MED13_HUMAN
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 03-AUG-2022, entry version 183.
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; 84.
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; 37.
DR MINT; Q9UHV7; -.
DR STRING; 9606.ENSP00000380888; -.
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; Q9UHV7; -.
DR PeptideAtlas; Q9UHV7; -.
DR PRIDE; Q9UHV7; -.
DR ProteomicsDB; 84417; -.
DR Antibodypedia; 31215; 82 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 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; 177884at2759; -.
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; 34 hits in 1099 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 208 other tissues.
DR ExpressionAtlas; Q9UHV7; baseline and differential.
DR Genevisible; Q9UHV7; HS.
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:0043433; P:negative regulation of DNA-binding transcription factor activity; IEA:Ensembl.
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 from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
DR InterPro; IPR009401; Med13_C.
DR InterPro; IPR041285; MID_MedPIWI.
DR Pfam; PF06333; Med13_C; 1.
DR Pfam; PF18296; MID_MedPIWI; 1.
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; unknown pathological
FT 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; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:29740699"
FT /id="VAR_083564"
FT VARIANT 2064
FT /note="A -> V (in MRD61; unknown pathological
FT 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
