TBC23_HUMAN
ID TBC23_HUMAN Reviewed; 699 AA.
AC Q9NUY8; B9A6M5; Q8TCN8; Q8WUB7; Q96D90; Q9NV75;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=TBC1 domain family member 23;
DE AltName: Full=HCV non-structural protein 4A-transactivated protein 1;
GN Name=TBC1D23; Synonyms=NS4ATP1;
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] (ISOFORM 2).
RC TISSUE=Placenta;
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] OF 3-684 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 353-684 (ISOFORM 2).
RC TISSUE=Colon, and Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 307-684 (ISOFORM 1).
RC TISSUE=Lymph node;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 365-684 (ISOFORM 1).
RA Liu Y., Cheng J., Ji D., Yan F., Gao X., Zhang L., Chen J.;
RT "Homo sapiens gene 1 transactivated by nonstructural protein 4A of
RT hepatitis C virus (NS4ATP1) mRNA.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474 AND THR-514, AND
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507 AND THR-514, 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 [9]
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 [10]
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 [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-300; SER-474; SER-507 AND
RP SER-520, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571, AND IDENTIFICATION BY
RP 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 [14]
RP INVOLVEMENT IN PCH11, AND FUNCTION.
RX PubMed=28823707; DOI=10.1016/j.ajhg.2017.07.010;
RA Ivanova E.L., Mau-Them F.T., Riazuddin S., Kahrizi K., Laugel V.,
RA Schaefer E., de Saint Martin A., Runge K., Iqbal Z., Spitz M.A., Laura M.,
RA Drouot N., Gerard B., Deleuze J.F., de Brouwer A.P.M., Razzaq A.,
RA Dollfus H., Assir M.Z., Nitchke P., Hinckelmann M.V., Ropers H.,
RA Riazuddin S., Najmabadi H., van Bokhoven H., Chelly J.;
RT "Homozygous truncating variants in TBC1D23 cause pontocerebellar hypoplasia
RT and alter cortical development.";
RL Am. J. Hum. Genet. 101:428-440(2017).
RN [15]
RP INVOLVEMENT IN PCH11, VARIANT PCH11 GLN-518, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=28823706; DOI=10.1016/j.ajhg.2017.07.015;
RA Marin-Valencia I., Gerondopoulos A., Zaki M.S., Ben-Omran T.,
RA Almureikhi M., Demir E., Guemez-Gamboa A., Gregor A., Issa M.Y.,
RA Appelhof B., Roosing S., Musaev D., Rosti B., Wirth S., Stanley V.,
RA Baas F., Barr F.A., Gleeson J.G.;
RT "Homozygous mutations in TBC1D23 lead to a non-degenerative form of
RT pontocerebellar hypoplasia.";
RL Am. J. Hum. Genet. 101:441-450(2017).
RN [16]
RP FUNCTION, INTERACTION WITH C17ORF75; FAM91A1; FKBP15; GOLGA1; GOLGA4;
RP WASHC1; WASHC2A AND WDR11, AND SUBCELLULAR LOCATION.
RX PubMed=29084197; DOI=10.1038/ncb3627;
RA Shin J.J.H., Gillingham A.K., Begum F., Chadwick J., Munro S.;
RT "TBC1D23 is a bridging factor for endosomal vesicle capture by golgins at
RT the trans-Golgi.";
RL Nat. Cell Biol. 19:1424-1432(2017).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE COMPLEX WDR11.
RX PubMed=29426865; DOI=10.1038/s41467-018-02919-4;
RA Navarro Negredo P., Edgar J.R., Manna P.T., Antrobus R., Robinson M.S.;
RT "The WDR11 complex facilitates the tethering of AP-1-derived vesicles.";
RL Nat. Commun. 9:596-596(2018).
CC -!- FUNCTION: Putative Rab GTPase-activating protein which plays a role in
CC vesicular trafficking (PubMed:28823707). Involved in endosome-to-Golgi
CC trafficking. Acts as a bridging protein by binding simultaneously to
CC golgins, including GOLGA1 and GOLGA4, located at the trans-Golgi, and
CC to the WASH complex, located on endosome-derived vesicles
CC (PubMed:29084197, PubMed:29426865). Together with WDR11 complex
CC facilitates the golgin-mediated capture of vesicles generated using AP-
CC 1 (PubMed:29426865). Plays a role in brain development, including in
CC cortical neuron positioning (By similarity). May also be important for
CC neurite outgrowth, possibly through its involvement in membrane
CC trafficking and cargo delivery, 2 processes that are essential for
CC axonal and dendritic growth (By similarity). May act as a general
CC inhibitor of innate immunity signaling, strongly inhibiting multiple
CC TLR and dectin/CLEC7A-signaling pathways. Does not alter initial
CC activation events, but instead affects maintenance of inflammatory gene
CC expression several hours after bacterial lipopolysaccharide (LPS)
CC challenge (By similarity). {ECO:0000250|UniProtKB:Q8K0F1,
CC ECO:0000269|PubMed:28823707, ECO:0000269|PubMed:29084197,
CC ECO:0000269|PubMed:29426865}.
CC -!- SUBUNIT: Directly interacts with GOLGA1 and GOLGA4 (PubMed:29084197).
CC Interacts with FAM91A1, C17ORF75 and WDR11; the interaction recruits
CC TBC1D23 to AP-1-derived vesicles (PubMed:29084197, PubMed:29426865).
CC Directly interacts with WASHC1 and WASHC2A/FAM21A (PubMed:29084197).
CC Interacts with FKBP15 (PubMed:29084197). {ECO:0000269|PubMed:29084197,
CC ECO:0000269|PubMed:29426865}.
CC -!- INTERACTION:
CC Q9NUY8; Q8TC20: CAGE1; NbExp=3; IntAct=EBI-2853126, EBI-10196469;
CC Q9NUY8; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-2853126, EBI-745689;
CC Q9NUY8; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-2853126, EBI-10171774;
CC Q9NUY8; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-2853126, EBI-10172052;
CC Q9NUY8; Q9BQ66: KRTAP4-12; NbExp=3; IntAct=EBI-2853126, EBI-739863;
CC Q9NUY8; Q9BWW4: SSBP3; NbExp=3; IntAct=EBI-2853126, EBI-2902395;
CC Q9NUY8; O43379: WDR62; NbExp=3; IntAct=EBI-2853126, EBI-714790;
CC Q9NUY8-2; Q8TC20: CAGE1; NbExp=3; IntAct=EBI-10314276, EBI-10196469;
CC Q9NUY8-2; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-10314276, EBI-10172052;
CC Q9NUY8-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-10314276, EBI-5235340;
CC Q9NUY8-2; Q9BWW4: SSBP3; NbExp=3; IntAct=EBI-10314276, EBI-2902395;
CC Q9NUY8-2; O43379: WDR62; NbExp=3; IntAct=EBI-10314276, EBI-714790;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:28823706, ECO:0000269|PubMed:29084197,
CC ECO:0000269|PubMed:29426865}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:29426865}. Note=Localization to the trans-Golgi is
CC regulated by ARL1 and ARL5B/ARL8. ARL1 increases Golgi localization,
CC while ARL5B decreases it. Recruitment to the trans-Golgi network
CC requires the presence of GOLGA1 and GOLGA4, but not that of FAM91A1
CC (PubMed:29084197, PubMed:28823706). Recruited on AP-1-derived vesicles
CC by WDR11 complex (PubMed:29426865). {ECO:0000269|PubMed:28823706,
CC ECO:0000269|PubMed:29084197, ECO:0000269|PubMed:29426865}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NUY8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NUY8-2; Sequence=VSP_025519;
CC -!- TISSUE SPECIFICITY: Isoform 1: Widely expressed, including in fetal
CC adult brain (corpus callosum, pons, cerebellum), spinal cord, heart,
CC skeletal muscle, thymus and bone marrow, and at lower levels in spleen.
CC Hardly detected in liver, kidney, colon and testis. Isoform 2:
CC Expressed at high levels in liver, kidney, colon and testis. Hardly
CC detected in tissues expressing high levels of isoform 1. Expressed at
CC low levels in spleen. {ECO:0000269|PubMed:28823706}.
CC -!- DISEASE: Pontocerebellar hypoplasia 11 (PCH11) [MIM:617695]: A non-
CC degenerative form of pontocerebellar hypoplasia, a disorder
CC characterized by structural defects of the pons and cerebellum, evident
CC upon brain imaging. PCH11 features include severely delayed psychomotor
CC development with intellectual disability and poor speech, microcephaly,
CC dysmorphic features, and pontocerebellar hypoplasia. PCH11 inheritance
CC is autosomal recessive. {ECO:0000269|PubMed:28823706,
CC ECO:0000269|PubMed:28823707}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10221.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH20955.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91881.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB449910; BAH16653.1; -; mRNA.
DR EMBL; AK001750; BAA91881.1; ALT_INIT; mRNA.
DR EMBL; AK001908; BAA91973.1; -; mRNA.
DR EMBL; AC078783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010221; AAH10221.1; ALT_INIT; mRNA.
DR EMBL; BC020955; AAH20955.1; ALT_INIT; mRNA.
DR EMBL; AL713684; CAD28488.1; -; mRNA.
DR EMBL; AY740521; AAW66944.1; -; mRNA.
DR CCDS; CCDS2936.1; -. [Q9NUY8-2]
DR CCDS; CCDS56265.1; -. [Q9NUY8-1]
DR RefSeq; NP_001186127.1; NM_001199198.2. [Q9NUY8-1]
DR RefSeq; NP_060779.2; NM_018309.4. [Q9NUY8-2]
DR PDB; 6JL7; X-ray; 2.50 A; A=17-460.
DR PDB; 6JM5; X-ray; 1.60 A; A/B=577-699.
DR PDBsum; 6JL7; -.
DR PDBsum; 6JM5; -.
DR AlphaFoldDB; Q9NUY8; -.
DR SMR; Q9NUY8; -.
DR BioGRID; 120889; 43.
DR IntAct; Q9NUY8; 20.
DR MINT; Q9NUY8; -.
DR STRING; 9606.ENSP00000377700; -.
DR iPTMnet; Q9NUY8; -.
DR PhosphoSitePlus; Q9NUY8; -.
DR BioMuta; TBC1D23; -.
DR DMDM; 300669675; -.
DR EPD; Q9NUY8; -.
DR jPOST; Q9NUY8; -.
DR MassIVE; Q9NUY8; -.
DR MaxQB; Q9NUY8; -.
DR PaxDb; Q9NUY8; -.
DR PeptideAtlas; Q9NUY8; -.
DR PRIDE; Q9NUY8; -.
DR ProteomicsDB; 82728; -. [Q9NUY8-1]
DR ProteomicsDB; 82729; -. [Q9NUY8-2]
DR Antibodypedia; 46507; 72 antibodies from 22 providers.
DR DNASU; 55773; -.
DR Ensembl; ENST00000344949.9; ENSP00000340693.5; ENSG00000036054.13. [Q9NUY8-2]
DR Ensembl; ENST00000394144.9; ENSP00000377700.4; ENSG00000036054.13. [Q9NUY8-1]
DR GeneID; 55773; -.
DR KEGG; hsa:55773; -.
DR MANE-Select; ENST00000394144.9; ENSP00000377700.4; NM_001199198.3; NP_001186127.1.
DR UCSC; uc003dts.5; human. [Q9NUY8-1]
DR CTD; 55773; -.
DR DisGeNET; 55773; -.
DR GeneCards; TBC1D23; -.
DR HGNC; HGNC:25622; TBC1D23.
DR HPA; ENSG00000036054; Low tissue specificity.
DR MalaCards; TBC1D23; -.
DR MIM; 617687; gene.
DR MIM; 617695; phenotype.
DR neXtProt; NX_Q9NUY8; -.
DR OpenTargets; ENSG00000036054; -.
DR PharmGKB; PA142670829; -.
DR VEuPathDB; HostDB:ENSG00000036054; -.
DR eggNOG; KOG3636; Eukaryota.
DR GeneTree; ENSGT00390000000191; -.
DR HOGENOM; CLU_026555_0_0_1; -.
DR InParanoid; Q9NUY8; -.
DR OMA; YNAGHLP; -.
DR OrthoDB; 429640at2759; -.
DR PhylomeDB; Q9NUY8; -.
DR TreeFam; TF105892; -.
DR PathwayCommons; Q9NUY8; -.
DR SignaLink; Q9NUY8; -.
DR BioGRID-ORCS; 55773; 17 hits in 1078 CRISPR screens.
DR ChiTaRS; TBC1D23; human.
DR GenomeRNAi; 55773; -.
DR Pharos; Q9NUY8; Tbio.
DR PRO; PR:Q9NUY8; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NUY8; protein.
DR Bgee; ENSG00000036054; Expressed in cardiac muscle of right atrium and 188 other tissues.
DR ExpressionAtlas; Q9NUY8; baseline and differential.
DR Genevisible; Q9NUY8; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:1990403; P:embryonic brain development; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR GO; GO:0099041; P:vesicle tethering to Golgi; IDA:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR039755; TBC1D23.
DR InterPro; IPR045799; TBC1D23_C.
DR PANTHER; PTHR13297; PTHR13297; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF19430; TBC1D23_C; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasmic vesicle;
KW Developmental protein; Disease variant; Golgi apparatus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..699
FT /note="TBC1 domain family member 23"
FT /id="PRO_0000287497"
FT DOMAIN 44..225
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT DOMAIN 334..446
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 459..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..699
FT /note="May mediate the interaction with WASHC1"
FT /evidence="ECO:0000250|UniProtKB:Q8K0F1"
FT REGION 514..573
FT /note="May mediate the interaction with C17orf75, FAM91A1
FT and WDR11"
FT /evidence="ECO:0000250|UniProtKB:Q8K0F1"
FT REGION 574..699
FT /note="May mediate the interaction with FKBP15 and WASHC2;
FT required for endosome to Golgi trafficking"
FT /evidence="ECO:0000250|UniProtKB:Q8K0F1"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K0F1"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 514
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 518..532
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:19077034"
FT /id="VSP_025519"
FT VARIANT 518
FT /note="R -> Q (in PCH11; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28823706"
FT /id="VAR_080040"
FT CONFLICT 66
FT /note="S -> C (in Ref. 1; BAH16653 and 2; BAA91973)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="L -> P (in Ref. 1; BAH16653 and 2; BAA91973)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="L -> S (in Ref. 2; BAA91973)"
FT /evidence="ECO:0000305"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 33..40
FT /evidence="ECO:0007829|PDB:6JL7"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 79..93
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 100..117
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 142..155
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:6JL7"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 193..203
FT /evidence="ECO:0007829|PDB:6JL7"
FT TURN 204..208
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 211..224
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 229..240
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 272..284
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:6JL7"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:6JL7"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:6JL7"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:6JL7"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:6JL7"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 346..351
FT /evidence="ECO:0007829|PDB:6JL7"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 369..389
FT /evidence="ECO:0007829|PDB:6JL7"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:6JL7"
FT TURN 406..410
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 411..421
FT /evidence="ECO:0007829|PDB:6JL7"
FT STRAND 425..430
FT /evidence="ECO:0007829|PDB:6JL7"
FT HELIX 433..444
FT /evidence="ECO:0007829|PDB:6JL7"
FT STRAND 450..454
FT /evidence="ECO:0007829|PDB:6JL7"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:6JL7"
FT STRAND 578..580
FT /evidence="ECO:0007829|PDB:6JM5"
FT HELIX 581..585
FT /evidence="ECO:0007829|PDB:6JM5"
FT STRAND 592..599
FT /evidence="ECO:0007829|PDB:6JM5"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:6JM5"
FT STRAND 605..612
FT /evidence="ECO:0007829|PDB:6JM5"
FT STRAND 614..622
FT /evidence="ECO:0007829|PDB:6JM5"
FT STRAND 629..637
FT /evidence="ECO:0007829|PDB:6JM5"
FT HELIX 638..640
FT /evidence="ECO:0007829|PDB:6JM5"
FT STRAND 641..647
FT /evidence="ECO:0007829|PDB:6JM5"
FT STRAND 650..662
FT /evidence="ECO:0007829|PDB:6JM5"
FT STRAND 665..675
FT /evidence="ECO:0007829|PDB:6JM5"
FT HELIX 679..694
FT /evidence="ECO:0007829|PDB:6JM5"
SQ SEQUENCE 699 AA; 78322 MW; C0AEB80E044B0F98 CRC64;
MAEGEDVPPL PTSSGDGWEK DLEEALEAGG CDLETLRNII QGRPLPADLR AKVWKIALNV
AGKGDSLASW DGILDLPEQN TIHKDCLQFI DQLSVPEEKA AELLLDIESV ITFYCKSRNI
KYSTSLSWIH LLKPLVHLQL PRSDLYNCFY AIMNKYIPRD CSQKGRPFHL FRLLIQYHEP
ELCSYLDTKK ITPDSYALNW LGSLFACYCS TEVTQAIWDG YLQQADPFFI YFLMLIILVN
AKEVILTQES DSKEEVIKFL ENTPSSLNIE DIEDLFSLAQ YYCSKTPASF RKDNHHLFGS
TLLGIKDDDA DLSQALCLAI SVSEILQANQ LQGEGVRFFV VDCRPAEQYN AGHLSTAFHL
DSDLMLQNPS EFAQSVKSLL EAQKQSIESG SIAGGEHLCF MGSGREEEDM YMNMVLAHFL
QKNKEYVSIA SGGFMALQQH LADINVDGPE NGYGHWIAST SGSRSSINSV DGESPNGSSD
RGMKSLVNKM TVALKTKSVN VREKVISFIE NTSTPVDRMS FNLPWPDRSC TERHVSSSDR
VGKPYRGVKP VFSIGDEEEY DTDEIDSSSM SDDDRKEVVN IQTWINKPDV KHHFPCKEVK
ESGHMFPSHL LVTATHMYCL REIVSRKGLA YIQSRQALNS VVKITSKKKH PELITFKYGN
SSASGIEILA IERYLIPNAG DATKAIKQQI MKVLDALES
