ESF1_HUMAN
ID ESF1_HUMAN Reviewed; 851 AA.
AC Q9H501; Q86X92; Q9H9Q5; Q9HA35; Q9NX93; Q9P1S6;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=ESF1 homolog;
DE AltName: Full=ABT1-associated protein;
GN Name=ESF1; Synonyms=ABTAP, C20orf6; ORFNames=HDCMC28P;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-681 AND 702-851, AND VARIANT
RP THR-550.
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-595, AND VARIANT THR-550.
RC TISSUE=Mammary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 185-672.
RC TISSUE=Dendritic cell;
RA Zhao Z., Huang X., Li N., Zhu X., Cao X.;
RT "A novel gene from human dendritic cell.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-77; SER-79; SER-82;
RP SER-153; SER-179; SER-180; SER-198; THR-311; SER-312; SER-313; SER-657;
RP SER-663; THR-693; SER-694 AND SER-823, AND IDENTIFICATION BY MASS
RP 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657 AND SER-663, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-77; SER-79; SER-82;
RP SER-153; SER-198; SER-296; THR-311; SER-312; SER-313; SER-657; SER-663 AND
RP SER-735, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-82; SER-153; SER-296;
RP SER-298; THR-311; SER-312; SER-313; SER-657; SER-663 AND SER-694, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-153; SER-179;
RP SER-198; SER-614; SER-694 AND SER-823, AND IDENTIFICATION BY MASS
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, 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).
CC -!- FUNCTION: May constitute a novel regulatory system for basal
CC transcription. Negatively regulates ABT1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ABT1. Forms a complex with ABT1 and suppresses
CC the ABT1-induced activation of polymerase II-directed transcription in
CC mammalian cells (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus,
CC nucleoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ESF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF65504.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA91123.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAB14167.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL161659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK000375; BAA91123.1; ALT_SEQ; mRNA.
DR EMBL; AK022369; BAB14023.1; -; mRNA.
DR EMBL; AK022670; BAB14167.1; ALT_INIT; mRNA.
DR EMBL; BC046107; AAH46107.1; -; mRNA.
DR EMBL; AF068285; AAF65504.1; ALT_FRAME; mRNA.
DR CCDS; CCDS13117.1; -.
DR RefSeq; NP_001263309.1; NM_001276380.1.
DR RefSeq; NP_057733.2; NM_016649.3.
DR RefSeq; XP_016883363.1; XM_017027874.1.
DR AlphaFoldDB; Q9H501; -.
DR BioGRID; 119620; 136.
DR IntAct; Q9H501; 27.
DR MINT; Q9H501; -.
DR STRING; 9606.ENSP00000202816; -.
DR GlyGen; Q9H501; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H501; -.
DR MetOSite; Q9H501; -.
DR PhosphoSitePlus; Q9H501; -.
DR BioMuta; ESF1; -.
DR DMDM; 25452905; -.
DR EPD; Q9H501; -.
DR jPOST; Q9H501; -.
DR MassIVE; Q9H501; -.
DR MaxQB; Q9H501; -.
DR PaxDb; Q9H501; -.
DR PeptideAtlas; Q9H501; -.
DR PRIDE; Q9H501; -.
DR ProteomicsDB; 80886; -.
DR Antibodypedia; 24268; 75 antibodies from 18 providers.
DR DNASU; 51575; -.
DR Ensembl; ENST00000202816.5; ENSP00000202816.1; ENSG00000089048.15.
DR Ensembl; ENST00000617257.2; ENSP00000480783.2; ENSG00000089048.15.
DR GeneID; 51575; -.
DR KEGG; hsa:51575; -.
DR MANE-Select; ENST00000617257.2; ENSP00000480783.2; NM_001276380.2; NP_001263309.1.
DR UCSC; uc002woj.3; human.
DR CTD; 51575; -.
DR DisGeNET; 51575; -.
DR GeneCards; ESF1; -.
DR HGNC; HGNC:15898; ESF1.
DR HPA; ENSG00000089048; Low tissue specificity.
DR MIM; 618765; gene.
DR neXtProt; NX_Q9H501; -.
DR OpenTargets; ENSG00000089048; -.
DR PharmGKB; PA162385420; -.
DR VEuPathDB; HostDB:ENSG00000089048; -.
DR eggNOG; KOG2318; Eukaryota.
DR GeneTree; ENSGT00390000004881; -.
DR InParanoid; Q9H501; -.
DR OMA; LTWDETA; -.
DR OrthoDB; 1300279at2759; -.
DR PhylomeDB; Q9H501; -.
DR TreeFam; TF105822; -.
DR PathwayCommons; Q9H501; -.
DR SignaLink; Q9H501; -.
DR BioGRID-ORCS; 51575; 561 hits in 1088 CRISPR screens.
DR ChiTaRS; ESF1; human.
DR GeneWiki; ESF1; -.
DR GenomeRNAi; 51575; -.
DR Pharos; Q9H501; Tbio.
DR PRO; PR:Q9H501; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H501; protein.
DR Bgee; ENSG00000089048; Expressed in secondary oocyte and 210 other tissues.
DR ExpressionAtlas; Q9H501; baseline and differential.
DR Genevisible; Q9H501; HS.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR039754; Esf1.
DR InterPro; IPR012580; NUC153.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR PANTHER; PTHR12202; PTHR12202; 1.
DR Pfam; PF08159; NUC153; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..851
FT /note="ESF1 homolog"
FT /id="PRO_0000079410"
FT REGION 74..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 730..824
FT /evidence="ECO:0000255"
FT COMPBIAS 100..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..255
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..296
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..559
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 311
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 693
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 823
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 386
FT /note="P -> L (in dbSNP:rs6079171)"
FT /id="VAR_053082"
FT VARIANT 550
FT /note="I -> T (in dbSNP:rs3180370)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_024331"
FT VARIANT 824
FT /note="I -> L (in dbSNP:rs34414644)"
FT /id="VAR_053083"
FT CONFLICT 186
FT /note="R -> K (in Ref. 4; AAF65504)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="S -> T (in Ref. 2; BAB14023)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="S -> P (in Ref. 2; BAA91123)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="S -> G (in Ref. 4; AAF65504)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="L -> S (in Ref. 2; BAA91123)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="A -> V (in Ref. 4; AAF65504)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="G -> R (in Ref. 4; AAF65504)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="F -> Y (in Ref. 4; AAF65504)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="I -> V (in Ref. 2; BAA91123)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="V -> A (in Ref. 4; AAF65504)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="T -> S (in Ref. 2; BAB14023)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="E -> K (in Ref. 3; AAH46107)"
FT /evidence="ECO:0000305"
FT CONFLICT 829
FT /note="S -> P (in Ref. 2; BAB14167)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 851 AA; 98796 MW; 1BA283E7A0A65432 CRC64;
MSSKQEIMSD QRFRRVAKDP RFWEMPEKDR KVKIDKRFRA MFHDKKFKLN YAVDKRGRPI
SHSTTEDLKR FYDLSDSDSN LSGEDSKALS QKKIKKKKTQ TKKEIDSKNL VEKKKETKKA
NHKGSENKTD LDNSIGIKKM KTSCKFKIDS NISPKKDSKE FTQKNKKEKK NIVQHTTDSS
LEEKQRTLDS GTSEIVKSPR IECSKTRREM QSVVQLIMTR DSDGYENSTD GEMCDKDALE
EDSESVSEIG SDEESENEIT SVGRASGDDD GSEDDEEEDE DEEEDEDEDS EDDDKSDSGP
DLARGKGNIE TSSEDEDDTA DLFPEESGFE HAWRELDKDA PRADEITRRL AVCNMDWDRL
KAKDLLALFN SFKPKGGVIF SVKIYPSEFG KERMKEEQVQ GPVELLSIPE DAPEKDWTSR
EKLRDYQFKR LKYYYAVVDC DSPETASKIY EDCDGLEFES SCSFIDLRFI PDDITFDDEP
KDVASEVNLT AYKPKYFTSA AMGTSTVEIT WDETDHERIT MLNRKFKKEE LLDMDFQAYL
ASSSEDEEEI EEELQGDDGV NVEEDGKTKK SQKDDEEQIA KYRQLLQVIQ EKEKKGKEND
MEMEIKWVPG LKESAEEMVK NKLEGKDKLT PWEQFLEKKK EKKRLKRKQK ALAEEASEEE
LPSDVDLNDP YFAEEVKQIG INKKSVKSAK DGTSPEEEIE IERQKAEMAL LMMDEDEDSK
KHFNYNKIVE HQNLSKKKKK QLMKKKELIE DDFEVNVNDA RFQAMYTSHL FNLDPSDPNF
KKTKAMEKIL EEKARQRERK EQELTQAIKK KESEIEKESQ RKSIDPALSM LIKSIKTKTE
QFQARKKQKV K
