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Mediator of RNA polymerase II transcription subunit 15 (Activator-recruited cofactor 105 kDa component) (ARC105) (CTG repeat protein 7a) (Mediator complex subunit 15) (Positive cofactor 2 glutamine/Q-rich-associated protein) (PC2 glutamine/Q-rich-associated protein) (TPA-inducible gene 1 protein) (TIG-1) (Trinucleotide repeat-containing gene 7 protein)

 MED15_HUMAN             Reviewed;         788 AA.
Q96RN5; D3DX31; D3DX32; O15413; Q6IC31; Q8NF16; Q96CT0; Q96IH7;
Q9P1T3;
16-APR-2002, integrated into UniProtKB/Swiss-Prot.
10-JAN-2003, sequence version 2.
25-OCT-2017, entry version 164.
RecName: Full=Mediator of RNA polymerase II transcription subunit 15;
AltName: Full=Activator-recruited cofactor 105 kDa component;
Short=ARC105;
AltName: Full=CTG repeat protein 7a;
AltName: Full=Mediator complex subunit 15;
AltName: Full=Positive cofactor 2 glutamine/Q-rich-associated protein;
Short=PC2 glutamine/Q-rich-associated protein;
AltName: Full=TPA-inducible gene 1 protein;
Short=TIG-1;
AltName: Full=Trinucleotide repeat-containing gene 7 protein;
Name=MED15; Synonyms=ARC105, CTG7A, PCQAP, TIG1, TNRC7;
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 2), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INDUCTION.
TISSUE=Megakaryocyte, and Placenta;
PubMed=11024300; DOI=10.1016/S0378-1119(00)00292-4;
Abraham S., Solomon W.B.;
"A novel glutamine-rich putative transcriptional adaptor protein (TIG-
1), preferentially expressed in placental and bone-marrow tissues.";
Gene 255:389-400(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND POLYMORPHISM OF POLY-GLN
REGION.
TISSUE=Cervix carcinoma;
PubMed=11414760; DOI=10.1006/geno.2001.6566;
Berti L., Mittler G., Przemeck G.K.H., Stelzer G., Guenzler B.,
Amati F., Conti E., Dallapiccola B., Hrabe' de Angelis M., Novelli G.,
Meisterernst M.;
"Isolation and characterization of a novel gene from the DiGeorge
chromosomal region that encodes for a mediator subunit.";
Genomics 74:320-332(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Hepatoma, and Spleen;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 405-788 (ISOFORM 1).
TISSUE=Eye, and Kidney;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 185-573 (ISOFORM 2).
TISSUE=Brain cortex;
PubMed=9225980; DOI=10.1007/s004390050476;
Margolis R.L., Abraham M.R., Gatchell S.B., Li S.-H., Kidwai A.S.,
Breschel T.S., Stine O.C., Callahan C., McInnis M.G., Ross C.A.;
"cDNAs with long CAG trinucleotide repeats from human brain.";
Hum. Genet. 100:114-122(1997).
[8]
IDENTIFICATION IN ARC COMPLEX, AND PROTEIN SEQUENCE OF 39-48 AND
525-536.
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).
[9]
FUNCTION, AND INTERACTION WITH SMAD1; SMAD2 AND SMAD3.
PubMed=12167862; DOI=10.1038/nature00969;
Kato Y., Habas R., Katsuyama Y., Naeaer A.M., He X.;
"A component of the ARC/Mediator complex required for TGF beta/Nodal
signalling.";
Nature 418:641-646(2002).
[10]
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).
[11]
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).
[12]
INTERACTION WITH TRIM11, UBIQUITINATION, AND SUBCELLULAR LOCATION.
PubMed=16904669; DOI=10.1016/j.febslet.2006.07.066;
Ishikawa H., Tachikawa H., Miura Y., Takahashi N.;
"TRIM11 binds to and destabilizes a key component of the activator-
mediated cofactor complex (ARC105) through the ubiquitin-proteasome
system.";
FEBS Lett. 580:4784-4792(2006).
[13]
FUNCTION.
PubMed=16630888; DOI=10.1016/j.molcel.2006.03.023;
Andrau J.-C., van de Pasch L., Lijnzaad P., Bijma T., Koerkamp M.G.,
van de Peppel J., Werner M., Holstege F.C.P.;
"Genome-wide location of the coactivator mediator: binding without
activation and transient Cdk8 interaction on DNA.";
Mol. Cell 22:179-192(2006).
[14]
INTERACTION WITH WWTR1.
PubMed=18568018; DOI=10.1038/ncb1748;
Varelas X., Sakuma R., Samavarchi-Tehrani P., Peerani R., Rao B.M.,
Dembowy J., Yaffe M.B., Zandstra P.W., Wrana J.L.;
"TAZ controls Smad nucleocytoplasmic shuttling and regulates human
embryonic stem-cell self-renewal.";
Nat. Cell Biol. 10:837-848(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, 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).
[16]
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).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
STRUCTURE BY NMR OF 5-78, FUNCTION, INTERACTION WITH SREBF1 AND
SREBF2, AND MUTAGENESIS OF GLU-42; LEU-58 AND ALA-60.
PubMed=16799563; DOI=10.1038/nature04942;
Yang F., Vought B.W., Satterlee J.S., Walker A.K., Jim Sun Z.-Y.,
Watts J.L., DeBeaumont R., Saito R.M., Hyberts S.G., Yang S.,
Macol C., Iyer L., Tjian R., van den Heuvel S., Hart A.C., Wagner G.,
Naeaer A.M.;
"An ARC/Mediator subunit required for SREBP control of cholesterol and
lipid homeostasis.";
Nature 442:700-704(2006).
-!- 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. Required for cholesterol-dependent gene
regulation. Positively regulates the Nodal signaling pathway.
{ECO:0000269|PubMed:12167862, ECO:0000269|PubMed:16630888,
ECO:0000269|PubMed:16799563}.
-!- 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 SMAD2, SMAD3, SREBF1 and SREBF2. Interacts
with WWTR1. Interacts with TRIM11. {ECO:0000269|PubMed:10235267,
ECO:0000269|PubMed:12167862, ECO:0000269|PubMed:15175163,
ECO:0000269|PubMed:15989967, ECO:0000269|PubMed:16799563,
ECO:0000269|PubMed:16904669, ECO:0000269|PubMed:18568018}.
-!- INTERACTION:
P42858:HTT; NbExp=3; IntAct=EBI-394506, EBI-466029;
O60244:MED14; NbExp=2; IntAct=EBI-394506, EBI-394489;
Q71SY5:MED25; NbExp=2; IntAct=EBI-394506, EBI-394558;
P36956-1:SREBF1; NbExp=7; IntAct=EBI-394506, EBI-948328;
P36956-3:SREBF1; NbExp=2; IntAct=EBI-394506, EBI-948338;
Q12772:SREBF2; NbExp=2; IntAct=EBI-394506, EBI-465059;
Q96F44:TRIM11; NbExp=5; IntAct=EBI-394506, EBI-851809;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q96RN5-1; Sequence=Displayed;
Name=2;
IsoId=Q96RN5-2; Sequence=VSP_003922;
Name=3;
IsoId=Q96RN5-3; Sequence=VSP_013024, VSP_003922;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in all tissues examined, including
heart, brain, lung, spleen, thymus, pancreas, blood leukocyte and
placenta. However, the level of expression varied, with highest
expression in the placenta and peripheral blood and lowest in the
pancreas and kidney. {ECO:0000269|PubMed:11024300}.
-!- INDUCTION: By 12-O-tetradecanoylphorbol-13-acetate (TPA).
{ECO:0000269|PubMed:11024300}.
-!- PTM: Ubiquitinated by TRIM11, leading to proteasomal degradation.
{ECO:0000269|PubMed:16904669}.
-!- POLYMORPHISM: The poly-Gln region from amino acids 235-262 of
PCQAP is polymorphic. There are from 15 to 18 repeats in the
Italian population.
-!- SIMILARITY: Belongs to the Mediator complex subunit 15 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC12944.1; Type=Frameshift; Positions=13, 600, 749; Evidence={ECO:0000305};
Sequence=BAB85034.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors.; Evidence={ECO:0000305};
Sequence=BAC03446.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF056191; AAC12944.1; ALT_FRAME; mRNA.
EMBL; AF328769; AAK58423.1; -; mRNA.
EMBL; AK074268; BAB85034.1; ALT_SEQ; mRNA.
EMBL; AK090465; BAC03446.1; ALT_INIT; mRNA.
EMBL; CR456537; CAG30423.1; -; mRNA.
EMBL; CH471176; EAX02951.1; -; Genomic_DNA.
EMBL; CH471176; EAX02952.1; -; Genomic_DNA.
EMBL; CH471176; EAX02954.1; -; Genomic_DNA.
EMBL; CH471176; EAX02956.1; -; Genomic_DNA.
EMBL; BC007529; AAH07529.1; -; mRNA.
EMBL; BC013985; AAH13985.1; -; mRNA.
EMBL; U80745; AAB91443.1; -; mRNA.
CCDS; CCDS13781.1; -. [Q96RN5-2]
CCDS; CCDS33602.1; -. [Q96RN5-1]
CCDS; CCDS74824.1; -. [Q96RN5-3]
RefSeq; NP_001003891.1; NM_001003891.2. [Q96RN5-1]
RefSeq; NP_001280164.1; NM_001293235.1.
RefSeq; NP_001280165.1; NM_001293236.1. [Q96RN5-3]
RefSeq; NP_056973.2; NM_015889.4. [Q96RN5-2]
UniGene; Hs.517421; -.
PDB; 2GUT; NMR; -; A=5-78.
PDBsum; 2GUT; -.
ProteinModelPortal; Q96RN5; -.
SMR; Q96RN5; -.
BioGrid; 119623; 66.
CORUM; Q96RN5; -.
DIP; DIP-32908N; -.
IntAct; Q96RN5; 36.
MINT; MINT-243991; -.
STRING; 9606.ENSP00000263205; -.
iPTMnet; Q96RN5; -.
PhosphoSitePlus; Q96RN5; -.
BioMuta; MED15; -.
DMDM; 27734440; -.
EPD; Q96RN5; -.
MaxQB; Q96RN5; -.
PaxDb; Q96RN5; -.
PeptideAtlas; Q96RN5; -.
PRIDE; Q96RN5; -.
DNASU; 51586; -.
Ensembl; ENST00000263205; ENSP00000263205; ENSG00000099917. [Q96RN5-1]
Ensembl; ENST00000292733; ENSP00000292733; ENSG00000099917. [Q96RN5-2]
Ensembl; ENST00000382974; ENSP00000372434; ENSG00000099917. [Q96RN5-3]
GeneID; 51586; -.
KEGG; hsa:51586; -.
UCSC; uc002zsp.4; human. [Q96RN5-1]
CTD; 51586; -.
DisGeNET; 51586; -.
EuPathDB; HostDB:ENSG00000099917.17; -.
GeneCards; MED15; -.
HGNC; HGNC:14248; MED15.
HPA; HPA003179; -.
MIM; 607372; gene.
neXtProt; NX_Q96RN5; -.
OpenTargets; ENSG00000099917; -.
PharmGKB; PA33088; -.
eggNOG; KOG4274; Eukaryota.
eggNOG; ENOG410YKAW; LUCA.
GeneTree; ENSGT00730000111140; -.
HOVERGEN; HBG053529; -.
InParanoid; Q96RN5; -.
KO; K15157; -.
OMA; ICCLDDK; -.
OrthoDB; EOG091G07KB; -.
PhylomeDB; Q96RN5; -.
TreeFam; TF324988; -.
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; MED15; human.
EvolutionaryTrace; Q96RN5; -.
GeneWiki; MED15; -.
GenomeRNAi; 51586; -.
PRO; PR:Q96RN5; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000099917; -.
CleanEx; HS_MED15; -.
ExpressionAtlas; Q96RN5; baseline and differential.
Genevisible; Q96RN5; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016592; C:mediator complex; IEA:InterPro.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0001104; F:RNA polymerase II transcription cofactor activity; IEA:InterPro.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
InterPro; IPR019087; Med15.
Pfam; PF09606; Med15; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Methylation; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Triplet repeat expansion; Ubl conjugation.
CHAIN 1 788 Mediator of RNA polymerase II
transcription subunit 15.
/FTId=PRO_0000058264.
REGION 9 73 Interaction with SREBF1.
{ECO:0000269|PubMed:16799563}.
MOTIF 547 564 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 161 174 Poly-Gln.
COMPBIAS 178 193 Poly-Gln.
COMPBIAS 205 218 Poly-Gln.
COMPBIAS 226 239 Poly-Gln.
COMPBIAS 243 262 Poly-Gln.
COMPBIAS 266 515 Pro-rich.
COMPBIAS 360 367 Poly-Gln.
COMPBIAS 449 456 Poly-Pro.
COMPBIAS 602 611 Poly-Pro.
MOD_RES 349 349 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q924H2}.
MOD_RES 603 603 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 80 151 DPMNALQSLTGGPAAGAAGIGMPPRGPGQSLGGMGSLGAMG
QPMSLSGQPPPGTSGMAPHSMAVVSTATPQT -> A (in
isoform 3).
{ECO:0000303|PubMed:15461802}.
/FTId=VSP_013024.
VAR_SEQ 385 424 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:11024300,
ECO:0000303|PubMed:11414760,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15461802,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9225980}.
/FTId=VSP_003922.
VARIANT 261 262 Missing.
/FTId=VAR_013136.
MUTAGEN 42 42 E->A: Abrogates interaction with SREBF1.
{ECO:0000269|PubMed:16799563}.
MUTAGEN 58 58 L->D: Abrogates interaction with SREBF1.
{ECO:0000269|PubMed:16799563}.
MUTAGEN 60 60 A->D: Abrogates interaction with SREBF1.
{ECO:0000269|PubMed:16799563}.
CONFLICT 12 12 S -> R (in Ref. 1; AAC12944).
{ECO:0000305}.
CONFLICT 116 116 L -> F (in Ref. 1; AAC12944).
{ECO:0000305}.
CONFLICT 154 154 Q -> H (in Ref. 3; BAC03446).
{ECO:0000305}.
CONFLICT 161 161 Q -> R (in Ref. 3; BAB85034).
{ECO:0000305}.
CONFLICT 185 186 QQ -> EL (in Ref. 7; AAB91443).
{ECO:0000305}.
CONFLICT 186 187 Missing (in Ref. 4; CAG30423).
{ECO:0000305}.
CONFLICT 218 218 Missing (in Ref. 4; CAG30423).
{ECO:0000305}.
CONFLICT 232 287 Missing (in Ref. 3; BAB85034).
{ECO:0000305}.
CONFLICT 265 265 Q -> E (in Ref. 1; AAC12944 and 7;
AAB91443). {ECO:0000305}.
CONFLICT 572 573 IL -> GI (in Ref. 7; AAB91443).
{ECO:0000305}.
CONFLICT 685 685 L -> V (in Ref. 3; BAB85034).
{ECO:0000305}.
HELIX 13 30 {ECO:0000244|PDB:2GUT}.
HELIX 38 48 {ECO:0000244|PDB:2GUT}.
HELIX 52 71 {ECO:0000244|PDB:2GUT}.
SEQUENCE 788 AA; 86753 MW; BB6AC6C63ED2F97E CRC64;
MDVSGQETDW RSTAFRQKLV SQIEDAMRKA GVAHSKSSKD MESHVFLKAK TRDEYLSLVA
RLIIHFRDIH NKKSQASVSD PMNALQSLTG GPAAGAAGIG MPPRGPGQSL GGMGSLGAMG
QPMSLSGQPP PGTSGMAPHS MAVVSTATPQ TQLQLQQVAL QQQQQQQQFQ QQQQAALQQQ
QQQQQQQQFQ AQQSAMQQQF QAVVQQQQQL QQQQQQQQHL IKLHHQNQQQ IQQQQQQLQR
IAQLQLQQQQ QQQQQQQQQQ QQALQAQPPI QQPPMQQPQP PPSQALPQQL QQMHHTQHHQ
PPPQPQQPPV AQNQPSQLPP QSQTQPLVSQ AQALPGQMLY TQPPLKFVRA PMVVQQPPVQ
PQVQQQQTAV QTAQAAQMVA PGVQMITEAL AQGGMHIRAR FPPTTAVSAI PSSSIPLGRQ
PMAQVSQSSL PMLSSPSPGQ QVQTPQSMPP PPQPSPQPGQ PSSQPNSNVS SGPAPSPSSF
LPSPSPQPSQ SPVTARTPQN FSVPSPGPLN TPVNPSSVMS PAGSSQAEEQ QYLDKLKQLS
KYIEPLRRMI NKIDKNEDRK KDLSKMKSLL DILTDPSKRC PLKTLQKCEI ALEKLKNDMA
VPTPPPPPVP PTKQQYLCQP LLDAVLANIR SPVFNHSLYR TFVPAMTAIH GPPITAPVVC
TRKRRLEDDE RQSIPSVLQG EVARLDPKFL VNLDPSHCSN NGTVHLICKL DDKDLPSVPP
LELSVPADYP AQSPLWIDRQ WQYDANPFLQ SVHRCMTSRL LQLPDKHSVT ALLNTWAQSV
HQACLSAA


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