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UniProtKB/Swiss-Prot entry P51151


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RAB9A_HUMAN
Primary accession number P51151
Secondary accession number Q6ICN1
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 96)
Name and origin of the protein
Protein name Ras-related protein Rab-9A
Synonym Rab-9A
Gene name
Name: RAB9A
Synonyms: RAB9
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1006/geno.1997.4644; PubMed=9126495 [NCBI, ExPASy, EBI, Israel, Japan]
Davies J.P., Cotter P.D., Ioannou Y.A.;
"Cloning and mapping of human Rab7 and Rab9 cDNA sequences and identification of a Rab9 pseudogene.";
Genomics 41:131-134(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[6]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U44103; AAC51200.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF498944; AAM21092.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR450362; CAG29358.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC017265; AAH17265.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00016372; -.
PIR G02361; G02361.
RefSeq NP_004242.1; -.
UniGene Hs.495704
3D structure databases
PDB
1WMS; X-ray; 1.25 A; A/B=1-177.[ExPASy / RCSB / EBI]
PDBsum 1WMS; -.
ModBase P51151.
PTM databases
PhosphoSite P51151; -.
Organism-specific databases
GeneCards GC0XP013617; -.
H-InvDB HIX0020661; -.
HGNC HGNC:9792; RAB9A.
GenAtlas RAB9A.
HPA CAB016411; -.
HPA003094; -.
MIM 300284; gene. [NCBI / EBI]
Gene expression databases
ArrayExpress P51151; -.
Bgee P51151; -.
CleanEx HS_RAB9A; -.
GermOnline ENSG00000123595; Homo sapiens.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0000139; Cellular component: Golgi membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005770; Cellular component: late endosome (inferred from direct assay from MGI).
GO:0005764; Cellular component: lysosome (inferred from direct assay from MGI).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005525; Molecular function: GTP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003924; Molecular function: GTPase activity (traceable author statement from ProtInc).
GO:0015031; Biological process: protein transport (inferred from electronic annotation from UniProtKB-KW).
GO:0007264; Biological process: small GTPase mediated signal transduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR003579; GTPase_Rab.
IPR013753; Ras.
IPR001806; Ras_GTPase.
IPR005225; Small_GTP_bd.
Graphical view of domain structure.
Pfam PF00071; Ras; 1.
Pfam graphical view of domain structure.
PRINTS PR00449; RASTRNSFRMNG.
SMART SM00175; RAB; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00231; small_GTP; 1.
PROSITE PS51419; RAB; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P51151; -.
PRIDE P51151; -.
Genome annotation databases
Ensembl ENSG00000123595; Homo sapiens. [Contig view]
GeneID 9367; -.
KEGG hsa:9367; -.
Phylogenomic databases
HOVERGEN P51151; -.
OMA P51151; VDISERQ.
Other
NextBio 35080; -.
SOURCE RAB9A; Homo sapiens.
ProtoNet P51151.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell membrane; Endoplasmic reticulum; Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   201  201     Ras-related protein Rab-9A. PRO_0000121139
NP_BIND   14    21  8     GTP (By similarity). 
NP_BIND   62    66  5     GTP (By similarity). 
NP_BIND   124   127  4     GTP (By similarity). 
MOTIF   36    44  9     Effector region (By similarity). 
MOD_RES   179   179        Phosphoserine. 
LIPID   200   200        S-geranylgeranyl cysteine (By similarity). 
LIPID   201   201        S-geranylgeranyl cysteine (By similarity). 
STRAND   5    13  9      
HELIX   20    29  10      
STRAND   41    51  11      
STRAND   54    62  9      
HELIX   67    69  3      
HELIX   70    73  4      
HELIX   74    77  4      
STRAND   81    88  8      
HELIX   92    96  5      
HELIX   98   109  12      
TURN   114   116  3      
STRAND   119   124  6      
HELIX   135   144  10      
STRAND   150   152  3      
TURN   155   157  3      
HELIX   161   173  13      
Sequence information
Length: 201 AA [This is the length of the unprocessed precursor] Molecular weight: 22838 Da [This is the MW of the unprocessed precursor] CRC64: 65B502C21E97DB72 [This is a checksum on the sequence]
        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 

P51151 in FASTA format

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