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P51151 (RAB9A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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-9A
Gene names
Name:RAB9A
Synonyms:RAB9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the transport of proteins between the endosomes and the trans Golgi network.

Subunit structure

Interacts (preferentially in its GTP-bound form) with GCC2 (via its GRIP domain). Ref.9 Ref.10

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential. Endoplasmic reticulum membrane Potential. Golgi apparatus membrane Potential. Late endosome. Cytoplasmic vesiclephagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Cytoplasmic vesiclephagosome. Note: Colocalizes with OSBPL1A at the late endosome. Recruited to phagosomes containing S.aureus or M.tuberculosis. Ref.7 Ref.14

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell membrane
Cytoplasmic vesicle
Endoplasmic reticulum
Endosome
Golgi apparatus
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Lipoprotein
Phosphoprotein
Prenylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from direct assay Ref.16. Source: GOC

positive regulation of exocytosis

Inferred from mutant phenotype PubMed 19966785. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

late endosome

Inferred from direct assay PubMed 15078902. Source: MGI

lysosome

Inferred from direct assay PubMed 15078902. Source: MGI

phagocytic vesicle

Inferred from direct assay Ref.14. Source: UniProtKB

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGDP binding

Inferred from direct assay Ref.16PubMed 20937701. Source: UniProtKB

GTP binding

Inferred from direct assay Ref.16. Source: UniProtKB

GTPase activity

Inferred from direct assay Ref.16. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.10PubMed 19490898. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 201200Ras-related protein Rab-9A
PRO_0000121139

Regions

Nucleotide binding14 – 229GTP
Nucleotide binding62 – 665GTP By similarity
Nucleotide binding124 – 1274GTP
Nucleotide binding154 – 1563GTP
Motif36 – 449Effector region By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.15
Modified residue1791Phosphoserine Ref.8
Lipidation2001S-geranylgeranyl cysteine By similarity
Lipidation2011S-geranylgeranyl cysteine By similarity

Secondary structure

............................... 201
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P51151 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 65B502C21E97DB72

FASTA20122,838
        10         20         30         40         50         60 
MAGKSSLFKV ILLGDGGVGK SSLMNRYVTN KFDTQLFHTI GVEFLNKDLE VDGHFVTMQI 

        70         80         90        100        110        120 
WDTAGQERFR SLRTPFYRGS DCCLLTFSVD DSQSFQNLSN WKKEFIYYAD VKEPESFPFV 

       130        140        150        160        170        180 
ILGNKIDISE RQVSTEEAQA WCRDNGDYPY FETSAKDATN VAAAFEEAVR RVLATEDRSD 

       190        200 
HLIQTDTVNL HRKPKPSSSC C 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and mapping of human Rab7 and Rab9 cDNA sequences and identification of a Rab9 pseudogene."
Davies J.P., Cotter P.D., Ioannou Y.A.
Genomics 41:131-134(1997) [PubMed] [Europe PMC] [Abstract]
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 open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Muscle.
[7]"The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments."
Johansson M., Lehto M., Tanhuanpaeae K., Cover T.L., Olkkonen V.M.
Mol. Biol. Cell 16:5480-5492(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A functional role for the GCC185 golgin in mannose 6-phosphate receptor recycling."
Reddy J.V., Burguete A.S., Sridevi K., Ganley I.G., Nottingham R.M., Pfeffer S.R.
Mol. Biol. Cell 17:4353-4363(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GCC2.
[10]"Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185."
Burguete A.S., Fenn T.D., Brunger A.T., Pfeffer S.R.
Cell 132:286-298(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GCC2.
[11]"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.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
[14]"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: SUBCELLULAR LOCATION.
[15]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[16]"High resolution crystal structure of human Rab9 GTPase: a novel antiviral drug target."
Chen L., DiGiammarino E., Zhou X.E., Wang Y., Toh D., Hodge T.W., Meehan E.J.
J. Biol. Chem. 279:40204-40208(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 1-177 IN COMPLEX WITH GDP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U44103 mRNA. Translation: AAC51200.1.
AF498944 mRNA. Translation: AAM21092.1.
CR450362 mRNA. Translation: CAG29358.1.
AK290505 mRNA. Translation: BAF83194.1.
CH471074 Genomic DNA. Translation: EAW98826.1.
BC017265 mRNA. Translation: AAH17265.1.
CCDSCCDS14156.1.
PIRG02361.
RefSeqNP_001182257.1. NM_001195328.1.
NP_004242.1. NM_004251.4.
UniGeneHs.495704.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WMSX-ray1.25A/B1-177[»]
ProteinModelPortalP51151.
SMRP51151. Positions 1-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114768. 10 interactions.
DIPDIP-46409N.
STRING9606.ENSP00000420127.

Chemistry

ChEMBLCHEMBL1293294.

PTM databases

PhosphoSiteP51151.

Polymorphism databases

DMDM1710003.

Proteomic databases

MaxQBP51151.
PaxDbP51151.
PeptideAtlasP51151.
PRIDEP51151.

Protocols and materials databases

DNASU9367.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000464506; ENSP00000420127; ENSG00000123595.
GeneID9367.
KEGGhsa:9367.
UCSCuc004cvm.3. human.

Organism-specific databases

CTD9367.
GeneCardsGC0XP013707.
HGNCHGNC:9792. RAB9A.
HPACAB016411.
HPA003094.
MIM300284. gene.
neXtProtNX_P51151.
PharmGKBPA34152.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidP51151.
KOK07899.
OMAAHLFHTI.
OrthoDBEOG7G4QG8.
PhylomeDBP51151.
TreeFamTF326442.

Gene expression databases

BgeeP51151.
CleanExHS_RAB9A.
GenevestigatorP51151.

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

EvolutionaryTraceP51151.
GeneWikiRAB9A.
GenomeRNAi9367.
NextBio35080.
PROP51151.
SOURCESearch...

Entry information

Entry nameRAB9A_HUMAN
AccessionPrimary (citable) accession number: P51151
Secondary accession number(s): A8K390, Q6ICN1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 149 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome X

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