019901molecular_functionprotein kinase binding
A0030030biological_processcell projection organization
A0030140cellular_componenttrans-Golgi network transport vesicle
A0030425cellular_componentdendrite
A0030496cellular_componentmidbody
A0030670cellular_componentphagocytic vesicle membrane
A0031267molecular_functionsmall GTPase binding
A0031410cellular_componentcytoplasmic vesicle
A0031489molecular_functionmyosin V binding
A0032456biological_processendocytic recycling
A0032588cellular_componenttrans-Golgi network membrane
A0032869biological_processcellular response to insulin stimulus
A0032880biological_processregulation of protein localization
A0036064cellular_componentciliary basal body
A0043025cellular_componentneuronal cell body
A0045202cellular_componentsynapse
A0045335cellular_componentphagocytic vesicle
A0048169biological_processregulation of long-term neuronal synaptic plasticity
A0048210biological_processGolgi vesicle fusion to target membrane
A0051223biological_processregulation of protein transport
A0055037cellular_componentrecycling endosome
A0055038cellular_componentrecycling endosome membrane
A0060170cellular_componentciliary membrane
A0060271biological_processcilium assembly
A0061512biological_processprotein localization to cilium
A0070062cellular_componentextracellular exosome
A0072659biological_processprotein localization to plasma membrane
A0097546cellular_componentciliary base
A0097730cellular_componentnon-motile cilium
A0098887biological_processneurotransmitter receptor transport, endosome to postsynaptic membrane
A0098969biological_processneurotransmitter receptor transport to postsynaptic membrane
A0098978cellular_componentglutamatergic synapse
A1990782molecular_functionprotein tyrosine kinase binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue GNP A 301
ChainResidue
ASER17
ASER35
APHE37
ASER39
ATHR40
AGLY66
AASN121
ALYS122
AASP124
ASER151
AALA152
AGLY18
ALYS153
AMG302
AHOH401
AHOH402
AVAL19
AGLY20
ALYS21
ATHR22
ACYS23
APHE33
AASN34

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 302
ChainResidue
ATHR22
ATHR40
AGNP301
AHOH401
AHOH402

Functional Information from PROSITE/UniProt
site_idPS00675
Number of Residues14
DetailsSIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. LLLiGDSGVGKtcV
ChainResidueDetails
ALEU11-VAL24

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsMotif: {"description":"Switch 1","evidences":[{"source":"UniProtKB","id":"P62820","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues17
DetailsMotif: {"description":"Switch 2","evidences":[{"source":"UniProtKB","id":"P62820","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21378754","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27552051","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3QBT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SZI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27552051","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5SZI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21378754","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27552051","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QBT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SZI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21378754","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3QBT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21378754","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QBT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by LRRK2","evidences":[{"source":"PubMed","id":"26824392","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29125462","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30209220","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30398148","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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