ID   MED13_HUMAN             Reviewed;        2174 AA.
AC   Q9UHV7; B2RU05; O60334;
DT   22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 3.
DT   24-JAN-2024, entry version 191.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 13 {ECO:0000305};
DE   AltName: Full=Activator-recruited cofactor 250 kDa component;
DE            Short=ARC250;
DE   AltName: Full=Mediator complex subunit 13;
DE   AltName: Full=Thyroid hormone receptor-associated protein 1;
DE   AltName: Full=Thyroid hormone receptor-associated protein complex 240 kDa component;
DE            Short=Trap240;
DE   AltName: Full=Vitamin D3 receptor-interacting protein complex component DRIP250;
DE            Short=DRIP250;
GN   Name=MED13 {ECO:0000312|HGNC:HGNC:22474};
GN   Synonyms=ARC250, KIAA0593, THRAP1, TRAP240;
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], PROTEIN SEQUENCE OF 696-713, TISSUE
RP   SPECIFICITY, AND IDENTIFICATION IN TRAP COMPLEX.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=10198638; DOI=10.1016/s1097-2765(00)80463-3;
RA   Ito M., Yuan C.-X., Malik S., Gu W., Fondell J.D., Yamamura S., Fu Z.-Y.,
RA   Zhang X., Qin J., Roeder R.G.;
RT   "Identity between TRAP and SMCC complexes indicates novel pathways for the
RT   function of nuclear receptors and diverse mammalian activators.";
RL   Mol. Cell 3:361-370(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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 170-2174.
RC   TISSUE=Brain;
RX   PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA   Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA   Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. IX. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:31-39(1998).
RN   [6]
RP   SEQUENCE REVISION.
RA   Ohara O., Nagase T., Ishikawa K.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   PROTEIN SEQUENCE OF 1401-1408 AND 1358-1367, AND IDENTIFICATION IN ARC
RP   COMPLEX.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=10235266; DOI=10.1038/19783;
RA   Rachez C., Lemon B.D., Suldan Z., Bromleigh V., Gamble M., Naeaer A.M.,
RA   Erdjument-Bromage H., Tempst P., Freedman L.P.;
RT   "Ligand-dependent transcription activation by nuclear receptors requires
RT   the DRIP complex.";
RL   Nature 398:824-828(1999).
RN   [8]
RP   IDENTIFICATION IN ARC COMPLEX, AND PROTEIN SEQUENCE OF 1429-1438; 1772-1783
RP   AND 2073-2084.
RX   PubMed=10235267; DOI=10.1038/19789;
RA   Naeaer A.M., Beaurang P.A., Zhou S., Abraham S., Solomon W.B., Tjian R.;
RT   "Composite co-activator ARC mediates chromatin-directed transcriptional
RT   activation.";
RL   Nature 398:828-832(1999).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR
RP   COMPLEX, AND INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
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   [10]
RP   INTERACTION WITH MED1; MED18; MED21; MED28; MED29 AND MED30, IDENTIFICATION
RP   BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, AND
RP   ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
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   [11]
RP   FUNCTION, AND INTERACTION WITH MED1 AND MED10.
RX   PubMed=16595664; DOI=10.1074/jbc.m601983200;
RA   Baek H.J., Kang Y.K., Roeder R.G.;
RT   "Human Mediator enhances basal transcription by facilitating recruitment of
RT   transcription factor IIB during preinitiation complex assembly.";
RL   J. Biol. Chem. 281:15172-15181(2006).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500 AND SER-1029, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504 AND SER-537, 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   [14]
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   [15]
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   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395; SER-504; SER-826 AND
RP   SER-890, AND 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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029, 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   [18]
RP   INVOLVEMENT IN MRD61, VARIANTS MRD61 131-LEU--LEU-2174 DEL; ILE-326;
RP   THR-326 DEL; GLN-327; SER-327; THR-540; 582-LEU--LEU-2174 DEL;
RP   1400-ARG--LEU-2174 DEL; LYS-2060 AND VAL-2064, AND CHARACTERIZATION OF
RP   VARIANT MRD61 1400-ARG--LEU-2174 DEL.
RX   PubMed=29740699; DOI=10.1007/s00439-018-1887-y;
RG   DDD study;
RA   Snijders Blok L., Hiatt S.M., Bowling K.M., Prokop J.W., Engel K.L.,
RA   Cochran J.N., Bebin E.M., Bijlsma E.K., Ruivenkamp C.A.L., Terhal P.,
RA   Simon M.E.H., Smith R., Hurst J.A., McLaughlin H., Person R., Crunk A.,
RA   Wangler M.F., Streff H., Symonds J.D., Zuberi S.M., Elliott K.S.,
RA   Sanders V.R., Masunga A., Hopkin R.J., Dubbs H.A., Ortiz-Gonzalez X.R.,
RA   Pfundt R., Brunner H.G., Fisher S.E., Kleefstra T., Cooper G.M.;
RT   "De novo mutations in MED13, a component of the Mediator complex, are
RT   associated with a novel neurodevelopmental disorder.";
RL   Hum. Genet. 137:375-388(2018).
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. {ECO:0000269|PubMed:16595664}.
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:10198638, ECO:0000269|PubMed:10235266,
CC       ECO:0000269|PubMed:10235267, ECO:0000269|PubMed:15175163,
CC       ECO:0000269|PubMed:15989967}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10198638}.
CC   -!- DISEASE: Intellectual developmental disorder, autosomal dominant 61
CC       (MRD61) [MIM:618009]: An autosomal dominant form of intellectual
CC       disability, a disorder characterized by significantly below average
CC       general intellectual functioning associated with impairments in
CC       adaptive behavior and manifested during the developmental period. MRD61
CC       is characterized by global developmental delay apparent in infancy with
CC       mildly impaired intellectual development, expressive speech delay, and
CC       behavioral abnormalities, including autism spectrum disorder and
CC       attention deficit-hyperactivity disorder. Additional features are
CC       highly variable and may include non-specific dysmorphic features,
CC       obstipation, ocular anomalies, and poor overall growth.
CC       {ECO:0000269|PubMed:29740699}. 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=AAD22032.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF117754; AAD22032.1; ALT_FRAME; mRNA.
DR   EMBL; AC008158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC018628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC060798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471179; EAW51438.1; -; Genomic_DNA.
DR   EMBL; BC140891; AAI40892.1; -; mRNA.
DR   EMBL; AB011165; BAA25519.2; -; mRNA.
DR   CCDS; CCDS42366.1; -.
DR   PIR; T01238; T01238.
DR   RefSeq; NP_005112.2; NM_005121.2.
DR   AlphaFoldDB; Q9UHV7; -.
DR   BioGRID; 115294; 88.
DR   ComplexPortal; CPX-3232; CKM complex variant 1.
DR   ComplexPortal; CPX-3263; CKM complex variant 2.
DR   CORUM; Q9UHV7; -.
DR   DIP; DIP-31468N; -.
DR   IntAct; Q9UHV7; 38.
DR   MINT; Q9UHV7; -.
DR   STRING; 9606.ENSP00000380888; -.
DR   GlyGen; Q9UHV7; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q9UHV7; -.
DR   PhosphoSitePlus; Q9UHV7; -.
DR   BioMuta; MED13; -.
DR   DMDM; 317373421; -.
DR   EPD; Q9UHV7; -.
DR   jPOST; Q9UHV7; -.
DR   MassIVE; Q9UHV7; -.
DR   MaxQB; Q9UHV7; -.
DR   PaxDb; 9606-ENSP00000380888; -.
DR   PeptideAtlas; Q9UHV7; -.
DR   ProteomicsDB; 84417; -.
DR   Pumba; Q9UHV7; -.
DR   Antibodypedia; 31215; 95 antibodies from 23 providers.
DR   DNASU; 9969; -.
DR   Ensembl; ENST00000397786.7; ENSP00000380888.2; ENSG00000108510.10.
DR   GeneID; 9969; -.
DR   KEGG; hsa:9969; -.
DR   MANE-Select; ENST00000397786.7; ENSP00000380888.2; NM_005121.3; NP_005112.2.
DR   UCSC; uc002izo.3; human.
DR   AGR; HGNC:22474; -.
DR   CTD; 9969; -.
DR   DisGeNET; 9969; -.
DR   GeneCards; MED13; -.
DR   HGNC; HGNC:22474; MED13.
DR   HPA; ENSG00000108510; Low tissue specificity.
DR   MalaCards; MED13; -.
DR   MIM; 603808; gene.
DR   MIM; 618009; phenotype.
DR   neXtProt; NX_Q9UHV7; -.
DR   OpenTargets; ENSG00000108510; -.
DR   Orphanet; 528084; Non-specific syndromic intellectual disability.
DR   PharmGKB; PA162395168; -.
DR   VEuPathDB; HostDB:ENSG00000108510; -.
DR   eggNOG; KOG3600; Eukaryota.
DR   GeneTree; ENSGT00390000013680; -.
DR   HOGENOM; CLU_000508_0_0_1; -.
DR   InParanoid; Q9UHV7; -.
DR   OMA; WWGEDPS; -.
DR   OrthoDB; 9289at2759; -.
DR   PhylomeDB; Q9UHV7; -.
DR   TreeFam; TF316867; -.
DR   PathwayCommons; Q9UHV7; -.
DR   Reactome; R-HSA-1989781; PPARA activates gene expression.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR   SignaLink; Q9UHV7; -.
DR   SIGNOR; Q9UHV7; -.
DR   BioGRID-ORCS; 9969; 39 hits in 1184 CRISPR screens.
DR   ChiTaRS; MED13; human.
DR   GeneWiki; MED13; -.
DR   GenomeRNAi; 9969; -.
DR   Pharos; Q9UHV7; Tbio.
DR   PRO; PR:Q9UHV7; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9UHV7; Protein.
DR   Bgee; ENSG00000108510; Expressed in endothelial cell and 210 other cell types or tissues.
DR   ExpressionAtlas; Q9UHV7; baseline and differential.
DR   GO; GO:1990508; C:CKM complex; IPI:ComplexPortal.
DR   GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0030374; F:nuclear receptor coactivator activity; NAS:UniProtKB.
DR   GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IDA:UniProtKB.
DR   GO; GO:0042809; F:nuclear vitamin D receptor binding; NAS:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
DR   GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
DR   InterPro; IPR009401; Med13_C.
DR   InterPro; IPR041285; MID_MedPIWI.
DR   PANTHER; PTHR48249; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 13; 1.
DR   PANTHER; PTHR48249:SF4; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 13; 1.
DR   Pfam; PF06333; Med13_C; 1.
DR   Pfam; PF18296; MID_MedPIWI; 1.
DR   Genevisible; Q9UHV7; HS.
PE   1: Evidence at protein level;
KW   Activator; Direct protein sequencing; Disease variant;
KW   Intellectual disability; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..2174
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   13"
FT                   /id="PRO_0000065584"
FT   REGION          435..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          709..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          749..769
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          787..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          959..1054
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1484..1505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1557..1617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2015..2048
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1188..1192
FT                   /note="LXXLL motif 1"
FT   MOTIF           1279..1283
FT                   /note="LXXLL motif 2"
FT   COMPBIAS        435..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..473
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..731
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        753..769
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        970..1002
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1032..1054
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1557..1612
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         395
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         500
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976"
FT   MOD_RES         504
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         530
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SWW4"
FT   MOD_RES         537
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         826
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         890
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1029
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:24275569"
FT   VARIANT         131..2174
FT                   /note="Missing (in MRD61)"
FT                   /evidence="ECO:0000269|PubMed:29740699"
FT                   /id="VAR_083556"
FT   VARIANT         326
FT                   /note="T -> I (in MRD61; dbSNP:rs1603405457)"
FT                   /evidence="ECO:0000269|PubMed:29740699"
FT                   /id="VAR_083557"
FT   VARIANT         326
FT                   /note="Missing (in MRD61)"
FT                   /evidence="ECO:0000269|PubMed:29740699"
FT                   /id="VAR_083558"
FT   VARIANT         327
FT                   /note="P -> Q (in MRD61)"
FT                   /evidence="ECO:0000269|PubMed:29740699"
FT                   /id="VAR_083559"
FT   VARIANT         327
FT                   /note="P -> S (in MRD61)"
FT                   /evidence="ECO:0000269|PubMed:29740699"
FT                   /id="VAR_083560"
FT   VARIANT         540
FT                   /note="P -> T (in MRD61; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:29740699"
FT                   /id="VAR_083561"
FT   VARIANT         582..2174
FT                   /note="Missing (in MRD61)"
FT                   /evidence="ECO:0000269|PubMed:29740699"
FT                   /id="VAR_083562"
FT   VARIANT         1370
FT                   /note="A -> P (in dbSNP:rs34805963)"
FT                   /id="VAR_057792"
FT   VARIANT         1385
FT                   /note="A -> P (in dbSNP:rs35996128)"
FT                   /id="VAR_057793"
FT   VARIANT         1400..2174
FT                   /note="Missing (in MRD61; no effect on protein levels)"
FT                   /evidence="ECO:0000269|PubMed:29740699"
FT                   /id="VAR_083563"
FT   VARIANT         2060
FT                   /note="Q -> K (in MRD61; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:29740699"
FT                   /id="VAR_083564"
FT   VARIANT         2064
FT                   /note="A -> V (in MRD61; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:29740699"
FT                   /id="VAR_083565"
FT   CONFLICT        106
FT                   /note="V -> M (in Ref. 1; AAD22032)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        392
FT                   /note="R -> K (in Ref. 1; AAD22032)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        467
FT                   /note="K -> E (in Ref. 1; AAD22032)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        712
FT                   /note="K -> A (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        800
FT                   /note="K -> R (in Ref. 1; AAD22032)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        930
FT                   /note="P -> L (in Ref. 1; AAD22032)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        984
FT                   /note="F -> C (in Ref. 1; AAD22032)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1090
FT                   /note="F -> S (in Ref. 1; AAD22032)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2174 AA;  239297 MW;  0FA54C84FE2C91E2 CRC64;
     MSASFVPNGA SLEDCHCNLF CLADLTGIKW KKYVWQGPTS APILFPVTEE DPILSSFSRC
     LKADVLGVWR RDQRPGRREL WIFWWGEDPS FADLIHHDLS EEEDGVWENG LSYECRTLLF
     KAVHNLLERC LMNRNFVRIG KWFVKPYEKD EKPINKSEHL SCSFTFFLHG DSNVCTSVEI
     NQHQPVYLLS EEHITLAQQS NSPFQVILCP FGLNGTLTGQ AFKMSDSATK KLIGEWKQFY
     PISCCLKEMS EEKQEDMDWE DDSLAAVEVL VAGVRMIYPA CFVLVPQSDI PTPSPVGSTH
     CSSSCLGVHQ VPASTRDPAM SSVTLTPPTS PEEVQTVDPQ SVQKWVKFSS VSDGFNSDST
     SHHGGKIPRK LANHVVDRVW QECNMNRAQN KRKYSASSGG LCEEATAAKV ASWDFVEATQ
     RTNCSCLRHK NLKSRNAGQQ GQAPSLGQQQ QILPKHKTNE KQEKSEKPQK RPLTPFHHRV
     SVSDDVGMDA DSASQRLVIS APDSQVRFSN IRTNDVAKTP QMHGTEMANS PQPPPLSPHP
     CDVVDEGVTK TPSTPQSQHF YQMPTPDPLV PSKPMEDRID SLSQSFPPQY QEAVEPTVYV
     GTAVNLEEDE ANIAWKYYKF PKKKDVEFLP PQLPSDKFKD DPVGPFGQES VTSVTELMVQ
     CKKPLKVSDE LVQQYQIKNQ CLSAIASDAE QEPKIDPYAF VEGDEEFLFP DKKDRQNSER
     EAGKKHKVED GTSSVTVLSH EEDAMSLFSP SIKQDAPRPT SHARPPSTSL IYDSDLAVSY
     TDLDNLFNSD EDELTPGSKK SANGSDDKAS CKESKTGNLD PLSCISTADL HKMYPTPPSL
     EQHIMGFSPM NMNNKEYGSM DTTPGGTVLE GNSSSIGAQF KIEVDEGFCS PKPSEIKDFS
     YVYKPENCQI LVGCSMFAPL KTLPSQYLPP IKLPEECIYR QSWTVGKLEL LSSGPSMPFI
     KEGDGSNMDQ EYGTAYTPQT HTSFGMPPSS APPSNSGAGI LPSPSTPRFP TPRTPRTPRT
     PRGAGGPASA QGSVKYENSD LYSPASTPST CRPLNSVEPA TVPSIPEAHS LYVNLILSES
     VMNLFKDCNF DSCCICVCNM NIKGADVGVY IPDPTQEAQY RCTCGFSAVM NRKFGNNSGL
     FLEDELDIIG RNTDCGKEAE KRFEALRATS AEHVNGGLKE SEKLSDDLIL LLQDQCTNLF
     SPFGAADQDP FPKSGVISNW VRVEERDCCN DCYLALEHGR QFMDNMSGGK VDEALVKSSC
     LHPWSKRNDV SMQCSQDILR MLLSLQPVLQ DAIQKKRTVR PWGVQGPLTW QQFHKMAGRG
     SYGTDESPEP LPIPTFLLGY DYDYLVLSPF ALPYWERLML EPYGSQRDIA YVVLCPENEA
     LLNGAKSFFR DLTAIYESCR LGQHRPVSRL LTDGIMRVGS TASKKLSEKL VAEWFSQAAD
     GNNEAFSKLK LYAQVCRYDL GPYLASLPLD SSLLSQPNLV APTSQSLITP PQMTNTGNAN
     TPSATLASAA SSTMTVTSGV AISTSVATAN STLTTASTSS SSSSNLNSGV SSNKLPSFPP
     FGSMNSNAAG SMSTQANTVQ SGQLGGQQTS ALQTAGISGE SSSLPTQPHP DVSESTMDRD
     KVGIPTDGDS HAVTYPPAIV VYIIDPFTYE NTDESTNSSS VWTLGLLRCF LEMVQTLPPH
     IKSTVSVQII PCQYLLQPVK HEDREIYPQH LKSLAFSAFT QCRRPLPTST NVKTLTGFGP
     GLAMETALRS PDRPECIRLY APPFILAPVK DKQTELGETF GEAGQKYNVL FVGYCLSHDQ
     RWILASCTDL YGELLETCII NIDVPNRARR KKSSARKFGL QKLWEWCLGL VQMSSLPWRV
     VIGRLGRIGH GELKDWSCLL SRRNLQSLSK RLKDMCRMCG ISAADSPSIL SACLVAMEPQ
     GSFVIMPDSV STGSVFGRST TLNMQTSQLN TPQDTSCTHI LVFPTSASVQ VASATYTTEN
     LDLAFNPNND GADGMGIFDL LDTGDDLDPD IINILPASPT GSPVHSPGSH YPHGGDAGKG
     QSTDRLLSTE PHEEVPNILQ QPLALGYFVS TAKAGPLPDW FWSACPQAQY QCPLFLKASL
     HLHVPSVQSD ELLHSKHSHP LDSNQTSDVL RFVLEQYNAL SWLTCDPATQ DRRSCLPIHF
     VVLNQLYNFI MNML
//