TBCD5_HUMAN
ID TBCD5_HUMAN Reviewed; 795 AA.
AC Q92609; A6NP25; C9JP52;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=TBC1 domain family member 5;
GN Name=TBC1D5; Synonyms=KIAA0210;
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 1).
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [6]
RP IDENTIFICATION BY 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42 AND SER-544, 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 [10]
RP FUNCTION.
RX PubMed=19531583; DOI=10.1242/jcs.048686;
RA Seaman M.N., Harbour M.E., Tattersall D., Read E., Bright N.;
RT "Membrane recruitment of the cargo-selective retromer subcomplex is
RT catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5.";
RL J. Cell Sci. 122:2371-2382(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541 AND SER-544, 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 [12]
RP FUNCTION, INTERACTION WITH VPS29, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ARG-169 AND GLN-204.
RX PubMed=20923837; DOI=10.1242/jcs.071472;
RA Harbour M.E., Breusegem S.Y., Antrobus R., Freeman C., Reid E.,
RA Seaman M.N.;
RT "The cargo-selective retromer complex is a recruiting hub for protein
RT complexes that regulate endosomal tubule dynamics.";
RL J. Cell Sci. 123:3703-3717(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-791, 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-791, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [16]
RP FUNCTION, INTERACTION WITH MAP1LC3A; MAP1LC3B; MAP1LC3C; GABARAP;
RP GABARAPL1; GABARAPL2; VPS35 AND VPS29, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF TRP-59.
RX PubMed=22354992; DOI=10.1128/mcb.06717-11;
RA Popovic D., Akutsu M., Novak I., Harper J.W., Behrends C., Dikic I.;
RT "Rab GTPase-activating proteins in autophagy: regulation of endocytic and
RT autophagy pathways by direct binding to human ATG8 modifiers.";
RL Mol. Cell. Biol. 32:1733-1744(2012).
RN [17]
RP DOMAIN, AND LIR MOTIF.
RX PubMed=23908376; DOI=10.1242/jcs.126128;
RA Birgisdottir A.B., Lamark T., Johansen T.;
RT "The LIR motif - crucial for selective autophagy.";
RL J. Cell Sci. 126:3237-3247(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-44; SER-460; SER-522;
RP SER-541; SER-544; SER-554; SER-570 AND SER-730, AND IDENTIFICATION BY MASS
RP 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 [19]
RP FUNCTION, AND INTERACTION WITH ATG9A; ULK1; ATG13 AND AP2M1.
RX PubMed=24603492; DOI=10.1002/embr.201337995;
RA Popovic D., Dikic I.;
RT "TBC1D5 and the AP2 complex regulate ATG9 trafficking and initiation of
RT autophagy.";
RL EMBO Rep. 15:392-401(2014).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522; SER-539; SER-541 AND
RP SER-544, AND 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).
CC -!- FUNCTION: May act as a GTPase-activating protein (GAP) for Rab family
CC protein(s). May act as a GAP for RAB7A. Can displace RAB7A and retromer
CC CSC subcomplex from the endosomal membrane to the cytosol; at least
CC retromer displacement seems to require its catalytic activity
CC (PubMed:19531583, PubMed:20923837). Required for retrograde transport
CC of cargo proteins from endosomes to the trans-Golgi network (TGN); the
CC function seems to require its catalytic activity. Involved in
CC regulation of autophagy (PubMed:22354992). May act as a molecular
CC switch between endosomal and autophagosomal transport and is involved
CC in reprogramming vesicle trafficking upon autophagy induction. Involved
CC in the trafficking of ATG9A upon activation of autophagy. May regulate
CC the recruitment of ATG9A-AP2-containing vesicles to autophagic
CC membranes (PubMed:24603492). {ECO:0000269|PubMed:19531583,
CC ECO:0000269|PubMed:20923837, ECO:0000269|PubMed:22354992,
CC ECO:0000269|PubMed:24603492, ECO:0000305|PubMed:19531583,
CC ECO:0000305|PubMed:22354992, ECO:0000305|PubMed:24603492}.
CC -!- SUBUNIT: Interacts with MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAP,
CC GABARAPL1, GABARAPL2. Interacts with VPS29 and VPS35; indicative for an
CC association with retromer CSC subcomplex. MAP1LC3A and VPS29 compete
CC for binding to TBC1D5 (PubMed:20923837, PubMed:22354992). Interacts
CC with AP2M1; indicative for an association with the AP2 complex.
CC Interacts with ULK1 and ATG13 (phosphorylated); indicative for an
CC association with the activated ULK1-ATG13-FIP200 complex. Interacts
CC with ATG9A; the interactions seems to be restricted to the AP2-
CC clathrin-associated fraction of ATG9A (PubMed:24603492).
CC {ECO:0000269|PubMed:20923837, ECO:0000269|PubMed:22354992,
CC ECO:0000269|PubMed:24603492, ECO:0000305|PubMed:24603492}.
CC -!- INTERACTION:
CC Q92609; Q96CW1: AP2M1; NbExp=4; IntAct=EBI-742381, EBI-297683;
CC Q92609; P54253: ATXN1; NbExp=2; IntAct=EBI-742381, EBI-930964;
CC Q92609; Q9BZP6: CHIA; NbExp=3; IntAct=EBI-742381, EBI-14357960;
CC Q92609; Q9UJT9: FBXL7; NbExp=3; IntAct=EBI-742381, EBI-914660;
CC Q92609; Q9H0R8: GABARAPL1; NbExp=5; IntAct=EBI-742381, EBI-746969;
CC Q92609; P60520: GABARAPL2; NbExp=5; IntAct=EBI-742381, EBI-720116;
CC Q92609; P42858: HTT; NbExp=3; IntAct=EBI-742381, EBI-466029;
CC Q92609; Q9UBQ0: VPS29; NbExp=4; IntAct=EBI-742381, EBI-718596;
CC Q92609; Q96QK1: VPS35; NbExp=6; IntAct=EBI-742381, EBI-1054634;
CC Q92609; P24278: ZBTB25; NbExp=3; IntAct=EBI-742381, EBI-739899;
CC Q92609; Q9QZ88: Vps29; Xeno; NbExp=5; IntAct=EBI-742381, EBI-8334188;
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:20923837}.
CC Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:22354992}.
CC Note=During starvation induced autophagy is relocalized from endosomal
CC localization to LC3-positive autophagosomes.
CC {ECO:0000269|PubMed:22354992}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92609-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92609-2; Sequence=VSP_045039;
CC -!- DOMAIN: The arginine and glutamine fingers are critical for the GTPase-
CC activating mechanism, they pull out Rab's 'switch 2' glutamine and
CC insert in Rab's active site. {ECO:0000250|UniProtKB:Q96BZ9}.
CC -!- DOMAIN: The LIR (LC3-interacting region) motif mediates the interaction
CC with ATG8 family proteins. LIR 1 is also implicated in interaction with
CC retromer; LIR 2 is only implicated in interaction with ATG8 family
CC proteins. {ECO:0000269|PubMed:22354992, ECO:0000305|PubMed:23908376}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13201.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D86965; BAA13201.2; ALT_INIT; mRNA.
DR EMBL; AK310539; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC090644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC137672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC140076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC144521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC144531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013145; AAH13145.1; -; mRNA.
DR CCDS; CCDS33714.1; -. [Q92609-1]
DR CCDS; CCDS46770.1; -. [Q92609-2]
DR RefSeq; NP_001127853.1; NM_001134381.1. [Q92609-2]
DR RefSeq; NP_055559.1; NM_014744.2. [Q92609-1]
DR RefSeq; XP_006713493.1; XM_006713430.1.
DR RefSeq; XP_011532583.1; XM_011534281.1. [Q92609-2]
DR RefSeq; XP_011532585.1; XM_011534283.2. [Q92609-2]
DR RefSeq; XP_011532586.1; XM_011534284.2. [Q92609-2]
DR RefSeq; XP_016863041.1; XM_017007552.1. [Q92609-2]
DR RefSeq; XP_016863042.1; XM_017007553.1. [Q92609-2]
DR RefSeq; XP_016863043.1; XM_017007554.1. [Q92609-2]
DR RefSeq; XP_016863044.1; XM_017007555.1. [Q92609-2]
DR RefSeq; XP_016863045.1; XM_017007556.1. [Q92609-2]
DR RefSeq; XP_016863046.1; XM_017007557.1. [Q92609-1]
DR PDB; 5GTU; X-ray; 1.50 A; B=132-158.
DR PDBsum; 5GTU; -.
DR AlphaFoldDB; Q92609; -.
DR SMR; Q92609; -.
DR BioGRID; 115123; 60.
DR ELM; Q92609; -.
DR IntAct; Q92609; 38.
DR MINT; Q92609; -.
DR STRING; 9606.ENSP00000402935; -.
DR TCDB; 8.A.87.2.1; the tbc1 domain (tbc1) family.
DR GlyGen; Q92609; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q92609; -.
DR MetOSite; Q92609; -.
DR PhosphoSitePlus; Q92609; -.
DR BioMuta; TBC1D5; -.
DR DMDM; 2495720; -.
DR EPD; Q92609; -.
DR jPOST; Q92609; -.
DR MassIVE; Q92609; -.
DR MaxQB; Q92609; -.
DR PaxDb; Q92609; -.
DR PeptideAtlas; Q92609; -.
DR PRIDE; Q92609; -.
DR ProteomicsDB; 11067; -.
DR ProteomicsDB; 75354; -. [Q92609-1]
DR Antibodypedia; 45185; 49 antibodies from 18 providers.
DR DNASU; 9779; -.
DR Ensembl; ENST00000253692.11; ENSP00000253692.6; ENSG00000131374.14. [Q92609-1]
DR Ensembl; ENST00000429383.8; ENSP00000398127.4; ENSG00000131374.14. [Q92609-1]
DR Ensembl; ENST00000446818.6; ENSP00000402935.2; ENSG00000131374.14. [Q92609-2]
DR GeneID; 9779; -.
DR KEGG; hsa:9779; -.
DR UCSC; uc003cbf.3; human. [Q92609-1]
DR CTD; 9779; -.
DR DisGeNET; 9779; -.
DR GeneCards; TBC1D5; -.
DR HGNC; HGNC:19166; TBC1D5.
DR HPA; ENSG00000131374; Low tissue specificity.
DR MIM; 615740; gene.
DR neXtProt; NX_Q92609; -.
DR OpenTargets; ENSG00000131374; -.
DR PharmGKB; PA38808; -.
DR VEuPathDB; HostDB:ENSG00000131374; -.
DR eggNOG; KOG1091; Eukaryota.
DR GeneTree; ENSGT00940000157121; -.
DR HOGENOM; CLU_020460_1_0_1; -.
DR InParanoid; Q92609; -.
DR OMA; YPPMGDV; -.
DR OrthoDB; 1373244at2759; -.
DR PhylomeDB; Q92609; -.
DR TreeFam; TF105784; -.
DR PathwayCommons; Q92609; -.
DR SignaLink; Q92609; -.
DR BioGRID-ORCS; 9779; 17 hits in 1082 CRISPR screens.
DR ChiTaRS; TBC1D5; human.
DR GenomeRNAi; 9779; -.
DR Pharos; Q92609; Tbio.
DR PRO; PR:Q92609; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q92609; protein.
DR Bgee; ENSG00000131374; Expressed in calcaneal tendon and 195 other tissues.
DR ExpressionAtlas; Q92609; baseline and differential.
DR Genevisible; Q92609; HS.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0030904; C:retromer complex; IDA:MGI.
DR GO; GO:0035612; F:AP-2 adaptor complex binding; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:GO_Central.
DR GO; GO:1905394; F:retromer complex binding; IMP:ParkinsonsUK-UCL.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IDA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IMP:ParkinsonsUK-UCL.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042594; P:response to starvation; 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 3D-structure; Alternative splicing; Autophagy; Cytoplasmic vesicle;
KW Endosome; GTPase activation; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..795
FT /note="TBC1 domain family member 5"
FT /id="PRO_0000208028"
FT DOMAIN 81..359
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..64
FT /note="Required for interaction with retromer; involved in
FT interaction with ATG8 family proteins"
FT /evidence="ECO:0000269|PubMed:22354992"
FT REGION 475..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..791
FT /note="Required for interaction with ATG8 family proteins"
FT /evidence="ECO:0000269|PubMed:22354992"
FT MOTIF 57..62
FT /note="LIR 1"
FT /evidence="ECO:0000305|PubMed:22354992,
FT ECO:0000305|PubMed:23908376"
FT MOTIF 785..789
FT /note="LIR 2"
FT /evidence="ECO:0000305|PubMed:22354992,
FT ECO:0000305|PubMed:23908376"
FT COMPBIAS 22..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 169
FT /note="Arginine finger"
FT /evidence="ECO:0000250|UniProtKB:Q96BZ9"
FT SITE 204
FT /note="Glutamine finger"
FT /evidence="ECO:0000250|UniProtKB:Q96BZ9"
FT MOD_RES 42
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80XQ2"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 791
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT VAR_SEQ 529
FT /note="K -> KGDVVTGSDAQVSVPVQTLTDLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045039"
FT VARIANT 696
FT /note="I -> V (in dbSNP:rs1138454)"
FT /id="VAR_052536"
FT MUTAGEN 59
FT /note="W->A: Disrupts interaction with VPS29."
FT /evidence="ECO:0000269|PubMed:22354992"
FT MUTAGEN 169
FT /note="R->A: Abolishes retromer displacement from endosome
FT membrane; no effect on interaction with VPS29; when
FT associated with A-204."
FT /evidence="ECO:0000269|PubMed:20923837"
FT MUTAGEN 204
FT /note="Q->A: Abolishes retromer displacement from endosome
FT membrane; no effect on interaction with VPS29; when
FT associated with A-169."
FT /evidence="ECO:0000269|PubMed:20923837"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:5GTU"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:5GTU"
SQ SEQUENCE 795 AA; 89004 MW; 598CE3B436835E1D CRC64;
MYHSLSETRH PLQPEEQEVG IDPLSSYSNK SGGDSNKNGR RTSSTLDSEG TFNSYRKEWE
ELFVNNNYLA TIRQKGINGQ LRSSRFRSIC WKLFLCVLPQ DKSQWISRIE ELRAWYSNIK
EIHITNPRKV VGQQDLMINN PLSQDEGSLW NKFFQDKELR SMIEQDVKRT FPEMQFFQQE
NVRKILTDVL FCYARENEQL LYKQGMHELL APIVFVLHCD HQAFLHASES AQPSEEMKTV
LNPEYLEHDA YAVFSQLMET AEPWFSTFEH DGQKGKETLM TPIPFARPQD LGPTIAIVTK
VNQIQDHLLK KHDIELYMHL NRLEIAPQIY GLRWVRLLFG REFPLQDLLV VWDALFADGL
SLGLVDYIFV AMLLYIRDAL ISSNYQTCLG LLMHYPFIGD VHSLILKALF LRDPKRNPRP
VTYQFHPNLD YYKARGADLM NKSRTNAKGA PLNINKVSNS LINFGRKLIS PAMAPGSAGG
PVPGGNSSSS SSVVIPTRTS AEAPSHHLQQ QQQQQRLMKS ESMPVQLNKG LSSKNISSSP
SVESLPGGRE FTGSPPSSAT KKDSFFSNIS RSRSHSKTMG RKESEEELEA QISFLQGQLN
DLDAMCKYCA KVMDTHLVNI QDVILQENLE KEDQILVSLA GLKQIKDILK GSLRFNQSQL
EAEENEQITI ADNHYCSSGQ GQGRGQGQSV QMSGAIKQAS SETPGCTDRG NSDDFILISK
DDDGSSARGS FSGQAQPLRT LRSTSGKSQA PVCSPLVFSD PLMGPASASS SNPSSSPDDD
SSKDSGFTIV SPLDI
