ID P4R3A_HUMAN Reviewed; 833 AA. AC Q6IN85; Q69YK6; Q86U23; Q86YI7; Q8IVG1; Q9H3F1; Q9H7U8; Q9NV01; Q9NWP1; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 168. DE RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 3A {ECO:0000312|HGNC:HGNC:20219}; DE AltName: Full=SMEK homolog 1; GN Name=PPP4R3A {ECO:0000312|HGNC:HGNC:20219}; GN Synonyms=KIAA2010, PP4R3A, SMEK1; ORFNames=MSTP033; 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 MRNA] (ISOFORM 2). RC TISSUE=Brain; RA Nagase T., Kikuno R., Ohara O.; RT "The nucleotide sequence of a long cDNA clone isolated from human."; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 98-833 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE RP SCALE MRNA] OF 165-422 (ISOFORM 1). RC TISSUE=Ileal mucosa, and Placenta; 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 GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4). RC TISSUE=Eye; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 238-833. RC TISSUE=Neuroblastoma; RA Li W.B., Gruber C., Jessee J., Polayes D.; RT "Full-length cDNA libraries and normalization."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 667-833. RC TISSUE=Melanoma; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 808-833. RC TISSUE=Aorta; RA Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y., RA Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y., RA Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., RA Zhao M.S., Hui R.T.; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [8] RP IDENTIFICATION IN THE PPP4C-PPP4R2-PPP4R3A COMPLEX, INTERACTION WITH PPP4C, RP AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16085932; DOI=10.1074/mcp.m500231-mcp200; RA Gingras A.-C., Caballero M., Zarske M., Sanchez A., Hazbun T.R., Fields S., RA Sonenberg N., Hafen E., Raught B., Aebersold R.; RT "A novel, evolutionarily conserved protein phosphatase complex involved in RT cisplatin sensitivity."; RL Mol. Cell. Proteomics 4:1725-1740(2005). RN [9] RP SUBCELLULAR LOCATION. RX PubMed=18487071; DOI=10.1016/j.biocel.2008.03.021; RA Martin-Granados C., Philp A., Oxenham S.K., Prescott A.R., Cohen P.T.W.; RT "Depletion of protein phosphatase 4 in human cells reveals essential roles RT in centrosome maturation, cell migration and the regulation of Rho RT GTPases."; RL Int. J. Biochem. Cell Biol. 40:2315-2332(2008). RN [10] RP IDENTIFICATION IN THE PPP4C-PPP4R2-PPP4R3A COMPLEX, AND FUNCTION OF THE RP PPP4C-PPP4R2-PPP4R3A COMPLEX. RX PubMed=18614045; DOI=10.1016/j.molcel.2008.05.016; RA Chowdhury D., Xu X., Zhong X., Ahmed F., Zhong J., Liao J., Dykxhoorn D.M., RA Weinstock D.M., Pfeifer G.P., Lieberman J.; RT "A PP4-phosphatase complex dephosphorylates gamma-H2AX generated during DNA RT replication."; RL Mol. Cell 31:33-46(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117 AND SER-771, AND RP IDENTIFICATION BY 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 [12] 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-771; SER-774 AND SER-777, 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 LYS-655, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741, AND IDENTIFICATION BY RP 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741, AND IDENTIFICATION BY RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-127 AND SER-698, AND 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: Regulatory subunit of serine/threonine-protein phosphatase 4. CC May regulate the activity of PPP4C at centrosomal microtubule CC organizing centers. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically CC dephosphorylates H2AX phosphorylated on 'Ser-140' (gamma-H2AX) CC generated during DNA replication and required for DNA DSB repair. CC {ECO:0000269|PubMed:18614045}. CC -!- SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in CC different assemblies of the catalytic and one or more regulatory CC subunits. Component of the PP4 complex PPP4C-PPP4R2-PPP4R3A. Interacts CC with PPP4C; the interaction requires PPP4R2. CC {ECO:0000269|PubMed:16085932, ECO:0000269|PubMed:18614045}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18487071}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:18487071}. Nucleus {ECO:0000269|PubMed:18487071}. CC Note=In interphase localized in the cytoplasm and in the nucleus (with CC higher levels). During metaphase located in pericentriolar regions. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q6IN85-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6IN85-2; Sequence=VSP_021253; CC Name=4; CC IsoId=Q6IN85-4; Sequence=VSP_021252; CC Name=5; CC IsoId=Q6IN85-5; Sequence=VSP_021253, VSP_021256; CC -!- SIMILARITY: Belongs to the SMEK family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG39284.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305}; CC Sequence=BAA91960.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA91960.1; Type=Miscellaneous discrepancy; Note=Probable intron retention.; Evidence={ECO:0000305}; CC Sequence=BAB14877.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC23106.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AB095930; BAC23106.1; ALT_INIT; mRNA. DR EMBL; AK000714; BAA91338.1; -; mRNA. DR EMBL; AK001885; BAA91960.1; ALT_SEQ; mRNA. DR EMBL; AK024297; BAB14877.1; ALT_INIT; mRNA. DR EMBL; AL133153; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC038932; AAH38932.1; -; mRNA. DR EMBL; BC072409; AAH72409.1; -; mRNA. DR EMBL; BX248247; CAD62575.1; -; mRNA. DR EMBL; AL832921; CAH10634.1; -; mRNA. DR EMBL; AF113213; AAG39284.1; ALT_SEQ; mRNA. DR CCDS; CCDS61532.1; -. [Q6IN85-4] DR CCDS; CCDS91918.1; -. [Q6IN85-1] DR CCDS; CCDS9895.1; -. [Q6IN85-2] DR RefSeq; NP_001271209.1; NM_001284280.1. [Q6IN85-2] DR RefSeq; NP_001271210.1; NM_001284281.1. [Q6IN85-4] DR RefSeq; XP_005267899.1; XM_005267842.2. [Q6IN85-1] DR PDB; 6R8I; X-ray; 1.52 A; A=1-117. DR PDBsum; 6R8I; -. DR AlphaFoldDB; Q6IN85; -. DR SMR; Q6IN85; -. DR BioGRID; 120803; 183. DR ComplexPortal; CPX-1843; PPP4C-PPP4R2-PPP4R3A protein phosphatase 4 complex. DR IntAct; Q6IN85; 54. DR MINT; Q6IN85; -. DR STRING; 9606.ENSP00000450864; -. DR GlyGen; Q6IN85; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q6IN85; -. DR MetOSite; Q6IN85; -. DR PhosphoSitePlus; Q6IN85; -. DR BioMuta; PPP4R3A; -. DR DMDM; 74736507; -. DR EPD; Q6IN85; -. DR jPOST; Q6IN85; -. DR MassIVE; Q6IN85; -. DR MaxQB; Q6IN85; -. DR PaxDb; 9606-ENSP00000450864; -. DR PeptideAtlas; Q6IN85; -. DR ProteomicsDB; 66444; -. [Q6IN85-1] DR ProteomicsDB; 66445; -. [Q6IN85-2] DR ProteomicsDB; 66446; -. [Q6IN85-4] DR ProteomicsDB; 66447; -. [Q6IN85-5] DR Pumba; Q6IN85; -. DR Antibodypedia; 119; 144 antibodies from 23 providers. DR DNASU; 55671; -. DR Ensembl; ENST00000554684.5; ENSP00000450864.1; ENSG00000100796.18. [Q6IN85-2] DR Ensembl; ENST00000554943.6; ENSP00000450883.1; ENSG00000100796.18. [Q6IN85-1] DR Ensembl; ENST00000555462.5; ENSP00000450891.1; ENSG00000100796.18. [Q6IN85-4] DR GeneID; 55671; -. DR KEGG; hsa:55671; -. DR MANE-Select; ENST00000554943.6; ENSP00000450883.1; NM_001366432.2; NP_001353361.1. DR UCSC; uc001xzn.5; human. [Q6IN85-1] DR AGR; HGNC:20219; -. DR CTD; 55671; -. DR DisGeNET; 55671; -. DR GeneCards; PPP4R3A; -. DR HGNC; HGNC:20219; PPP4R3A. DR HPA; ENSG00000100796; Low tissue specificity. DR MIM; 610351; gene. DR neXtProt; NX_Q6IN85; -. DR OpenTargets; ENSG00000100796; -. DR PharmGKB; PA162403940; -. DR VEuPathDB; HostDB:ENSG00000100796; -. DR eggNOG; KOG2175; Eukaryota. DR GeneTree; ENSGT00390000018199; -. DR InParanoid; Q6IN85; -. DR OMA; ALMTHNN; -. DR OrthoDB; 151182at2759; -. DR PhylomeDB; Q6IN85; -. DR TreeFam; TF315190; -. DR PathwayCommons; Q6IN85; -. DR SignaLink; Q6IN85; -. DR SIGNOR; Q6IN85; -. DR BioGRID-ORCS; 55671; 76 hits in 1152 CRISPR screens. DR ChiTaRS; PPP4R3A; human. DR GenomeRNAi; 55671; -. DR Pharos; Q6IN85; Tbio. DR PRO; PR:Q6IN85; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q6IN85; Protein. DR Bgee; ENSG00000100796; Expressed in ventricular zone and 196 other cell types or tissues. DR ExpressionAtlas; Q6IN85; baseline and differential. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0030289; C:protein phosphatase 4 complex; IBA:GO_Central. DR GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central. DR GO; GO:0006974; P:DNA damage response; IBA:GO_Central. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR006887; P4R3-like_central_dom. DR InterPro; IPR011993; PH-like_dom_sf. DR PANTHER; PTHR23318; ATP SYNTHASE GAMMA-RELATED; 1. DR PANTHER; PTHR23318:SF3; SERINE_THREONINE-PROTEIN PHOSPHATASE 4 REGULATORY SUBUNIT 3A; 1. DR Pfam; PF04802; PP4R3; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR Genevisible; Q6IN85; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton; KW Nucleus; Phosphoprotein; Reference proteome. FT CHAIN 1..833 FT /note="Serine/threonine-protein phosphatase 4 regulatory FT subunit 3A" FT /id="PRO_0000254598" FT DOMAIN 1..100 FT /note="WH1" FT REGION 683..712 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 733..833 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 695..712 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 734..770 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 780..796 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 805..820 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 117 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:24275569" FT MOD_RES 127 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 655 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 698 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 741 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 768 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6P2K6" FT MOD_RES 771 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 774 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 777 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 780 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6P2K6" FT VAR_SEQ 67..305 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_021252" FT VAR_SEQ 410..422 FT /note="Missing (in isoform 2 and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1" FT /id="VSP_021253" FT VAR_SEQ 554..833 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_021256" FT STRAND 7..13 FT /evidence="ECO:0007829|PDB:6R8I" FT STRAND 17..32 FT /evidence="ECO:0007829|PDB:6R8I" FT TURN 33..36 FT /evidence="ECO:0007829|PDB:6R8I" FT STRAND 37..44 FT /evidence="ECO:0007829|PDB:6R8I" FT TURN 45..47 FT /evidence="ECO:0007829|PDB:6R8I" FT STRAND 50..55 FT /evidence="ECO:0007829|PDB:6R8I" FT STRAND 63..66 FT /evidence="ECO:0007829|PDB:6R8I" FT STRAND 69..75 FT /evidence="ECO:0007829|PDB:6R8I" FT STRAND 78..85 FT /evidence="ECO:0007829|PDB:6R8I" FT HELIX 87..101 FT /evidence="ECO:0007829|PDB:6R8I" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:6R8I" SQ SEQUENCE 833 AA; 95368 MW; EDDB4E1F47197A94 CRC64; MTDTRRRVKV YTLNEDRQWD DRGTGHVSSG YVERLKGMSL LVRAESDGSL LLESKINPNT AYQKQQDTLI VWSEAENYDL ALSFQEKAGC DEIWEKICQV QGKDPSVDIT QDLVDESEEE RFDDMSSPGL ELPSCELSRL EEIAELVASS LPSPLRREKL ALALENEGYI KKLLELFHVC EDLENIEGLH HLYEIIKGIF LLNRTALFEV MFSEECIMDV IGCLEYDPAL SQPRKHREFL TKTAKFKEVI PISDPELKQK IHQTYRVQYI QDMVLPTPSV FEENMLSTLH SFIFFNKVEI VGMLQEDEKF LTDLFAQLTD EATDEEKRQE LVNFLKEFCA FSQTLQPQNR DAFFKTLSNM GILPALEVIL GMDDTQVRSA ATDIFSYLVE YNPSMVREFV MQEAQQNDDV SKKLTEQKIT SKDILLINLI IEHMICDTDP ELGGAVQLMG LLRTLVDPEN MLATANKTEK TEFLGFFYKH CMHVLTAPLL ANTTEDKPSK DDFQTAQLLA LVLELLTFCV EHHTYHIKNY IINKDILRRV LVLMASKHAF LALCALRFKR KIIGLKDEFY NRYIMKSFLF EPVVKAFLNN GSRYNLMNSA IIEMFEFIRV EDIKSLTAHV IENYWKALED VDYVQTFKGL KLRFEQQRER QDNPKLDSMR SILRNHRYRR DARTLEDEEE MWFNTDEDDM EDGEAVVSPS DKTKNDDDIM DPISKFMERK KLKESEEKEV LLKTNLSGRQ SPSFKLSLSS GTKTNLTSQS STTNLPGSPG SPGSPGSPGS PGSVPKNTSQ TAAITTKGGL VGLVDYPDDD EDDDEDEDKE DTLPLSKKAK FDS //