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TB10B_MOUSE
ID   TB10B_MOUSE             Reviewed;         798 AA.
AC   Q8BHL3; Q6GQW9; Q6PIZ5; Q91XR3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=TBC1 domain family member 10B;
DE   AltName: Full=Protein wz3-85;
GN   Name=Tbc1d10b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 180-798.
RC   TISSUE=Spleen;
RA   Tian W., Chua K., Strober W., Chu C.C.;
RT   "Characterization of an unknown wz3-85 gene.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 119-798.
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Kidney;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664 AND SER-673, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; THR-136; SER-647;
RP   SER-650 AND SER-673, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-170, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: Acts as GTPase-activating protein for RAB3A, RAB22A, RAB27A,
CC       AND RAB35. Does not act on RAB2A and RAB6A (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH25889.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH72576.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAK82984.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC33022.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC33025.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK047320; BAC33022.1; ALT_INIT; mRNA.
DR   EMBL; AK047327; BAC33025.1; ALT_INIT; mRNA.
DR   EMBL; AC122537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF285112; AAK82984.1; ALT_INIT; mRNA.
DR   EMBL; BC025889; AAH25889.1; ALT_INIT; mRNA.
DR   EMBL; BC072576; AAH72576.2; ALT_INIT; mRNA.
DR   CCDS; CCDS40139.2; -.
DR   RefSeq; NP_653105.3; NM_144522.5.
DR   AlphaFoldDB; Q8BHL3; -.
DR   SMR; Q8BHL3; -.
DR   BioGRID; 212858; 7.
DR   IntAct; Q8BHL3; 2.
DR   MINT; Q8BHL3; -.
DR   STRING; 10090.ENSMUSP00000113307; -.
DR   iPTMnet; Q8BHL3; -.
DR   PhosphoSitePlus; Q8BHL3; -.
DR   EPD; Q8BHL3; -.
DR   jPOST; Q8BHL3; -.
DR   MaxQB; Q8BHL3; -.
DR   PaxDb; Q8BHL3; -.
DR   PeptideAtlas; Q8BHL3; -.
DR   PRIDE; Q8BHL3; -.
DR   ProteomicsDB; 254855; -.
DR   Antibodypedia; 27194; 105 antibodies from 22 providers.
DR   DNASU; 68449; -.
DR   Ensembl; ENSMUST00000120705; ENSMUSP00000113307; ENSMUSG00000042492.
DR   GeneID; 68449; -.
DR   KEGG; mmu:68449; -.
DR   UCSC; uc009juo.3; mouse.
DR   CTD; 26000; -.
DR   MGI; MGI:1915699; Tbc1d10b.
DR   VEuPathDB; HostDB:ENSMUSG00000042492; -.
DR   eggNOG; KOG2221; Eukaryota.
DR   GeneTree; ENSGT00940000159805; -.
DR   HOGENOM; CLU_005350_8_0_1; -.
DR   InParanoid; Q8BHL3; -.
DR   OMA; NNWDKWL; -.
DR   OrthoDB; 976276at2759; -.
DR   PhylomeDB; Q8BHL3; -.
DR   TreeFam; TF313293; -.
DR   Reactome; R-MMU-8854214; TBC/RABGAPs.
DR   BioGRID-ORCS; 68449; 12 hits in 74 CRISPR screens.
DR   ChiTaRS; Tbc1d10b; mouse.
DR   PRO; PR:Q8BHL3; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q8BHL3; protein.
DR   Bgee; ENSMUSG00000042492; Expressed in granulocyte and 252 other tissues.
DR   ExpressionAtlas; Q8BHL3; baseline and differential.
DR   Genevisible; Q8BHL3; MM.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR   GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
DR   InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR   InterPro; IPR035969; Rab-GTPase_TBC_sf.
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   Coiled coil; Cytoplasm; GTPase activation; Methylation; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..798
FT                   /note="TBC1 domain family member 10B"
FT                   /id="PRO_0000315717"
FT   DOMAIN          346..534
FT                   /note="Rab-GAP TBC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          618..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          702..769
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        11..25
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..636
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..651
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..790
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KMP7"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         136
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         170
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         644
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KMP7"
FT   MOD_RES         647
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         650
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         664
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         673
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   CONFLICT        31
FT                   /note="G -> R (in Ref. 1; BAC33022/BAC33025)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        221
FT                   /note="P -> S (in Ref. 3; AAK82984)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        697
FT                   /note="N -> S (in Ref. 3; AAK82984)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        751
FT                   /note="Q -> R (in Ref. 3; AAK82984)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   798 AA;  87275 MW;  B9CB616C2BA01913 CRC64;
     METGPAPLVA PPRRHGAPAA PSPPPRGSRA GSHLVVEPGP PVTTATSAPV ELVAPGEARP
     ACVPGSSQTS ASTPTTATSS TVVMLTLEAS PEAAKTQEFP APAAETGAET SVALALGTDT
     QKTEEVRASP VPGPGTPTRT PSRMAPGALT AKPPLAPKPG TTVASGVTAR GGVGQVAGGH
     EAATSASAGS VPEDPSGPVT GPPGTCEAPA PTPVAVVTVT PAPEPVENFQ DLGSTSSLGP
     GISGPRGQAP DTLSYLDSVS LMSGTLESLP DDVSSMGSDS EINGMALRKT DKYGFLGGSQ
     YSGSLESSIP VDVARQRELK WLEMFSNWDK WLSRRFQKVK LRCRKGIPSS LRAKAWQYLS
     NSKELLEQNP GKFEELERAA GDPKWLDVIE KDLHRQFPFH EMFAARGGHG QQDLYRILKA
     YTIYRPDEGY CQAQAPVAAV LLMHMPAEQA FWCLVQICDK YLPGYYSAGL EAIQLDGEIF
     FALLRRVSPL AHRHLRRQRI DPVLYMTEWF MCIFARTLPW ASVLRVWDMF FCEGVKIIFR
     VALVLLRHTL GSVEKLRSCQ GMYETMEQLR NLPQQCMQED FLVHEVTNLP VTEAWIEREN
     AAQLKKWRET RGELQYRPSR RLHGSRAIHE ERRRQQPPLG PSSSLLSLPS LKSRGSRAVG
     GAPSPPPPVR RASAGPVPGA VVIAEGLHPS LPSPTGNSTP LGTSKEIRRQ EKERQKQEKD
     REKERQRQEK ERERQEKERQ KWEKEQEKEQ QKQEKERQKL EKKGQGRKLS LRRRADGPPA
     SHDGGDRSAA EARQDAYF
 
 
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