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Microspherule protein 1 (58 kDa microspherule protein) (Cell cycle-regulated factor p78) (INO80 complex subunit J) (MCRS2)

 MCRS1_HUMAN             Reviewed;         462 AA.
Q96EZ8; O14742; O75497; Q6VN53; Q7Z372;
01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
27-SEP-2017, entry version 155.
RecName: Full=Microspherule protein 1;
AltName: Full=58 kDa microspherule protein;
AltName: Full=Cell cycle-regulated factor p78;
AltName: Full=INO80 complex subunit J;
AltName: Full=MCRS2;
Name=MCRS1; Synonyms=INO80Q, MSP58;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH NOP2, AND
SUBCELLULAR LOCATION.
TISSUE=Cervix carcinoma;
PubMed=9654073; DOI=10.1046/j.1432-1327.1998.2530734.x;
Ren Y., Busch R.K., Perlaky L., Busch H.;
"The 58-kDa microspherule protein (MSP58), a nucleolar protein,
interacts with nucleolar protein p120.";
Eur. J. Biochem. 253:734-742(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND INTERACTION WITH ICP22.
TISSUE=Cervix carcinoma;
PubMed=9765390;
Bruni R., Roizman B.;
"Herpes simplex virus 1 regulatory protein ICP22 interacts with a new
cell cycle-regulated factor and accumulates in a cell cycle-dependent
fashion in infected cells.";
J. Virol. 72:8525-8531(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION,
INTERACTION WITH PINX1 AND TERT, AND FUNCTION.
PubMed=15044100; DOI=10.1016/j.bbrc.2004.02.166;
Song H., Li Y., Chen G., Xing Z., Zhao J., Yokoyama K.K., Li T.,
Zhao M.;
"Human MCRS2, a cell-cycle-dependent protein, associates with
LPTS/PinX1 and reduces the telomere length.";
Biochem. Biophys. Res. Commun. 316:1116-1123(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Rectum tumor;
The German cDNA Consortium;
Bloecker H., Boecher M., Brandt P., Mewes H.W., Weil B., Amid C.,
Osanger A., Fobo G., Han M., Wiemann S.;
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, AND INTERACTION WITH DAXX.
PubMed=11948183; DOI=10.1074/jbc.M200633200;
Lin D.-Y., Shih H.-M.;
"Essential role of the 58-kDa microspherule protein in the modulation
of Daxx-dependent transcriptional repression as revealed by nucleolar
sequestration.";
J. Biol. Chem. 277:25446-25456(2002).
[9]
IDENTIFICATION IN THE MLL1/MLL COMPLEX.
PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
"Physical association and coordinate function of the H3 K4
methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
Cell 121:873-885(2005).
[10]
IDENTIFICATION IN INO80 COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=16230350; DOI=10.1074/jbc.M509128200;
Jin J., Cai Y., Yao T., Gottschalk A.J., Florens L., Swanson S.K.,
Gutierrez J.L., Coleman M.K., Workman J.L., Mushegian A.,
Washburn M.P., Conaway R.C., Conaway J.W.;
"A mammalian chromatin remodeling complex with similarities to the
yeast INO80 complex.";
J. Biol. Chem. 280:41207-41212(2005).
[11]
INTERACTION WITH CCDC85B.
PubMed=17014843; DOI=10.1016/j.yexmp.2006.07.008;
Du X., Wang Q., Hirohashi Y., Greene M.I.;
"DIPA, which can localize to the centrosome, associates with
p78/MCRS1/MSP58 and acts as a repressor of gene transcription.";
Exp. Mol. Pathol. 81:184-190(2006).
[12]
INTERACTION WITH FMR1; FXR1 AND FXR2, RNA-BINDING, AND SUBCELLULAR
LOCATION.
PubMed=16571602; DOI=10.1093/hmg/ddl074;
Davidovic L., Bechara E., Gravel M., Jaglin X.H., Tremblay S., Sik A.,
Bardoni B., Khandjian E.W.;
"The nuclear microspherule protein 58 is a novel RNA-binding protein
that interacts with fragile X mental retardation protein in
polyribosomal mRNPs from neurons.";
Hum. Mol. Genet. 15:1525-1538(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-103 AND SER-108, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[14]
IDENTIFICATION IN THE INO80 COMPLEX, SUBCELLULAR LOCATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18922472; DOI=10.1016/j.molcel.2008.08.027;
Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K.,
Washburn M.P., Florens L., Conaway R.C., Cohen R.E., Conaway J.W.;
"Distinct modes of regulation of the Uch37 deubiquitinating enzyme in
the proteasome and in the Ino80 chromatin-remodeling complex.";
Mol. Cell 31:909-917(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-282, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-282, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123 AND LYS-130, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[19]
FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, AND
SUBCELLULAR LOCATION.
PubMed=20018852; DOI=10.1074/jbc.C109.087981;
Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L.,
Washburn M.P., Conaway J.W., Conaway R.C.;
"Subunit composition and substrate specificity of a MOF-containing
histone acetyltransferase distinct from the male-specific lethal (MSL)
complex.";
J. Biol. Chem. 285:4268-4272(2010).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-108 AND SER-282,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
IDENTIFICATION IN THE INO80 COMPLEX.
PubMed=21303910; DOI=10.1074/jbc.M111.222505;
Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P.,
Conaway J.W., Conaway R.C.;
"Subunit organization of the human INO80 chromatin remodeling complex:
An evolutionarily conserved core complex catalyzes ATP-dependent
nucleosome remodeling.";
J. Biol. Chem. 286:11283-11289(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-282, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
VARIANT [LARGE SCALE ANALYSIS] ILE-441.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Modulates the transcription repressor activity of DAXX
by recruiting it to the nucleolus (PubMed:11948183). As part of
the NSL complex it may be involved in acetylation of nucleosomal
histone H4 on several lysine residues (PubMed:20018852). Putative
regulatory component of the chromatin remodeling INO80 complex
which is involved in transcriptional regulation, DNA replication
and probably DNA repair. May also be an inhibitor of TERT
telomerase activity (PubMed:15044100). Binds to G-quadruplex
structures in mRNA (PubMed:16571602). Binds to RNA homopolymer
poly(G) and poly(U) (PubMed:16571602).
{ECO:0000269|PubMed:11948183, ECO:0000269|PubMed:15044100,
ECO:0000269|PubMed:16571602, ECO:0000269|PubMed:20018852}.
-!- SUBUNIT: Component of the chromatin remodeling INO80 complex;
specifically part of a complex module associated with the N-
terminus of INO80 (PubMed:16230350, PubMed:18922472,
PubMed:21303910). Component of some MLL1/MLL complex, at least
composed of the core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and
RBBP5, as well as the facultative components BAP18, CHD8, E2F6,
HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1,
PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1,
TAF4, TAF6, TAF7, TAF9 and TEX10 (PubMed:15960975). Component of
the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2,
KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 (PubMed:20018852).
Interacts with NOP2 (PubMed:9654073). Interacts with PINX1
(PubMed:15044100). Interacts with TERT (PubMed:15044100).
Interacts with CCDC85B (PubMed:17014843). Interacts with DAXX
(PubMed:11948183). Interacts (via N-terminus) with FMR1 (via
phosphorylated form) (PubMed:16571602). Interacts with FXR1 AND
FXR2 (PubMed:16571602). {ECO:0000269|PubMed:11948183,
ECO:0000269|PubMed:15044100, ECO:0000269|PubMed:15960975,
ECO:0000269|PubMed:16230350, ECO:0000269|PubMed:16571602,
ECO:0000269|PubMed:17014843, ECO:0000269|PubMed:18922472,
ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:21303910,
ECO:0000269|PubMed:9654073}.
-!- SUBUNIT: (Microbial infection) Interacts with Herpes simplex virus
ICP22. {ECO:0000269|PubMed:9765390}.
-!- INTERACTION:
Q6ZUT1:C11orf57; NbExp=4; IntAct=EBI-348259, EBI-3920396;
Q96GN5:CDCA7L; NbExp=4; IntAct=EBI-348259, EBI-5278764;
Q9C0F1:CEP44; NbExp=3; IntAct=EBI-348259, EBI-744115;
Q9UER7:DAXX; NbExp=10; IntAct=EBI-348259, EBI-77321;
P51116:FXR2; NbExp=3; IntAct=EBI-348259, EBI-740459;
Q86WP2:GPBP1; NbExp=4; IntAct=EBI-348259, EBI-2349758;
Q6NT76:HMBOX1; NbExp=4; IntAct=EBI-348259, EBI-2549423;
Q13422:IKZF1; NbExp=3; IntAct=EBI-348259, EBI-745305;
Q8NBZ0:INO80E; NbExp=7; IntAct=EBI-348259, EBI-769401;
Q8N8K9:KIAA1958; NbExp=3; IntAct=EBI-348259, EBI-10181113;
Q9BQD3:KXD1; NbExp=3; IntAct=EBI-348259, EBI-739657;
P43360:MAGEA6; NbExp=4; IntAct=EBI-348259, EBI-1045155;
Q99683:MAP3K5; NbExp=3; IntAct=EBI-348259, EBI-476263;
Q9NPJ6:MED4; NbExp=5; IntAct=EBI-348259, EBI-394607;
Q8IXK0:PHC2; NbExp=2; IntAct=EBI-348259, EBI-713786;
Q96KQ4:PPP1R13B; NbExp=4; IntAct=EBI-348259, EBI-1105153;
Q15276:RABEP1; NbExp=4; IntAct=EBI-348259, EBI-447043;
O94972:TRIM37; NbExp=4; IntAct=EBI-348259, EBI-741602;
Q8N6Y0:USHBP1; NbExp=5; IntAct=EBI-348259, EBI-739895;
Q9Y3C0:WASHC3; NbExp=8; IntAct=EBI-348259, EBI-712969;
Q9Y2W2:WBP11; NbExp=3; IntAct=EBI-348259, EBI-714455;
O15209:ZBTB22; NbExp=5; IntAct=EBI-348259, EBI-723574;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15044100,
ECO:0000269|PubMed:16571602, ECO:0000269|PubMed:18922472,
ECO:0000269|PubMed:20018852}. Nucleus, nucleolus
{ECO:0000269|PubMed:16571602, ECO:0000269|PubMed:9654073}.
Cytoplasm {ECO:0000269|PubMed:16571602}. Note=In microspherules in
the nucleolus. {ECO:0000269|PubMed:9654073}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q96EZ8-1; Sequence=Displayed;
Name=2; Synonyms=MCRS2;
IsoId=Q96EZ8-2; Sequence=VSP_016260;
Name=3;
IsoId=Q96EZ8-3; Sequence=VSP_016259;
Note=No experimental confirmation available. May be due to
intron retention.;
Name=4;
IsoId=Q96EZ8-4; Sequence=VSP_054571;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in testis, and at lower levels in
spleen, thymus, prostate, uterus, small intestine, colon and
leukocytes.
-!- DEVELOPMENTAL STAGE: Cell-cycle regulated: levels are highest
early in S phase; not detectable in G2.
-!- SEQUENCE CAUTION:
Sequence=AAC68599.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
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EMBL; AF015308; AAC52086.1; -; mRNA.
EMBL; AF068007; AAC68599.1; ALT_FRAME; mRNA.
EMBL; AY336730; AAQ84517.1; -; mRNA.
EMBL; BX538079; CAD98003.1; -; mRNA.
EMBL; AC020612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471111; EAW58078.1; -; Genomic_DNA.
EMBL; BC011794; AAH11794.1; -; mRNA.
CCDS; CCDS31795.1; -. [Q96EZ8-2]
CCDS; CCDS61118.1; -. [Q96EZ8-4]
CCDS; CCDS8787.1; -. [Q96EZ8-1]
RefSeq; NP_001012300.1; NM_001012300.1. [Q96EZ8-2]
RefSeq; NP_001265270.1; NM_001278341.1. [Q96EZ8-4]
RefSeq; NP_006328.2; NM_006337.4. [Q96EZ8-1]
RefSeq; XP_005268629.1; XM_005268572.3. [Q96EZ8-1]
RefSeq; XP_016874178.1; XM_017018689.1. [Q96EZ8-2]
RefSeq; XP_016874179.1; XM_017018690.1. [Q96EZ8-2]
UniGene; Hs.25313; -.
ProteinModelPortal; Q96EZ8; -.
BioGrid; 115710; 77.
CORUM; Q96EZ8; -.
IntAct; Q96EZ8; 124.
MINT; MINT-1033866; -.
STRING; 9606.ENSP00000349640; -.
iPTMnet; Q96EZ8; -.
PhosphoSitePlus; Q96EZ8; -.
SwissPalm; Q96EZ8; -.
BioMuta; MCRS1; -.
DMDM; 24638035; -.
EPD; Q96EZ8; -.
MaxQB; Q96EZ8; -.
PaxDb; Q96EZ8; -.
PeptideAtlas; Q96EZ8; -.
PRIDE; Q96EZ8; -.
DNASU; 10445; -.
Ensembl; ENST00000343810; ENSP00000345358; ENSG00000187778. [Q96EZ8-1]
Ensembl; ENST00000357123; ENSP00000349640; ENSG00000187778. [Q96EZ8-2]
Ensembl; ENST00000546244; ENSP00000444982; ENSG00000187778. [Q96EZ8-4]
Ensembl; ENST00000550165; ENSP00000448056; ENSG00000187778. [Q96EZ8-1]
GeneID; 10445; -.
KEGG; hsa:10445; -.
UCSC; uc001rui.3; human. [Q96EZ8-1]
CTD; 10445; -.
DisGeNET; 10445; -.
EuPathDB; HostDB:ENSG00000187778.13; -.
GeneCards; MCRS1; -.
HGNC; HGNC:6960; MCRS1.
HPA; HPA039057; -.
MIM; 609504; gene.
neXtProt; NX_Q96EZ8; -.
OpenTargets; ENSG00000187778; -.
PharmGKB; PA30708; -.
eggNOG; KOG2293; Eukaryota.
eggNOG; ENOG410XS0S; LUCA.
GeneTree; ENSGT00390000005536; -.
HOGENOM; HOG000007227; -.
HOVERGEN; HBG052434; -.
InParanoid; Q96EZ8; -.
KO; K11674; -.
OMA; FLVNYEL; -.
OrthoDB; EOG091G07QN; -.
PhylomeDB; Q96EZ8; -.
TreeFam; TF318119; -.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
ChiTaRS; MCRS1; human.
GeneWiki; MCRS1; -.
GenomeRNAi; 10445; -.
PRO; PR:Q96EZ8; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000187778; -.
CleanEx; HS_MCRS1; -.
ExpressionAtlas; Q96EZ8; baseline and differential.
Genevisible; Q96EZ8; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
GO; GO:0005844; C:polysome; ISS:UniProtKB.
GO; GO:0002151; F:G-quadruplex RNA binding; IDA:UniProtKB.
GO; GO:0034046; F:poly(G) binding; IDA:UniProtKB.
GO; GO:0008266; F:poly(U) RNA binding; IDA:UniProtKB.
GO; GO:0010521; F:telomerase inhibitor activity; IDA:BHF-UCL.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB.
GO; GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
GO; GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
GO; GO:0051974; P:negative regulation of telomerase activity; IDA:BHF-UCL.
GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; IDA:BHF-UCL.
GO; GO:1904751; P:positive regulation of protein localization to nucleolus; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR000253; FHA_dom.
InterPro; IPR025999; MCRS_N.
InterPro; IPR008984; SMAD_FHA_domain.
Pfam; PF00498; FHA; 1.
Pfam; PF13325; MCRS_N; 1.
SMART; SM00240; FHA; 1.
SUPFAM; SSF49879; SSF49879; 1.
PROSITE; PS50006; FHA_DOMAIN; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Chromatin regulator; Coiled coil;
Complete proteome; Cytoplasm; DNA damage; DNA recombination;
DNA repair; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Transcription; Transcription regulation.
CHAIN 1 462 Microspherule protein 1.
/FTId=PRO_0000096305.
DOMAIN 363 419 FHA. {ECO:0000255|PROSITE-
ProRule:PRU00086}.
COILED 301 335 {ECO:0000255}.
MOTIF 113 123 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 11 102 Ser-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000250|UniProtKB:Q99L90}.
MOD_RES 103 103 Phosphothreonine.
{ECO:0000244|PubMed:16964243}.
MOD_RES 108 108 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 123 123 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 130 130 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 282 282 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 191 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_054571.
VAR_SEQ 1 13 Missing (in isoform 3).
{ECO:0000303|PubMed:9765390}.
/FTId=VSP_016259.
VAR_SEQ 1 3 MDK -> MTRGTGGTAQRGRSGP (in isoform 2).
{ECO:0000303|PubMed:15044100}.
/FTId=VSP_016260.
VARIANT 441 441 V -> I (in a colorectal cancer sample;
somatic mutation; dbSNP:rs780785469).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035473.
CONFLICT 245 245 A -> G (in Ref. 1; AAC52086).
{ECO:0000305}.
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


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