Full text data of TBC1D10B
TBC1D10B
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
TBC1 domain family member 10B (Rab27A-GAP-beta)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
TBC1 domain family member 10B (Rab27A-GAP-beta)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q4KMP7
ID TB10B_HUMAN Reviewed; 808 AA.
AC Q4KMP7; B9A6L0; Q6IN54; Q6P530; Q71RG7; Q86VC5; Q9H8Z2; Q9NUN6;
read moreAC Q9UFP2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 3.
DT 22-JAN-2014, entry version 73.
DE RecName: Full=TBC1 domain family member 10B;
DE AltName: Full=Rab27A-GAP-beta;
GN Name=TBC1D10B; ORFNames=FP2461;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
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 [4]
RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and Teratocarcinoma;
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 PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Ovary, PNS, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 170-808, FUNCTION, AND MUTAGENESIS OF
RP ARG-409.
RC TISSUE=Brain;
RX PubMed=19077034; DOI=10.1111/j.1365-2443.2008.01251.x;
RA Ishibashi K., Kanno E., Itoh T., Fukuda M.;
RT "Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC)
RT protein that possesses Rab3A-GAP activity.";
RL Genes Cells 14:41-52(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 281-808 (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, 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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16923811; DOI=10.1074/jbc.M603808200;
RA Itoh T., Fukuda M.;
RT "Identification of EPI64 as a GTPase-activating protein specific for
RT Rab27A.";
RL J. Biol. Chem. 281:31823-31831(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658; SER-661 AND
RP SER-687, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658; SER-661 AND
RP SER-687, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661 AND SER-687, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Acts as GTPase-activating protein for RAB3A, RAB22A,
CC RAB27A, AND RAB35. Does not act on RAB2A and RAB6A.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=In melanocytes, located at
CC the periphery of cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4KMP7-1; Sequence=Displayed;
CC Note=No experimental confirmation available. Gene prediction
CC based on similarity to mouse ortholog;
CC Name=2;
CC IsoId=Q4KMP7-2; Sequence=VSP_030670;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50523.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH63112.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH72453.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH93814.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH93816.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH98419.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAQ15206.1; Type=Frameshift; Positions=154, 379, 401;
CC Sequence=BAA92086.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB14454.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAH16638.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC Sequence=EAW52256.1; Type=Erroneous gene model prediction;
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DR EMBL; AL117408; CAB55908.1; -; mRNA.
DR EMBL; AC106782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471192; EAW52256.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK002101; BAA92086.1; ALT_INIT; mRNA.
DR EMBL; AK023192; BAB14454.1; ALT_INIT; mRNA.
DR EMBL; BC050523; AAH50523.2; ALT_INIT; mRNA.
DR EMBL; BC063112; AAH63112.1; ALT_INIT; mRNA.
DR EMBL; BC072453; AAH72453.2; ALT_INIT; mRNA.
DR EMBL; BC093814; AAH93814.1; ALT_INIT; mRNA.
DR EMBL; BC093816; AAH93816.1; ALT_INIT; mRNA.
DR EMBL; BC098419; AAH98419.1; ALT_INIT; mRNA.
DR EMBL; AB449895; BAH16638.1; ALT_SEQ; mRNA.
DR EMBL; AF370370; AAQ15206.1; ALT_FRAME; mRNA.
DR PIR; T17218; T17218.
DR RefSeq; NP_056342.3; NM_015527.3.
DR UniGene; Hs.632182; -.
DR ProteinModelPortal; Q4KMP7; -.
DR SMR; Q4KMP7; 327-605.
DR STRING; 9606.ENSP00000386538; -.
DR PhosphoSite; Q4KMP7; -.
DR DMDM; 294862492; -.
DR PaxDb; Q4KMP7; -.
DR PRIDE; Q4KMP7; -.
DR DNASU; 26000; -.
DR Ensembl; ENST00000409939; ENSP00000386538; ENSG00000169221.
DR GeneID; 26000; -.
DR KEGG; hsa:26000; -.
DR UCSC; uc002dxu.2; human.
DR CTD; 26000; -.
DR GeneCards; GC16M030368; -.
DR H-InvDB; HIX0012950; -.
DR HGNC; HGNC:24510; TBC1D10B.
DR HPA; HPA048894; -.
DR MIM; 613620; gene.
DR neXtProt; NX_Q4KMP7; -.
DR PharmGKB; PA142670835; -.
DR eggNOG; COG5210; -.
DR HOVERGEN; HBG070028; -.
DR InParanoid; Q4KMP7; -.
DR OMA; PSGTCEA; -.
DR OrthoDB; EOG7RJPR8; -.
DR ChiTaRS; TBC1D10B; human.
DR GenomeRNAi; 26000; -.
DR NextBio; 47722; -.
DR PRO; PR:Q4KMP7; -.
DR ArrayExpress; Q4KMP7; -.
DR Bgee; Q4KMP7; -.
DR CleanEx; HS_TBC1D10B; -.
DR Genevestigator; Q4KMP7; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005097; F:Rab GTPase activator activity; IDA:UniProtKB.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1 808 TBC1 domain family member 10B.
FT /FTId=PRO_0000315716.
FT DOMAIN 360 548 Rab-GAP TBC.
FT COILED 716 782 Potential.
FT COMPBIAS 7 175 Pro-rich.
FT COMPBIAS 677 682 Poly-Pro.
FT MOD_RES 658 658 Phosphoserine.
FT MOD_RES 661 661 Phosphoserine.
FT MOD_RES 678 678 Phosphoserine.
FT MOD_RES 687 687 Phosphoserine.
FT VAR_SEQ 1 575 Missing (in isoform 2).
FT /FTId=VSP_030670.
FT MUTAGEN 409 409 R->L: Loss of GAP activity.
FT CONFLICT 187 187 S -> G (in Ref. 5; AAH50523).
FT CONFLICT 350 350 F -> L (in Ref. 7; AAQ15206).
FT CONFLICT 669 669 G -> D (in Ref. 6; BAH16638).
FT CONFLICT 690 690 P -> S (in Ref. 6; BAH16638).
FT CONFLICT 761 761 E -> G (in Ref. 5; AAH50523/AAH63112).
SQ SEQUENCE 808 AA; 87199 MW; 50D8884B8E3BBFBE CRC64;
METGTAPLVA PPRRHGAPAA PSPPPRGSRA GPVVVVAPGP PVTTATSAPV TLVAPGEARP
AWVPGSAETS APAPAPAPAP APAVTGSTVV VLTLEASPEA PKPQLPSGPE SPEPAAVAGV
ETSRALAAGA DSPKTEEARP SPAPGPGTPT GTPTRTPSRT APGALTAKPP LAPKPGTTVA
SGVTARSASG QVTGGHGAAA ATSASAGQAP EDPSGPGTGP SGTCEAPVAV VTVTPAPEPA
ENSQDLGSTS SLGPGISGPR GQAPDTLSYL DSVSLMSGTL ESLADDVSSM GSDSEINGLA
LRKTDKYGFL GGSQYSGSLE SSIPVDVARQ RELKWLDMFS NWDKWLSRRF QKVKLRCRKG
IPSSLRAKAW QYLSNSKELL EQNPGKFEEL ERAPGDPKWL DVIEKDLHRQ FPFHEMFAAR
GGHGQQDLYR ILKAYTIYRP DEGYCQAQAP VAAVLLMHMP AEQAFWCLVQ ICDKYLPGYY
SAGLEAIQLD GEIFFALLRR ASPLAHRHLR RQRIDPVLYM TEWFMCIFAR TLPWASVLRV
WDMFFCEGVK IIFRVALVLL RHTLGSVEKL RSCQGMYETM EQLRNLPQQC MQEDFLVHEV
TNLPVTEALI ERENAAQLKK WRETRGELQY RPSRRLHGSR AIHEERRRQQ PPLGPSSSLL
SLPGLKSRGS RAAGGAPSPP PPVRRASAGP APGPVVTAEG LHPSLPSPTG NSTPLGSSKE
TRKQEKERQK QEKERQKQEK EREKERQKQE KEREKQEKER EKQEKERQKQ EKKAQGRKLS
LRRKADGPPG PHDGGDRPSA EARQDAYF
//
ID TB10B_HUMAN Reviewed; 808 AA.
AC Q4KMP7; B9A6L0; Q6IN54; Q6P530; Q71RG7; Q86VC5; Q9H8Z2; Q9NUN6;
read moreAC Q9UFP2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 3.
DT 22-JAN-2014, entry version 73.
DE RecName: Full=TBC1 domain family member 10B;
DE AltName: Full=Rab27A-GAP-beta;
GN Name=TBC1D10B; ORFNames=FP2461;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
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 [4]
RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and Teratocarcinoma;
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 PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Ovary, PNS, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 170-808, FUNCTION, AND MUTAGENESIS OF
RP ARG-409.
RC TISSUE=Brain;
RX PubMed=19077034; DOI=10.1111/j.1365-2443.2008.01251.x;
RA Ishibashi K., Kanno E., Itoh T., Fukuda M.;
RT "Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC)
RT protein that possesses Rab3A-GAP activity.";
RL Genes Cells 14:41-52(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 281-808 (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, 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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16923811; DOI=10.1074/jbc.M603808200;
RA Itoh T., Fukuda M.;
RT "Identification of EPI64 as a GTPase-activating protein specific for
RT Rab27A.";
RL J. Biol. Chem. 281:31823-31831(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658; SER-661 AND
RP SER-687, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658; SER-661 AND
RP SER-687, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661 AND SER-687, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Acts as GTPase-activating protein for RAB3A, RAB22A,
CC RAB27A, AND RAB35. Does not act on RAB2A and RAB6A.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=In melanocytes, located at
CC the periphery of cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4KMP7-1; Sequence=Displayed;
CC Note=No experimental confirmation available. Gene prediction
CC based on similarity to mouse ortholog;
CC Name=2;
CC IsoId=Q4KMP7-2; Sequence=VSP_030670;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50523.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH63112.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH72453.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH93814.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH93816.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH98419.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAQ15206.1; Type=Frameshift; Positions=154, 379, 401;
CC Sequence=BAA92086.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB14454.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAH16638.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC Sequence=EAW52256.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
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DR EMBL; AL117408; CAB55908.1; -; mRNA.
DR EMBL; AC106782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471192; EAW52256.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK002101; BAA92086.1; ALT_INIT; mRNA.
DR EMBL; AK023192; BAB14454.1; ALT_INIT; mRNA.
DR EMBL; BC050523; AAH50523.2; ALT_INIT; mRNA.
DR EMBL; BC063112; AAH63112.1; ALT_INIT; mRNA.
DR EMBL; BC072453; AAH72453.2; ALT_INIT; mRNA.
DR EMBL; BC093814; AAH93814.1; ALT_INIT; mRNA.
DR EMBL; BC093816; AAH93816.1; ALT_INIT; mRNA.
DR EMBL; BC098419; AAH98419.1; ALT_INIT; mRNA.
DR EMBL; AB449895; BAH16638.1; ALT_SEQ; mRNA.
DR EMBL; AF370370; AAQ15206.1; ALT_FRAME; mRNA.
DR PIR; T17218; T17218.
DR RefSeq; NP_056342.3; NM_015527.3.
DR UniGene; Hs.632182; -.
DR ProteinModelPortal; Q4KMP7; -.
DR SMR; Q4KMP7; 327-605.
DR STRING; 9606.ENSP00000386538; -.
DR PhosphoSite; Q4KMP7; -.
DR DMDM; 294862492; -.
DR PaxDb; Q4KMP7; -.
DR PRIDE; Q4KMP7; -.
DR DNASU; 26000; -.
DR Ensembl; ENST00000409939; ENSP00000386538; ENSG00000169221.
DR GeneID; 26000; -.
DR KEGG; hsa:26000; -.
DR UCSC; uc002dxu.2; human.
DR CTD; 26000; -.
DR GeneCards; GC16M030368; -.
DR H-InvDB; HIX0012950; -.
DR HGNC; HGNC:24510; TBC1D10B.
DR HPA; HPA048894; -.
DR MIM; 613620; gene.
DR neXtProt; NX_Q4KMP7; -.
DR PharmGKB; PA142670835; -.
DR eggNOG; COG5210; -.
DR HOVERGEN; HBG070028; -.
DR InParanoid; Q4KMP7; -.
DR OMA; PSGTCEA; -.
DR OrthoDB; EOG7RJPR8; -.
DR ChiTaRS; TBC1D10B; human.
DR GenomeRNAi; 26000; -.
DR NextBio; 47722; -.
DR PRO; PR:Q4KMP7; -.
DR ArrayExpress; Q4KMP7; -.
DR Bgee; Q4KMP7; -.
DR CleanEx; HS_TBC1D10B; -.
DR Genevestigator; Q4KMP7; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005097; F:Rab GTPase activator activity; IDA:UniProtKB.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1 808 TBC1 domain family member 10B.
FT /FTId=PRO_0000315716.
FT DOMAIN 360 548 Rab-GAP TBC.
FT COILED 716 782 Potential.
FT COMPBIAS 7 175 Pro-rich.
FT COMPBIAS 677 682 Poly-Pro.
FT MOD_RES 658 658 Phosphoserine.
FT MOD_RES 661 661 Phosphoserine.
FT MOD_RES 678 678 Phosphoserine.
FT MOD_RES 687 687 Phosphoserine.
FT VAR_SEQ 1 575 Missing (in isoform 2).
FT /FTId=VSP_030670.
FT MUTAGEN 409 409 R->L: Loss of GAP activity.
FT CONFLICT 187 187 S -> G (in Ref. 5; AAH50523).
FT CONFLICT 350 350 F -> L (in Ref. 7; AAQ15206).
FT CONFLICT 669 669 G -> D (in Ref. 6; BAH16638).
FT CONFLICT 690 690 P -> S (in Ref. 6; BAH16638).
FT CONFLICT 761 761 E -> G (in Ref. 5; AAH50523/AAH63112).
SQ SEQUENCE 808 AA; 87199 MW; 50D8884B8E3BBFBE CRC64;
METGTAPLVA PPRRHGAPAA PSPPPRGSRA GPVVVVAPGP PVTTATSAPV TLVAPGEARP
AWVPGSAETS APAPAPAPAP APAVTGSTVV VLTLEASPEA PKPQLPSGPE SPEPAAVAGV
ETSRALAAGA DSPKTEEARP SPAPGPGTPT GTPTRTPSRT APGALTAKPP LAPKPGTTVA
SGVTARSASG QVTGGHGAAA ATSASAGQAP EDPSGPGTGP SGTCEAPVAV VTVTPAPEPA
ENSQDLGSTS SLGPGISGPR GQAPDTLSYL DSVSLMSGTL ESLADDVSSM GSDSEINGLA
LRKTDKYGFL GGSQYSGSLE SSIPVDVARQ RELKWLDMFS NWDKWLSRRF QKVKLRCRKG
IPSSLRAKAW QYLSNSKELL EQNPGKFEEL ERAPGDPKWL DVIEKDLHRQ FPFHEMFAAR
GGHGQQDLYR ILKAYTIYRP DEGYCQAQAP VAAVLLMHMP AEQAFWCLVQ ICDKYLPGYY
SAGLEAIQLD GEIFFALLRR ASPLAHRHLR RQRIDPVLYM TEWFMCIFAR TLPWASVLRV
WDMFFCEGVK IIFRVALVLL RHTLGSVEKL RSCQGMYETM EQLRNLPQQC MQEDFLVHEV
TNLPVTEALI ERENAAQLKK WRETRGELQY RPSRRLHGSR AIHEERRRQQ PPLGPSSSLL
SLPGLKSRGS RAAGGAPSPP PPVRRASAGP APGPVVTAEG LHPSLPSPTG NSTPLGSSKE
TRKQEKERQK QEKERQKQEK EREKERQKQE KEREKQEKER EKQEKERQKQ EKKAQGRKLS
LRRKADGPPG PHDGGDRPSA EARQDAYF
//
MIM
613620
*RECORD*
*FIELD* NO
613620
*FIELD* TI
*613620 TBC1 DOMAIN FAMILY, MEMBER 10B; TBC1D10B
;;RAB27AGAP-BETA
*FIELD* TX
DESCRIPTION
read more
Small G proteins of the RAB family (see 179508) function in
intracellular vesicle trafficking by switching from the GTP-bound state
to the GDP-bound state with the assistance of guanine nucleotide
exchange factors (GEFs; see 609700) and GTPase-activating proteins
(GAPs). TBC1D10B functions as a GAP for several proteins of the Rab
family (Ishibashi et al., 2009).
CLONING
By database analysis, Itoh and Fukuda (2006) determined that the deduced
533-amino acid TBC1D10B protein, which they called RAB27AGAP-beta,
contains a central TRE2 (USP6; 604334)/yeast Bub2/CDC16 (603461) (TBC)
domain and a C-terminal DAYF motif. The TBC domain is predicted to
function as a RabGAP, and the DAYF motif is predicted to interact with
PDZ domains. TBC1D10B shares highest sequence similarity with EPI64
(TBC1D10A; 610020). The TBC domains of TBC1D10B and TBC1D10A are 81%
identical, and both contain a highly conserved catalytic arginine.
Fluorescence-tagged TBC1D10B localized to the plasma membrane of
transfected mouse melanoma cells.
Ishibashi et al. (2009) found that fluorescence-tagged TBC1D10B
localized near the plasma membrane of differentiated rat PC12
pheochromocytoma cells.
GENE FUNCTION
By screening human and mouse cDNAs encoding putative RabGAPs for the
ability to catalyze GTP exchange in Rab proteins, Itoh and Fukuda (2006)
found that both TBC1D10A and TBC1D10B functioned as GAPs for mouse
Rab27a (603868) and induced melanosome aggregation in a mouse melanocyte
cell line. Both TBC1D10A and TBC1D10B increased the GTPase activity of
Rab27a and reduced the amount of GTP-Rab27a when coexpressed with
Rab27a.
Endogenous Rab3a (179490) is present on dense-core vesicles in the
distal portion of neurites in differentiated rat PC12 cells. By
overexpressing TBC1D10B in PC12 cells, Ishibashi et al. (2009) found
that TBC1D10B functioned as a GAP for Rab3a, reducing association of
Rab3a with neurites. Mutation of the catalytic arg134 in the TBC domain
of TBC1D10B completely inhibited its GAP activity against Rab3a in PC12
and transfected COS-7 cells. TBC1D10B also showed significant GAP
activity toward Rab22a (612966), Rab27a, and Rab35 (604199), but not
Rab2a (RAB2; 179509) or Rab6a (179513).
MAPPING
Hartz (2010) mapped the TBC1D10B gene to chromosome 16p11.2 based on an
alignment of the TBC1D10B sequence (GenBank GENBANK BC063112) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 10/22/2010.
2. Ishibashi, K.; Kanno, E.; Itoh, T.; Fukuda, M.: Identification
and characterization of a novel Tre-2/Bub2/Cdc16 (TBC) protein that
possesses Rab3A-GAP activity. Genes Cells 14: 41-52, 2009.
3. Itoh, T.; Fukuda, M.: Identification of EPI64 as a GTPase-activating
protein specific for Rab27A. J. Biol. Chem. 281: 31823-31831, 2006.
*FIELD* CD
Patricia A. Hartz: 10/29/2010
*FIELD* ED
mgross: 10/29/2010
*RECORD*
*FIELD* NO
613620
*FIELD* TI
*613620 TBC1 DOMAIN FAMILY, MEMBER 10B; TBC1D10B
;;RAB27AGAP-BETA
*FIELD* TX
DESCRIPTION
read more
Small G proteins of the RAB family (see 179508) function in
intracellular vesicle trafficking by switching from the GTP-bound state
to the GDP-bound state with the assistance of guanine nucleotide
exchange factors (GEFs; see 609700) and GTPase-activating proteins
(GAPs). TBC1D10B functions as a GAP for several proteins of the Rab
family (Ishibashi et al., 2009).
CLONING
By database analysis, Itoh and Fukuda (2006) determined that the deduced
533-amino acid TBC1D10B protein, which they called RAB27AGAP-beta,
contains a central TRE2 (USP6; 604334)/yeast Bub2/CDC16 (603461) (TBC)
domain and a C-terminal DAYF motif. The TBC domain is predicted to
function as a RabGAP, and the DAYF motif is predicted to interact with
PDZ domains. TBC1D10B shares highest sequence similarity with EPI64
(TBC1D10A; 610020). The TBC domains of TBC1D10B and TBC1D10A are 81%
identical, and both contain a highly conserved catalytic arginine.
Fluorescence-tagged TBC1D10B localized to the plasma membrane of
transfected mouse melanoma cells.
Ishibashi et al. (2009) found that fluorescence-tagged TBC1D10B
localized near the plasma membrane of differentiated rat PC12
pheochromocytoma cells.
GENE FUNCTION
By screening human and mouse cDNAs encoding putative RabGAPs for the
ability to catalyze GTP exchange in Rab proteins, Itoh and Fukuda (2006)
found that both TBC1D10A and TBC1D10B functioned as GAPs for mouse
Rab27a (603868) and induced melanosome aggregation in a mouse melanocyte
cell line. Both TBC1D10A and TBC1D10B increased the GTPase activity of
Rab27a and reduced the amount of GTP-Rab27a when coexpressed with
Rab27a.
Endogenous Rab3a (179490) is present on dense-core vesicles in the
distal portion of neurites in differentiated rat PC12 cells. By
overexpressing TBC1D10B in PC12 cells, Ishibashi et al. (2009) found
that TBC1D10B functioned as a GAP for Rab3a, reducing association of
Rab3a with neurites. Mutation of the catalytic arg134 in the TBC domain
of TBC1D10B completely inhibited its GAP activity against Rab3a in PC12
and transfected COS-7 cells. TBC1D10B also showed significant GAP
activity toward Rab22a (612966), Rab27a, and Rab35 (604199), but not
Rab2a (RAB2; 179509) or Rab6a (179513).
MAPPING
Hartz (2010) mapped the TBC1D10B gene to chromosome 16p11.2 based on an
alignment of the TBC1D10B sequence (GenBank GENBANK BC063112) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 10/22/2010.
2. Ishibashi, K.; Kanno, E.; Itoh, T.; Fukuda, M.: Identification
and characterization of a novel Tre-2/Bub2/Cdc16 (TBC) protein that
possesses Rab3A-GAP activity. Genes Cells 14: 41-52, 2009.
3. Itoh, T.; Fukuda, M.: Identification of EPI64 as a GTPase-activating
protein specific for Rab27A. J. Biol. Chem. 281: 31823-31831, 2006.
*FIELD* CD
Patricia A. Hartz: 10/29/2010
*FIELD* ED
mgross: 10/29/2010