TCF20_HUMAN
ID TCF20_HUMAN Reviewed; 1960 AA.
AC Q9UGU0; A9JX12; O14528; Q13078; Q4V353; Q9H4M0;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Transcription factor 20;
DE Short=TCF-20;
DE AltName: Full=Nuclear factor SPBP;
DE AltName: Full=Protein AR1;
DE AltName: Full=Stromelysin-1 PDGF-responsive element-binding protein;
DE Short=SPRE-binding protein;
GN Name=TCF20; Synonyms=KIAA0292, SPBP;
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 [GENOMIC DNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, CHARACTERIZATION, AND ALTERNATIVE SPLICING.
RX PubMed=10995766; DOI=10.1074/jbc.m006978200;
RA Rekdal C., Sjoettem E., Johansen T.;
RT "The nuclear factor SPBP contains different functional domains and
RT stimulates the activity of various transcriptional activators.";
RL J. Biol. Chem. 275:40288-40300(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 245-1960 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9179496; DOI=10.1093/dnares/4.1.53;
RA Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N.,
RA Nomura N.;
RT "Construction and characterization of human brain cDNA libraries suitable
RT for analysis of cDNA clones encoding relatively large proteins.";
RL DNA Res. 4:53-59(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1083-1938 (ISOFORM 2).
RX PubMed=9730594; DOI=10.1159/000015021;
RA Rajadhyaksha A., Riviere M., Van Vooren P., Szpirer J., Szpirer C.,
RA Babin J., Bina M.;
RT "Assignment of AR1, transcription factor 20 (TCF20), to human chromosome
RT 22q13.3 with somatic cell hybrids and in situ hybridization.";
RL Cytogenet. Cell Genet. 81:176-177(1998).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-574; SER-583;
RP SER-871; SER-1335; SER-1361; SER-1522; SER-1669 AND THR-1671, 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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871; SER-966; SER-1053;
RP SER-1522 AND THR-1671, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1522 AND THR-1671, AND
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-559; SER-574;
RP SER-583; SER-640; SER-871; SER-1005; SER-1305; SER-1522 AND THR-1671, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-60 AND ARG-1024, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-823; LYS-844; LYS-929 AND
RP LYS-1446, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-929, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-710; LYS-844; LYS-929 AND
RP LYS-1446, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-823; LYS-844; LYS-929; LYS-957;
RP LYS-1137 AND LYS-1446, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-304; LYS-710; LYS-733; LYS-748;
RP LYS-823; LYS-832; LYS-844; LYS-920; LYS-922; LYS-929; LYS-957; LYS-1015;
RP LYS-1086; LYS-1098; LYS-1173; LYS-1178; LYS-1183; LYS-1210; LYS-1231;
RP LYS-1267; LYS-1274; LYS-1309; LYS-1338; LYS-1389; LYS-1409; LYS-1428;
RP LYS-1446; LYS-1510; LYS-1524 AND LYS-1613, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [18]
RP INVOLVEMENT IN DDVIBA, VARIANTS DDVIBA GLU-512; LEU-1557; LEU-1937 AND
RP HIS-1942, AND VARIANTS THR-16; GLN-322 DEL; VAL-405; GLY-722 AND ILE-1165.
RX PubMed=25228304; DOI=10.1136/jmedgenet-2014-102582;
RG International Molecular Genetic Study of Autism Consortium (IMGSAC);
RA Babbs C., Lloyd D., Pagnamenta A.T., Twigg S.R., Green J., McGowan S.J.,
RA Mirza G., Naples R., Sharma V.P., Volpi E.V., Buckle V.J., Wall S.A.,
RA Knight S.J., Parr J.R., Wilkie A.O.;
RT "De novo and rare inherited mutations implicate the transcriptional
RT coregulator TCF20/SPBP in autism spectrum disorder.";
RL J. Med. Genet. 51:737-747(2014).
RN [19]
RP INVOLVEMENT IN DDVIBA, AND VARIANT DDVIBA 319-GLN--GLY-1960 DEL.
RX PubMed=27436265; DOI=10.1038/ejhg.2016.90;
RA Schaefgen J., Cremer K., Becker J., Wieland T., Zink A.M., Kim S.,
RA Windheuser I.C., Kreiss M., Aretz S., Strom T.M., Wieczorek D., Engels H.;
RT "De novo nonsense and frameshift variants of TCF20 in individuals with
RT intellectual disability and postnatal overgrowth.";
RL Eur. J. Hum. Genet. 24:1739-1745(2016).
RN [20]
RP VARIANTS DDVIBA 330-GLN--GLY-1960 DEL; 754-GLN--GLY-1960 DEL;
RP 1009-TYR--GLY-1960 DEL; 1269-GLN--GLY-1960 DEL; ARG-1710 AND
RP 1907-ARG--GLY-1960 DEL.
RX PubMed=30819258; DOI=10.1186/s13073-019-0623-0;
RG DDD study;
RA Vetrini F., McKee S., Rosenfeld J.A., Suri M., Lewis A.M., Nugent K.M.,
RA Roeder E., Littlejohn R.O., Holder S., Zhu W., Alaimo J.T., Graham B.,
RA Harris J.M., Gibson J.B., Pastore M., McBride K.L., Komara M.,
RA Al-Gazali L., Al Shamsi A., Fanning E.A., Wierenga K.J., Scott D.A.,
RA Ben-Neriah Z., Meiner V., Cassuto H., Elpeleg O., Holder J.L. Jr.,
RA Burrage L.C., Seaver L.H., Van Maldergem L., Mahida S., Soul J.S.,
RA Marlatt M., Matyakhina L., Vogt J., Gold J.A., Park S.M., Varghese V.,
RA Lampe A.K., Kumar A., Lees M., Holder-Espinasse M., McConnell V.,
RA Bernhard B., Blair E., Harrison V., Muzny D.M., Gibbs R.A., Elsea S.H.,
RA Posey J.E., Bi W., Lalani S., Xia F., Yang Y., Eng C.M., Lupski J.R.,
RA Liu P.;
RT "De novo and inherited TCF20 pathogenic variants are associated with
RT intellectual disability, dysmorphic features, hypotonia, and neurological
RT impairments with similarities to Smith-Magenis syndrome.";
RL Genome Med. 11:12-12(2019).
RN [21]
RP VARIANTS DDVIBA 233-GLN--GLY-1960 DEL; 654-GLN--GLY-1960 DEL;
RP 719-ARG--GLY-1960 DEL; 742-ARG--GLY-1960 DEL; 865-SER--GLY-1960 DEL;
RP 961-TYR--GLY-1960 DEL; 1592-GLN--GLY-1960 DEL; 1596-ARG--GLY-1960 DEL AND
RP TYR-1909.
RX PubMed=30739909; DOI=10.1038/s41436-019-0454-9;
RA Torti E., Keren B., Palmer E.E., Zhu Z., Afenjar A., Anderson I.J.,
RA Andrews M.V., Atkinson C., Au M., Berry S.A., Bowling K.M., Boyle J.,
RA Buratti J., Cathey S.S., Charles P., Cogne B., Courtin T., Escobar L.F.,
RA Finley S.L., Graham J.M. Jr., Grange D.K., Heron D., Hewson S., Hiatt S.M.,
RA Hibbs K.A., Jayakar P., Kalsner L., Larcher L., Lesca G., Mark P.R.,
RA Miller K., Nava C., Nizon M., Pai G.S., Pappas J., Parsons G., Payne K.,
RA Putoux A., Rabin R., Sabatier I., Shinawi M., Shur N., Skinner S.A.,
RA Valence S., Warren H., Whalen S., Crunk A., Douglas G., Monaghan K.G.,
RA Person R.E., Willaert R., Solomon B.D., Juusola J.;
RT "Variants in TCF20 in neurodevelopmental disability: description of 27 new
RT patients and review of literature.";
RL Genet. Med. 21:2036-2042(2019).
CC -!- FUNCTION: Transcriptional activator that binds to the regulatory region
CC of MMP3 and thereby controls stromelysin expression. It stimulates the
CC activity of various transcriptional activators such as JUN, SP1, PAX6
CC and ETS1, suggesting a function as a coactivator.
CC {ECO:0000269|PubMed:10995766}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with RNF4 and JUN (By
CC similarity). {ECO:0000250|UniProtKB:Q9EPQ8, ECO:0000305}.
CC -!- INTERACTION:
CC Q9UGU0; Q92547: TOPBP1; NbExp=8; IntAct=EBI-3444158, EBI-308302;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10995766}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UGU0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UGU0-2; Sequence=VSP_003984, VSP_003985;
CC -!- TISSUE SPECIFICITY: Expressed in most tissues, except in ovary and
CC prostate. Isoform 1 is exclusively expressed in brain, heart and
CC testis, and this form predominates in liver and kidney. Isoform 2
CC predominates in lung. {ECO:0000269|PubMed:10995766}.
CC -!- DOMAIN: The atypical PHD domain functions as a negative modulator of
CC cofactor binding. {ECO:0000250}.
CC -!- DISEASE: Developmental delay with variable intellectual impairment and
CC behavioral abnormalities (DDVIBA) [MIM:618430]: An autosomal dominant
CC disorder characterized by impaired intellectual development with speech
CC difficulties, dysmorphic features, and behavioral abnormalities
CC including autism spectrum disorder, attention deficit and
CC hyperactivity. Additional variable features may include hypotonia,
CC somatic overgrowth, macrocephaly, mild distal skeletal anomalies, sleep
CC disturbances, movement disorders, and gastrointestinal issues, such as
CC constipation. {ECO:0000269|PubMed:25228304,
CC ECO:0000269|PubMed:27436265, ECO:0000269|PubMed:30739909,
CC ECO:0000269|PubMed:30819258}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC36392.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY007595; AAG28930.1; -; Genomic_DNA.
DR EMBL; AL031346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX247885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60495.1; -; Genomic_DNA.
DR EMBL; AB006630; BAA22961.1; -; mRNA.
DR EMBL; U19345; AAC36392.1; ALT_FRAME; mRNA.
DR CCDS; CCDS14032.1; -. [Q9UGU0-2]
DR CCDS; CCDS14033.1; -. [Q9UGU0-1]
DR RefSeq; NP_005641.1; NM_005650.3. [Q9UGU0-1]
DR RefSeq; NP_852469.1; NM_181492.2. [Q9UGU0-2]
DR RefSeq; XP_005261779.1; XM_005261722.3. [Q9UGU0-1]
DR RefSeq; XP_006724376.1; XM_006724313.3.
DR RefSeq; XP_011528656.1; XM_011530354.2.
DR AlphaFoldDB; Q9UGU0; -.
DR SMR; Q9UGU0; -.
DR BioGRID; 112802; 102.
DR IntAct; Q9UGU0; 53.
DR MINT; Q9UGU0; -.
DR STRING; 9606.ENSP00000352463; -.
DR GlyGen; Q9UGU0; 15 sites, 2 O-linked glycans (15 sites).
DR iPTMnet; Q9UGU0; -.
DR PhosphoSitePlus; Q9UGU0; -.
DR BioMuta; TCF20; -.
DR DMDM; 92090378; -.
DR EPD; Q9UGU0; -.
DR jPOST; Q9UGU0; -.
DR MassIVE; Q9UGU0; -.
DR MaxQB; Q9UGU0; -.
DR PaxDb; Q9UGU0; -.
DR PeptideAtlas; Q9UGU0; -.
DR PRIDE; Q9UGU0; -.
DR ProteomicsDB; 84264; -. [Q9UGU0-1]
DR ProteomicsDB; 84265; -. [Q9UGU0-2]
DR Antibodypedia; 57349; 71 antibodies from 15 providers.
DR DNASU; 6942; -.
DR Ensembl; ENST00000335626.8; ENSP00000335561.4; ENSG00000100207.21. [Q9UGU0-2]
DR Ensembl; ENST00000359486.8; ENSP00000352463.3; ENSG00000100207.21. [Q9UGU0-1]
DR Ensembl; ENST00000574943.5; ENSP00000460328.1; ENSG00000262024.6. [Q9UGU0-1]
DR Ensembl; ENST00000576946.5; ENSP00000460587.1; ENSG00000262024.6. [Q9UGU0-2]
DR Ensembl; ENST00000619505.3; ENSP00000478503.2; ENSG00000276461.4. [Q9UGU0-2]
DR Ensembl; ENST00000621408.4; ENSP00000483199.1; ENSG00000276461.4. [Q9UGU0-1]
DR Ensembl; ENST00000626486.2; ENSP00000487465.1; ENSG00000280467.5. [Q9UGU0-2]
DR Ensembl; ENST00000626726.4; ENSP00000487302.1; ENSG00000281897.5. [Q9UGU0-1]
DR Ensembl; ENST00000628774.4; ENSP00000487296.1; ENSG00000280467.5. [Q9UGU0-1]
DR Ensembl; ENST00000629538.2; ENSP00000486940.1; ENSG00000281897.5. [Q9UGU0-2]
DR Ensembl; ENST00000634489.1; ENSP00000489099.1; ENSG00000282892.4. [Q9UGU0-2]
DR Ensembl; ENST00000634616.3; ENSP00000489614.1; ENSG00000283026.4. [Q9UGU0-1]
DR Ensembl; ENST00000635146.3; ENSP00000489215.1; ENSG00000282892.4. [Q9UGU0-1]
DR Ensembl; ENST00000635421.1; ENSP00000489006.1; ENSG00000283026.4. [Q9UGU0-2]
DR Ensembl; ENST00000636799.3; ENSP00000490305.1; ENSG00000283681.4. [Q9UGU0-1]
DR Ensembl; ENST00000637355.1; ENSP00000489734.1; ENSG00000283681.4. [Q9UGU0-2]
DR Ensembl; ENST00000677622.1; ENSP00000503828.1; ENSG00000100207.21. [Q9UGU0-1]
DR Ensembl; ENST00000683686.1; ENSP00000508272.1; ENSG00000100207.21. [Q9UGU0-1]
DR GeneID; 6942; -.
DR KEGG; hsa:6942; -.
DR MANE-Select; ENST00000677622.1; ENSP00000503828.1; NM_001378418.1; NP_001365347.1.
DR UCSC; uc003bck.3; human. [Q9UGU0-1]
DR CTD; 6942; -.
DR DisGeNET; 6942; -.
DR GeneCards; TCF20; -.
DR HGNC; HGNC:11631; TCF20.
DR HPA; ENSG00000100207; Low tissue specificity.
DR MalaCards; TCF20; -.
DR MIM; 603107; gene.
DR MIM; 618430; phenotype.
DR neXtProt; NX_Q9UGU0; -.
DR OpenTargets; ENSG00000100207; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA36386; -.
DR VEuPathDB; HostDB:ENSG00000100207; -.
DR eggNOG; KOG1084; Eukaryota.
DR GeneTree; ENSGT00940000157896; -.
DR HOGENOM; CLU_234705_0_0_1; -.
DR InParanoid; Q9UGU0; -.
DR OMA; LNRQHQM; -.
DR PhylomeDB; Q9UGU0; -.
DR TreeFam; TF331317; -.
DR PathwayCommons; Q9UGU0; -.
DR SignaLink; Q9UGU0; -.
DR SIGNOR; Q9UGU0; -.
DR BioGRID-ORCS; 6942; 11 hits in 1079 CRISPR screens.
DR ChiTaRS; TCF20; human.
DR GeneWiki; TCF20; -.
DR GenomeRNAi; 6942; -.
DR Pharos; Q9UGU0; Tbio.
DR PRO; PR:Q9UGU0; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9UGU0; protein.
DR Bgee; ENSG00000100207; Expressed in cortical plate and 107 other tissues.
DR ExpressionAtlas; Q9UGU0; baseline and differential.
DR Genevisible; Q9UGU0; HS.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ARUK-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; NAS:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd15699; ePHD_TCF20; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR041972; TCF-20_ePHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR SMART; SM00249; PHD; 1.
DR PROSITE; PS51805; EPHD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Disease variant; DNA-binding;
KW Intellectual disability; Isopeptide bond; Metal-binding; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1960
FT /note="Transcription factor 20"
FT /id="PRO_0000072448"
FT DNA_BIND 1537..1551
FT /note="A.T hook"
FT ZN_FING 1829..1865
FT /note="C2HC pre-PHD-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 1885..1933
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 1..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1191
FT /note="Leucine-zipper"
FT REGION 1303..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1384..1607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1660..1683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1732..1839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1939..1960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1254..1268
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 1576..1600
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 1785..1792
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1018
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1553..1570
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1580..1595
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1669..1683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1745..1774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1817..1831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 602
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPQ8"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 966
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1005
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1024
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1053
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1669
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1671
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1762
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPQ8"
FT MOD_RES 1764
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPQ8"
FT CROSSLNK 304
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 710
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 733
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 748
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 823
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 832
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 844
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 920
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 922
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 929
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 929
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 957
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1015
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1086
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1098
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297"
FT CROSSLNK 1173
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1183
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1231
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1267
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1309
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1338
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1389
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1409
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1428
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1446
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1510
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1524
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1613
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1934..1938
FT /note="PPLPC -> VRLWR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9730594"
FT /id="VSP_003984"
FT VAR_SEQ 1939..1960
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9730594"
FT /id="VSP_003985"
FT VARIANT 16
FT /note="S -> T"
FT /evidence="ECO:0000269|PubMed:25228304"
FT /id="VAR_082677"
FT VARIANT 233..1960
FT /note="Missing (in DDVIBA)"
FT /evidence="ECO:0000269|PubMed:30739909"
FT /id="VAR_082678"
FT VARIANT 319..1960
FT /note="Missing (in DDVIBA)"
FT /evidence="ECO:0000269|PubMed:27436265"
FT /id="VAR_082679"
FT VARIANT 322
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:25228304"
FT /id="VAR_082680"
FT VARIANT 330..1960
FT /note="Missing (in DDVIBA)"
FT /evidence="ECO:0000269|PubMed:30819258"
FT /id="VAR_082681"
FT VARIANT 405
FT /note="M -> V (in dbSNP:rs34030679)"
FT /evidence="ECO:0000269|PubMed:25228304"
FT /id="VAR_051419"
FT VARIANT 485
FT /note="T -> N (in dbSNP:rs6002656)"
FT /id="VAR_025427"
FT VARIANT 512
FT /note="K -> E (in DDVIBA; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:25228304"
FT /id="VAR_082682"
FT VARIANT 654..1960
FT /note="Missing (in DDVIBA)"
FT /evidence="ECO:0000269|PubMed:30739909"
FT /id="VAR_082683"
FT VARIANT 719..1960
FT /note="Missing (in DDVIBA)"
FT /evidence="ECO:0000269|PubMed:30739909"
FT /id="VAR_082684"
FT VARIANT 722
FT /note="S -> G (in dbSNP:rs5758651)"
FT /evidence="ECO:0000269|PubMed:25228304"
FT /id="VAR_025428"
FT VARIANT 742..1960
FT /note="Missing (in DDVIBA)"
FT /evidence="ECO:0000269|PubMed:30739909"
FT /id="VAR_082685"
FT VARIANT 754..1960
FT /note="Missing (in DDVIBA)"
FT /evidence="ECO:0000269|PubMed:30819258"
FT /id="VAR_082686"
FT VARIANT 865..1960
FT /note="Missing (in DDVIBA)"
FT /evidence="ECO:0000269|PubMed:30739909"
FT /id="VAR_082687"
FT VARIANT 961..1960
FT /note="Missing (in DDVIBA)"
FT /evidence="ECO:0000269|PubMed:30739909"
FT /id="VAR_082688"
FT VARIANT 1009..1960
FT /note="Missing (in DDVIBA)"
FT /evidence="ECO:0000269|PubMed:30819258"
FT /id="VAR_082689"
FT VARIANT 1165
FT /note="M -> I (in dbSNP:rs17002890)"
FT /evidence="ECO:0000269|PubMed:25228304"
FT /id="VAR_025429"
FT VARIANT 1269..1960
FT /note="Missing (in DDVIBA)"
FT /evidence="ECO:0000269|PubMed:30819258"
FT /id="VAR_082690"
FT VARIANT 1325
FT /note="S -> N (in dbSNP:rs17002888)"
FT /id="VAR_025430"
FT VARIANT 1557
FT /note="P -> L (in DDVIBA; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:25228304"
FT /id="VAR_082691"
FT VARIANT 1592..1960
FT /note="Missing (in DDVIBA)"
FT /evidence="ECO:0000269|PubMed:30739909"
FT /id="VAR_082692"
FT VARIANT 1596..1960
FT /note="Missing (in DDVIBA)"
FT /evidence="ECO:0000269|PubMed:30739909"
FT /id="VAR_082693"
FT VARIANT 1710
FT /note="K -> R (in DDVIBA; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30819258"
FT /id="VAR_082694"
FT VARIANT 1907..1960
FT /note="Missing (in DDVIBA)"
FT /evidence="ECO:0000269|PubMed:30819258"
FT /id="VAR_082695"
FT VARIANT 1909
FT /note="H -> Y (in DDVIBA)"
FT /evidence="ECO:0000269|PubMed:30739909"
FT /id="VAR_082696"
FT VARIANT 1910
FT /note="Y -> C (in dbSNP:rs17002865)"
FT /id="VAR_051420"
FT VARIANT 1937
FT /note="P -> L (in DDVIBA; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:25228304"
FT /id="VAR_082697"
FT VARIANT 1942
FT /note="P -> H (in DDVIBA; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:25228304"
FT /id="VAR_082698"
FT CONFLICT 122
FT /note="Q -> R (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="Q -> K (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1960 AA; 211771 MW; D3E34B1FAA6ED06F CRC64;
MQSFREQSSY HGNQQSYPQE VHGSSRLEEF SPRQAQMFQN FGGTGGSSGS SGSGSGGGRR
GAAAAAAAMA SETSGHQGYQ GFRKEAGDFY YMAGNKDPVT TGTPQPPQRR PSGPVQSYGP
PQGSSFGNQY GSEGHVGQFQ AQHSGLGGVS HYQQDYTGPF SPGSAQYQQQ ASSQQQQQQV
QQLRQQLYQS HQPLPQATGQ PASSSSHLQP MQRPSTLPSS AAGYQLRVGQ FGQHYQSSAS
SSSSSSFPSP QRFSQSGQSY DGSYNVNAGS QYEGHNVGSN AQAYGTQSNY SYQPQSMKNF
EQAKIPQGTQ QGQQQQQPQQ QQHPSQHVMQ YTNAATKLPL QSQVGQYNQP EVPVRSPMQF
HQNFSPISNP SPAASVVQSP SCSSTPSPLM QTGENLQCGQ GSVPMGSRNR ILQLMPQLSP
TPSMMPSPNS HAAGFKGFGL EGVPEKRLTD PGLSSLSALS TQVANLPNTV QHMLLSDALT
PQKKTSKRPS SSKKADSCTN SEGSSQPEEQ LKSPMAESLD GGCSSSSEDQ GERVRQLSGQ
STSSDTTYKG GASEKAGSSP AQGAQNEPPR LNASPAAREE ATSPGAKDMP LSSDGNPKVN
EKTVGVIVSR EAMTGRVEKP GGQDKGSQED DPAATQRPPS NGGAKETSHA SLPQPEPPGG
GGSKGNKNGD NNSNHNGEGN GQSGHSAAGP GFTSRTEPSK SPGSLRYSYK DSFGSAVPRN
VSGFPQYPTG QEKGDFTGHG ERKGRNEKFP SLLQEVLQGY HHHPDRRYSR STQEHQGMAG
SLEGTTRPNV LVSQTNELAS RGLLNKSIGS LLENPHWGPW ERKSSSTAPE MKQINLTDYP
IPRKFEIEPQ SSAHEPGGSL SERRSVICDI SPLRQIVRDP GAHSLGHMSA DTRIGRNDRL
NPTLSQSVIL PGGLVSMETK LKSQSGQIKE EDFEQSKSQA SFNNKKSGDH CHPPSIKHES
YRGNASPGAA THDSLSDYGP QDSRPTPMRR VPGRVGGREG MRGRSPSQYH DFAEKLKMSP
GRSRGPGGDP HHMNPHMTFS ERANRSSLHT PFSPNSETLA SAYHANTRAH AYGDPNAGLN
SQLHYKRQMY QQQPEEYKDW SSGSAQGVIA AAQHRQEGPR KSPRQQQFLD RVRSPLKNDK
DGMMYGPPVG TYHDPSAQEA GRCLMSSDGL PNKGMELKHG SQKLQESCWD LSRQTSPAKS
SGPPGMSSQK RYGPPHETDG HGLAEATQSS KPGSVMLRLP GQEDHSSQNP LIMRRRVRSF
ISPIPSKRQS QDVKNSSTED KGRLLHSSKE GADKAFNSYA HLSHSQDIKS IPKRDSSKDL
PSPDSRNCPA VTLTSPAKTK ILPPRKGRGL KLEAIVQKIT SPNIRRSASS NSAEAGGDTV
TLDDILSLKS GPPEGGSVAV QDADIEKRKG EVASDLVSPA NQELHVEKPL PRSSEEWRGS
VDDKVKTETH AETVTAGKEP PGAMTSTTSQ KPGSNQGRPD GSLGGTAPLI FPDSKNVPPV
GILAPEANPK AEEKENDTVT ISPKQEGFPP KGYFPSGKKK GRPIGSVNKQ KKQQQPPPPP
PQPPQIPEGS ADGEPKPKKQ RQRRERRKPG AQPRKRKTKQ AVPIVEPQEP EIKLKYATQP
LDKTDAKNKS FYPYIHVVNK CELGAVCTII NAEEEEQTKL VRGRKGQRSL TPPPSSTESK
ALPASSFMLQ GPVVTESSVM GHLVCCLCGK WASYRNMGDL FGPFYPQDYA ATLPKNPPPK
RATEMQSKVK VRHKSASNGS KTDTEEEEEQ QQQQKEQRSL AAHPRFKRRH RSEDCGGGPR
SLSRGLPCKK AATEGSSEKT VLDSKPSVPT TSEGGPELEL QIPELPLDSN EFWVHEGCIL
WANGIYLVCG RLYGLQEALE IAREMKCSHC QEAGATLGCY NKGCSFRYHY PCAIDADCLL
HEENFSVRCP KHKPPLPCPL PPLQNKTAKG SLSTEQSERG
