TBCD1_HUMAN
ID TBCD1_HUMAN Reviewed; 1168 AA.
AC Q86TI0; B7Z3D9; E9PGH8; Q96K82; Q9UPP4;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=TBC1 domain family member 1;
GN Name=TBC1D1; Synonyms=KIAA1108;
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), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 482-1168 (ISOFORM 1), AND VARIANT PRO-14.
RC TISSUE=Embryo, and Hippocampus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 406-1168 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507; SER-565; SER-570 AND
RP SER-585, AND 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 [8]
RP INTERACTION WITH APPL2, AND PHOSPHORYLATION AT SER-235 AND THR-596.
RX PubMed=24879834; DOI=10.2337/db14-0337;
RA Cheng K.K., Zhu W., Chen B., Wang Y., Wu D., Sweeney G., Wang B., Lam K.S.,
RA Xu A.;
RT "The adaptor protein APPL2 inhibits insulin-stimulated glucose uptake by
RT interacting with TBC1D1 in skeletal muscle.";
RL Diabetes 63:3748-3758(2014).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND SER-585, 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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 750-1072, AND MUTAGENESIS OF
RP MET-930 AND LEU-1019.
RX PubMed=21454505; DOI=10.1074/jbc.m110.217323;
RA Park S.Y., Jin W., Woo J.R., Shoelson S.E.;
RT "Crystal structures of human TBC1D1 and TBC1D4 (AS160) RabGTPase-activating
RT protein (RabGAP) domains reveal critical elements for GLUT4
RT translocation.";
RL J. Biol. Chem. 286:18130-18138(2011).
RN [11]
RP VARIANT TRP-125.
RX PubMed=16893906; DOI=10.1093/hmg/ddl204;
RA Stone S., Abkevich V., Russell D.L., Riley R., Timms K., Tran T., Trem D.,
RA Frank D., Jammulapati S., Neff C.D., Iliev D., Gress R., He G., Frech G.C.,
RA Adams T.D., Skolnick M.H., Lanchbury J.S., Gutin A., Hunt S.C.,
RA Shattuck D.;
RT "TBC1D1 is a candidate for a severe obesity gene and evidence for a
RT gene/gene interaction in obesity predisposition.";
RL Hum. Mol. Genet. 15:2709-2720(2006).
RN [12]
RP VARIANT TRP-125.
RX PubMed=18325908; DOI=10.1093/hmg/ddn070;
RA Meyre D., Farge M., Lecoeur C., Proenca C., Durand E., Allegaert F.,
RA Tichet J., Marre M., Balkau B., Weill J., Delplanque J., Froguel P.;
RT "R125W coding variant in TBC1D1 confers risk for familial obesity and
RT contributes to linkage on chromosome 4p14 in the French population.";
RL Hum. Mol. Genet. 17:1798-1802(2008).
CC -!- FUNCTION: May act as a GTPase-activating protein for Rab family
CC protein(s). May play a role in the cell cycle and differentiation of
CC various tissues. Involved in the trafficking and translocation of
CC GLUT4-containing vesicles and insulin-stimulated glucose uptake into
CC cells (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with APPL2 (via BAR domain); interaction is
CC dependent of TBC1D1 phosphorylation at Ser-235; interaction diminishes
CC the phosphorylation of TBC1D1 at Thr-596, resulting in inhibition of
CC SLC2A4/GLUT4 translocation and glucose uptake.
CC {ECO:0000269|PubMed:24879834}.
CC -!- INTERACTION:
CC Q86TI0; Q8NEU8: APPL2; NbExp=4; IntAct=EBI-1644036, EBI-741261;
CC Q86TI0; Q8N715: CCDC185; NbExp=3; IntAct=EBI-1644036, EBI-740814;
CC Q86TI0; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-1644036, EBI-5453285;
CC Q86TI0; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-1644036, EBI-2349927;
CC Q86TI0; Q3B820: FAM161A; NbExp=3; IntAct=EBI-1644036, EBI-719941;
CC Q86TI0; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-1644036, EBI-742802;
CC Q86TI0; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-1644036, EBI-2548508;
CC Q86TI0; P31273: HOXC8; NbExp=3; IntAct=EBI-1644036, EBI-1752118;
CC Q86TI0; O75031: HSF2BP; NbExp=3; IntAct=EBI-1644036, EBI-7116203;
CC Q86TI0; O95678: KRT75; NbExp=3; IntAct=EBI-1644036, EBI-2949715;
CC Q86TI0; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-1644036, EBI-11985629;
CC Q86TI0; Q68G74: LHX8; NbExp=3; IntAct=EBI-1644036, EBI-8474075;
CC Q86TI0; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-1644036, EBI-739832;
CC Q86TI0; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-1644036, EBI-1216080;
CC Q86TI0; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-1644036, EBI-348259;
CC Q86TI0; Q96T60: PNKP; NbExp=3; IntAct=EBI-1644036, EBI-1045072;
CC Q86TI0; Q13671: RIN1; NbExp=3; IntAct=EBI-1644036, EBI-366017;
CC Q86TI0; Q96C24: SYTL4; NbExp=3; IntAct=EBI-1644036, EBI-747142;
CC Q86TI0; Q15560: TCEA2; NbExp=3; IntAct=EBI-1644036, EBI-710310;
CC Q86TI0; P02585: TNNC2; NbExp=3; IntAct=EBI-1644036, EBI-10249681;
CC Q86TI0; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-1644036, EBI-10241197;
CC Q86TI0; P40222: TXLNA; NbExp=3; IntAct=EBI-1644036, EBI-359793;
CC Q86TI0; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-1644036, EBI-2799833;
CC Q86TI0; Q6P2D0: ZFP1; NbExp=3; IntAct=EBI-1644036, EBI-2555749;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86TI0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86TI0-2; Sequence=VSP_044749, VSP_044750;
CC -!- PTM: Insulin-stimulated phosphorylation by AKT family kinases
CC stimulates SLC2A4/GLUT4 translocation. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55057.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK027355; BAB55057.1; ALT_INIT; mRNA.
DR EMBL; AK295746; BAH12175.1; -; mRNA.
DR EMBL; AC021106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC098680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050321; AAH50321.3; -; mRNA.
DR EMBL; AB029031; BAA83060.1; -; mRNA.
DR CCDS; CCDS33972.1; -. [Q86TI0-1]
DR CCDS; CCDS58897.1; -. [Q86TI0-2]
DR RefSeq; NP_001240841.1; NM_001253912.1. [Q86TI0-2]
DR RefSeq; NP_055988.2; NM_015173.3. [Q86TI0-1]
DR PDB; 3QYE; X-ray; 2.20 A; A/B=746-1072.
DR PDBsum; 3QYE; -.
DR AlphaFoldDB; Q86TI0; -.
DR SMR; Q86TI0; -.
DR BioGRID; 116823; 62.
DR IntAct; Q86TI0; 37.
DR MINT; Q86TI0; -.
DR STRING; 9606.ENSP00000261439; -.
DR TCDB; 8.A.87.1.4; the tbc1 domain (tbc1) family.
DR iPTMnet; Q86TI0; -.
DR PhosphoSitePlus; Q86TI0; -.
DR BioMuta; TBC1D1; -.
DR DMDM; 116242816; -.
DR EPD; Q86TI0; -.
DR jPOST; Q86TI0; -.
DR MassIVE; Q86TI0; -.
DR MaxQB; Q86TI0; -.
DR PaxDb; Q86TI0; -.
DR PeptideAtlas; Q86TI0; -.
DR PRIDE; Q86TI0; -.
DR ProteomicsDB; 20323; -.
DR ProteomicsDB; 69696; -. [Q86TI0-1]
DR Antibodypedia; 10398; 222 antibodies from 34 providers.
DR DNASU; 23216; -.
DR Ensembl; ENST00000261439.9; ENSP00000261439.4; ENSG00000065882.17. [Q86TI0-1]
DR Ensembl; ENST00000508802.5; ENSP00000423651.1; ENSG00000065882.17. [Q86TI0-2]
DR GeneID; 23216; -.
DR KEGG; hsa:23216; -.
DR UCSC; uc003gtb.4; human. [Q86TI0-1]
DR CTD; 23216; -.
DR DisGeNET; 23216; -.
DR GeneCards; TBC1D1; -.
DR HGNC; HGNC:11578; TBC1D1.
DR HPA; ENSG00000065882; Low tissue specificity.
DR MIM; 609850; gene.
DR neXtProt; NX_Q86TI0; -.
DR OpenTargets; ENSG00000065882; -.
DR PharmGKB; PA36342; -.
DR VEuPathDB; HostDB:ENSG00000065882; -.
DR eggNOG; KOG4436; Eukaryota.
DR GeneTree; ENSGT00940000157949; -.
DR InParanoid; Q86TI0; -.
DR OMA; CERIEXK; -.
DR OrthoDB; 323342at2759; -.
DR PhylomeDB; Q86TI0; -.
DR TreeFam; TF317184; -.
DR PathwayCommons; Q86TI0; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR SignaLink; Q86TI0; -.
DR SIGNOR; Q86TI0; -.
DR BioGRID-ORCS; 23216; 15 hits in 1085 CRISPR screens.
DR ChiTaRS; TBC1D1; human.
DR GeneWiki; TBC1D1; -.
DR GenomeRNAi; 23216; -.
DR Pharos; Q86TI0; Tbio.
DR PRO; PR:Q86TI0; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q86TI0; protein.
DR Bgee; ENSG00000065882; Expressed in ventricular zone and 195 other tissues.
DR ExpressionAtlas; Q86TI0; baseline and differential.
DR Genevisible; Q86TI0; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR021785; DUF3350.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR Pfam; PF11830; DUF3350; 1.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00462; PTB; 2.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; GTPase activation; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1168
FT /note="TBC1 domain family member 1"
FT /id="PRO_0000208022"
FT DOMAIN 246..404
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 800..994
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 203..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 235
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000269|PubMed:24879834"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 505
FT /note="Phosphothreonine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 596
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24879834"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 627
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 941
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 952
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 1131
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT VAR_SEQ 637
FT /note="K -> NVDPSPVGESKHRPGQSSAPAPPPRLNPSASSPNFFKYLKHNSSGEQ
FT SGNAVPKSISYRNALRKKLHSSSSVPNFLKFLAPVDENNTSDFMNTKR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044749"
FT VAR_SEQ 934..1036
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044750"
FT VARIANT 14
FT /note="S -> P (in dbSNP:rs2279027)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_028089"
FT VARIANT 55
FT /note="T -> I (in dbSNP:rs4008480)"
FT /id="VAR_028090"
FT VARIANT 125
FT /note="R -> W (may be associated with risk of familial
FT obesity; dbSNP:rs35859249)"
FT /evidence="ECO:0000269|PubMed:16893906,
FT ECO:0000269|PubMed:18325908"
FT /id="VAR_054392"
FT VARIANT 228
FT /note="V -> G (in dbSNP:rs10501)"
FT /id="VAR_028091"
FT VARIANT 685
FT /note="Y -> S (in dbSNP:rs7677030)"
FT /id="VAR_028092"
FT VARIANT 1136
FT /note="R -> Q (in dbSNP:rs13110318)"
FT /id="VAR_028093"
FT MUTAGEN 930
FT /note="M->A: Substantially reduced RabGAP GTPase hydrolysis
FT activity."
FT /evidence="ECO:0000269|PubMed:21454505"
FT MUTAGEN 1019
FT /note="L->A: Substantially reduced RabGAP GTPase hydrolysis
FT activity."
FT /evidence="ECO:0000269|PubMed:21454505"
FT CONFLICT 730
FT /note="Q -> K (in Ref. 3; AAH50321)"
FT /evidence="ECO:0000305"
FT CONFLICT 1095
FT /note="L -> H (in Ref. 1; BAH12175)"
FT /evidence="ECO:0000305"
FT HELIX 751..757
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 768..778
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 783..785
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 790..798
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 803..805
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 806..820
FT /evidence="ECO:0007829|PDB:3QYE"
FT STRAND 825..827
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 834..837
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 845..852
FT /evidence="ECO:0007829|PDB:3QYE"
FT TURN 860..862
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 868..883
FT /evidence="ECO:0007829|PDB:3QYE"
FT TURN 885..887
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 893..901
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 906..917
FT /evidence="ECO:0007829|PDB:3QYE"
FT TURN 918..920
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 922..926
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 931..947
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 949..957
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 962..964
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 967..971
FT /evidence="ECO:0007829|PDB:3QYE"
FT TURN 973..977
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 980..993
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 997..1008
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 1010..1014
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 1019..1028
FT /evidence="ECO:0007829|PDB:3QYE"
FT TURN 1029..1031
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 1035..1047
FT /evidence="ECO:0007829|PDB:3QYE"
FT HELIX 1051..1065
FT /evidence="ECO:0007829|PDB:3QYE"
SQ SEQUENCE 1168 AA; 133084 MW; 5EFEA168F04C88E0 CRC64;
MEPITFTARK HLLSNEVSVD FGLQLVGSLP VHSLTTMPML PWVVAEVRRL SRQSTRKEPV
TKQVRLCVSP SGLRCEPEPG RSQQWDPLIY SSIFECKPQR VHKLIHNSHD PSYFACLIKE
DAVHRQSICY VFKADDQTKV PEIISSIRQA GKIARQEELH CPSEFDDTFS KKFEVLFCGR
VTVAHKKAPP ALIDECIEKF NHVSGSRGSE SPRPNPPHAA PTGSQEPVRR PMRKSFSQPG
LRSLAFRKEL QDGGLRSSGF FSSFEESDIE NHLISGHNIV QPTDIEENRT MLFTIGQSEV
YLISPDTKKI ALEKNFKEIS FCSQGIRHVD HFGFICRESS GGGGFHFVCY VFQCTNEALV
DEIMMTLKQA FTVAAVQQTA KAPAQLCEGC PLQSLHKLCE RIEGMNSSKT KLELQKHLTT
LTNQEQATIF EEVQKLRPRN EQRENELIIS FLRCLYEEKQ KEHIHIGEMK QTSQMAAENI
GSELPPSATR FRLDMLKNKA KRSLTESLES ILSRGNKARG LQEHSISVDL DSSLSSTLSN
TSKEPSVCEK EALPISESSF KLLGSSEDLS SDSESHLPEE PAPLSPQQAF RRRANTLSHF
PIECQEPPQP ARGSPGVSQR KLMRYHSVST ETPHERKDFE SKANHLGDSG GTPVKTRRHS
WRQQIFLRVA TPQKACDSSS RYEDYSELGE LPPRSPLEPV CEDGPFGPPP EEKKRTSREL
RELWQKAILQ QILLLRMEKE NQKLQASEND LLNKRLKLDY EEITPCLKEV TTVWEKMLST
PGRSKIKFDM EKMHSAVGQG VPRHHRGEIW KFLAEQFHLK HQFPSKQQPK DVPYKELLKQ
LTSQQHAILI DLGRTFPTHP YFSAQLGAGQ LSLYNILKAY SLLDQEVGYC QGLSFVAGIL
LLHMSEEEAF KMLKFLMFDM GLRKQYRPDM IILQIQMYQL SRLLHDYHRD LYNHLEEHEI
GPSLYAAPWF LTMFASQFPL GFVARVFDMI FLQGTEVIFK VALSLLGSHK PLILQHENLE
TIVDFIKSTL PNLGLVQMEK TINQVFEMDI AKQLQAYEVE YHVLQEELID SSPLSDNQRM
DKLEKTNSSL RKQNLDLLEQ LQVANGRIQS LEATIEKLLS SESKLKQAML TLELERSALL
QTVEELRRRS AEPSDREPEC TQPEPTGD
