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RNA polymerase-associated protein CTR9 homolog (SH2 domain-binding protein 1)

 CTR9_HUMAN              Reviewed;        1173 AA.
Q6PD62; D3DQV8; Q15015;
04-APR-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-APR-2018, entry version 141.
RecName: Full=RNA polymerase-associated protein CTR9 homolog;
AltName: Full=SH2 domain-binding protein 1;
Name=CTR9; Synonyms=KIAA0155, SH2BP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND TISSUE SPECIFICITY.
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).
[2]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R., Nomura N.;
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
[3]
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
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).
[5]
FUNCTION, AND IDENTIFICATION IN THE PAF1 COMPLEX.
PubMed=16024656; DOI=10.1101/gad.1292105;
Zhu B., Mandal S.S., Pham A.D., Zheng Y., Erdjument-Bromage H.,
Batra S.K., Tempst P., Reinberg D.;
"The human PAF complex coordinates transcription with events
downstream of RNA synthesis.";
Genes Dev. 19:1668-1673(2005).
[6]
FUNCTION.
PubMed=16307923; DOI=10.1016/j.molcel.2005.09.025;
Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H.,
Tempst P., Reinberg D.;
"Monoubiquitination of human histone H2B: the factors involved and
their roles in HOX gene regulation.";
Mol. Cell 20:601-611(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-941; SER-943
AND SER-970, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-941; SER-943; SER-1020
AND SER-1021, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, AND 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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925 AND SER-970, 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).
[12]
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).
[13]
FUNCTION.
PubMed=19345177; DOI=10.1016/j.stem.2009.03.009;
Ding L., Paszkowski-Rogacz M., Nitzsche A., Slabicki M.M.,
Heninger A.K., de Vries I., Kittler R., Junqueira M., Shevchenko A.,
Schulz H., Hubner N., Doss M.X., Sachinidis A., Hescheler J.,
Iacone R., Anastassiadis K., Stewart A.F., Pisabarro M.T.,
Caldarelli A., Poser I., Theis M., Buchholz F.;
"A genome-scale RNAi screen for Oct4 modulators defines a role of the
Paf1 complex for embryonic stem cell identity.";
Cell Stem Cell 4:403-415(2009).
[14]
IDENTIFICATION IN THE PAF1 COMPLEX, AND FUNCTION OF THE PAF1 COMPLEX.
PubMed=19952111; DOI=10.1101/gad.1834709;
Chen Y., Yamaguchi Y., Tsugeno Y., Yamamoto J., Yamada T.,
Nakamura M., Hisatake K., Handa H.;
"DSIF, the Paf1 complex, and Tat-SF1 have nonredundant, cooperative
roles in RNA polymerase II elongation.";
Genes Dev. 23:2765-2777(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925 AND SER-932, 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).
[16]
FUNCTION OF THE PAF1 COMPLEX, AND INTERACTION WITH KMT2A.
PubMed=20541477; DOI=10.1016/j.ccr.2010.04.012;
Muntean A.G., Tan J., Sitwala K., Huang Y., Bronstein J.,
Connelly J.A., Basrur V., Elenitoba-Johnson K.S., Hess J.L.;
"The PAF complex synergizes with MLL fusion proteins at HOX loci to
promote leukemogenesis.";
Cancer Cell 17:609-621(2010).
[17]
IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX,
AND FUNCTION OF THE PAF1 COMPLEX.
PubMed=20178742; DOI=10.1016/j.cell.2009.12.050;
Kim J., Guermah M., Roeder R.G.;
"The human PAF1 complex acts in chromatin transcription elongation
both independently and cooperatively with SII/TFIIS.";
Cell 140:491-503(2010).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-941; SER-943
AND SER-970, 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).
[19]
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).
[20]
FUNCTION, AND FUNCTION OF THE PAF1 COMPLEX.
PubMed=21329879; DOI=10.1016/j.molcel.2011.01.022;
Nagaike T., Logan C., Hotta I., Rozenblatt-Rosen O., Meyerson M.,
Manley J.L.;
"Transcriptional activators enhance polyadenylation of mRNA
precursors.";
Mol. Cell 41:409-418(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-941; SER-943;
SER-970; SER-1020; SER-1021; SER-1097 AND SER-1102, 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 THR-925 AND SER-970, 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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925 AND SER-1087, 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).
-!- FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple
functions during transcription by RNA polymerase II and is
implicated in regulation of development and maintenance of
embryonic stem cell pluripotency. PAF1C associates with RNA
polymerase II through interaction with POLR2A CTD non-
phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and
is involved in transcriptional elongation, acting both
indepentently and synergistically with TCEA1 and in cooperation
with the DSIF complex and HTATSF1. PAF1C is required for
transcription of Hox and Wnt target genes. PAF1C is involved in
hematopoiesis and stimulates transcriptional activity of
KMT2A/MLL1; it promotes leukemogenesis through association with
KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9
and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone
modifications such as ubiquitination of histone H2B and
methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the
RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme
UBE2A or UBE2B to chromatin which mediate monoubiquitination of
'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B
ubiquitination is proposed to be coupled to transcription. PAF1C
is involved in mRNA 3' end formation probably through association
with cleavage and poly(A) factors. In case of infection by
influenza A strain H3N2, PAF1C associates with viral NS1 protein,
thereby regulating gene transcription. Required for mono- and
trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation
on histone H3 'Lys-79' (H3K4me3). Required for Hox gene
transcription. Required for the trimethylation of histone H3 'Lys-
4' (H3K4me3) on genes involved in stem cell pluripotency; this
function is synergistic with CXXC1 indicative for an involvement
of the SET1 complex. Involved in transcriptional regulation of
IL6-responsive genes and in JAK-STAT pathway; may regulate DNA-
association of STAT3 (By similarity). {ECO:0000250,
ECO:0000269|PubMed:16024656, ECO:0000269|PubMed:16307923,
ECO:0000269|PubMed:19345177, ECO:0000269|PubMed:19952111,
ECO:0000269|PubMed:20178742, ECO:0000269|PubMed:20541477,
ECO:0000269|PubMed:21329879}.
-!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73,
PAF1, LEO1, CTR9, RTF1 and WDR61 (PubMed:16024656,
PubMed:19952111, PubMed:20178742). The PAF1 complex interacts with
PHF5A (By similarity). Interacts with KMT2A/MLL1
(PubMed:20541477). Interacts with STAT3. Interacts with SETD5.
{ECO:0000250|UniProtKB:Q62018, ECO:0000269|PubMed:16024656,
ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742,
ECO:0000269|PubMed:20541477}.
-!- INTERACTION:
Q6P1J9:CDC73; NbExp=19; IntAct=EBI-1019583, EBI-930143;
Q03164:KMT2A; NbExp=5; IntAct=EBI-1019583, EBI-591370;
Q8WVC0:LEO1; NbExp=13; IntAct=EBI-1019583, EBI-932432;
Q8N7H5:PAF1; NbExp=23; IntAct=EBI-1019583, EBI-2607770;
Q9GZS3:WDR61; NbExp=10; IntAct=EBI-1019583, EBI-358545;
-!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Note=Found in
speckles. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:8590280}.
-!- SEQUENCE CAUTION:
Sequence=BAA09925.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; D63875; BAA09925.2; ALT_INIT; mRNA.
EMBL; CH471064; EAW68557.1; -; Genomic_DNA.
EMBL; CH471064; EAW68558.1; -; Genomic_DNA.
EMBL; BC058914; AAH58914.1; -; mRNA.
CCDS; CCDS7805.1; -.
RefSeq; NP_055448.1; NM_014633.4.
UniGene; Hs.725151; -.
ProteinModelPortal; Q6PD62; -.
SMR; Q6PD62; -.
BioGrid; 115004; 110.
CORUM; Q6PD62; -.
DIP; DIP-31693N; -.
IntAct; Q6PD62; 89.
MINT; Q6PD62; -.
STRING; 9606.ENSP00000355013; -.
iPTMnet; Q6PD62; -.
PhosphoSitePlus; Q6PD62; -.
BioMuta; CTR9; -.
DMDM; 74758318; -.
EPD; Q6PD62; -.
MaxQB; Q6PD62; -.
PaxDb; Q6PD62; -.
PeptideAtlas; Q6PD62; -.
PRIDE; Q6PD62; -.
Ensembl; ENST00000361367; ENSP00000355013; ENSG00000198730.
GeneID; 9646; -.
KEGG; hsa:9646; -.
UCSC; uc001mja.4; human.
CTD; 9646; -.
DisGeNET; 9646; -.
EuPathDB; HostDB:ENSG00000198730.7; -.
GeneCards; CTR9; -.
HGNC; HGNC:16850; CTR9.
HPA; HPA061027; -.
HPA; HPA068122; -.
MIM; 609366; gene.
neXtProt; NX_Q6PD62; -.
OpenTargets; ENSG00000198730; -.
PharmGKB; PA134896774; -.
eggNOG; KOG2002; Eukaryota.
eggNOG; COG0457; LUCA.
GeneTree; ENSGT00390000005097; -.
HOGENOM; HOG000246926; -.
HOVERGEN; HBG081372; -.
InParanoid; Q6PD62; -.
KO; K15176; -.
OMA; WLNLAHI; -.
OrthoDB; EOG091G01GC; -.
PhylomeDB; Q6PD62; -.
TreeFam; TF314342; -.
Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
ChiTaRS; CTR9; human.
GeneWiki; CTR9; -.
GenomeRNAi; 9646; -.
PMAP-CutDB; Q6PD62; -.
PRO; PR:Q6PD62; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000198730; -.
CleanEx; HS_CTR9; -.
ExpressionAtlas; Q6PD62; baseline and differential.
Genevisible; Q6PD62; HS.
GO; GO:0016593; C:Cdc73/Paf1 complex; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0035327; C:transcriptionally active chromatin; ISS:UniProtKB.
GO; GO:0000993; F:RNA polymerase II core binding; IBA:GO_Central.
GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
GO; GO:0001832; P:blastocyst growth; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
GO; GO:0001711; P:endodermal cell fate commitment; ISS:UniProtKB.
GO; GO:0033523; P:histone H2B ubiquitination; IDA:UniProtKB.
GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB.
GO; GO:0010390; P:histone monoubiquitination; IDA:UniProtKB.
GO; GO:0001826; P:inner cell mass cell differentiation; IEA:Ensembl.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0007259; P:JAK-STAT cascade; ISS:UniProtKB.
GO; GO:1900364; P:negative regulation of mRNA polyadenylation; IMP:UniProtKB.
GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:2001168; P:positive regulation of histone H2B ubiquitination; IMP:UniProtKB.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
GO; GO:2001162; P:positive regulation of histone H3-K79 methylation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:2000653; P:regulation of genetic imprinting; IEA:Ensembl.
GO; GO:0019827; P:stem cell population maintenance; IDA:UniProtKB.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0001829; P:trophectodermal cell differentiation; IEA:Ensembl.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
Gene3D; 1.25.40.10; -; 3.
InterPro; IPR031101; Ctr9.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR14027; PTHR14027; 2.
Pfam; PF13181; TPR_8; 4.
SMART; SM00028; TPR; 10.
SUPFAM; SSF48452; SSF48452; 3.
PROSITE; PS50005; TPR; 10.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
Complete proteome; Nucleus; Phosphoprotein; Reference proteome;
Repeat; TPR repeat; Transcription; Transcription regulation;
Wnt signaling pathway.
CHAIN 1 1173 RNA polymerase-associated protein CTR9
homolog.
/FTId=PRO_0000231588.
REPEAT 41 75 TPR 1.
REPEAT 129 162 TPR 2.
REPEAT 163 196 TPR 3.
REPEAT 198 231 TPR 4.
REPEAT 235 268 TPR 5.
REPEAT 306 339 TPR 6.
REPEAT 341 374 TPR 7.
REPEAT 412 444 TPR 8.
REPEAT 451 484 TPR 9.
REPEAT 497 530 TPR 10.
REPEAT 531 564 TPR 11.
REPEAT 566 598 TPR 12.
REPEAT 613 646 TPR 13.
REPEAT 647 680 TPR 14.
REPEAT 681 714 TPR 15.
REPEAT 717 750 TPR 16.
COMPBIAS 844 1011 Lys-rich.
COMPBIAS 904 908 Poly-Gly.
COMPBIAS 933 936 Poly-Lys.
COMPBIAS 956 959 Poly-Lys.
COMPBIAS 1015 1172 Ser-rich.
MOD_RES 925 925 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 932 932 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 941 941 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 943 943 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 970 970 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1020 1020 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:21406692}.
MOD_RES 1021 1021 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:21406692}.
MOD_RES 1039 1039 Phosphoserine.
{ECO:0000250|UniProtKB:Q62018}.
MOD_RES 1041 1041 Phosphoserine.
{ECO:0000250|UniProtKB:Q62018}.
MOD_RES 1043 1043 Phosphoserine.
{ECO:0000250|UniProtKB:Q62018}.
MOD_RES 1081 1081 Phosphoserine.
{ECO:0000250|UniProtKB:Q62018}.
MOD_RES 1085 1085 Phosphoserine.
{ECO:0000250|UniProtKB:Q62018}.
MOD_RES 1087 1087 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1097 1097 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1102 1102 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
SEQUENCE 1173 AA; 133502 MW; 4B5AC22A5C5573C6 CRC64;
MSRGSIEIPL RDTDEVIELD FDQLPEGDEV ISILKQEHTQ LHIWIALALE YYKQGKTEEF
VKLLEAARID GNLDYRDHEK DQMTCLDTLA AYYVQQARKE KNKDNKKDLI TQATLLYTMA
DKIIMYDQNH LLGRACFCLL EGDKMDQADA QFHFVLNQSP NNIPALLGKA CISFNKKDYR
GALAYYKKAL RTNPGCPAEV RLGMGHCFVK LNKLEKARLA FSRALELNSK CVGALVGLAV
LELNNKEADS IKNGVQLLSR AYTIDPSNPM VLNHLANHFF FKKDYSKVQH LALHAFHNTE
VEAMQAESCY QLARSFHVQE DYDQAFQYYY QATQFASSSF VLPFFGLGQM YIYRGDKENA
SQCFEKVLKA YPNNYETMKI LGSLYAASED QEKRDIAKGH LKKVTEQYPD DVEAWIELAQ
ILEQTDIQGA LSAYGTATRI LQEKVQADVP PEILNNVGAL HFRLGNLGEA KKYFLASLDR
AKAEAEHDEH YYNAISVTTS YNLARLYEAM CEFHEAEKLY KNILREHPNY VDCYLRLGAM
ARDKGNFYEA SDWFKEALQI NQDHPDAWSL IGNLHLAKQE WGPGQKKFER ILKQPSTQSD
TYSMLALGNV WLQTLHQPTR DREKEKRHQD RALAIYKQVL RNDAKNLYAA NGIGAVLAHK
GYFREARDVF AQVREATADI SDVWLNLAHI YVEQKQYISA VQMYENCLRK FYKHQNTEVV
LYLARALFKC GKLQECKQTL LKARHVAPSD TVLMFNVALV LQRLATSVLK DEKSNLKEVL
NAVKELELAH RYFSYLSKVG DKMRFDLALA ATEARQCSDL LSQAQYHVAR ARKQDEEERE
LRAKQEQEKE LLRQKLLKEQ EEKRLREKEE QKKLLEQRAQ YVEKTKNILM FTGETEATKE
KKRGGGGGRR SKKGGEFDEF VNDDTDDDLP ISKKKKRRKG SGSEQEGEDE EGGERKKKKR
RRHPKGEEGS DDDETENGPK PKKRRPPKAE KKKAPKPERL PPSMKGKIKS KAIISSSDDS
SDEDKLKIAD EGHPRNSNSN SDSDEDEQRK KCASSESDSD ENQNKSGSEA GSPRRPRRQR
SDQDSDSDQP SRKRRPSGSE QSDNESVQSG RSHSGVSEND SRPASPSAES DHESERGSDN
EGSGQGSGNE SEPEGSNNEA SDRGSEHGSD DSD


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