RBCC

Full text data of RAB6B

RAB6B [Confidence: high (present in two of the MS resources)]
Ras-related protein Rab-6B

hRBCD IPI00016891
IPI00016891 Ras-related protein Rab-6B Seems to have a role in retrograde membrane traffic at the level of the Golgi complex soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a golgi n/a found at its expected molecular weight found at molecular weight

UniProt Q9NRW1
ID RAB6B_HUMAN Reviewed; 208 AA.
AC Q9NRW1; B2R5Z9; D3DND3; Q92929;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Ras-related protein Rab-6B;
GN Name=RAB6B;
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 PubMed=10893188;
RA Opdam F.J.M., Echard A., Croes H.J.E., van den Hurk J.A.J.M.,
RA van de Vorstenbosch R.A., Ginsel L.A., Goud B., Fransen J.A.M.;
RT "The small GTPase Rab6B, a novel Rab6 subfamily member, is cell-type
RT specifically expressed and localised to the Golgi apparatus.";
RL J. Cell Sci. 113:2725-2735(2000).
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 Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 72-124.
RX PubMed=9030196; DOI=10.1016/S0167-4889(96)00169-3;
RA Chen D., Guo J., Gahl W.A.;
RT "RAB GTPases expressed in human melanoma cells.";
RL Biochim. Biophys. Acta 1355:1-6(1997).
RN [8]
RP FUNCTION, INTERACTION WITH BICD1, AND SUBCELLULAR LOCATION.
RX PubMed=17707369; DOI=10.1016/j.yexcr.2007.05.032;
RA Wanschers B.F.J.F., van de Vorstenbosch R., Schlager M.A.,
RA Splinter D., Akhmanova A., Hoogenraad C.C., Wieringa B., Fransen J.A.;
RT "A role for the Rab6B Bicaudal-D1 interaction in retrograde transport
RT in neuronal cells.";
RL Exp. Cell Res. 313:3408-3420(2007).
RN [9]
RP INTERACTION WITH DYNLRB1, AND SUBCELLULAR LOCATION.
RX PubMed=18044744; DOI=10.1002/cm.20254;
RA Wanschers B.F.J., van de Vorstenbosch R., Wijers M., Wieringa B.,
RA King S.M., Fransen J.;
RT "Rab6 family proteins interact with the dynein light chain protein
RT DYNLRB1.";
RL Cell Motil. Cytoskeleton 65:183-196(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 AMPYLATION AT TYR-82.
RX PubMed=21822290; DOI=10.1038/nature10335;
RA Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.;
RT "Modulation of Rab GTPase function by a protein phosphocholine
RT transferase.";
RL Nature 477:103-106(2011).
RN [12]
RP INTERACTION WITH APBA1, AND MUTAGENESIS OF THR-27 AND GLN-72.
RX PubMed=23737971; DOI=10.1371/journal.pone.0064149;
RA Thyrock A., Ossendorf E., Stehling M., Kail M., Kurtz T., Pohlentz G.,
RA Waschbusch D., Eggert S., Formstecher E., Muthing J., Dreisewerd K.,
RA Kins S., Goud B., Barnekow A.;
RT "A new Mint1 isoform, but not the conventional Mint1, interacts with
RT the small GTPase Rab6.";
RL PLoS ONE 8:E64149-E64149(2013).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 13-174.
RX PubMed=16790928; DOI=10.1107/S0907444906015319;
RA Garcia-Saez I., Tcherniuk S., Kozielski F.;
RT "The structure of human neuronal Rab6B in the active and inactive
RT form.";
RL Acta Crystallogr. D 62:725-733(2006).
CC -!- FUNCTION: Seems to have a role in retrograde membrane traffic at
CC the level of the Golgi complex. May function in retrograde
CC transport in neuronal cells.
CC -!- SUBUNIT: Interacts with CCDC64/BICDR1; leads to its accumulation
CC in the pericentrosomal region (By similarity). Interacts with
CC RAB6KIFL. Interacts (GTP-bound) with BICD1 (via C-terminus); the
CC interaction is direct. Interacts (GDP-bound) with DYNLRB1.
CC Interacts (GTP-bound) with APBA1/MINT1 isoform 2, also called
CC Mint1_826, but not with isoform 1.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor.
CC Cytoplasmic vesicle. Note=Colocalizes with BICD1 at vesicular
CC structures that align along microtubules.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR EMBL; AF166492; AAF61637.1; -; mRNA.
DR EMBL; AF498940; AAM21088.1; -; mRNA.
DR EMBL; BT007263; AAP35927.1; -; mRNA.
DR EMBL; AK312378; BAG35296.1; -; mRNA.
DR EMBL; CH471052; EAW79158.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79159.1; -; Genomic_DNA.
DR EMBL; BC002510; AAH02510.1; -; mRNA.
DR EMBL; U66623; AAC51198.1; -; mRNA.
DR RefSeq; NP_057661.3; NM_016577.3.
DR UniGene; Hs.715344; -.
DR PDB; 2E9S; X-ray; 1.78 A; A/B/C=13-174.
DR PDB; 2FE4; X-ray; 2.30 A; A=13-174.
DR PDB; 2FFQ; X-ray; 1.78 A; A=13-174.
DR PDBsum; 2E9S; -.
DR PDBsum; 2FE4; -.
DR PDBsum; 2FFQ; -.
DR ProteinModelPortal; Q9NRW1; -.
DR SMR; Q9NRW1; 13-174.
DR IntAct; Q9NRW1; 1.
DR STRING; 9606.ENSP00000285208; -.
DR PhosphoSite; Q9NRW1; -.
DR DMDM; 13633595; -.
DR PaxDb; Q9NRW1; -.
DR PRIDE; Q9NRW1; -.
DR DNASU; 51560; -.
DR Ensembl; ENST00000285208; ENSP00000285208; ENSG00000154917.
DR Ensembl; ENST00000543906; ENSP00000437797; ENSG00000154917.
DR GeneID; 51560; -.
DR KEGG; hsa:51560; -.
DR UCSC; uc003epy.3; human.
DR CTD; 51560; -.
DR GeneCards; GC03M133543; -.
DR HGNC; HGNC:14902; RAB6B.
DR HPA; CAB017713; -.
DR neXtProt; NX_Q9NRW1; -.
DR PharmGKB; PA34147; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233968; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; Q9NRW1; -.
DR KO; K07894; -.
DR OMA; MESVQEK; -.
DR OrthoDB; EOG77DJ7M; -.
DR PhylomeDB; Q9NRW1; -.
DR ChiTaRS; RAB6B; human.
DR EvolutionaryTrace; Q9NRW1; -.
DR GeneWiki; RAB6B; -.
DR GenomeRNAi; 51560; -.
DR NextBio; 55358; -.
DR PRO; PR:Q9NRW1; -.
DR ArrayExpress; Q9NRW1; -.
DR Bgee; Q9NRW1; -.
DR Genevestigator; Q9NRW1; -.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; NAS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; NAS:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003579; Small_GTPase_Rab_type.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasmic vesicle;
KW ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 208 Ras-related protein Rab-6B.
FT /FTId=PRO_0000121115.
FT NP_BIND 20 27 GTP.
FT NP_BIND 68 72 GTP.
FT NP_BIND 126 129 GTP.
FT MOTIF 42 50 Effector region (By similarity).
FT BINDING 45 45 GTP.
FT MOD_RES 2 2 N-acetylserine (By similarity).
FT MOD_RES 82 82 O-AMP-tyrosine; by Legionella DrrA.
FT MOD_RES 208 208 Cysteine methyl ester (By similarity).
FT LIPID 206 206 S-geranylgeranyl cysteine (By
FT similarity).
FT LIPID 208 208 S-geranylgeranyl cysteine (By
FT similarity).
FT MUTAGEN 27 27 T->N: Loss of APBA1-binding.
FT MUTAGEN 72 72 Q->L: Interacts with APBA1.
FT STRAND 15 19
FT HELIX 26 35
FT STRAND 47 57
FT STRAND 60 69
FT HELIX 73 78
FT HELIX 79 84
FT STRAND 87 94
FT HELIX 98 102
FT HELIX 104 115
FT STRAND 118 126
FT HELIX 131 133
FT HELIX 138 147
FT STRAND 151 154
FT TURN 157 159
FT HELIX 163 174
SQ SEQUENCE 208 AA; 23462 MW; E81C831996E2446D CRC64;
MSAGGDFGNP LRKFKLVFLG EQSVGKTSLI TRFMYDSFDN TYQATIGIDF LSKTMYLEDR
TVRLQLWDTA GQERFRSLIP SYIRDSTVAV VVYDITNLNS FQQTSKWIDD VRTERGSDVI
IMLVGNKTDL ADKRQITIEE GEQRAKELSV MFIETSAKTG YNVKQLFRRV ASALPGMENV
QEKSKEGMID IKLDKPQEPP ASEGGCSC
//

RBCC Red Blood Cell Collection

Full text data of RAB6B