MD13L_HUMAN
ID MD13L_HUMAN Reviewed; 2210 AA.
AC Q71F56; A1L469; Q68DN4; Q9H8C0; Q9NSY9; Q9UFD8; Q9UPX5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 13-like;
DE AltName: Full=Mediator complex subunit 13-like;
DE AltName: Full=Thyroid hormone receptor-associated protein 2;
DE AltName: Full=Thyroid hormone receptor-associated protein complex 240 kDa component-like;
GN Name=MED13L; Synonyms=KIAA1025, PROSIT240, THRAP2, TRAP240L;
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], TISSUE SPECIFICITY, VARIANT MRFACD GLY-251,
RP VARIANTS HIS-1872 AND GLY-2023, AND CHROMOSOMAL TRANSLOCATION.
RX PubMed=14638541; DOI=10.1161/01.cir.0000103684.77636.cd;
RA Muncke N., Jung C., Ruediger H., Ulmer H., Roeth R., Hubert A.,
RA Goldmuntz E., Driscoll D., Goodship J., Schoen K., Rappold G.;
RT "Missense mutations and gene interruption in PROSIT240, a novel TRAP240-
RT like gene, in patients with congenital heart defect (transposition of the
RT great arteries).";
RL Circulation 108:2843-2850(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15145061; DOI=10.1016/j.gene.2004.02.044;
RA Musante L., Bartsch O., Ropers H.-H., Kalscheuer V.M.;
RT "cDNA cloning and characterization of the human THRAP2 gene which maps to
RT chromosome 12q24, and its mouse ortholog Thrap2.";
RL Gene 332:119-127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 142-2210.
RC TISSUE=Fetal kidney;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 294-2210.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [6]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1077-2210.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MEDIATOR
RP COMPLEX.
RX PubMed=15175163; DOI=10.1016/j.molcel.2004.05.006;
RA Sato S., Tomomori-Sato C., Parmely T.J., Florens L., Zybailov B.,
RA Swanson S.K., Banks C.A.S., Jin J., Cai Y., Washburn M.P., Conaway J.W.,
RA Conaway R.C.;
RT "A set of consensus mammalian mediator subunits identified by
RT multidimensional protein identification technology.";
RL Mol. Cell 14:685-691(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MEDIATOR
RP COMPLEX.
RX PubMed=15989967; DOI=10.1016/j.molcel.2005.05.015;
RA Zhang X., Krutchinsky A., Fukuda A., Chen W., Yamamura S., Chait B.T.,
RA Roeder R.G.;
RT "MED1/TRAP220 exists predominantly in a TRAP/Mediator subpopulation
RT enriched in RNA polymerase II and is required for ER-mediated
RT transcription.";
RL Mol. Cell 19:89-100(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817; SER-826 AND SER-2083,
RP AND 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817 AND SER-2083, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; SER-560 AND SER-817, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-923 AND SER-2083, 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 [14]
RP INVOLVEMENT IN MRFACD.
RX PubMed=25167861; DOI=10.1136/jmedgenet-2014-102554;
RA Redin C., Gerard B., Lauer J., Herenger Y., Muller J., Quartier A.,
RA Masurel-Paulet A., Willems M., Lesca G., El-Chehadeh S., Le Gras S.,
RA Vicaire S., Philipps M., Dumas M., Geoffroy V., Feger C., Haumesser N.,
RA Alembik Y., Barth M., Bonneau D., Colin E., Dollfus H., Doray B.,
RA Delrue M.A., Drouin-Garraud V., Flori E., Fradin M., Francannet C.,
RA Goldenberg A., Lumbroso S., Mathieu-Dramard M., Martin-Coignard D.,
RA Lacombe D., Morin G., Polge A., Sukno S., Thauvin-Robinet C., Thevenon J.,
RA Doco-Fenzy M., Genevieve D., Sarda P., Edery P., Isidor B., Jost B.,
RA Olivier-Faivre L., Mandel J.L., Piton A.;
RT "Efficient strategy for the molecular diagnosis of intellectual disability
RT using targeted high-throughput sequencing.";
RL J. Med. Genet. 51:724-736(2014).
RN [15]
RP INVOLVEMENT IN MRFACD.
RX PubMed=25356899; DOI=10.1371/journal.pgen.1004772;
RA Hamdan F.F., Srour M., Capo-Chichi J.M., Daoud H., Nassif C., Patry L.,
RA Massicotte C., Ambalavanan A., Spiegelman D., Diallo O., Henrion E.,
RA Dionne-Laporte A., Fougerat A., Pshezhetsky A.V., Venkateswaran S.,
RA Rouleau G.A., Michaud J.L.;
RT "De novo mutations in moderate or severe intellectual disability.";
RL PLoS Genet. 10:E1004772-E1004772(2014).
RN [16]
RP VARIANT MRFACD 160-SER--GLU-174 DEL.
RX PubMed=24781760; DOI=10.1038/ejhg.2014.69;
RA van Haelst M.M., Monroe G.R., Duran K., van Binsbergen E., Breur J.M.,
RA Giltay J.C., van Haaften G.;
RT "Further confirmation of the MED13L haploinsufficiency syndrome.";
RL Eur. J. Hum. Genet. 23:135-138(2015).
RN [17]
RP INVOLVEMENT IN MRFACD.
RX PubMed=25758992; DOI=10.1038/ejhg.2015.26;
RA Adegbola A., Musante L., Callewaert B., Maciel P., Hu H., Isidor B.,
RA Picker-Minh S., Le Caignec C., Delle Chiaie B., Vanakker O., Menten B.,
RA Dheedene A., Bockaert N., Roelens F., Decaestecker K., Silva J., Soares G.,
RA Lopes F., Najmabadi H., Kahrizi K., Cox G.F., Angus S.P., Staropoli J.F.,
RA Fischer U., Suckow V., Bartsch O., Chess A., Ropers H.H., Wienker T.F.,
RA Huebner C., Kaindl A.M., Kalscheuer V.M.;
RT "Redefining the MED13L syndrome.";
RL Eur. J. Hum. Genet. 23:1308-1317(2015).
RN [18]
RP INVOLVEMENT IN MRFACD.
RX PubMed=25712080; DOI=10.1038/ejhg.2015.19;
RA Cafiero C., Marangi G., Orteschi D., Ali M., Asaro A., Ponzi E.,
RA Moncada A., Ricciardi S., Murdolo M., Mancano G., Contaldo I., Leuzzi V.,
RA Battaglia D., Mercuri E., Slavotinek A.M., Zollino M.;
RT "Novel de novo heterozygous loss-of-function variants in MED13L and further
RT delineation of the MED13L haploinsufficiency syndrome.";
RL Eur. J. Hum. Genet. 23:1499-1504(2015).
CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC the regulated transcription of nearly all RNA polymerase II-dependent
CC genes. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. Mediator is recruited to promoters by direct
CC interactions with regulatory proteins and serves as a scaffold for the
CC assembly of a functional preinitiation complex with RNA polymerase II
CC and the general transcription factors. This subunit may specifically
CC regulate transcription of targets of the Wnt signaling pathway and SHH
CC signaling pathway.
CC -!- SUBUNIT: Component of the Mediator complex, which is composed of MED1,
CC MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L,
CC MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23,
CC MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and
CC CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct
CC module termed the CDK8 module. Mediator containing the CDK8 module is
CC less active than Mediator lacking this module in supporting
CC transcriptional activation. Individual preparations of the Mediator
CC complex lacking one or more distinct subunits have been variously
CC termed ARC, CRSP, DRIP, PC2, SMCC and TRAP.
CC {ECO:0000269|PubMed:15175163, ECO:0000269|PubMed:15989967}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain (cerebellum), heart
CC (aorta), skeletal muscle, kidney, placenta and peripheral blood
CC leukocytes. Highly expressed in fetal brain.
CC {ECO:0000269|PubMed:14638541, ECO:0000269|PubMed:15145061}.
CC -!- DISEASE: Note=A chromosomal aberration involving MED13L is found in a
CC patient with transposition of the great arteries, dextro-looped and
CC intellectual disability. Translocation t(12;17)(q24.1;q21).
CC {ECO:0000269|PubMed:14638541}.
CC -!- DISEASE: Impaired intellectual development and distinctive facial
CC features with or without cardiac defects (MRFACD) [MIM:616789]: An
CC autosomal dominant syndrome characterized by intellectual disability,
CC delayed psychomotor development, profound language impairment, and
CC facial dysmorphism, including frontal bossing, upslanting palpebral
CC fissures, depressed nasal bridge with bulbous tip, and macrostomia.
CC There is variable penetrance of cardiac malformations, ranging from no
CC malformations to patent foramen ovale to septal defects and/or
CC transposition of the great arteries. {ECO:0000269|PubMed:14638541,
CC ECO:0000269|PubMed:24781760, ECO:0000269|PubMed:25167861,
CC ECO:0000269|PubMed:25356899, ECO:0000269|PubMed:25712080,
CC ECO:0000269|PubMed:25758992}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 13 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14697.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF515599; AAQ08182.1; -; mRNA.
DR EMBL; AY338463; AAR08418.1; -; mRNA.
DR EMBL; BC130422; AAI30423.1; -; mRNA.
DR EMBL; AL133033; CAB61363.1; -; mRNA.
DR EMBL; AL137644; CAB70855.1; -; mRNA.
DR EMBL; CR749332; CAH18186.1; -; mRNA.
DR EMBL; AB028948; BAA82977.2; -; mRNA.
DR EMBL; AK023837; BAB14697.1; ALT_INIT; mRNA.
DR CCDS; CCDS9177.1; -.
DR PIR; T42707; T42707.
DR RefSeq; NP_056150.1; NM_015335.4.
DR AlphaFoldDB; Q71F56; -.
DR BioGRID; 116964; 68.
DR CORUM; Q71F56; -.
DR IntAct; Q71F56; 31.
DR MINT; Q71F56; -.
DR STRING; 9606.ENSP00000281928; -.
DR iPTMnet; Q71F56; -.
DR PhosphoSitePlus; Q71F56; -.
DR BioMuta; MED13L; -.
DR DMDM; 74749769; -.
DR EPD; Q71F56; -.
DR jPOST; Q71F56; -.
DR MassIVE; Q71F56; -.
DR MaxQB; Q71F56; -.
DR PaxDb; Q71F56; -.
DR PeptideAtlas; Q71F56; -.
DR PRIDE; Q71F56; -.
DR ProteomicsDB; 68600; -.
DR Antibodypedia; 31301; 99 antibodies from 24 providers.
DR DNASU; 23389; -.
DR Ensembl; ENST00000281928.9; ENSP00000281928.3; ENSG00000123066.9.
DR GeneID; 23389; -.
DR KEGG; hsa:23389; -.
DR MANE-Select; ENST00000281928.9; ENSP00000281928.3; NM_015335.5; NP_056150.1.
DR UCSC; uc001tvw.4; human.
DR CTD; 23389; -.
DR DisGeNET; 23389; -.
DR GeneCards; MED13L; -.
DR HGNC; HGNC:22962; MED13L.
DR HPA; ENSG00000123066; Low tissue specificity.
DR MalaCards; MED13L; -.
DR MIM; 608771; gene.
DR MIM; 616789; phenotype.
DR neXtProt; NX_Q71F56; -.
DR OpenTargets; ENSG00000123066; -.
DR Orphanet; 369891; Developmental delay-facial dysmorphism syndrome due to MED13L deficiency.
DR Orphanet; 216718; Isolated congenitally uncorrected transposition of the great arteries.
DR PharmGKB; PA162395233; -.
DR VEuPathDB; HostDB:ENSG00000123066; -.
DR eggNOG; KOG3600; Eukaryota.
DR GeneTree; ENSGT00390000013680; -.
DR HOGENOM; CLU_000508_0_0_1; -.
DR InParanoid; Q71F56; -.
DR OrthoDB; 177884at2759; -.
DR PhylomeDB; Q71F56; -.
DR TreeFam; TF316867; -.
DR PathwayCommons; Q71F56; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; Q71F56; -.
DR SIGNOR; Q71F56; -.
DR BioGRID-ORCS; 23389; 48 hits in 1091 CRISPR screens.
DR ChiTaRS; MED13L; human.
DR GenomeRNAi; 23389; -.
DR Pharos; Q71F56; Tbio.
DR PRO; PR:Q71F56; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q71F56; protein.
DR Bgee; ENSG00000123066; Expressed in calcaneal tendon and 211 other tissues.
DR ExpressionAtlas; Q71F56; baseline and differential.
DR Genevisible; Q71F56; HS.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR009401; Med13_C.
DR InterPro; IPR021643; Mediator_Med13_N.
DR InterPro; IPR041285; MID_MedPIWI.
DR Pfam; PF06333; Med13_C; 1.
DR Pfam; PF11597; Med13_N; 1.
DR Pfam; PF18296; MID_MedPIWI; 1.
PE 1: Evidence at protein level;
KW Activator; Chromosomal rearrangement; Disease variant;
KW Intellectual disability; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..2210
FT /note="Mediator of RNA polymerase II transcription subunit
FT 13-like"
FT /id="PRO_0000076352"
FT REGION 391..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1380..1401
FT /note="Leucine-zipper"
FT REGION 1530..1656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2045..2080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 669..673
FT /note="LXXLL motif 1"
FT MOTIF 1225..1229
FT /note="LXXLL motif 2"
FT COMPBIAS 391..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2083
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"
FT VARIANT 160..174
FT /note="Missing (in MRFACD)"
FT /evidence="ECO:0000269|PubMed:24781760"
FT /id="VAR_076332"
FT VARIANT 251
FT /note="E -> G (in MRFACD; unknown pathological
FT significance; dbSNP:rs28940309)"
FT /evidence="ECO:0000269|PubMed:14638541"
FT /id="VAR_024024"
FT VARIANT 1872
FT /note="R -> H (in a patient with dextro-looped
FT transposition of the great arteries; unknown pathological
FT significance; dbSNP:rs28940310)"
FT /evidence="ECO:0000269|PubMed:14638541"
FT /id="VAR_024025"
FT VARIANT 2023
FT /note="D -> G (in a patient with dextro-looped
FT transposition of the great arteries; unknown pathological
FT significance; dbSNP:rs121918333)"
FT /evidence="ECO:0000269|PubMed:14638541"
FT /id="VAR_024026"
FT CONFLICT 295..299
FT /note="PQSVA -> SISLI (in Ref. 5; BAA82977)"
FT /evidence="ECO:0000305"
FT CONFLICT 861
FT /note="L -> S (in Ref. 4; CAH18186)"
FT /evidence="ECO:0000305"
FT CONFLICT 1258
FT /note="S -> G (in Ref. 4; CAH18186)"
FT /evidence="ECO:0000305"
FT CONFLICT 1455
FT /note="P -> L (in Ref. 7; BAB14697)"
FT /evidence="ECO:0000305"
FT CONFLICT 1577
FT /note="S -> N (in Ref. 7; BAB14697)"
FT /evidence="ECO:0000305"
FT CONFLICT 1703
FT /note="L -> M (in Ref. 7; BAB14697)"
FT /evidence="ECO:0000305"
FT CONFLICT 1971
FT /note="V -> F (in Ref. 7; BAB14697)"
FT /evidence="ECO:0000305"
FT CONFLICT 2194
FT /note="V -> A (in Ref. 7; BAB14697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2210 AA; 242602 MW; A8B566B1662B570C CRC64;
MTAAANWVAN GASLEDCHSN LFSLAELTGI KWRRYNFGGH GDCGPIISAP AQDDPILLSF
IRCLQANLLC VWRRDVKPDC KELWIFWWGD EPNLVGVIHH ELQVVEEGLW ENGLSYECRT
LLFKAIHNLL ERCLMDKNFV RIGKWFVRPY EKDEKPVNKS EHLSCAFTFF LHGESNVCTS
VEIAQHQPIY LINEEHIHMA QSSPAPFQVL VSPYGLNGTL TGQAYKMSDP ATRKLIEEWQ
YFYPMVLKKK EESKEEDELG YDDDFPVAVE VIVGGVRMVY PSAFVLISQN DIPVPQSVAS
AGGHIAVGQQ GLGSVKDPSN CGMPLTPPTS PEQAILGESG GMQSAASHLV SQDGGMITMH
SPKRSGKIPP KLHNHMVHRV WKECILNRTQ SKRSQMSTPT LEEEPASNPA TWDFVDPTQR
VSCSCSRHKL LKRCAVGPNR PPTVSQPGFS AGPSSSSSLP PPASSKHKTA ERQEKGDKLQ
KRPLIPFHHR PSVAEELCME QDTPGQKLGL AGIDSSLEVS SSRKYDKQMA VPSRNTSKQM
NLNPMDSPHS PISPLPPTLS PQPRGQETES LDPPSVPVNP ALYGNGLELQ QLSTLDDRTV
LVGQRLPLMA EVSETALYCG IRPSNPESSE KWWHSYRLPP SDDAEFRPPE LQGERCDAKM
EVNSESTALQ RLLAQPNKRF KIWQDKQPQL QPLHFLDPLP LSQQPGDSLG EVNDPYTFED
GDIKYIFTAN KKCKQGTEKD SLKKNKSEDG FGTKDVTTPG HSTPVPDGKN AMSIFSSATK
TDVRQDNAAG RAGSSSLTQV TDLAPSLHDL DNIFDNSDDD ELGAVSPALR SSKMPAVGTE
DRPLGKDGRA AVPYPPTVAD LQRMFPTPPS LEQHPAFSPV MNYKDGISSE TVTALGMMES
PMVSMVSTQL TEFKMEVEDG LGSPKPEEIK DFSYVHKVPS FQPFVGSSMF APLKMLPSHC
LLPLKIPDAC LFRPSWAIPP KIEQLPMPPA ATFIRDGYNN VPSVGSLADP DYLNTPQMNT
PVTLNSAAPA SNSGAGVLPS PATPRFSVPT PRTPRTPRTP RGGGTASGQG SVKYDSTDQG
SPASTPSTTR PLNSVEPATM QPIPEAHSLY VTLILSDSVM NIFKDRNFDS CCICACNMNI
KGADVGLYIP DSSNEDQYRC TCGFSAIMNR KLGYNSGLFL EDELDIFGKN SDIGQAAERR
LMMCQSTFLP QVEGTKKPQE PPISLLLLLQ NQHTQPFASL NFLDYISSNN RQTLPCVSWS
YDRVQADNND YWTECFNALE QGRQYVDNPT GGKVDEALVR SATVHSWPHS NVLDISMLSS
QDVVRMLLSL QPFLQDAIQK KRTGRTWENI QHVQGPLTWQ QFHKMAGRGT YGSEESPEPL
PIPTLLVGYD KDFLTISPFS LPFWERLLLD PYGGHRDVAY IVVCPENEAL LEGAKTFFRD
LSAVYEMCRL GQHKPICKVL RDGIMRVGKT VAQKLTDELV SEWFNQPWSG EENDNHSRLK
LYAQVCRHHL APYLATLQLD SSLLIPPKYQ TPPAAAQGQA TPGNAGPLAP NGSAAPPAGS
AFNPTSNSSS TNPAASSSAS GSSVPPVSSS ASAPGISQIS TTSSSGFSGS VGGQNPSTGG
ISADRTQGNI GCGGDTDPGQ SSSQPSQDGQ ESVTERERIG IPTEPDSADS HAHPPAVVIY
MVDPFTYAAE EDSTSGNFWL LSLMRCYTEM LDNLPEHMRN SFILQIVPCQ YMLQTMKDEQ
VFYIQYLKSM AFSVYCQCRR PLPTQIHIKS LTGFGPAASI EMTLKNPERP SPIQLYSPPF
ILAPIKDKQT ELGETFGEAS QKYNVLFVGY CLSHDQRWLL ASCTDLHGEL LETCVVNIAL
PNRSRRSKVS ARKIGLQKLW EWCIGIVQMT SLPWRVVIGR LGRLGHGELK DWSILLGECS
LQTISKKLKD VCRMCGISAA DSPSILSACL VAMEPQGSFV VMPDAVTMGS VFGRSTALNM
QSSQLNTPQD ASCTHILVFP TSSTIQVAPA NYPNEDGFSP NNDDMFVDLP FPDDMDNDIG
ILMTGNLHSS PNSSPVPSPG SPSGIGVGSH FQHSRSQGER LLSREAPEEL KQQPLALGYF
VSTAKAENLP QWFWSSCPQA QNQCPLFLKA SLHHHISVAQ TDELLPARNS QRVPHPLDSK
TTSDVLRFVL EQYNALSWLT CNPATQDRTS CLPVHFVVLT QLYNAIMNIL
