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Protein

Ras-related protein Rab-32

Gene

RAB32

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as an A-kinase anchoring protein by binding to the type II regulatory subunit of protein kinase A and anchoring it to the mitochondrion. Also involved in synchronization of mitochondrial fission (PubMed:12186851). Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis (PubMed:21255211). Plays an important role in the control of melanin production and melanosome biogenesis (PubMed:23084991). In concert with RAB38, regulates the proper trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes (By similarity).By similarity3 Publications

Enzyme regulationi

Regulated by a guanine nucleotide-exchange factor (GEF) and a GTPase-activating protein (GAP) and alternates between an inactive GDP-bound and an active GTP-bound form. The BLOC-3 complex composed of HPS1 and HPS4 acts as its GEF, promotes the exchange of GDP to GTP, converting it from an inactive GDP-bound form into an active GTP-bound form (By similarity). SGSM2 acts as its GAP and inactivates it by stimulating its GTPase activity (PubMed:21269460).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi32 – 39GTPBy similarity8
Nucleotide bindingi81 – 85GTPBy similarity5
Nucleotide bindingi143 – 146GTPBy similarity4

GO - Molecular functioni

  • AP-1 adaptor complex binding Source: ParkinsonsUK-UCL
  • AP-3 adaptor complex binding Source: ParkinsonsUK-UCL
  • BLOC-2 complex binding Source: ParkinsonsUK-UCL
  • GTPase activity Source: UniProtKB
  • GTP binding Source: ParkinsonsUK-UCL
  • GTP-dependent protein binding Source: ParkinsonsUK-UCL

GO - Biological processi

  • antigen processing and presentation Source: UniProtKB
  • endosome to melanosome transport Source: ParkinsonsUK-UCL
  • melanosome assembly Source: UniProtKB
  • membrane organization Source: Reactome
  • mitochondrion organization Source: ParkinsonsUK-UCL
  • phagosome maturation Source: UniProtKB
  • protein localization to membrane Source: ParkinsonsUK-UCL
  • vesicle-mediated transport Source: InterPro

Keywordsi

LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-8873719. RAB geranylgeranylation.
R-HSA-8876198. RAB GEFs exchange GTP for GDP on RABs.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-32
Gene namesi
Name:RAB32
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000118508.4.
HGNCiHGNC:9772. RAB32.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi39T → N: Decreased GTP-binding activity. 1 Publication1
Mutagenesisi85Q → L: No change in GTPase activity. 1 Publication1
Mutagenesisi89G → T: Impairs interaction with ANKRD27; when associated with S-90 and L-94. 1 Publication1
Mutagenesisi90N → S: Impairs interaction with ANKRD27; when associated with T-89 and L-94. 1 Publication1
Mutagenesisi91M → S: Impairs interaction with ANKRD27; when associated with S-93. 1 Publication1
Mutagenesisi93R → S: Impairs interaction with ANKRD27; when associated with M-91. 1 Publication1
Mutagenesisi94V → L: Impairs interaction with ANKRD27; when associated with T-89 and S-90. 1 Publication1
Mutagenesisi185A → F: Abolishes binding to protein kinase A type II regulatory subunit. 1 Publication1
Mutagenesisi188L → P: Abolishes binding to protein kinase A type II regulatory subunit. 1 Publication1

Organism-specific databases

DisGeNETi10981.
OpenTargetsiENSG00000118508.
PharmGKBiPA34123.

Polymorphism and mutation databases

BioMutaiRAB32.
DMDMi2833245.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00001212352 – 225Ras-related protein Rab-32Add BLAST224

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources2 Publications1
Modified residuei71PhosphoserineCombined sources1
Lipidationi224S-geranylgeranyl cysteineBy similarity1
Lipidationi225S-geranylgeranyl cysteineBy similarity1

Keywords - PTMi

Acetylation, Lipoprotein, Phosphoprotein, Prenylation

Proteomic databases

EPDiQ13637.
MaxQBiQ13637.
PaxDbiQ13637.
PeptideAtlasiQ13637.
PRIDEiQ13637.

PTM databases

iPTMnetiQ13637.
PhosphoSitePlusiQ13637.

Expressioni

Tissue specificityi

Widely expressed with high levels in heart, liver, kidney, bone marrow, testis, colon and fetal lung.2 Publications

Gene expression databases

BgeeiENSG00000118508.
CleanExiHS_RAB32.
GenevisibleiQ13637. HS.

Organism-specific databases

HPAiHPA025731.

Interactioni

Subunit structurei

Interacts with ANKRD27 (PubMed:24856514, PubMed:21269460). A decreased interaction with ANKRD27 seen in the presence of SGSM2 (PubMed:21269460).1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • AP-1 adaptor complex binding Source: ParkinsonsUK-UCL
  • AP-3 adaptor complex binding Source: ParkinsonsUK-UCL
  • BLOC-2 complex binding Source: ParkinsonsUK-UCL
  • GTP-dependent protein binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi116177. 26 interactors.
DIPiDIP-61889N.
IntActiQ13637. 21 interactors.
STRINGi9606.ENSP00000356465.

Structurei

Secondary structure

1225
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 31Combined sources9
Helixi38 – 47Combined sources10
Beta strandi59 – 68Combined sources10
Beta strandi70 – 72Combined sources3
Beta strandi74 – 82Combined sources9
Helixi84 – 88Combined sources5
Helixi92 – 96Combined sources5
Beta strandi101 – 107Combined sources7
Helixi111 – 115Combined sources5
Helixi117 – 127Combined sources11
Beta strandi138 – 143Combined sources6
Helixi155 – 164Combined sources10
Beta strandi167 – 174Combined sources8
Turni175 – 178Combined sources4
Helixi181 – 195Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4CYMX-ray2.80A/B/C1-225[»]
4CZ2X-ray2.97A/B/C1-225[»]
ProteinModelPortaliQ13637.
SMRiQ13637.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni178 – 197PKA-RII subunit binding domainAdd BLAST20

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi54 – 62Effector regionBy similarity9

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiKOG4423. Eukaryota.
ENOG410YITC. LUCA.
GeneTreeiENSGT00760000119125.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ13637.
KOiK07918.
OMAiCDQKKDS.
OrthoDBiEOG091G0K53.
PhylomeDBiQ13637.
TreeFamiTF324491.

Family and domain databases

CDDicd04107. Rab32_Rab38. 1 hit.
InterProiView protein in InterPro
IPR027417. P-loop_NTPase.
IPR030697. Rab29/Rab38/Rab32.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
PfamiView protein in Pfam
PF00071. Ras. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiView protein in PROSITE
PS51419. RAB. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q13637-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGGGAGDPG LGAAAAPAPE TREHLFKVLV IGELGVGKTS IIKRYVHQLF
60 70 80 90 100
SQHYRATIGV DFALKVLNWD SRTLVRLQLW DIAGQERFGN MTRVYYKEAV
110 120 130 140 150
GAFVVFDISR SSTFEAVLKW KSDLDSKVHL PNGSPIPAVL LANKCDQNKD
160 170 180 190 200
SSQSPSQVDQ FCKEHGFAGW FETSAKDNIN IEEAARFLVE KILVNHQSFP
210 220
NEENDVDKIK LDQETLRAEN KSQCC
Length:225
Mass (Da):24,997
Last modified:January 23, 2007 - v3
Checksum:i91D41BAC1E3434CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U71127 mRNA. Translation: AAB09599.1.
AF498958 mRNA. Translation: AAM21106.1.
BT020016 mRNA. Translation: AAV38819.1.
AL133539 Genomic DNA. No translation available.
BC015061 mRNA. Translation: AAH15061.1.
U59878 mRNA. Translation: AAB02833.1.
CCDSiCCDS5210.1.
RefSeqiNP_006825.1. NM_006834.4.
UniGeneiHs.287714.

Genome annotation databases

EnsembliENST00000367495; ENSP00000356465; ENSG00000118508.
GeneIDi10981.
KEGGihsa:10981.
UCSCiuc003qln.2. human.

Similar proteinsi

Entry informationi

Entry nameiRAB32_HUMAN
AccessioniPrimary (citable) accession number: Q13637
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 162 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families