P4R3A_HUMAN
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 03-AUG-2022, entry version 159.
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};
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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; 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; 122.
DR ComplexPortal; CPX-1843; PPP4C-PPP4R2-PPP4R3A protein phosphatase 4 complex.
DR IntAct; Q6IN85; 52.
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; Q6IN85; -.
DR PeptideAtlas; Q6IN85; -.
DR PRIDE; Q6IN85; -.
DR ProteomicsDB; 66444; -. [Q6IN85-1]
DR ProteomicsDB; 66445; -. [Q6IN85-2]
DR ProteomicsDB; 66446; -. [Q6IN85-4]
DR ProteomicsDB; 66447; -. [Q6IN85-5]
DR Antibodypedia; 119; 120 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 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; MMRGYML; -.
DR OrthoDB; 388216at2759; -.
DR PhylomeDB; Q6IN85; -.
DR TreeFam; TF315190; -.
DR PathwayCommons; Q6IN85; -.
DR SignaLink; Q6IN85; -.
DR SIGNOR; Q6IN85; -.
DR BioGRID-ORCS; 55671; 72 hits in 1076 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 194 other tissues.
DR ExpressionAtlas; Q6IN85; baseline and differential.
DR Genevisible; Q6IN85; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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; IPI:ComplexPortal.
DR GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR006887; DUF625.
DR InterPro; IPR011993; PH-like_dom_sf.
DR Pfam; PF04802; SMK-1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
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
