TB10B_HUMAN
ID TB10B_HUMAN Reviewed; 808 AA.
AC Q4KMP7; B9A6L0; Q6IN54; Q6P530; Q71RG7; Q86VC5; Q9H8Z2; Q9NUN6; Q9UFP2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 3.
DT 03-AUG-2022, entry version 138.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., 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., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 project:
RT 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., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658; SER-661 AND SER-687, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658; SER-661 AND SER-687, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658; SER-678 AND SER-687, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-678 AND SER-687, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Acts as GTPase-activating protein for RAB3A, RAB22A, RAB27A,
CC AND RAB35. Does not act on RAB2A and RAB6A.
CC {ECO:0000269|PubMed:16923811, ECO:0000269|PubMed:19077034}.
CC -!- INTERACTION:
CC Q4KMP7; Q6NSX1: CCDC70; NbExp=3; IntAct=EBI-4402442, EBI-6873045;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16923811}. Note=In
CC melanocytes, located at the periphery of cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4KMP7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4KMP7-2; Sequence=VSP_030670;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50523.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH63112.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH72453.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH93814.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH93816.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH98419.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAQ15206.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA92086.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14454.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAH16638.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=EAW52256.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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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 CCDS; CCDS10676.2; -. [Q4KMP7-1]
DR PIR; T17218; T17218.
DR RefSeq; NP_056342.3; NM_015527.3. [Q4KMP7-1]
DR AlphaFoldDB; Q4KMP7; -.
DR SMR; Q4KMP7; -.
DR BioGRID; 117476; 72.
DR IntAct; Q4KMP7; 9.
DR MINT; Q4KMP7; -.
DR STRING; 9606.ENSP00000386538; -.
DR GlyGen; Q4KMP7; 6 sites, 1 O-linked glycan (6 sites).
DR iPTMnet; Q4KMP7; -.
DR PhosphoSitePlus; Q4KMP7; -.
DR BioMuta; TBC1D10B; -.
DR DMDM; 294862492; -.
DR EPD; Q4KMP7; -.
DR jPOST; Q4KMP7; -.
DR MassIVE; Q4KMP7; -.
DR MaxQB; Q4KMP7; -.
DR PaxDb; Q4KMP7; -.
DR PeptideAtlas; Q4KMP7; -.
DR PRIDE; Q4KMP7; -.
DR ProteomicsDB; 62197; -. [Q4KMP7-1]
DR ProteomicsDB; 62198; -. [Q4KMP7-2]
DR Antibodypedia; 27194; 105 antibodies from 22 providers.
DR DNASU; 26000; -.
DR Ensembl; ENST00000409939.8; ENSP00000386538.3; ENSG00000169221.14. [Q4KMP7-1]
DR GeneID; 26000; -.
DR KEGG; hsa:26000; -.
DR MANE-Select; ENST00000409939.8; ENSP00000386538.3; NM_015527.4; NP_056342.3.
DR UCSC; uc002dxu.3; human. [Q4KMP7-1]
DR CTD; 26000; -.
DR GeneCards; TBC1D10B; -.
DR HGNC; HGNC:24510; TBC1D10B.
DR HPA; ENSG00000169221; Low tissue specificity.
DR MIM; 613620; gene.
DR neXtProt; NX_Q4KMP7; -.
DR OpenTargets; ENSG00000169221; -.
DR PharmGKB; PA142670835; -.
DR VEuPathDB; HostDB:ENSG00000169221; -.
DR eggNOG; KOG2221; Eukaryota.
DR GeneTree; ENSGT00940000159805; -.
DR HOGENOM; CLU_005350_8_0_1; -.
DR InParanoid; Q4KMP7; -.
DR OMA; NNWDKWL; -.
DR OrthoDB; 976276at2759; -.
DR PhylomeDB; Q4KMP7; -.
DR TreeFam; TF313293; -.
DR PathwayCommons; Q4KMP7; -.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR SignaLink; Q4KMP7; -.
DR BioGRID-ORCS; 26000; 41 hits in 1083 CRISPR screens.
DR ChiTaRS; TBC1D10B; human.
DR GenomeRNAi; 26000; -.
DR Pharos; Q4KMP7; Tbio.
DR PRO; PR:Q4KMP7; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q4KMP7; protein.
DR Bgee; ENSG00000169221; Expressed in left testis and 180 other tissues.
DR ExpressionAtlas; Q4KMP7; baseline and differential.
DR Genevisible; Q4KMP7; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
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 Alternative splicing; Coiled coil; Cytoplasm; GTPase activation;
KW Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..808
FT /note="TBC1 domain family member 10B"
FT /id="PRO_0000315716"
FT DOMAIN 360..548
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 716..782
FT /evidence="ECO:0000255"
FT COMPBIAS 14..28
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BHL3"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BHL3"
FT MOD_RES 186
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BHL3"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..575
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_030670"
FT MUTAGEN 409
FT /note="R->L: Loss of GAP activity."
FT /evidence="ECO:0000269|PubMed:19077034"
FT CONFLICT 187
FT /note="S -> G (in Ref. 5; AAH50523)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="F -> L (in Ref. 7; AAQ15206)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="G -> D (in Ref. 6; BAH16638)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="P -> S (in Ref. 6; BAH16638)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="E -> G (in Ref. 5; AAH50523/AAH63112)"
FT /evidence="ECO:0000305"
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
