MCRS1_HUMAN
ID MCRS1_HUMAN Reviewed; 462 AA.
AC Q96EZ8; O14742; O75497; Q6VN53; Q7Z372;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Microspherule protein 1;
DE AltName: Full=58 kDa microspherule protein;
DE AltName: Full=Cell cycle-regulated factor p78;
DE AltName: Full=INO80 complex subunit J;
DE AltName: Full=MCRS2;
GN Name=MCRS1; Synonyms=INO80Q, MSP58;
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] (ISOFORM 1), INTERACTION WITH NOP2, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=9654073; DOI=10.1046/j.1432-1327.1998.2530734.x;
RA Ren Y., Busch R.K., Perlaky L., Busch H.;
RT "The 58-kDa microspherule protein (MSP58), a nucleolar protein, interacts
RT with nucleolar protein p120.";
RL Eur. J. Biochem. 253:734-742(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND INTERACTION WITH ICP22.
RC TISSUE=Cervix carcinoma;
RX PubMed=9765390; DOI=10.1128/jvi.72.11.8525-8531.1998;
RA Bruni R., Roizman B.;
RT "Herpes simplex virus 1 regulatory protein ICP22 interacts with a new cell
RT cycle-regulated factor and accumulates in a cell cycle-dependent fashion in
RT infected cells.";
RL J. Virol. 72:8525-8531(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, INTERACTION
RP WITH PINX1 AND TERT, AND FUNCTION.
RX PubMed=15044100; DOI=10.1016/j.bbrc.2004.02.166;
RA Song H., Li Y., Chen G., Xing Z., Zhao J., Yokoyama K.K., Li T., Zhao M.;
RT "Human MCRS2, a cell-cycle-dependent protein, associates with LPTS/PinX1
RT and reduces the telomere length.";
RL Biochem. Biophys. Res. Commun. 316:1116-1123(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Rectum tumor;
RG The German cDNA Consortium;
RA Bloecker H., Boecher M., Brandt P., Mewes H.W., Weil B., Amid C.,
RA Osanger A., Fobo G., Han M., Wiemann S.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [8]
RP FUNCTION, AND INTERACTION WITH DAXX.
RX PubMed=11948183; DOI=10.1074/jbc.m200633200;
RA Lin D.-Y., Shih H.-M.;
RT "Essential role of the 58-kDa microspherule protein in the modulation of
RT Daxx-dependent transcriptional repression as revealed by nucleolar
RT sequestration.";
RL J. Biol. Chem. 277:25446-25456(2002).
RN [9]
RP IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT "Physical association and coordinate function of the H3 K4
RT methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL Cell 121:873-885(2005).
RN [10]
RP IDENTIFICATION IN INO80 COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16230350; DOI=10.1074/jbc.m509128200;
RA Jin J., Cai Y., Yao T., Gottschalk A.J., Florens L., Swanson S.K.,
RA Gutierrez J.L., Coleman M.K., Workman J.L., Mushegian A., Washburn M.P.,
RA Conaway R.C., Conaway J.W.;
RT "A mammalian chromatin remodeling complex with similarities to the yeast
RT INO80 complex.";
RL J. Biol. Chem. 280:41207-41212(2005).
RN [11]
RP INTERACTION WITH CCDC85B.
RX PubMed=17014843; DOI=10.1016/j.yexmp.2006.07.008;
RA Du X., Wang Q., Hirohashi Y., Greene M.I.;
RT "DIPA, which can localize to the centrosome, associates with
RT p78/MCRS1/MSP58 and acts as a repressor of gene transcription.";
RL Exp. Mol. Pathol. 81:184-190(2006).
RN [12]
RP INTERACTION WITH FMR1; FXR1 AND FXR2, RNA-BINDING, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16571602; DOI=10.1093/hmg/ddl074;
RA Davidovic L., Bechara E., Gravel M., Jaglin X.H., Tremblay S., Sik A.,
RA Bardoni B., Khandjian E.W.;
RT "The nuclear microspherule protein 58 is a novel RNA-binding protein that
RT interacts with fragile X mental retardation protein in polyribosomal mRNPs
RT from neurons.";
RL Hum. Mol. Genet. 15:1525-1538(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-103 AND SER-108, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [14]
RP IDENTIFICATION IN THE INO80 COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18922472; DOI=10.1016/j.molcel.2008.08.027;
RA Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P.,
RA Florens L., Conaway R.C., Cohen R.E., Conaway J.W.;
RT "Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the
RT proteasome and in the Ino80 chromatin-remodeling complex.";
RL Mol. Cell 31:909-917(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-282, 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-282, 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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123 AND LYS-130, AND
RP IDENTIFICATION BY MASS 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 [19]
RP FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20018852; DOI=10.1074/jbc.c109.087981;
RA Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L.,
RA Washburn M.P., Conaway J.W., Conaway R.C.;
RT "Subunit composition and substrate specificity of a MOF-containing histone
RT acetyltransferase distinct from the male-specific lethal (MSL) complex.";
RL J. Biol. Chem. 285:4268-4272(2010).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-108 AND SER-282, AND
RP 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 [21]
RP IDENTIFICATION IN THE INO80 COMPLEX.
RX PubMed=21303910; DOI=10.1074/jbc.m111.222505;
RA Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P.,
RA Conaway J.W., Conaway R.C.;
RT "Subunit organization of the human INO80 chromatin remodeling complex: An
RT evolutionarily conserved core complex catalyzes ATP-dependent nucleosome
RT remodeling.";
RL J. Biol. Chem. 286:11283-11289(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, 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 [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-282, AND
RP 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, 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).
RN [26]
RP VARIANT [LARGE SCALE ANALYSIS] ILE-441.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Modulates the transcription repressor activity of DAXX by
CC recruiting it to the nucleolus (PubMed:11948183). As part of the NSL
CC complex it may be involved in acetylation of nucleosomal histone H4 on
CC several lysine residues (PubMed:20018852). Putative regulatory
CC component of the chromatin remodeling INO80 complex which is involved
CC in transcriptional regulation, DNA replication and probably DNA repair.
CC May also be an inhibitor of TERT telomerase activity (PubMed:15044100).
CC Binds to G-quadruplex structures in mRNA (PubMed:16571602). Binds to
CC RNA homomer poly(G) and poly(U) (PubMed:16571602).
CC {ECO:0000269|PubMed:11948183, ECO:0000269|PubMed:15044100,
CC ECO:0000269|PubMed:16571602, ECO:0000269|PubMed:20018852}.
CC -!- SUBUNIT: Component of the chromatin remodeling INO80 complex;
CC specifically part of a complex module associated with the N-terminus of
CC INO80 (PubMed:16230350, PubMed:18922472, PubMed:21303910). Component of
CC some MLL1/MLL complex, at least composed of the core components
CC KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as well as the facultative
CC components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1,
CC MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B,
CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (PubMed:15960975).
CC Component of the NSL complex at least composed of MOF/KAT8, KANSL1,
CC KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1
CC (PubMed:20018852). Interacts with NOP2 (PubMed:9654073). Interacts with
CC PINX1 (PubMed:15044100). Interacts with TERT (PubMed:15044100).
CC Interacts with CCDC85B (PubMed:17014843). Interacts with DAXX
CC (PubMed:11948183). Interacts (via N-terminus) with FMR1 (via
CC phosphorylated form) (PubMed:16571602). Interacts with FXR1 AND FXR2
CC (PubMed:16571602). {ECO:0000269|PubMed:11948183,
CC ECO:0000269|PubMed:15044100, ECO:0000269|PubMed:15960975,
CC ECO:0000269|PubMed:16230350, ECO:0000269|PubMed:16571602,
CC ECO:0000269|PubMed:17014843, ECO:0000269|PubMed:18922472,
CC ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:21303910,
CC ECO:0000269|PubMed:9654073}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Herpes simplex virus
CC ICP22. {ECO:0000269|PubMed:9765390}.
CC -!- INTERACTION:
CC Q96EZ8; Q8N302: AGGF1; NbExp=3; IntAct=EBI-348259, EBI-747899;
CC Q96EZ8; Q9Y2T1: AXIN2; NbExp=3; IntAct=EBI-348259, EBI-4400025;
CC Q96EZ8; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-348259, EBI-1642333;
CC Q96EZ8; Q5T5X7: BEND3; NbExp=3; IntAct=EBI-348259, EBI-1211496;
CC Q96EZ8; Q7RTU4: BHLHA9; NbExp=3; IntAct=EBI-348259, EBI-17508719;
CC Q96EZ8; O14503: BHLHE40; NbExp=3; IntAct=EBI-348259, EBI-711810;
CC Q96EZ8; Q9H0E9-2: BRD8; NbExp=3; IntAct=EBI-348259, EBI-10304361;
CC Q96EZ8; Q9HCU9: BRMS1; NbExp=3; IntAct=EBI-348259, EBI-714781;
CC Q96EZ8; Q5PSV4: BRMS1L; NbExp=5; IntAct=EBI-348259, EBI-5666615;
CC Q96EZ8; Q96B23: C18orf25; NbExp=5; IntAct=EBI-348259, EBI-742108;
CC Q96EZ8; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-348259, EBI-739879;
CC Q96EZ8; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-348259, EBI-11530605;
CC Q96EZ8; O95810: CAVIN2; NbExp=3; IntAct=EBI-348259, EBI-742141;
CC Q96EZ8; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-348259, EBI-11524851;
CC Q96EZ8; Q8IYE1: CCDC13; NbExp=6; IntAct=EBI-348259, EBI-10961312;
CC Q96EZ8; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-348259, EBI-10175300;
CC Q96EZ8; P51946: CCNH; NbExp=3; IntAct=EBI-348259, EBI-741406;
CC Q96EZ8; Q96GN5: CDCA7L; NbExp=6; IntAct=EBI-348259, EBI-5278764;
CC Q96EZ8; Q9C0F1: CEP44; NbExp=6; IntAct=EBI-348259, EBI-744115;
CC Q96EZ8; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-348259, EBI-739624;
CC Q96EZ8; Q8N137: CNTROB; NbExp=3; IntAct=EBI-348259, EBI-947360;
CC Q96EZ8; P38432: COIL; NbExp=3; IntAct=EBI-348259, EBI-945751;
CC Q96EZ8; Q68CJ9: CREB3L3; NbExp=3; IntAct=EBI-348259, EBI-852194;
CC Q96EZ8; Q96S65: CSRNP1; NbExp=3; IntAct=EBI-348259, EBI-4311573;
CC Q96EZ8; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-348259, EBI-3867333;
CC Q96EZ8; O60759: CYTIP; NbExp=3; IntAct=EBI-348259, EBI-997814;
CC Q96EZ8; Q9UER7: DAXX; NbExp=11; IntAct=EBI-348259, EBI-77321;
CC Q96EZ8; Q14919: DRAP1; NbExp=3; IntAct=EBI-348259, EBI-712941;
CC Q96EZ8; P50548: ERF; NbExp=3; IntAct=EBI-348259, EBI-8465203;
CC Q96EZ8; O60447: EVI5; NbExp=3; IntAct=EBI-348259, EBI-852291;
CC Q96EZ8; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-348259, EBI-8468186;
CC Q96EZ8; P22607: FGFR3; NbExp=3; IntAct=EBI-348259, EBI-348399;
CC Q96EZ8; Q8TC99: FNDC8; NbExp=3; IntAct=EBI-348259, EBI-12903902;
CC Q96EZ8; A1L4K1: FSD2; NbExp=3; IntAct=EBI-348259, EBI-5661036;
CC Q96EZ8; P51114-2: FXR1; NbExp=3; IntAct=EBI-348259, EBI-11022345;
CC Q96EZ8; P51116: FXR2; NbExp=4; IntAct=EBI-348259, EBI-740459;
CC Q96EZ8; O60861-1: GAS7; NbExp=3; IntAct=EBI-348259, EBI-11745923;
CC Q96EZ8; Q96CN9: GCC1; NbExp=3; IntAct=EBI-348259, EBI-746252;
CC Q96EZ8; P55040: GEM; NbExp=3; IntAct=EBI-348259, EBI-744104;
CC Q96EZ8; P14136: GFAP; NbExp=3; IntAct=EBI-348259, EBI-744302;
CC Q96EZ8; O75420: GIGYF1; NbExp=3; IntAct=EBI-348259, EBI-947774;
CC Q96EZ8; Q08379: GOLGA2; NbExp=3; IntAct=EBI-348259, EBI-618309;
CC Q96EZ8; Q86WP2: GPBP1; NbExp=5; IntAct=EBI-348259, EBI-2349758;
CC Q96EZ8; P06396: GSN; NbExp=3; IntAct=EBI-348259, EBI-351506;
CC Q96EZ8; Q6NT76: HMBOX1; NbExp=8; IntAct=EBI-348259, EBI-2549423;
CC Q96EZ8; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-348259, EBI-10961706;
CC Q96EZ8; P01112: HRAS; NbExp=3; IntAct=EBI-348259, EBI-350145;
CC Q96EZ8; P42858: HTT; NbExp=3; IntAct=EBI-348259, EBI-466029;
CC Q96EZ8; Q13422: IKZF1; NbExp=3; IntAct=EBI-348259, EBI-745305;
CC Q96EZ8; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-348259, EBI-11522367;
CC Q96EZ8; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-348259, EBI-747204;
CC Q96EZ8; Q9H2S9: IKZF4; NbExp=3; IntAct=EBI-348259, EBI-1640423;
CC Q96EZ8; Q8NBZ0: INO80E; NbExp=8; IntAct=EBI-348259, EBI-769401;
CC Q96EZ8; Q2T9L4: INSYN1; NbExp=3; IntAct=EBI-348259, EBI-4311436;
CC Q96EZ8; Q96N16: JAKMIP1; NbExp=3; IntAct=EBI-348259, EBI-2680803;
CC Q96EZ8; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-348259, EBI-2556193;
CC Q96EZ8; O95251: KAT7; NbExp=3; IntAct=EBI-348259, EBI-473199;
CC Q96EZ8; Q8N8K9: KIAA1958; NbExp=3; IntAct=EBI-348259, EBI-10181113;
CC Q96EZ8; Q92764: KRT35; NbExp=3; IntAct=EBI-348259, EBI-1058674;
CC Q96EZ8; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-348259, EBI-10172290;
CC Q96EZ8; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-348259, EBI-14065470;
CC Q96EZ8; Q9BQD3: KXD1; NbExp=4; IntAct=EBI-348259, EBI-739657;
CC Q96EZ8; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-348259, EBI-1216080;
CC Q96EZ8; P43360: MAGEA6; NbExp=3; IntAct=EBI-348259, EBI-1045155;
CC Q96EZ8; Q99683: MAP3K5; NbExp=3; IntAct=EBI-348259, EBI-476263;
CC Q96EZ8; P45984: MAPK9; NbExp=3; IntAct=EBI-348259, EBI-713568;
CC Q96EZ8; Q9NPJ6: MED4; NbExp=4; IntAct=EBI-348259, EBI-394607;
CC Q96EZ8; P50221: MEOX1; NbExp=3; IntAct=EBI-348259, EBI-2864512;
CC Q96EZ8; P55081: MFAP1; NbExp=3; IntAct=EBI-348259, EBI-1048159;
CC Q96EZ8; Q8N344: MIER2; NbExp=5; IntAct=EBI-348259, EBI-3504938;
CC Q96EZ8; Q7Z3K6-2: MIER3; NbExp=3; IntAct=EBI-348259, EBI-12224671;
CC Q96EZ8; P41227: NAA10; NbExp=3; IntAct=EBI-348259, EBI-747693;
CC Q96EZ8; Q15742: NAB2; NbExp=3; IntAct=EBI-348259, EBI-8641936;
CC Q96EZ8; Q6ZUT1: NKAPD1; NbExp=6; IntAct=EBI-348259, EBI-3920396;
CC Q96EZ8; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-348259, EBI-1051317;
CC Q96EZ8; Q96KB5: PBK; NbExp=3; IntAct=EBI-348259, EBI-536853;
CC Q96EZ8; Q15154-3: PCM1; NbExp=3; IntAct=EBI-348259, EBI-11742977;
CC Q96EZ8; Q8IXK0: PHC2; NbExp=2; IntAct=EBI-348259, EBI-713786;
CC Q96EZ8; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-348259, EBI-14066006;
CC Q96EZ8; Q96KN3: PKNOX2; NbExp=3; IntAct=EBI-348259, EBI-2692890;
CC Q96EZ8; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-348259, EBI-1105153;
CC Q96EZ8; O43586: PSTPIP1; NbExp=3; IntAct=EBI-348259, EBI-1050964;
CC Q96EZ8; Q15276: RABEP1; NbExp=3; IntAct=EBI-348259, EBI-447043;
CC Q96EZ8; P10276: RARA; NbExp=3; IntAct=EBI-348259, EBI-413374;
CC Q96EZ8; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-348259, EBI-10192441;
CC Q96EZ8; P57055: RIPPLY3; NbExp=3; IntAct=EBI-348259, EBI-12092053;
CC Q96EZ8; O14492-2: SH2B2; NbExp=3; IntAct=EBI-348259, EBI-19952306;
CC Q96EZ8; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-348259, EBI-12004298;
CC Q96EZ8; Q02446: SP4; NbExp=3; IntAct=EBI-348259, EBI-10198587;
CC Q96EZ8; A7MD48: SRRM4; NbExp=3; IntAct=EBI-348259, EBI-3867173;
CC Q96EZ8; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-348259, EBI-17280858;
CC Q96EZ8; Q86TJ2-3: TADA2B; NbExp=3; IntAct=EBI-348259, EBI-18173581;
CC Q96EZ8; Q86TI0: TBC1D1; NbExp=3; IntAct=EBI-348259, EBI-1644036;
CC Q96EZ8; Q01664: TFAP4; NbExp=3; IntAct=EBI-348259, EBI-2514218;
CC Q96EZ8; Q08117-2: TLE5; NbExp=3; IntAct=EBI-348259, EBI-11741437;
CC Q96EZ8; Q15025: TNIP1; NbExp=3; IntAct=EBI-348259, EBI-357849;
CC Q96EZ8; P19237: TNNI1; NbExp=3; IntAct=EBI-348259, EBI-746692;
CC Q96EZ8; Q9H3D4: TP63; NbExp=3; IntAct=EBI-348259, EBI-2337775;
CC Q96EZ8; O94972: TRIM37; NbExp=4; IntAct=EBI-348259, EBI-741602;
CC Q96EZ8; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-348259, EBI-725997;
CC Q96EZ8; Q9H2G4: TSPYL2; NbExp=5; IntAct=EBI-348259, EBI-947459;
CC Q96EZ8; Q8N6Y0: USHBP1; NbExp=6; IntAct=EBI-348259, EBI-739895;
CC Q96EZ8; Q9Y3C0: WASHC3; NbExp=13; IntAct=EBI-348259, EBI-712969;
CC Q96EZ8; Q9Y2W2: WBP11; NbExp=5; IntAct=EBI-348259, EBI-714455;
CC Q96EZ8; P98170: XIAP; NbExp=3; IntAct=EBI-348259, EBI-517127;
CC Q96EZ8; O15209: ZBTB22; NbExp=6; IntAct=EBI-348259, EBI-723574;
CC Q96EZ8; Q8TBK6: ZCCHC10; NbExp=3; IntAct=EBI-348259, EBI-597063;
CC Q96EZ8; Q6PEW1: ZCCHC12; NbExp=3; IntAct=EBI-348259, EBI-748373;
CC Q96EZ8; P17027: ZNF23; NbExp=3; IntAct=EBI-348259, EBI-5657766;
CC Q96EZ8; Q9UID6: ZNF639; NbExp=3; IntAct=EBI-348259, EBI-947476;
CC Q96EZ8; P17098: ZNF8; NbExp=3; IntAct=EBI-348259, EBI-2555757;
CC Q96EZ8; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-348259, EBI-527853;
CC Q96EZ8; Q9Y649; NbExp=3; IntAct=EBI-348259, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15044100,
CC ECO:0000269|PubMed:16571602, ECO:0000269|PubMed:18922472,
CC ECO:0000269|PubMed:20018852}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:16571602, ECO:0000269|PubMed:9654073}. Cytoplasm
CC {ECO:0000269|PubMed:16571602}. Note=In microspherules in the nucleolus.
CC {ECO:0000269|PubMed:9654073}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96EZ8-1; Sequence=Displayed;
CC Name=2; Synonyms=MCRS2;
CC IsoId=Q96EZ8-2; Sequence=VSP_016260;
CC Name=3;
CC IsoId=Q96EZ8-3; Sequence=VSP_016259;
CC Name=4;
CC IsoId=Q96EZ8-4; Sequence=VSP_054571;
CC -!- TISSUE SPECIFICITY: Detected in testis, and at lower levels in spleen,
CC thymus, prostate, uterus, small intestine, colon and leukocytes.
CC -!- DEVELOPMENTAL STAGE: Cell-cycle regulated: levels are highest early in
CC S phase; not detectable in G2.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC68599.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF015308; AAC52086.1; -; mRNA.
DR EMBL; AF068007; AAC68599.1; ALT_FRAME; mRNA.
DR EMBL; AY336730; AAQ84517.1; -; mRNA.
DR EMBL; BX538079; CAD98003.1; -; mRNA.
DR EMBL; AC020612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471111; EAW58078.1; -; Genomic_DNA.
DR EMBL; BC011794; AAH11794.1; -; mRNA.
DR CCDS; CCDS31795.1; -. [Q96EZ8-2]
DR CCDS; CCDS61118.1; -. [Q96EZ8-4]
DR CCDS; CCDS8787.1; -. [Q96EZ8-1]
DR RefSeq; NP_001012300.1; NM_001012300.1. [Q96EZ8-2]
DR RefSeq; NP_001265270.1; NM_001278341.1. [Q96EZ8-4]
DR RefSeq; NP_006328.2; NM_006337.4. [Q96EZ8-1]
DR RefSeq; XP_005268629.1; XM_005268572.3. [Q96EZ8-1]
DR RefSeq; XP_016874178.1; XM_017018689.1. [Q96EZ8-2]
DR RefSeq; XP_016874179.1; XM_017018690.1. [Q96EZ8-2]
DR AlphaFoldDB; Q96EZ8; -.
DR SMR; Q96EZ8; -.
DR BioGRID; 115710; 230.
DR ComplexPortal; CPX-809; NSL histone acetyltransferase complex.
DR ComplexPortal; CPX-846; INO80 chromatin remodeling complex.
DR CORUM; Q96EZ8; -.
DR IntAct; Q96EZ8; 174.
DR MINT; Q96EZ8; -.
DR STRING; 9606.ENSP00000349640; -.
DR iPTMnet; Q96EZ8; -.
DR PhosphoSitePlus; Q96EZ8; -.
DR SwissPalm; Q96EZ8; -.
DR BioMuta; MCRS1; -.
DR DMDM; 24638035; -.
DR EPD; Q96EZ8; -.
DR jPOST; Q96EZ8; -.
DR MassIVE; Q96EZ8; -.
DR MaxQB; Q96EZ8; -.
DR PaxDb; Q96EZ8; -.
DR PeptideAtlas; Q96EZ8; -.
DR PRIDE; Q96EZ8; -.
DR ProteomicsDB; 69010; -.
DR ProteomicsDB; 76477; -. [Q96EZ8-1]
DR ProteomicsDB; 76478; -. [Q96EZ8-2]
DR ProteomicsDB; 76479; -. [Q96EZ8-3]
DR Antibodypedia; 25985; 166 antibodies from 25 providers.
DR DNASU; 10445; -.
DR Ensembl; ENST00000343810.9; ENSP00000345358.4; ENSG00000187778.14. [Q96EZ8-1]
DR Ensembl; ENST00000357123.8; ENSP00000349640.4; ENSG00000187778.14. [Q96EZ8-2]
DR Ensembl; ENST00000546244.5; ENSP00000444982.1; ENSG00000187778.14. [Q96EZ8-4]
DR Ensembl; ENST00000550165.5; ENSP00000448056.1; ENSG00000187778.14. [Q96EZ8-1]
DR GeneID; 10445; -.
DR KEGG; hsa:10445; -.
DR MANE-Select; ENST00000343810.9; ENSP00000345358.4; NM_006337.5; NP_006328.2.
DR UCSC; uc001rui.3; human. [Q96EZ8-1]
DR CTD; 10445; -.
DR DisGeNET; 10445; -.
DR GeneCards; MCRS1; -.
DR HGNC; HGNC:6960; MCRS1.
DR HPA; ENSG00000187778; Low tissue specificity.
DR MIM; 609504; gene.
DR neXtProt; NX_Q96EZ8; -.
DR OpenTargets; ENSG00000187778; -.
DR PharmGKB; PA30708; -.
DR VEuPathDB; HostDB:ENSG00000187778; -.
DR eggNOG; KOG2293; Eukaryota.
DR GeneTree; ENSGT00390000005536; -.
DR HOGENOM; CLU_035858_0_0_1; -.
DR InParanoid; Q96EZ8; -.
DR OMA; EIQQRWY; -.
DR OrthoDB; 1091011at2759; -.
DR PhylomeDB; Q96EZ8; -.
DR TreeFam; TF318119; -.
DR PathwayCommons; Q96EZ8; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR SignaLink; Q96EZ8; -.
DR SIGNOR; Q96EZ8; -.
DR BioGRID-ORCS; 10445; 463 hits in 1082 CRISPR screens.
DR ChiTaRS; MCRS1; human.
DR GeneWiki; MCRS1; -.
DR GenomeRNAi; 10445; -.
DR Pharos; Q96EZ8; Tbio.
DR PRO; PR:Q96EZ8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96EZ8; protein.
DR Bgee; ENSG00000187778; Expressed in apex of heart and 196 other tissues.
DR ExpressionAtlas; Q96EZ8; baseline and differential.
DR Genevisible; Q96EZ8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR GO; GO:0044545; C:NSL complex; IDA:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0005844; C:polysome; ISS:UniProtKB.
DR GO; GO:0002151; F:G-quadruplex RNA binding; IDA:UniProtKB.
DR GO; GO:0034046; F:poly(G) binding; IDA:UniProtKB.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:UniProtKB.
DR GO; GO:0010521; F:telomerase inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
DR GO; GO:0051974; P:negative regulation of telomerase activity; IDA:BHF-UCL.
DR GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; IDA:BHF-UCL.
DR GO; GO:0045739; P:positive regulation of DNA repair; IEA:Ensembl.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IDA:ComplexPortal.
DR GO; GO:1904751; P:positive regulation of protein localization to nucleolus; IDA:UniProtKB.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0033044; P:regulation of chromosome organization; IMP:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:ComplexPortal.
DR GO; GO:0060382; P:regulation of DNA strand elongation; IMP:ComplexPortal.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IEA:Ensembl.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
DR GO; GO:0000723; P:telomere maintenance; IEA:Ensembl.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR037912; MCRS1.
DR InterPro; IPR025999; MCRS_N.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR13233; PTHR13233; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF13325; MCRS_N; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromatin regulator; Coiled coil;
KW Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW Host-virus interaction; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..462
FT /note="Microspherule protein 1"
FT /id="PRO_0000096305"
FT DOMAIN 363..419
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 1..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 301..335
FT /evidence="ECO:0000255"
FT MOTIF 113..123
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 9..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99L90"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 130
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..191
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_054571"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9765390"
FT /id="VSP_016259"
FT VAR_SEQ 1..3
FT /note="MDK -> MTRGTGGTAQRGRSGP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15044100"
FT /id="VSP_016260"
FT VARIANT 441
FT /note="V -> I (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs780785469)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035473"
FT CONFLICT 245
FT /note="A -> G (in Ref. 1; AAC52086)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 51803 MW; F6B7CC8A2AAF16BC CRC64;
MDKDSQGLLD SSLMASGTAS RSEDEESLAG QKRASSQALG TIPKRRSSSR FIKRKKFDDE
LVESSLAKSS TRAKGASGVE PGRCSGSEPS SSEKKKVSKA PSTPVPPSPA PAPGLTKRVK
KSKQPLQVTK DLGRWKPADD LLLINAVLQT NDLTSVHLGV KFSCRFTLRE VQERWYALLY
DPVISKLACQ AMRQLHPEAI AAIQSKALFS KAEEQLLSKV GSTSQPTLET FQDLLHRHPD
AFYLARTAKA LQAHWQLMKQ YYLLEDQTVQ PLPKGDQVLN FSDAEDLIDD SKLKDMRDEV
LEHELMVADR RQKREIRQLE QELHKWQVLV DSITGMSSPD FDNQTLAVLR GRMVRYLMRS
REITLGRATK DNQIDVDLSL EGPAWKISRK QGVIKLKNNG DFFIANEGRR PIYIDGRPVL
CGSKWRLSNN SVVEIASLRF VFLINQDLIA LIRAEAAKIT PQ
