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Q13637

- RAB32_HUMAN

UniProt

Q13637 - RAB32_HUMAN

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Protein

Ras-related protein Rab-32

Gene
RAB32
Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 398GTP By similarity
Nucleotide bindingi81 – 855GTP By similarity
Nucleotide bindingi143 – 1464GTP By similarity

GO - Molecular functioni

  1. AP-1 adaptor complex binding Source: BHF-UCL
  2. AP-3 adaptor complex binding Source: BHF-UCL
  3. GTP binding Source: BHF-UCL
  4. GTP-dependent protein binding Source: BHF-UCL
  5. protein binding Source: BHF-UCL
  6. protein complex binding Source: BHF-UCL

GO - Biological processi

  1. antigen processing and presentation Source: UniProt
  2. endosome to melanosome transport Source: BHF-UCL
  3. melanosome organization Source: BHF-UCL
  4. phagosome maturation Source: UniProtKB
  5. protein transport Source: InterPro
  6. small GTPase mediated signal transduction Source: InterPro
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; Lipid-anchor; Cytoplasmic side By similarity
Note: Recruited to phagosomes containing S.aureus or M.tuberculosis.2 Publications

GO - Cellular componenti

  1. early endosome Source: BHF-UCL
  2. melanosome Source: BHF-UCL
  3. membrane Source: BHF-UCL
  4. mitochondrion Source: UniProtKB-SubCell
  5. phagocytic vesicle Source: UniProtKB
  6. phagocytic vesicle membrane Source: UniProtKB-SubCell
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
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 – 11Removed1 Publication
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 cysteine By similarity
Lipidationi225 – 2251S-geranylgeranyl cysteine By 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

Protein-protein interaction databases

BioGridi116177. 3 interactions.
STRINGi9606.ENSP00000356465.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CYMX-ray2.80A/B/C1-225[»]
4CZ2X-ray2.97A/B/C1-225[»]
ProteinModelPortaliQ13637.
SMRiQ13637. Positions 23-186.

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 region By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ13637.
KOiK07918.
OMAiFCREGGF.
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

MAGGGAGDPG LGAAAAPAPE TREHLFKVLV IGELGVGKTS IIKRYVHQLF    50
SQHYRATIGV DFALKVLNWD SRTLVRLQLW DIAGQERFGN MTRVYYKEAV 100
GAFVVFDISR SSTFEAVLKW KSDLDSKVHL PNGSPIPAVL LANKCDQNKD 150
SSQSPSQVDQ FCKEHGFAGW FETSAKDNIN IEEAARFLVE KILVNHQSFP 200
NEENDVDKIK LDQETLRAEN KSQCC 225
Length:225
Mass (Da):24,997
Last modified:January 23, 2007 - v3
Checksum:i91D41BAC1E3434CA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS5210.1.
RefSeqi NP_006825.1. NM_006834.3.
UniGenei Hs.287714.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4CYM X-ray 2.80 A/B/C 1-225 [» ]
4CZ2 X-ray 2.97 A/B/C 1-225 [» ]
ProteinModelPortali Q13637.
SMRi Q13637. Positions 23-186.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116177. 3 interactions.
STRINGi 9606.ENSP00000356465.

PTM databases

PhosphoSitei Q13637.

Polymorphism databases

DMDMi 2833245.

Proteomic databases

MaxQBi Q13637.
PaxDbi Q13637.
PRIDEi Q13637.

Protocols and materials databases

DNASUi 10981.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367495 ; ENSP00000356465 ; ENSG00000118508 .
GeneIDi 10981.
KEGGi hsa:10981.
UCSCi uc003qln.1. human.

Organism-specific databases

CTDi 10981.
GeneCardsi GC06P146906.
HGNCi HGNC:9772. RAB32.
HPAi HPA025731.
MIMi 612906. gene.
neXtProti NX_Q13637.
PharmGKBi PA34123.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
HOGENOMi HOG000233968.
HOVERGENi HBG009351.
InParanoidi Q13637.
KOi K07918.
OMAi FCREGGF.
OrthoDBi EOG78M02X.
PhylomeDBi Q13637.
TreeFami TF324491.

Miscellaneous databases

GenomeRNAii 10981.
NextBioi 41722.
PROi Q13637.
SOURCEi Search...

Gene expression databases

Bgeei Q13637.
CleanExi HS_RAB32.
Genevestigatori Q13637.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view ]
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00175. RAB. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51419. RAB. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].

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: September 3, 2014
This is version 129 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

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