PURB_HUMAN
ID PURB_HUMAN Reviewed; 312 AA.
AC Q96QR8; A4D2L7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Transcriptional activator protein Pur-beta;
DE AltName: Full=Purine-rich element-binding protein B;
GN Name=PURB;
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], SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=1448097; DOI=10.1128/mcb.12.12.5673-5682.1992;
RA Bergemann A.D., Ma Z.-W., Johnson E.M.;
RT "Sequence of cDNA comprising the human pur gene and sequence-specific
RT single-stranded-DNA-binding properties of the encoded protein.";
RL Mol. Cell. Biol. 12:5673-5682(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [6]
RP INVOLVEMENT IN MDS.
RX PubMed=11417483; DOI=10.1038/sj.leu.2402108;
RA Lezon-Geyda K., Najfeld V., Johnson E.M.;
RT "Deletions of PURA, at 5q31, and PURB, at 7p13, in myelodysplastic syndrome
RT and progression to acute myelogenous leukemia.";
RL Leukemia 15:954-962(2001).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=12933792; DOI=10.1074/jbc.m307696200;
RA Gupta M., Sueblinvong V., Raman J., Jeevanandam V., Gupta M.P.;
RT "Single-stranded DNA-binding proteins PURalpha and PURbeta bind to a
RT purine-rich negative regulatory element of the alpha-myosin heavy chain
RT gene and control transcriptional and translational regulation of the gene
RT expression. Implications in the repression of alpha-myosin heavy chain
RT during heart failure.";
RL J. Biol. Chem. 278:44935-44948(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-298, AND
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-6; SER-8 AND SER-304, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-298 AND SER-304, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-8; SER-101 AND
RP SER-304, 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 [18]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Has capacity to bind repeated elements in single-stranded DNA
CC such as the purine-rich single strand of the PUR element located
CC upstream of the MYC gene. Plays a role in the control of vascular
CC smooth muscle (VSM) alpha-actin gene transcription as repressor in
CC myoblasts and fibroblasts. Participates in transcriptional and
CC translational regulation of alpha-MHC expression in cardiac myocytes by
CC binding to the purine-rich negative regulatory (PNR) element. Modulates
CC constitutive liver galectin-3 gene transcription by binding to its
CC promoter. May play a role in the dendritic transport of a subset of
CC mRNAs (By similarity). {ECO:0000250, ECO:0000269|PubMed:1448097}.
CC -!- SUBUNIT: Homodimer, heterodimer with PURA and heterotrimer with PURA
CC and YBX1/Y-box protein 1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q96QR8; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-2880222, EBI-541426;
CC Q96QR8; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-2880222, EBI-739832;
CC Q96QR8; Q9UBB5: MBD2; NbExp=3; IntAct=EBI-2880222, EBI-923391;
CC Q96QR8; Q96AH0: NABP1; NbExp=3; IntAct=EBI-2880222, EBI-2889252;
CC Q96QR8; Q9Y5E9: PCDHB14; NbExp=3; IntAct=EBI-2880222, EBI-10329013;
CC Q96QR8; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-2880222, EBI-10486136;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1448097}.
CC -!- TISSUE SPECIFICITY: Expressed in myocardium of heart failure patients.
CC {ECO:0000269|PubMed:12933792}.
CC -!- MISCELLANEOUS: Defects in PURB may be a cause of progression of
CC myelodysplastic syndrome (MDS) towards acute myelogenous leukemia
CC (AML). MDS refers to a heterogeneous group of closely related
CC hematopoietic disorders. All are characterized by a cellular marrow
CC with impaired morphology and maturation (dysmyelopoiesis) and
CC peripheral blood cytopenias, resulting from ineffective blood cell
CC production. Some patients with MDS develop acute myelogenous leukemia
CC (AML), a malignant disease in which hematopoietic precursors are
CC arrested in an early stage of development.
CC -!- SIMILARITY: Belongs to the PUR DNA-binding protein family.
CC {ECO:0000305}.
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DR EMBL; AY039216; AAK72462.1; -; mRNA.
DR EMBL; AC004854; AAS00366.1; -; Genomic_DNA.
DR EMBL; CH236960; EAL23749.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61073.1; -; Genomic_DNA.
DR EMBL; BC101735; AAI01736.1; -; mRNA.
DR EMBL; BC101737; AAI01738.1; -; mRNA.
DR CCDS; CCDS5499.1; -.
DR PIR; B45036; B45036.
DR RefSeq; NP_150093.1; NM_033224.4.
DR AlphaFoldDB; Q96QR8; -.
DR SMR; Q96QR8; -.
DR BioGRID; 111773; 312.
DR IntAct; Q96QR8; 29.
DR MINT; Q96QR8; -.
DR STRING; 9606.ENSP00000379051; -.
DR GlyGen; Q96QR8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96QR8; -.
DR PhosphoSitePlus; Q96QR8; -.
DR BioMuta; PURB; -.
DR DMDM; 74732688; -.
DR EPD; Q96QR8; -.
DR jPOST; Q96QR8; -.
DR MassIVE; Q96QR8; -.
DR MaxQB; Q96QR8; -.
DR PaxDb; Q96QR8; -.
DR PeptideAtlas; Q96QR8; -.
DR PRIDE; Q96QR8; -.
DR ProteomicsDB; 77888; -.
DR Antibodypedia; 44598; 98 antibodies from 19 providers.
DR DNASU; 5814; -.
DR Ensembl; ENST00000395699.5; ENSP00000379051.2; ENSG00000146676.10.
DR GeneID; 5814; -.
DR KEGG; hsa:5814; -.
DR MANE-Select; ENST00000395699.5; ENSP00000379051.2; NM_033224.5; NP_150093.1.
DR UCSC; uc003tme.5; human.
DR CTD; 5814; -.
DR DisGeNET; 5814; -.
DR GeneCards; PURB; -.
DR HGNC; HGNC:9702; PURB.
DR HPA; ENSG00000146676; Low tissue specificity.
DR MIM; 608887; gene.
DR neXtProt; NX_Q96QR8; -.
DR OpenTargets; ENSG00000146676; -.
DR PharmGKB; PA34046; -.
DR VEuPathDB; HostDB:ENSG00000146676; -.
DR eggNOG; KOG3074; Eukaryota.
DR GeneTree; ENSGT00950000183162; -.
DR HOGENOM; CLU_057873_1_1_1; -.
DR InParanoid; Q96QR8; -.
DR OMA; RFIRVEN; -.
DR OrthoDB; 1248813at2759; -.
DR PhylomeDB; Q96QR8; -.
DR TreeFam; TF313701; -.
DR PathwayCommons; Q96QR8; -.
DR SignaLink; Q96QR8; -.
DR SIGNOR; Q96QR8; -.
DR BioGRID-ORCS; 5814; 13 hits in 1084 CRISPR screens.
DR ChiTaRS; PURB; human.
DR GeneWiki; PURB; -.
DR GenomeRNAi; 5814; -.
DR Pharos; Q96QR8; Tbio.
DR PRO; PR:Q96QR8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q96QR8; protein.
DR Bgee; ENSG00000146676; Expressed in upper arm skin and 193 other tissues.
DR Genevisible; Q96QR8; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0032422; F:purine-rich negative regulatory element binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:InterPro.
DR GO; GO:0008283; P:cell population proliferation; IEA:InterPro.
DR GO; GO:0045637; P:regulation of myeloid cell differentiation; NAS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR006628; PUR-bd_fam.
DR InterPro; IPR030499; PURbeta.
DR PANTHER; PTHR12611; PTHR12611; 1.
DR PANTHER; PTHR12611:SF4; PTHR12611:SF4; 1.
DR Pfam; PF04845; PurA; 1.
DR SMART; SM00712; PUR; 3.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT CHAIN 2..312
FT /note="Transcriptional activator protein Pur-beta"
FT /id="PRO_0000225615"
FT DNA_BIND 28..254
FT /evidence="ECO:0000250"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 24
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O35295"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35295"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 152
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O35295"
FT MOD_RES 267
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35295"
FT MOD_RES 294
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O35295"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
SQ SEQUENCE 312 AA; 33241 MW; E39E84E8D2957A18 CRC64;
MADGDSGSER GGGGGPCGFQ PASRGGGEQE TQELASKRLD IQNKRFYLDV KQNAKGRFLK
IAEVGAGGSK SRLTLSMAVA AEFRDSLGDF IEHYAQLGPS SPEQLAAGAE EGGGPRRALK
SEFLVRENRK YYLDLKENQR GRFLRIRQTV NRGGGGFGAG PGPGGLQSGQ TIALPAQGLI
EFRDALAKLI DDYGGEDDEL AGGPGGGAGG PGGGLYGELP EGTSITVDSK RFFFDVGCNK
YGVFLRVSEV KPSYRNAITV PFKAWGKFGG AFCRYADEMK EIQERQRDKL YERRGGGSGG
GEESEGEEVD ED
