TBC15_HUMAN
ID TBC15_HUMAN Reviewed; 691 AA.
AC Q8TC07; B4DMT9; B9A6L6; J3KNI9; Q9HA83;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=TBC1 domain family member 15;
DE AltName: Full=GTPase-activating protein RAB7;
DE Short=GAP for RAB7;
DE Short=Rab7-GAP;
GN Name=TBC1D15;
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 [MRNA] (ISOFORM 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-675 AND THR-689, 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-205 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-213 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND IDENTIFICATION BY
RP 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 [11]
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., Buerckstuemmer T.,
RA 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-205 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-213 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-274 AND SER-675, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-640 AND SER-675, 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RAB8A.
RX PubMed=26824392; DOI=10.7554/elife.12813;
RA Steger M., Tonelli F., Ito G., Davies P., Trost M., Vetter M., Wachter S.,
RA Lorentzen E., Duddy G., Wilson S., Baptista M.A., Fiske B.K., Fell M.J.,
RA Morrow J.A., Reith A.D., Alessi D.R., Mann M.;
RT "Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates
RT a subset of Rab GTPases.";
RL Elife 5:0-0(2016).
RN [16]
RP INTERACTION WITH ARMC12, AND TISSUE SPECIFICITY.
RX PubMed=33536340; DOI=10.1073/pnas.2018355118;
RA Shimada K., Park S., Miyata H., Yu Z., Morohoshi A., Oura S., Matzuk M.M.,
RA Ikawa M.;
RT "ARMC12 regulates spatiotemporal mitochondrial dynamics during
RT spermiogenesis and is required for male fertility.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Acts as a GTPase activating protein for RAB7A. Does not act
CC on RAB4, RAB5 or RAB6 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with non-phosphorylated form of RAB8A;
CC phosphorylation of RAB8A at 'Thr-72' disrupts this interaction
CC (PubMed:26824392). Interacts with ARMC12 (PubMed:33536340).
CC {ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:33536340}.
CC -!- INTERACTION:
CC Q8TC07; Q9P1Z2: CALCOCO1; NbExp=3; IntAct=EBI-1048247, EBI-749920;
CC Q8TC07; Q96MT8: CEP63; NbExp=5; IntAct=EBI-1048247, EBI-741977;
CC Q8TC07; Q96MT8-3: CEP63; NbExp=3; IntAct=EBI-1048247, EBI-11522539;
CC Q8TC07; O95166: GABARAP; NbExp=5; IntAct=EBI-1048247, EBI-712001;
CC Q8TC07; Q9H0R8: GABARAPL1; NbExp=2; IntAct=EBI-1048247, EBI-746969;
CC Q8TC07; P60520: GABARAPL2; NbExp=2; IntAct=EBI-1048247, EBI-720116;
CC Q8TC07; Q9GZQ8: MAP1LC3B; NbExp=2; IntAct=EBI-1048247, EBI-373144;
CC Q8TC07; Q96CV9: OPTN; NbExp=9; IntAct=EBI-1048247, EBI-748974;
CC Q8TC07; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-1048247, EBI-529518;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TC07-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TC07-2; Sequence=VSP_023094;
CC Name=3;
CC IsoId=Q8TC07-3; Sequence=VSP_046402, VSP_023094;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:33536340}.
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DR EMBL; AB449901; BAH16644.1; -; mRNA.
DR EMBL; AK022147; BAB13971.1; -; mRNA.
DR EMBL; AK297626; BAG60001.1; -; mRNA.
DR EMBL; AC089984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028352; AAH28352.1; -; mRNA.
DR CCDS; CCDS31858.1; -. [Q8TC07-1]
DR CCDS; CCDS53814.1; -. [Q8TC07-2]
DR RefSeq; NP_001139685.2; NM_001146213.1. [Q8TC07-2]
DR RefSeq; NP_001139686.1; NM_001146214.1.
DR RefSeq; NP_073608.4; NM_022771.4. [Q8TC07-1]
DR AlphaFoldDB; Q8TC07; -.
DR SMR; Q8TC07; -.
DR BioGRID; 122296; 161.
DR IntAct; Q8TC07; 58.
DR MINT; Q8TC07; -.
DR STRING; 9606.ENSP00000448182; -.
DR ChEMBL; CHEMBL4295905; -.
DR GlyGen; Q8TC07; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TC07; -.
DR PhosphoSitePlus; Q8TC07; -.
DR BioMuta; TBC1D15; -.
DR DMDM; 143811467; -.
DR EPD; Q8TC07; -.
DR jPOST; Q8TC07; -.
DR MassIVE; Q8TC07; -.
DR MaxQB; Q8TC07; -.
DR PaxDb; Q8TC07; -.
DR PeptideAtlas; Q8TC07; -.
DR PRIDE; Q8TC07; -.
DR ProteomicsDB; 74067; -. [Q8TC07-1]
DR ProteomicsDB; 74068; -. [Q8TC07-2]
DR Antibodypedia; 2850; 97 antibodies from 17 providers.
DR DNASU; 64786; -.
DR Ensembl; ENST00000319106.12; ENSP00000318262.6; ENSG00000121749.16. [Q8TC07-3]
DR Ensembl; ENST00000485960.7; ENSP00000420678.2; ENSG00000121749.16. [Q8TC07-2]
DR Ensembl; ENST00000550746.5; ENSP00000448182.1; ENSG00000121749.16. [Q8TC07-1]
DR GeneID; 64786; -.
DR KEGG; hsa:64786; -.
DR MANE-Select; ENST00000485960.7; ENSP00000420678.2; NM_001146213.3; NP_001139685.2. [Q8TC07-2]
DR UCSC; uc001swu.4; human. [Q8TC07-1]
DR CTD; 64786; -.
DR GeneCards; TBC1D15; -.
DR HGNC; HGNC:25694; TBC1D15.
DR HPA; ENSG00000121749; Low tissue specificity.
DR MIM; 612662; gene.
DR neXtProt; NX_Q8TC07; -.
DR OpenTargets; ENSG00000121749; -.
DR PharmGKB; PA134946839; -.
DR VEuPathDB; HostDB:ENSG00000121749; -.
DR eggNOG; KOG2197; Eukaryota.
DR GeneTree; ENSGT00940000156429; -.
DR HOGENOM; CLU_004457_2_2_1; -.
DR InParanoid; Q8TC07; -.
DR OMA; SVVEWTP; -.
DR OrthoDB; 1495285at2759; -.
DR PhylomeDB; Q8TC07; -.
DR TreeFam; TF314296; -.
DR PathwayCommons; Q8TC07; -.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR SignaLink; Q8TC07; -.
DR BioGRID-ORCS; 64786; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; TBC1D15; human.
DR GenomeRNAi; 64786; -.
DR Pharos; Q8TC07; Tbio.
DR PRO; PR:Q8TC07; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8TC07; protein.
DR Bgee; ENSG00000121749; Expressed in calcaneal tendon and 193 other tissues.
DR ExpressionAtlas; Q8TC07; baseline and differential.
DR Genevisible; Q8TC07; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:Ensembl.
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 InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR021935; SGSM1/2_RBD.
DR Pfam; PF12068; PH_RBD; 1.
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 Acetylation; Alternative splicing; Cytoplasm; GTPase activation;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..691
FT /note="TBC1 domain family member 15"
FT /id="PRO_0000208042"
FT DOMAIN 346..556
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CXF4"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 689
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..10
FT /note="MAAAGVVSGK -> MCPGLYPYSSLLEYGRSM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046402"
FT VAR_SEQ 220..236
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:19077034"
FT /id="VSP_023094"
FT CONFLICT 52
FT /note="R -> G (in Ref. 1; BAB13971)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="E -> G (in Ref. 2; BAG60001)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="Q -> R (in Ref. 2; BAG60001)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="S -> G (in Ref. 3; AAH28352)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="S -> G (in Ref. 1; BAB13971)"
FT /evidence="ECO:0000305"
FT MOD_RES Q8TC07-2:205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES Q8TC07-3:213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
SQ SEQUENCE 691 AA; 79491 MW; D880DBE4D5758EC7 CRC64;
MAAAGVVSGK IIYEQEGVYI HSSCGKTNDQ DGLISGILRV LEKDAEVIVD WRPLDDALDS
SSILYARKDS SSVVEWTQAP KERGHRGSEH LNSYEAEWDM VNTVSFKRKP HTNGDAPSHR
NGKSKWSFLF SLTDLKSIKQ NKEGMGWSYL VFCLKDDVVL PALHFHQGDS KLLIESLEKY
VVLCESPQDK RTLLVNCQNK SLSQSFENLL DEPAYGLIQA GLLDRRKLLW AIHHWKKIKK
DPYTATMIGF SKVTNYIFDS LRGSDPSTHQ RPPSEMADFL SDAIPGLKIN QQEEPGFEVI
TRIDLGERPV VQRREPVSLE EWTKNIDSEG RILNVDNMKQ MIFRGGLSHA LRKQAWKFLL
GYFPWDSTKE ERTQLQKQKT DEYFRMKLQW KSISQEQEKR NSRLRDYRSL IEKDVNRTDR
TNKFYEGQDN PGLILLHDIL MTYCMYDFDL GYVQGMSDLL SPLLYVMENE VDAFWCFASY
MDQMHQNFEE QMQGMKTQLI QLSTLLRLLD SGFCSYLESQ DSGYLYFCFR WLLIRFKREF
SFLDILRLWE VMWTELPCTN FHLLLCCAIL ESEKQQIMEK HYGFNEILKH INELSMKIDV
EDILCKAEAI SLQMVKCKEL PQAVCEILGL QGSEVTTPDS DVGEDENVVM TPCPTSAFQS
NALPTLSASG ARNDSPTQIP VSSDVCRLTP A
