TBCK_HUMAN
ID TBCK_HUMAN Reviewed; 893 AA.
AC Q8TEA7; B9A6J1; Q4W5B3; Q4W5E1; Q6NUP4; Q8N7M8; Q8WW57; Q96GV6; Q9P080;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=TBC domain-containing protein kinase-like protein;
GN Name=TBCK {ECO:0000303|PubMed:12471243}; Synonyms=TBCKL; ORFNames=HSPC302;
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 1), AND VARIANT GLU-266.
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] {ECO:0000305, ECO:0000312|EMBL:BAB85045.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 261-893 (ISOFORMS 1/2/3), AND VARIANT GLU-266.
RC TISSUE=Hepatoma {ECO:0000312|EMBL:BAB85045.1}, and
RC Trachea {ECO:0000312|EMBL:BAC05244.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAY40979.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-266.
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAF28980.1}
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 [5] {ECO:0000305, ECO:0000312|EMBL:AAH68496.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 608-893 (ISOFORMS 1/2/3).
RC TISSUE=Lymph {ECO:0000312|EMBL:AAH09208.2},
RC Placenta {ECO:0000312|EMBL:AAH68496.1}, and
RC Prostate {ECO:0000312|EMBL:AAH20853.2};
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] {ECO:0000305, ECO:0000312|EMBL:AAF28980.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 388-893 (ISOFORMS 1/2/3), AND
RP VARIANT GLU-266.
RC TISSUE=Umbilical cord blood;
RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT "Human partial CDS from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000305}
RP NOMENCLATURE.
RX PubMed=12471243; DOI=10.1126/science.1075762;
RA Manning G., Whyte D.B., Martinez R., Hunter T., Sudarsanam S.;
RT "The protein kinase complement of the human genome.";
RL Science 298:1912-1934(2002).
RN [8]
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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23977024; DOI=10.1371/journal.pone.0071349;
RA Liu Y., Yan X., Zhou T.;
RT "TBCK influences cell proliferation, cell size and mTOR signaling
RT pathway.";
RL PLoS ONE 8:E71349-E71349(2013).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24576458; DOI=10.1016/j.jgg.2013.12.006;
RA Wu J., Li Q., Li Y., Lin J., Yang D., Zhu G., Wang L., He D., Lu G.,
RA Zeng C.;
RT "A long type of TBCK is a novel cytoplasmic and mitotic apparatus-
RT associated protein likely suppressing cell proliferation.";
RL J. Genet. Genomics 41:69-72(2014).
RN [11]
RP INVOLVEMENT IN IHPRF3.
RX PubMed=25558065; DOI=10.1016/j.celrep.2014.12.015;
RA Alazami A.M., Patel N., Shamseldin H.E., Anazi S., Al-Dosari M.S.,
RA Alzahrani F., Hijazi H., Alshammari M., Aldahmesh M.A., Salih M.A.,
RA Faqeih E., Alhashem A., Bashiri F.A., Al-Owain M., Kentab A.Y., Sogaty S.,
RA Al Tala S., Temsah M.H., Tulbah M., Aljelaify R.F., Alshahwan S.A.,
RA Seidahmed M.Z., Alhadid A.A., Aldhalaan H., Alqallaf F., Kurdi W.,
RA Alfadhel M., Babay Z., Alsogheer M., Kaya N., Al-Hassnan Z.N.,
RA Abdel-Salam G.M., Al-Sannaa N., Al Mutairi F., El Khashab H.Y., Bohlega S.,
RA Jia X., Nguyen H.C., Hammami R., Adly N., Mohamed J.Y., Abdulwahab F.,
RA Ibrahim N., Naim E.A., Al-Younes B., Meyer B.F., Hashem M., Shaheen R.,
RA Xiong Y., Abouelhoda M., Aldeeri A.A., Monies D.M., Alkuraya F.S.;
RT "Accelerating novel candidate gene discovery in neurogenetic disorders via
RT whole-exome sequencing of prescreened multiplex consanguineous families.";
RL Cell Rep. 10:148-161(2015).
RN [12]
RP INVOLVEMENT IN IHPRF3, AND VARIANT IHPRF3 HIS-511.
RX PubMed=27040692; DOI=10.1016/j.ajhg.2016.01.016;
RG University of Washington Center for Mendelian Genomics;
RA Chong J.X., Caputo V., Phelps I.G., Stella L., Worgan L., Dempsey J.C.,
RA Nguyen A., Leuzzi V., Webster R., Pizzuti A., Marvin C.T., Ishak G.E.,
RA Ardern-Holmes S., Richmond Z., Bamshad M.J., Ortiz-Gonzalez X.R.,
RA Tartaglia M., Chopra M., Doherty D.;
RT "Recessive inactivating mutations in TBCK, encoding a RAB GTPase-activating
RT protein, cause severe infantile syndromic encephalopathy.";
RL Am. J. Hum. Genet. 98:772-781(2016).
RN [13]
RP FUNCTION, INVOLVEMENT IN IHPRF3, AND VARIANT IHPRF3 PRO-551.
RX PubMed=27040691; DOI=10.1016/j.ajhg.2016.03.016;
RA Bhoj E.J., Li D., Harr M., Edvardson S., Elpeleg O., Chisholm E.,
RA Juusola J., Douglas G., Guillen Sacoto M.J., Siquier-Pernet K., Saadi A.,
RA Bole-Feysot C., Nitschke P., Narravula A., Walke M., Horner M.B.,
RA Day-Salvatore D.L., Jayakar P., Vergano S.A., Tarnopolsky M.A., Hegde M.,
RA Colleaux L., Crino P., Hakonarson H.;
RT "Mutations in TBCK, encoding TBC1-domain-containing kinase, lead to a
RT recognizable syndrome of intellectual disability and hypotonia.";
RL Am. J. Hum. Genet. 98:782-788(2016).
RN [14]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-66; MET-151; ASN-265; MET-425; ILE-471;
RP ASN-489; ILE-503; CYS-692 AND VAL-806.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Involved in the modulation of mTOR signaling and expression
CC of mTOR complex components (PubMed:27040691, PubMed:23977024). Involved
CC in the regulation of cell proliferation and growth (PubMed:23977024,
CC PubMed:24576458). Involved in the control of actin-cytoskeleton
CC organization (PubMed:23977024). {ECO:0000269|PubMed:23977024,
CC ECO:0000269|PubMed:24576458, ECO:0000269|PubMed:27040691}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23977024,
CC ECO:0000269|PubMed:24576458}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:24576458}. Midbody {ECO:0000269|PubMed:24576458}.
CC Note=Mainly localized in the cytoplasm during interphase. During
CC metaphase, TBCK accumulates at the mitotic spindle. At the end of
CC mitosis, it is detected at the midbody. {ECO:0000269|PubMed:24576458}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:14702039};
CC IsoId=Q8TEA7-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q8TEA7-2; Sequence=VSP_052275;
CC Name=3 {ECO:0000269|PubMed:15489334};
CC IsoId=Q8TEA7-3; Sequence=VSP_052274;
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255}.
CC -!- DISEASE: Hypotonia, infantile, with psychomotor retardation and
CC characteristic facies 3 (IHPRF3) [MIM:616900]: An autosomal recessive
CC neurodevelopmental disorder characterized by profound developmental
CC disability, intellectual disability and severe hypotonia. Many patients
CC have seizures, and show brain atrophy, dysgenesis of the corpus
CC callosum and white-matter changes on neuroimaging. Non-specific facial
CC dysmorphism is noted in some individuals. {ECO:0000269|PubMed:25558065,
CC ECO:0000269|PubMed:27040691, ECO:0000269|PubMed:27040692}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28980.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC05244.1; Type=Miscellaneous discrepancy; Note=intron retention.; Evidence={ECO:0000305};
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DR EMBL; AB449876; BAH16619.1; -; mRNA.
DR EMBL; AK074305; BAB85045.1; -; mRNA.
DR EMBL; AK098157; BAC05244.1; ALT_SEQ; mRNA.
DR EMBL; AC093680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107381; AAY40979.1; -; Genomic_DNA.
DR EMBL; AC109361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114734; AAY41041.1; -; Genomic_DNA.
DR EMBL; AC125469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX06201.1; -; Genomic_DNA.
DR EMBL; BC009208; AAH09208.2; -; mRNA.
DR EMBL; BC020853; AAH20853.2; -; mRNA.
DR EMBL; BC068496; AAH68496.1; -; mRNA.
DR EMBL; AF161420; AAF28980.1; ALT_FRAME; mRNA.
DR CCDS; CCDS3673.1; -. [Q8TEA7-3]
DR CCDS; CCDS54788.1; -. [Q8TEA7-1]
DR CCDS; CCDS54789.1; -. [Q8TEA7-2]
DR RefSeq; NP_001156907.1; NM_001163435.2. [Q8TEA7-1]
DR RefSeq; NP_001156908.1; NM_001163436.2. [Q8TEA7-1]
DR RefSeq; NP_001156909.1; NM_001163437.2. [Q8TEA7-2]
DR RefSeq; NP_149106.2; NM_033115.4. [Q8TEA7-3]
DR RefSeq; XP_011530719.1; XM_011532417.2. [Q8TEA7-1]
DR RefSeq; XP_016864335.1; XM_017008846.1. [Q8TEA7-1]
DR AlphaFoldDB; Q8TEA7; -.
DR SMR; Q8TEA7; -.
DR BioGRID; 125042; 14.
DR IntAct; Q8TEA7; 74.
DR MINT; Q8TEA7; -.
DR STRING; 9606.ENSP00000273980; -.
DR iPTMnet; Q8TEA7; -.
DR PhosphoSitePlus; Q8TEA7; -.
DR BioMuta; TBCK; -.
DR DMDM; 317373548; -.
DR EPD; Q8TEA7; -.
DR jPOST; Q8TEA7; -.
DR MassIVE; Q8TEA7; -.
DR MaxQB; Q8TEA7; -.
DR PaxDb; Q8TEA7; -.
DR PeptideAtlas; Q8TEA7; -.
DR PRIDE; Q8TEA7; -.
DR ProteomicsDB; 74430; -. [Q8TEA7-1]
DR ProteomicsDB; 74431; -. [Q8TEA7-2]
DR ProteomicsDB; 74432; -. [Q8TEA7-3]
DR Antibodypedia; 26201; 130 antibodies from 21 providers.
DR DNASU; 93627; -.
DR Ensembl; ENST00000273980.10; ENSP00000273980.4; ENSG00000145348.17. [Q8TEA7-1]
DR Ensembl; ENST00000361687.8; ENSP00000355338.4; ENSG00000145348.17. [Q8TEA7-3]
DR Ensembl; ENST00000394706.7; ENSP00000378196.3; ENSG00000145348.17. [Q8TEA7-2]
DR Ensembl; ENST00000394708.7; ENSP00000378198.2; ENSG00000145348.17. [Q8TEA7-1]
DR GeneID; 93627; -.
DR KEGG; hsa:93627; -.
DR MANE-Select; ENST00000394708.7; ENSP00000378198.2; NM_001163435.3; NP_001156907.2.
DR UCSC; uc003hyc.3; human. [Q8TEA7-1]
DR CTD; 93627; -.
DR DisGeNET; 93627; -.
DR GeneCards; TBCK; -.
DR HGNC; HGNC:28261; TBCK.
DR HPA; ENSG00000145348; Low tissue specificity.
DR MalaCards; TBCK; -.
DR MIM; 616899; gene.
DR MIM; 616900; phenotype.
DR neXtProt; NX_Q8TEA7; -.
DR OpenTargets; ENSG00000145348; -.
DR Orphanet; 488632; TBCK-related intellectual disability syndrome.
DR PharmGKB; PA165664603; -.
DR VEuPathDB; HostDB:ENSG00000145348; -.
DR eggNOG; KOG1093; Eukaryota.
DR GeneTree; ENSGT00940000158244; -.
DR HOGENOM; CLU_011160_0_0_1; -.
DR InParanoid; Q8TEA7; -.
DR OMA; HHMTKGG; -.
DR OrthoDB; 472287at2759; -.
DR PhylomeDB; Q8TEA7; -.
DR TreeFam; TF106242; -.
DR PathwayCommons; Q8TEA7; -.
DR SignaLink; Q8TEA7; -.
DR SIGNOR; Q8TEA7; -.
DR BioGRID-ORCS; 93627; 16 hits in 1113 CRISPR screens.
DR ChiTaRS; TBCK; human.
DR GenomeRNAi; 93627; -.
DR Pharos; Q8TEA7; Tbio.
DR PRO; PR:Q8TEA7; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8TEA7; protein.
DR Bgee; ENSG00000145348; Expressed in kidney epithelium and 186 other tissues.
DR ExpressionAtlas; Q8TEA7; baseline and differential.
DR Genevisible; Q8TEA7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; NAS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR GO; GO:0032006; P:regulation of TOR signaling; IMP:UniProtKB.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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 Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR SUPFAM; SSF52821; SSF52821; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Disease variant;
KW Reference proteome.
FT CHAIN 1..893
FT /note="TBC domain-containing protein kinase-like protein"
FT /id="PRO_0000273278"
FT DOMAIN 1..273
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 466..651
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT DOMAIN 790..889
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 710..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 89..152
FT /note="SCSTVLCIAFEVLQGLQYMNKHGIVHRALSPHNILLDRKGHIKLAKFGLYHM
FT TAHGDDVDFPIG -> R (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052274"
FT VAR_SEQ 161..199
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052275"
FT VARIANT 66
FT /note="R -> L (in dbSNP:rs35784409)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041380"
FT VARIANT 151
FT /note="I -> M (in dbSNP:rs35835241)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041381"
FT VARIANT 265
FT /note="D -> N (in dbSNP:rs34770077)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041382"
FT VARIANT 266
FT /note="Q -> E (in dbSNP:rs3775091)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15815621, ECO:0000269|PubMed:19077034,
FT ECO:0000269|Ref.6"
FT /id="VAR_030123"
FT VARIANT 425
FT /note="T -> M (in dbSNP:rs34307452)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041383"
FT VARIANT 471
FT /note="M -> I (in dbSNP:rs34961213)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041384"
FT VARIANT 489
FT /note="K -> N (in dbSNP:rs2305685)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_030124"
FT VARIANT 503
FT /note="R -> I (in a colorectal adenocarcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041385"
FT VARIANT 511
FT /note="R -> H (in IHPRF3; dbSNP:rs869320711)"
FT /evidence="ECO:0000269|PubMed:27040692"
FT /id="VAR_077816"
FT VARIANT 551
FT /note="L -> P (in IHPRF3)"
FT /evidence="ECO:0000269|PubMed:27040691"
FT /id="VAR_077817"
FT VARIANT 692
FT /note="R -> C (in dbSNP:rs35790205)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041386"
FT VARIANT 806
FT /note="I -> V (in a head & Neck squamous cell carcinoma
FT sample; somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041387"
FT CONFLICT 601
FT /note="I -> N (in Ref. 6; AAF28980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 893 AA; 100679 MW; 7B5A11E37A49D03B CRC64;
MFPLKDAEMG AFTFFASALP HDVCGSNGLP LTPNSIKILG RFQILKTITH PRLCQYVDIS
RGKHERLVVV AEHCERSLED LLRERKPVSC STVLCIAFEV LQGLQYMNKH GIVHRALSPH
NILLDRKGHI KLAKFGLYHM TAHGDDVDFP IGYPSYLAPE VIAQGIFKTT DHMPSKKPLP
SGPKSDVWSL GIILFELCVG RKLFQSLDIS ERLKFLLTLD CVDDTLIVLA EEHGCLDIIK
ELPETVIDLL NKCLTFHPSK RPTPDQLMKD KVFSEVSPLY TPFTKPASLF SSSLRCADLT
LPEDISQLCK DINNDYLAER SIEEVYYLWC LAGGDLEKEL VNKEIIRSKP PICTLPNFLF
EDGESFGQGR DRSSLLDDTT VTLSLCQLRN RLKDVGGEAF YPLLEDDQSN LPHSNSNNEL
SAAATLPLII REKDTEYQLN RIILFDRLLK AYPYKKNQIW KEARVDIPPL MRGLTWAALL
GVEGAIHAKY DAIDKDTPIP TDRQIEVDIP RCHQYDELLS SPEGHAKFRR VLKAWVVSHP
DLVYWQGLDS LCAPFLYLNF NNEALAYACM SAFIPKYLYN FFLKDNSHVI QEYLTVFSQM
IAFHDPELSN HLNEIGFIPD LYAIPWFLTM FTHVFPLHKI FHLWDTLLLG NSSFPFCIGV
AILQQLRDRL LANGFNECIL LFSDLPEIDI ERCVRESINL FCWTPKSATY RQHAQPPKPS
SDSSGGRSSA PYFSAECPDP PKTDLSRESI PLNDLKSEVS PRISAEDLID LCELTVTGHF
KTPSKKTKSS KPKLLVVDIR NSEDFIRGHI SGSINIPFSA AFTAEGELTQ GPYTAMLQNF
KGKVIVIVGH VAKHTAEFAA HLVKMKYPRI CILDGGINKI KPTGLLTIPS PQI
