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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
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005768cellular_componentendosome
A0005794cellular_componentGolgi apparatus
A0005813cellular_componentcentrosome
A0005814cellular_componentcentriole
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005929cellular_componentcilium
A0006887biological_processexocytosis
A0006904biological_processvesicle docking involved in exocytosis
A0006914biological_processautophagy
A0007030biological_processGolgi organization
A0007409biological_processaxonogenesis
A0008021cellular_componentsynaptic vesicle
A0009306biological_processprotein secretion
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
A0043005cellular_componentneuron projection
A0043025cellular_componentneuronal cell body
A0043197cellular_componentdendritic spine
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
A0099003biological_processvesicle-mediated transport in 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 Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BMET631
AASN34
AASN121

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9H0U4, ECO:0000269|PubMed:27552051, ECO:0007744|PDB:5SZI
ChainResidueDetails
AASP63
AALA152

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by LRRK2 => ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:30398148
ChainResidueDetails
ATHR72

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER181

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER185

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Cysteine methyl ester => ECO:0000255
ChainResidueDetails
ACYS204

site_idSWS_FT_FI7
Number of Residues1
DetailsLIPID: S-geranylgeranyl cysteine => ECO:0000269|PubMed:8375503
ChainResidueDetails
ACYS204

225158

PDB entries from 2024-09-18

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