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Q13637 (RAB32_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-32
Gene names
Name:RAB32
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length225 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.12

Subcellular location

Mitochondrion. Cytoplasmic vesiclephagosome. Cytoplasmic vesiclephagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Note: Recruited to phagosomes containing S.aureus or M.tuberculosis. Ref.8 Ref.12

Tissue specificity

Widely expressed with high levels in heart, liver, kidney, bone marrow, testis, colon and fetal lung. Ref.7 Ref.8

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 225224Ras-related protein Rab-32
PRO_0000121235

Regions

Nucleotide binding32 – 398GTP By similarity
Nucleotide binding81 – 855GTP By similarity
Nucleotide binding143 – 1464GTP By similarity
Region178 – 19720PKA-RII subunit binding domain
Motif54 – 629Effector region By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.13
Lipidation2241S-geranylgeranyl cysteine By similarity
Lipidation2251S-geranylgeranyl cysteine By similarity

Experimental info

Mutagenesis391T → N: Decreased GTP-binding activity. Ref.8
Mutagenesis851Q → L: No change in GTPase activity. Ref.7
Mutagenesis1851A → F: Abolishes binding to protein kinase A type II regulatory subunit. Ref.8
Mutagenesis1881L → P: Abolishes binding to protein kinase A type II regulatory subunit. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Q13637 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 91D41BAC1E3434CA

FASTA22524,997
        10         20         30         40         50         60 
MAGGGAGDPG LGAAAAPAPE TREHLFKVLV IGELGVGKTS IIKRYVHQLF SQHYRATIGV 

        70         80         90        100        110        120 
DFALKVLNWD SRTLVRLQLW DIAGQERFGN MTRVYYKEAV GAFVVFDISR SSTFEAVLKW 

       130        140        150        160        170        180 
KSDLDSKVHL PNGSPIPAVL LANKCDQNKD SSQSPSQVDQ FCKEHGFAGW FETSAKDNIN 

       190        200        210        220 
IEEAARFLVE KILVNHQSFP NEENDVDKIK LDQETLRAEN KSQCC 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS5210.1.
RefSeqNP_006825.1. NM_006834.3.
UniGeneHs.287714.

3D structure databases

ProteinModelPortalQ13637.
SMRQ13637. Positions 23-186.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116177. 3 interactions.
STRING9606.ENSP00000356465.

PTM databases

PhosphoSiteQ13637.

Polymorphism databases

DMDM2833245.

Proteomic databases

MaxQBQ13637.
PaxDbQ13637.
PRIDEQ13637.

Protocols and materials databases

DNASU10981.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367495; ENSP00000356465; ENSG00000118508.
GeneID10981.
KEGGhsa:10981.
UCSCuc003qln.1. human.

Organism-specific databases

CTD10981.
GeneCardsGC06P146906.
HGNCHGNC:9772. RAB32.
HPAHPA025731.
MIM612906. gene.
neXtProtNX_Q13637.
PharmGKBPA34123.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidQ13637.
KOK07918.
OMAFCREGGF.
OrthoDBEOG78M02X.
PhylomeDBQ13637.
TreeFamTF324491.

Gene expression databases

BgeeQ13637.
CleanExHS_RAB32.
GenevestigatorQ13637.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi10981.
NextBio41722.
PROQ13637.
SOURCESearch...

Entry information

Entry nameRAB32_HUMAN
AccessionPrimary (citable) accession number: Q13637
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM