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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. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 398GTPBy similarity
Nucleotide bindingi81 – 855GTPBy similarity
Nucleotide bindingi143 – 1464GTPBy similarity

GO - Molecular functioni

  1. AP-1 adaptor complex binding Source: ParkinsonsUK-UCL
  2. AP-3 adaptor complex binding Source: ParkinsonsUK-UCL
  3. BLOC-2 complex binding Source: ParkinsonsUK-UCL
  4. GDP binding Source: GO_Central
  5. GTPase activity Source: UniProtKB
  6. GTP binding Source: ParkinsonsUK-UCL
  7. GTP-dependent protein binding Source: ParkinsonsUK-UCL

GO - Biological processi

  1. antigen processing and presentation Source: UniProtKB
  2. endosome to melanosome transport Source: ParkinsonsUK-UCL
  3. GTP catabolic process Source: UniProtKB
  4. intracellular protein transport Source: GO_Central
  5. melanosome assembly Source: ParkinsonsUK-UCL
  6. phagosome maturation Source: UniProtKB
  7. Rab protein signal transduction Source: GO_Central
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-32
Gene namesi
Name:RAB32
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:9772. RAB32.

Subcellular locationi

Mitochondrion. Cytoplasmic vesiclephagosome. Cytoplasmic vesiclephagosome membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity
Note: Recruited to phagosomes containing S.aureus or M.tuberculosis.

GO - Cellular componenti

  1. early endosome Source: ParkinsonsUK-UCL
  2. melanosome Source: ParkinsonsUK-UCL
  3. membrane Source: ParkinsonsUK-UCL
  4. mitochondrion Source: GO_Central
  5. phagocytic vesicle Source: UniProtKB
  6. phagocytic vesicle membrane Source: UniProtKB-SubCell
  7. trans-Golgi network Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391T → N: Decreased GTP-binding activity. 1 Publication
Mutagenesisi85 – 851Q → L: No change in GTPase activity. 1 Publication
Mutagenesisi89 – 891G → T: Impairs interaction with ANKRD27; when associated with S-90 and L-94. 1 Publication
Mutagenesisi90 – 901N → S: Impairs interaction with ANKRD27; when associated with T-89 and L-94. 1 Publication
Mutagenesisi91 – 911M → S: Impairs interaction with ANKRD27; when associated with S-93. 1 Publication
Mutagenesisi93 – 931R → S: Impairs interaction with ANKRD27; when associated with M-91. 1 Publication
Mutagenesisi94 – 941V → L: Impairs interaction with ANKRD27; when associated with T-89 and S-90. 1 Publication
Mutagenesisi185 – 1851A → F: Abolishes binding to protein kinase A type II regulatory subunit. 1 Publication
Mutagenesisi188 – 1881L → P: Abolishes binding to protein kinase A type II regulatory subunit. 1 Publication

Organism-specific databases

PharmGKBiPA34123.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 225224Ras-related protein Rab-32PRO_0000121235Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Lipidationi224 – 2241S-geranylgeranyl cysteineBy similarity
Lipidationi225 – 2251S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Prenylation

Proteomic databases

MaxQBiQ13637.
PaxDbiQ13637.
PRIDEiQ13637.

PTM databases

PhosphoSiteiQ13637.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ13637.
CleanExiHS_RAB32.
GenevestigatoriQ13637.

Organism-specific databases

HPAiHPA025731.

Interactioni

Subunit structurei

Interacts with ANKRD27 (PubMed:24856514).1 Publication

Protein-protein interaction databases

BioGridi116177. 7 interactions.
STRINGi9606.ENSP00000356465.

Structurei

Secondary structure

1
225
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 319Combined sources
Helixi38 – 4710Combined sources
Beta strandi59 – 6810Combined sources
Beta strandi70 – 723Combined sources
Beta strandi74 – 829Combined sources
Helixi84 – 885Combined sources
Helixi92 – 965Combined sources
Beta strandi101 – 1077Combined sources
Helixi111 – 1155Combined sources
Helixi117 – 12711Combined sources
Beta strandi138 – 1436Combined sources
Helixi155 – 16410Combined sources
Beta strandi167 – 1748Combined sources
Turni175 – 1784Combined sources
Helixi181 – 19515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CYMX-ray2.80A/B/C1-225[»]
4CZ2X-ray2.97A/B/C1-225[»]
ProteinModelPortaliQ13637.
SMRiQ13637. Positions 22-198.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni178 – 19720PKA-RII subunit binding domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi54 – 629Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119125.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ13637.
KOiK07918.
OMAiMDQFCRE.
OrthoDBiEOG78M02X.
PhylomeDBiQ13637.
TreeFamiTF324491.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

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. Translation: CAC34968.1.
BC015061 mRNA. Translation: AAH15061.1.
U59878 mRNA. Translation: AAB02833.1.
CCDSiCCDS5210.1.
RefSeqiNP_006825.1. NM_006834.3.
UniGeneiHs.287714.

Genome annotation databases

EnsembliENST00000367495; ENSP00000356465; ENSG00000118508.
GeneIDi10981.
KEGGihsa:10981.
UCSCiuc003qln.1. human.

Polymorphism databases

DMDMi2833245.

Cross-referencesi

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. Translation: CAC34968.1.
BC015061 mRNA. Translation: AAH15061.1.
U59878 mRNA. Translation: AAB02833.1.
CCDSiCCDS5210.1.
RefSeqiNP_006825.1. NM_006834.3.
UniGeneiHs.287714.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CYMX-ray2.80A/B/C1-225[»]
4CZ2X-ray2.97A/B/C1-225[»]
ProteinModelPortaliQ13637.
SMRiQ13637. Positions 22-198.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116177. 7 interactions.
STRINGi9606.ENSP00000356465.

PTM databases

PhosphoSiteiQ13637.

Polymorphism databases

DMDMi2833245.

Proteomic databases

MaxQBiQ13637.
PaxDbiQ13637.
PRIDEiQ13637.

Protocols and materials databases

DNASUi10981.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367495; ENSP00000356465; ENSG00000118508.
GeneIDi10981.
KEGGihsa:10981.
UCSCiuc003qln.1. human.

Organism-specific databases

CTDi10981.
GeneCardsiGC06P146906.
HGNCiHGNC:9772. RAB32.
HPAiHPA025731.
MIMi612906. gene.
neXtProtiNX_Q13637.
PharmGKBiPA34123.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119125.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ13637.
KOiK07918.
OMAiMDQFCRE.
OrthoDBiEOG78M02X.
PhylomeDBiQ13637.
TreeFamiTF324491.

Miscellaneous databases

GenomeRNAii10981.
NextBioi41722.
PROiQ13637.
SOURCEiSearch...

Gene expression databases

BgeeiQ13637.
CleanExiHS_RAB32.
GenevestigatoriQ13637.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of novel Rab proteins with the yeast two-hybrid system."
    Burke S., Seabra M.C.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. Bienvenut W.V., Claeys D.
    Submitted (NOV-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-22; 28-38; 66-72; 77-87; 111-119; 128-144; 164-186 AND 211-217, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Platelet.
  7. "Molecular cloning, bacterial expression and properties of Rab31 and Rab32."
    Bao X., Faris A.E., Jang E.K., Haslam R.J.
    Eur. J. Biochem. 269:259-271(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-225, TISSUE SPECIFICITY, MUTAGENESIS OF GLN-85.
    Tissue: Platelet.
  8. "Rab32 is an A-kinase anchoring protein and participates in mitochondrial dynamics."
    Alto N.M., Soderling J., Scott J.D.
    J. Cell Biol. 158:659-668(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF THR-39; ALA-185 AND LEU-188.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes."
    Seto S., Tsujimura K., Koide Y.
    Traffic 12:407-420(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "VARP is recruited on to endosomes by direct interaction with retromer, where together they function in export to the cell surface."
    Hesketh G.G., Perez-Dorado I., Jackson L.P., Wartosch L., Schafer I.B., Gray S.R., McCoy A.J., Zeldin O.B., Garman E.F., Harbour M.E., Evans P.R., Seaman M.N., Luzio J.P., Owen D.J.
    Dev. Cell 29:591-606(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-225 IN COMPLEX WITH ANKRD27, MUTAGENESIS OF GLY-89; ASN-90; MET-91; ARG-93 AND VAL-94.

Entry informationi

Entry nameiRAB32_HUMAN
AccessioniPrimary (citable) accession number: Q13637
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 133 of the entry and version 3 of the sequence. [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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.