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P51151

- RAB9A_HUMAN

UniProt

P51151 - RAB9A_HUMAN

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Protein

Ras-related protein Rab-9A

Gene

RAB9A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 229GTP
Nucleotide bindingi62 – 665GTPBy similarity
Nucleotide bindingi124 – 1274GTP
Nucleotide bindingi154 – 1563GTP

GO - Molecular functioni

  1. GDP binding Source: UniProtKB
  2. GTPase activity Source: UniProtKB
  3. GTP binding Source: UniProtKB

GO - Biological processi

  1. GTP catabolic process Source: GOC
  2. positive regulation of exocytosis Source: UniProtKB
  3. protein transport Source: UniProtKB-KW
  4. small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-9A
Gene namesi
Name:RAB9A
Synonyms:RAB9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:9792. RAB9A.

Subcellular locationi

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

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: UniProt
  3. Golgi apparatus Source: UniProtKB-KW
  4. late endosome Source: MGI
  5. lysosome Source: MGI
  6. phagocytic vesicle Source: UniProtKB
  7. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34152.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 201200Ras-related protein Rab-9APRO_0000121139Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei179 – 1791Phosphoserine1 Publication
Lipidationi200 – 2001S-geranylgeranyl cysteineBy similarity
Lipidationi201 – 2011S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP51151.
PaxDbiP51151.
PeptideAtlasiP51151.
PRIDEiP51151.

PTM databases

PhosphoSiteiP51151.

Expressioni

Gene expression databases

BgeeiP51151.
CleanExiHS_RAB9A.
GenevestigatoriP51151.

Organism-specific databases

HPAiCAB016411.
HPA003094.

Interactioni

Subunit structurei

Interacts (preferentially in its GTP-bound form) with GCC2 (via its GRIP domain).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NISCHQ9Y2I15EBI-4401353,EBI-2688731

Protein-protein interaction databases

BioGridi114768. 12 interactions.
DIPiDIP-46409N.
IntActiP51151. 2 interactions.
STRINGi9606.ENSP00000420127.

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 139Combined sources
Helixi20 – 2910Combined sources
Beta strandi41 – 5111Combined sources
Beta strandi54 – 629Combined sources
Helixi67 – 693Combined sources
Helixi70 – 734Combined sources
Helixi74 – 774Combined sources
Beta strandi81 – 888Combined sources
Helixi92 – 965Combined sources
Helixi98 – 10912Combined sources
Turni114 – 1163Combined sources
Beta strandi119 – 1246Combined sources
Helixi135 – 14410Combined sources
Beta strandi150 – 1523Combined sources
Turni155 – 1573Combined sources
Helixi161 – 17313Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WMSX-ray1.25A/B1-177[»]
ProteinModelPortaliP51151.
SMRiP51151. Positions 1-173.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51151.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi36 – 449Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119125.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP51151.
KOiK07899.
OMAiAHLFHTI.
OrthoDBiEOG7G4QG8.
PhylomeDBiP51151.
TreeFamiTF326442.

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.

P51151-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGKSSLFKV ILLGDGGVGK SSLMNRYVTN KFDTQLFHTI GVEFLNKDLE
60 70 80 90 100
VDGHFVTMQI WDTAGQERFR SLRTPFYRGS DCCLLTFSVD DSQSFQNLSN
110 120 130 140 150
WKKEFIYYAD VKEPESFPFV ILGNKIDISE RQVSTEEAQA WCRDNGDYPY
160 170 180 190 200
FETSAKDATN VAAAFEEAVR RVLATEDRSD HLIQTDTVNL HRKPKPSSSC

C
Length:201
Mass (Da):22,838
Last modified:October 1, 1996 - v1
Checksum:i65B502C21E97DB72
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14156.1.
PIRiG02361.
RefSeqiNP_001182257.1. NM_001195328.1.
NP_004242.1. NM_004251.4.
UniGeneiHs.495704.

Genome annotation databases

EnsembliENST00000464506; ENSP00000420127; ENSG00000123595.
ENST00000618931; ENSP00000480777; ENSG00000123595.
GeneIDi9367.
KEGGihsa:9367.
UCSCiuc004cvm.3. human.

Polymorphism databases

DMDMi1710003.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14156.1.
PIRi G02361.
RefSeqi NP_001182257.1. NM_001195328.1.
NP_004242.1. NM_004251.4.
UniGenei Hs.495704.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WMS X-ray 1.25 A/B 1-177 [» ]
ProteinModelPortali P51151.
SMRi P51151. Positions 1-173.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114768. 12 interactions.
DIPi DIP-46409N.
IntActi P51151. 2 interactions.
STRINGi 9606.ENSP00000420127.

Chemistry

ChEMBLi CHEMBL1293294.

PTM databases

PhosphoSitei P51151.

Polymorphism databases

DMDMi 1710003.

Proteomic databases

MaxQBi P51151.
PaxDbi P51151.
PeptideAtlasi P51151.
PRIDEi P51151.

Protocols and materials databases

DNASUi 9367.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000464506 ; ENSP00000420127 ; ENSG00000123595 .
ENST00000618931 ; ENSP00000480777 ; ENSG00000123595 .
GeneIDi 9367.
KEGGi hsa:9367.
UCSCi uc004cvm.3. human.

Organism-specific databases

CTDi 9367.
GeneCardsi GC0XP013707.
HGNCi HGNC:9792. RAB9A.
HPAi CAB016411.
HPA003094.
MIMi 300284. gene.
neXtProti NX_P51151.
PharmGKBi PA34152.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
GeneTreei ENSGT00760000119125.
HOGENOMi HOG000233968.
HOVERGENi HBG009351.
InParanoidi P51151.
KOi K07899.
OMAi AHLFHTI.
OrthoDBi EOG7G4QG8.
PhylomeDBi P51151.
TreeFami TF326442.

Miscellaneous databases

EvolutionaryTracei P51151.
GeneWikii RAB9A.
GenomeRNAii 9367.
NextBioi 35080.
PROi P51151.
SOURCEi Search...

Gene expression databases

Bgeei P51151.
CleanExi HS_RAB9A.
Genevestigatori P51151.

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 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. 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. 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. 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. 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.

Entry informationi

Entry nameiRAB9A_HUMAN
AccessioniPrimary (citable) accession number: P51151
Secondary accession number(s): A8K390, Q6ICN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 152 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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