ID RAB9A_HUMAN Reviewed; 201 AA. AC P51151; A8K390; Q6ICN1; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 25-JAN-2012, entry version 124. DE RecName: Full=Ras-related protein Rab-9A; GN Name=RAB9A; Synonyms=RAB9; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=97271569; PubMed=9126495; DOI=10.1006/geno.1997.4644; RA Davies J.P., Cotter P.D., Ioannou Y.A.; RT "Cloning and mapping of human Rab7 and Rab9 cDNA sequences and RT identification of a Rab9 pseudogene."; RL Genomics 41:131-134(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [8] RP INTERACTION WITH GCC2. RX PubMed=16885419; DOI=10.1091/mbc.E06-02-0153; RA Reddy J.V., Burguete A.S., Sridevi K., Ganley I.G., Nottingham R.M., RA Pfeffer S.R.; RT "A functional role for the GCC185 golgin in mannose 6-phosphate RT receptor recycling."; RL Mol. Biol. Cell 17:4353-4363(2006). RN [9] RP INTERACTION WITH GCC2. RX PubMed=18243103; DOI=10.1016/j.cell.2007.11.048; RA Burguete A.S., Fenn T.D., Brunger A.T., Pfeffer S.R.; RT "Rab and Arl GTPase family members cooperate in the localization of RT the golgin GCC185."; RL Cell 132:286-298(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 1-177 IN COMPLEX WITH GDP. RX PubMed=15263003; DOI=10.1074/jbc.M407114200; RA Chen L., DiGiammarino E., Zhou X.E., Wang Y., Toh D., Hodge T.W., RA Meehan E.J.; RT "High resolution crystal structure of human Rab9 GTPase: a novel RT antiviral drug target."; RL J. Biol. Chem. 279:40204-40208(2004). CC -!- FUNCTION: Involved in the transport of proteins between the CC endosomes and the trans Golgi network. CC -!- SUBUNIT: Interacts (preferentially in its GTP-bound form) with CC GCC2 (via its GRIP domain). CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic CC side (Potential). Endoplasmic reticulum membrane (Potential). CC Golgi apparatus membrane (Potential). CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U44103; AAC51200.1; -; mRNA. DR EMBL; AF498944; AAM21092.1; -; mRNA. DR EMBL; CR450362; CAG29358.1; -; mRNA. DR EMBL; AK290505; BAF83194.1; -; mRNA. DR EMBL; CH471074; EAW98826.1; -; Genomic_DNA. DR EMBL; BC017265; AAH17265.1; -; mRNA. DR IPI; IPI00016372; -. DR PIR; G02361; G02361. DR RefSeq; NP_001182257.1; NM_001195328.1. DR RefSeq; NP_004242.1; NM_004251.4. DR UniGene; Hs.495704; -. DR UniGene; Hs.728400; -. DR PDB; 1WMS; X-ray; 1.25 A; A/B=1-177. DR PDBsum; 1WMS; -. DR ProteinModelPortal; P51151; -. DR SMR; P51151; 1-173. DR DIP; DIP-46409N; -. DR STRING; P51151; -. DR PhosphoSite; P51151; -. DR DMDM; 1710003; -. DR PeptideAtlas; P51151; -. DR PRIDE; P51151; -. DR Ensembl; ENST00000464506; ENSP00000420127; ENSG00000123595. DR GeneID; 9367; -. DR KEGG; hsa:9367; -. DR UCSC; uc004cvm.1; human. DR CTD; 9367; -. DR GeneCards; GC0XP013707; -. DR H-InvDB; HIX0203301; -. DR HGNC; HGNC:9792; RAB9A. DR HPA; CAB016411; -. DR HPA; HPA003094; -. DR MIM; 300284; gene. DR neXtProt; NX_P51151; -. DR PharmGKB; PA34152; -. DR eggNOG; prNOG06590; -. DR GeneTree; ENSGT00600000084038; -. DR HOGENOM; HBG745225; -. DR HOVERGEN; HBG009351; -. DR InParanoid; P51151; -. DR OMA; VDISERQ; -. DR OrthoDB; EOG4R7VBS; -. DR PhylomeDB; P51151; -. DR NextBio; 35080; -. DR ArrayExpress; P51151; -. DR Bgee; P51151; -. DR CleanEx; HS_RAB9A; -. DR Genevestigator; P51151; -. DR GermOnline; ENSG00000123595; Homo sapiens. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005770; C:late endosome; IDA:MGI. DR GO; GO:0005764; C:lysosome; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0045921; P:positive regulation of exocytosis; IMP:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR InterPro; IPR003579; Small_GTPase_Rab_type. DR KO; K07899; -. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR TIGRFAMs; TIGR00231; Small_GTP; 1. DR PROSITE; PS51419; RAB; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Endoplasmic reticulum; KW Golgi apparatus; GTP-binding; Lipoprotein; Membrane; KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport; KW Reference proteome; Transport. FT CHAIN 1 201 Ras-related protein Rab-9A. FT /FTId=PRO_0000121139. FT NP_BIND 14 22 GTP. FT NP_BIND 62 66 GTP (By similarity). FT NP_BIND 124 127 GTP. FT NP_BIND 154 156 GTP. FT MOTIF 36 44 Effector region (By similarity). FT MOD_RES 179 179 Phosphoserine. FT LIPID 200 200 S-geranylgeranyl cysteine (By FT similarity). FT LIPID 201 201 S-geranylgeranyl cysteine (By FT similarity). FT STRAND 5 13 FT HELIX 20 29 FT STRAND 41 51 FT STRAND 54 62 FT HELIX 67 69 FT HELIX 70 73 FT HELIX 74 77 FT STRAND 81 88 FT HELIX 92 96 FT HELIX 98 109 FT TURN 114 116 FT STRAND 119 124 FT HELIX 135 144 FT STRAND 150 152 FT TURN 155 157 FT HELIX 161 173 SQ SEQUENCE 201 AA; 22838 MW; 65B502C21E97DB72 CRC64; MAGKSSLFKV ILLGDGGVGK SSLMNRYVTN KFDTQLFHTI GVEFLNKDLE VDGHFVTMQI WDTAGQERFR SLRTPFYRGS DCCLLTFSVD DSQSFQNLSN WKKEFIYYAD VKEPESFPFV ILGNKIDISE RQVSTEEAQA WCRDNGDYPY FETSAKDATN VAAAFEEAVR RVLATEDRSD HLIQTDTVNL HRKPKPSSSC C //