Q13637 (RAB32_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-32

Gene names

Name:

RAB32

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	225 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 vesicle › phagosome. Cytoplasmic vesicle › phagosome 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.

Ontologies

Keywords
Cellular component	Cytoplasmic vesicle Membrane Mitochondrion
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Lipoprotein Prenylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	phagosome maturation Inferred from mutant phenotype Ref.12. Source: UniProtKB protein transport Inferred from electronic annotation. Source: InterPro small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell phagocytic vesicle Inferred from direct assay Ref.12. Source: UniProtKB phagocytic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 225	224	Ras-related protein Rab-32		PRO_0000121235
Regions
	Nucleotide binding	32 – 39	8	GTP By similarity
	Nucleotide binding	81 – 85	5	GTP By similarity
	Nucleotide binding	143 – 146	4	GTP By similarity
	Region	178 – 197	20	PKA-RII subunit binding domain
	Motif	54 – 62	9	Effector region By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.6
	Lipidation	224	1	S-geranylgeranyl cysteine By similarity
	Lipidation	225	1	S-geranylgeranyl cysteine By similarity
Experimental info
	Mutagenesis	39	1	T → N: Decreased GTP-binding activity. Ref.8
	Mutagenesis	85	1	Q → L: No change in GTPase activity. Ref.7
	Mutagenesis	185	1	A → F: Abolishes binding to protein kinase A type II regulatory subunit. Ref.8
	Mutagenesis	188	1	L → P: Abolishes binding to protein kinase A type II regulatory subunit. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Q13637 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 91D41BAC1E3434CA	FASTA	225	24,997
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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.

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.
IPI	IPI00014377.
RefSeq	NP_006825.1. NM_006834.3.
UniGene	Hs.287714.
3D structure databases
ProteinModelPortal	Q13637.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000356465.
PTM databases
PhosphoSite	Q13637.
Polymorphism databases
DMDM	2833245.
Proteomic databases
PaxDb	Q13637.
PRIDE	Q13637.
Protocols and materials databases
DNASU	10981.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000367495; ENSP00000356465; ENSG00000118508.
GeneID	10981.
KEGG	hsa:10981.
UCSC	uc003qln.1. human.
Organism-specific databases
CTD	10981.
GeneCards	GC06P146906.
HGNC	HGNC:9772. RAB32.
HPA	HPA025731.
MIM	612906. gene.
neXtProt	NX_Q13637.
PharmGKB	PA34123.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1100.
HOGENOM	HOG000233968.
HOVERGEN	HBG009351.
InParanoid	Q13637.
KO	K07918.
OMA	FCREGGF.
OrthoDB	EOG4F7NM0.
PhylomeDB	Q13637.
Gene expression databases
Bgee	Q13637.
CleanEx	HS_RAB32.
Genevestigator	Q13637.
GermOnline	ENSG00000118508. Homo sapiens.
Family and domain databases
InterPro	IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR003579. Small_GTPase_Rab_type. [Graphical view]
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
SMART	SM00175. RAB. 1 hit. [Graphical view]
TIGRFAMs	TIGR00231. small_GTP. 1 hit.
PROSITE	PS51419. RAB. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	10981.
NextBio	41722.
SOURCE	Search...

Entry information

Entry name

RAB32_HUMAN

Accession

Primary (citable) accession number: Q13637

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.