P51151 (RAB9A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-9A

Gene names

Name:	RAB9A
Synonyms:	RAB9

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	201 AA.
Sequence status	Complete.
Protein existence	Evidence 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 vesicle › phagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Cytoplasmic vesicle › phagosome. Note: Co-localizes 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 process	Protein transport Transport
Cellular component	Cell membrane Cytoplasmic vesicle Endoplasmic reticulum Endosome Golgi apparatus Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell 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_function	GDP binding Inferred from direct assay Ref.15PubMed 20937701. Source: UniProtKB GTP binding Inferred from direct assay Ref.15. Source: UniProtKB GTPase activity Inferred from direct assay Ref.15. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 201

201

Ras-related protein Rab-9A

PRO_0000121139

Regions

Nucleotide binding

14 – 22

9

GTP

Nucleotide binding

62 – 66

5

GTP By similarity

Nucleotide binding

124 – 127

4

GTP

Nucleotide binding

154 – 156

3

GTP

Motif

36 – 44

9

Effector region By similarity

Amino acid modifications

Modified residue

179

1

Phosphoserine Ref.8

Lipidation

200

1

S-geranylgeranyl cysteine By similarity

Lipidation

201

1

S-geranylgeranyl cysteine By similarity

Secondary structure

1

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201

Helix Strand Turn

Details...

Beta strand

5 – 13

9

Helix

20 – 29

10

Beta strand

41 – 51

11

Beta strand

54 – 62

9

Helix

67 – 69

3

Helix

70 – 73

4

Helix

74 – 77

4

Beta strand

81 – 88

8

Helix

92 – 96

5

Helix

98 – 109

12

Turn

114 – 116

3

Beta strand

119 – 124

6

Helix

135 – 144

10

Beta strand

150 – 152

3

Turn

155 – 157

3

Helix

161 – 173

13

Sequences

	Sequence		Length	Mass (Da)
	P51151 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 65B502C21E97DB72	FASTA	201	22,838
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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]	"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.

IPI

IPI00016372.

PIR

G02361.

RefSeq

NP_001182257.1. NM_001195328.1.
NP_004242.1. NM_004251.4.

UniGene

Hs.495704.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WMS	X-ray	1.25	A/B	1-177	[»]

ProteinModelPortal

P51151.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46409N.

STRING

9606.ENSP00000420127.

PTM databases

PhosphoSite

P51151.

Polymorphism databases

DMDM

1710003.

Proteomic databases

PaxDb

P51151.

PeptideAtlas

P51151.

PRIDE

P51151.

Protocols and materials databases

DNASU

9367.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000464506; ENSP00000420127; ENSG00000123595.

GeneID

9367.

KEGG

hsa:9367.

UCSC

uc004cvm.3. human.

Organism-specific databases

CTD

9367.

GeneCards

GC0XP013707.

HGNC

HGNC:9792. RAB9A.

HPA

CAB016411.
HPA003094.

MIM

300284. gene.

neXtProt

NX_P51151.

PharmGKB

PA34152.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000233968.

HOVERGEN

HBG009351.

InParanoid

P51151.

KO

K07899.

OMA

LIPTDTV.

OrthoDB

EOG4R7VBS.

PhylomeDB

P51151.

Gene expression databases

Bgee

P51151.

CleanEx

HS_RAB9A.

Genevestigator

P51151.

GermOnline

ENSG00000123595. 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

ChEMBL

CHEMBL1293294.

EvolutionaryTrace

P51151.

GenomeRNAi

9367.

NextBio

35080.

SOURCE

Search...

Entry information

Entry name

RAB9A_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 137 of the entry and version 1 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.