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Mediator of RNA polymerase II transcription subunit 24 (Activator-recruited cofactor 100 kDa component) (ARC100) (Cofactor required for Sp1 transcriptional activation subunit 4) (CRSP complex subunit 4) (Mediator complex subunit 24) (Thyroid hormone receptor-associated protein 4) (Thyroid hormone receptor-associated protein complex 100 kDa component) (Trap100) (hTRAP100) (Vitamin D3 receptor-interacting protein complex 100 kDa component) (DRIP100)

 MED24_HUMAN             Reviewed;         989 AA.
O75448; A8K4S5; B3KMR9; Q14143; Q9NNY5;
24-JUN-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
25-OCT-2017, entry version 161.
RecName: Full=Mediator of RNA polymerase II transcription subunit 24;
AltName: Full=Activator-recruited cofactor 100 kDa component;
Short=ARC100;
AltName: Full=Cofactor required for Sp1 transcriptional activation subunit 4;
Short=CRSP complex subunit 4;
AltName: Full=Mediator complex subunit 24;
AltName: Full=Thyroid hormone receptor-associated protein 4;
AltName: Full=Thyroid hormone receptor-associated protein complex 100 kDa component;
Short=Trap100;
Short=hTRAP100;
AltName: Full=Vitamin D3 receptor-interacting protein complex 100 kDa component;
Short=DRIP100;
Name=MED24;
Synonyms=ARC100, CRSP4, DRIP100, KIAA0130, THRAP4, TRAP100;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 1-15, AND
TISSUE SPECIFICITY.
PubMed=9653119; DOI=10.1073/pnas.95.14.7939;
Yuan C.-X., Ito M., Fondell J.D., Fu Z.-Y., Roeder R.G.;
"The TRAP220 component of a thyroid hormone receptor-associated
protein (TRAP) coactivator complex interacts directly with nuclear
receptors in a ligand-dependent fashion.";
Proc. Natl. Acad. Sci. U.S.A. 95:7939-7944(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND IDENTIFICATION IN DRIP
COMPLEX.
PubMed=9637681; DOI=10.1101/gad.12.12.1787;
Rachez C., Suldan Z., Ward J., Chang C.-P.B., Burakov D.,
Erdjument-Bromage H., Tempst P., Freedman L.P.;
"A novel protein complex that interacts with the vitamin D3 receptor
in a ligand-dependent manner and enhances VDR transactivation in a
cell-free system.";
Genes Dev. 12:1787-1800(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
THR-204.
TISSUE=Bone marrow;
PubMed=8590280; DOI=10.1093/dnares/2.4.167;
Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. IV.
The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:167-174(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 1-11 AND 957-965, AND IDENTIFICATION IN ARC
COMPLEX.
PubMed=10235267; DOI=10.1038/19789;
Naeaer A.M., Beaurang P.A., Zhou S., Abraham S., Solomon W.B.,
Tjian R.;
"Composite co-activator ARC mediates chromatin-directed
transcriptional activation.";
Nature 398:828-832(1999).
[8]
PROTEIN SEQUENCE OF 467-489, AND IDENTIFICATION IN ARC COMPLEX.
TISSUE=Cervix carcinoma;
PubMed=10235266; DOI=10.1038/19783;
Rachez C., Lemon B.D., Suldan Z., Bromleigh V., Gamble M.,
Naeaer A.M., Erdjument-Bromage H., Tempst P., Freedman L.P.;
"Ligand-dependent transcription activation by nuclear receptors
requires the DRIP complex.";
Nature 398:824-828(1999).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SMCC
COMPLEX.
PubMed=10024883; DOI=10.1016/S1097-2765(00)80178-1;
Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X.,
Martinez E., Qin J., Roeder R.G.;
"A novel human SRB/MED-containing cofactor complex, SMCC, involved in
transcription regulation.";
Mol. Cell 3:97-108(1999).
[10]
ERRATUM.
Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X.,
Martinez E., Qin J., Roeder R.G.;
Mol. Cell 3:541-541(1999).
[11]
FUNCTION, AND INTERACTION WITH AR.
PubMed=12218053; DOI=10.1074/jbc.M206061200;
Wang Q., Sharma D., Ren Y., Fondell J.D.;
"A coregulatory role for the TRAP-mediator complex in androgen
receptor-mediated gene expression.";
J. Biol. Chem. 277:42852-42858(2002).
[12]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
MEDIATOR COMPLEX.
PubMed=15175163; DOI=10.1016/j.molcel.2004.05.006;
Sato S., Tomomori-Sato C., Parmely T.J., Florens L., Zybailov B.,
Swanson S.K., Banks C.A.S., Jin J., Cai Y., Washburn M.P.,
Conaway J.W., Conaway R.C.;
"A set of consensus mammalian mediator subunits identified by
multidimensional protein identification technology.";
Mol. Cell 14:685-691(2004).
[13]
INTERACTION WITH MED1; MED10; MED21 AND MED30, IDENTIFICATION BY MASS
SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, AND ASSOCIATION
OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
PubMed=15989967; DOI=10.1016/j.molcel.2005.05.015;
Zhang X., Krutchinsky A., Fukuda A., Chen W., Yamamura S., Chait B.T.,
Roeder R.G.;
"MED1/TRAP220 exists predominantly in a TRAP/Mediator subpopulation
enriched in RNA polymerase II and is required for ER-mediated
transcription.";
Mol. Cell 19:89-100(2005).
[14]
FUNCTION, AND INTERACTION WITH MED1 AND MED10.
PubMed=16595664; DOI=10.1074/jbc.M601983200;
Baek H.J., Kang Y.K., Roeder R.G.;
"Human Mediator enhances basal transcription by facilitating
recruitment of transcription factor IIB during preinitiation complex
assembly.";
J. Biol. Chem. 281:15172-15181(2006).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862 AND SER-873, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862 AND SER-873, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862 AND SER-873, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862 AND SER-873, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Component of the Mediator complex, a coactivator
involved in the regulated transcription of nearly all RNA
polymerase II-dependent genes. Mediator functions as a bridge to
convey information from gene-specific regulatory proteins to the
basal RNA polymerase II transcription machinery. Mediator is
recruited to promoters by direct interactions with regulatory
proteins and serves as a scaffold for the assembly of a functional
preinitiation complex with RNA polymerase II and the general
transcription factors. {ECO:0000269|PubMed:12218053,
ECO:0000269|PubMed:16595664}.
-!- SUBUNIT: Component of the Mediator complex, which is composed of
MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13,
MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21,
MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31,
CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8
subunits form a distinct module termed the CDK8 module. Mediator
containing the CDK8 module is less active than Mediator lacking
this module in supporting transcriptional activation. Individual
preparations of the Mediator complex lacking one or more distinct
subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and
TRAP. Interacts with AR. {ECO:0000269|PubMed:10024883,
ECO:0000269|PubMed:10235266, ECO:0000269|PubMed:10235267,
ECO:0000269|PubMed:12218053, ECO:0000269|PubMed:15175163,
ECO:0000269|PubMed:15989967, ECO:0000269|PubMed:16595664,
ECO:0000269|PubMed:9637681}.
-!- INTERACTION:
Q9Y2X0:MED16; NbExp=2; IntAct=EBI-394523, EBI-394541;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O75448-1; Sequence=Displayed;
Name=2;
IsoId=O75448-2; Sequence=VSP_041125;
-!- TISSUE SPECIFICITY: Ubiquitous. Abundant in skeletal muscle, heart
and placenta. {ECO:0000269|PubMed:9653119}.
-!- SIMILARITY: Belongs to the Mediator complex subunit 24 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA09479.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF055995; AAC39855.1; -; mRNA.
EMBL; AF277379; AAF78764.1; -; mRNA.
EMBL; D50920; BAA09479.2; ALT_INIT; mRNA.
EMBL; AK022508; BAG51081.1; -; mRNA.
EMBL; AK291040; BAF83729.1; -; mRNA.
EMBL; AC090844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC102799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC011375; AAH11375.1; -; mRNA.
CCDS; CCDS11359.1; -. [O75448-1]
CCDS; CCDS42315.1; -. [O75448-2]
RefSeq; NP_001072986.1; NM_001079518.1. [O75448-2]
RefSeq; NP_001254726.1; NM_001267797.1. [O75448-2]
RefSeq; NP_055630.2; NM_014815.3. [O75448-1]
RefSeq; XP_016880955.1; XM_017025466.1. [O75448-1]
UniGene; Hs.462983; -.
ProteinModelPortal; O75448; -.
BioGrid; 115196; 77.
CORUM; O75448; -.
DIP; DIP-31462N; -.
IntAct; O75448; 37.
MINT; MINT-244199; -.
STRING; 9606.ENSP00000377686; -.
iPTMnet; O75448; -.
PhosphoSitePlus; O75448; -.
BioMuta; MED24; -.
EPD; O75448; -.
MaxQB; O75448; -.
PaxDb; O75448; -.
PeptideAtlas; O75448; -.
PRIDE; O75448; -.
DNASU; 9862; -.
Ensembl; ENST00000356271; ENSP00000348610; ENSG00000008838. [O75448-2]
Ensembl; ENST00000394127; ENSP00000377685; ENSG00000008838. [O75448-2]
Ensembl; ENST00000394128; ENSP00000377686; ENSG00000008838. [O75448-1]
GeneID; 9862; -.
KEGG; hsa:9862; -.
UCSC; uc002htt.4; human. [O75448-1]
CTD; 9862; -.
DisGeNET; 9862; -.
EuPathDB; HostDB:ENSG00000008838.17; -.
GeneCards; MED24; -.
H-InvDB; HIX0174136; -.
HGNC; HGNC:22963; MED24.
MIM; 607000; gene.
neXtProt; NX_O75448; -.
OpenTargets; ENSG00000008838; -.
PharmGKB; PA162395566; -.
eggNOG; ENOG410IF72; Eukaryota.
eggNOG; ENOG410YPDT; LUCA.
GeneTree; ENSGT00390000016438; -.
HOGENOM; HOG000293419; -.
HOVERGEN; HBG055588; -.
InParanoid; O75448; -.
KO; K15167; -.
PhylomeDB; O75448; -.
TreeFam; TF323565; -.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-212436; Generic Transcription Pathway.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
ChiTaRS; MED24; human.
GeneWiki; MED24; -.
GenomeRNAi; 9862; -.
PRO; PR:O75448; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000008838; -.
CleanEx; HS_MED24; -.
ExpressionAtlas; O75448; baseline and differential.
Genevisible; O75448; HS.
GO; GO:0016592; C:mediator complex; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; NAS:UniProtKB.
GO; GO:0004872; F:receptor activity; IDA:UniProtKB.
GO; GO:0001104; F:RNA polymerase II transcription cofactor activity; IDA:UniProtKB.
GO; GO:0046966; F:thyroid hormone receptor binding; IDA:UniProtKB.
GO; GO:0003712; F:transcription cofactor activity; IDA:UniProtKB.
GO; GO:0042809; F:vitamin D receptor binding; NAS:UniProtKB.
GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
InterPro; IPR021429; Mediator_Med24_N.
Pfam; PF11277; Med24_N; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome;
Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transcription; Transcription regulation.
CHAIN 1 989 Mediator of RNA polymerase II
transcription subunit 24.
/FTId=PRO_0000065582.
MOTIF 128 132 LXXLL motif 1.
MOTIF 344 348 LXXLL motif 2.
MOTIF 448 452 LXXLL motif 3.
MOTIF 557 561 LXXLL motif 4.
MOTIF 788 792 LXXLL motif 5.
MOTIF 857 861 LXXLL motif 6.
MOD_RES 862 862 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 873 873 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 72 84 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041125.
VARIANT 204 204 A -> T (in dbSNP:rs34585432).
{ECO:0000269|PubMed:8590280}.
/FTId=VAR_053969.
CONFLICT 20 20 D -> Y (in Ref. 3; BAA09479).
{ECO:0000305}.
CONFLICT 476 476 Missing (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 555 555 E -> G (in Ref. 2; AAF78764).
{ECO:0000305}.
CONFLICT 710 710 V -> E (in Ref. 4; BAG51081).
{ECO:0000305}.
CONFLICT 741 741 V -> A (in Ref. 4; BAG51081).
{ECO:0000305}.
CONFLICT 969 969 A -> P (in Ref. 4; BAG51081).
{ECO:0000305}.
SEQUENCE 989 AA; 110305 MW; CCEDE7D4E74D890C CRC64;
MKVVNLKQAI LQAWKERWSD YQWAINMKKF FPKGATWDIL NLADALLEQA MIGPSPNPLI
LSYLKYAISS QMVSYSSVLT AISKFDDFSR DLCVQALLDI MDMFCDRLSC HGKAEECIGL
CRALLSALHW LLRCTAASAE RLREGLEAGT PAAGEKQLAM CLQRLEKTLS STKNRALLHI
AKLEEASSWT AIEHSLLKLG EILANLSNPQ LRSQAEQCGT LIRSIPTMLS VHAEQMHKTG
FPTVHAVILL EGTMNLTGET QSLVEQLTMV KRMQHIPTPL FVLEIWKACF VGLIESPEGT
EELKWTAFTF LKIPQVLVKL KKYSHGDKDF TEDVNCAFEF LLKLTPLLDK ADQRCNCDCT
NFLLQECGKQ GLLSEASVNN LMAKRKADRE HAPQQKSGEN ANIQPNIQLI LRAEPTVTNI
LKTMDADHSK SPEGLLGVLG HMLSGKSLDL LLAAAAATGK LKSFARKFIN LNEFTTYGSE
ESTKPASVRA LLFDISFLML CHVAQTYGSE VILSESRTGA EVPFFETWMQ TCMPEEGKIL
NPDHPCFRPD STKVESLVAL LNNSSEMKLV QMKWHEACLS ISAAILEILN AWENGVLAFE
SIQKITDNIK GKVCSLAVCA VAWLVAHVRM LGLDEREKSL QMIRQLAGPL FSENTLQFYN
ERVVIMNSIL ERMCADVLQQ TATQIKFPST GVDTMPYWNL LPPKRPIKEV LTDIFAKVLE
KGWVDSRSIH IFDTLLHMGG VYWFCNNLIK ELLKETRKEH TLRAVELLYS IFCLDMQQVT
LVLLGHILPG LLTDSSKWHS LMDPPGTALA KLAVWCALSS YSSHKGQAST RQKKRHREDI
EDYISLFPLD DVQPSKLMRL LSSNEDDANI LSSPTDRSMS SSLSASQLHT VNMRDPLNRV
LANLFLLISS ILGSRTAGPH TQFVQWFMEE CVDCLEQGGR GSVLQFMPFT TVSELVKVSA
MSSPKVVLAI TDLSLPLGRQ VAAKAIAAL


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