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Q96EZ8 (MCRS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microspherule protein 1
Alternative name(s):
58 kDa microspherule protein
Cell cycle-regulated factor p78
INO80 complex subunit J
MCRS2
Gene names
Name:MCRS1
Synonyms:INO80Q, MSP58
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Modulates the transcription repressor activity of DAXX by recruiting it to the nucleolus. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. 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. Ref.3 Ref.5 Ref.15

Subunit structure

Binds to NOP2, DAXX, PINX1, TERT and Herpes simplex virus ICP22. Interacts with CCDC85B. Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the N-terminus of INO80. 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. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. Ref.1 Ref.2 Ref.3 Ref.6 Ref.7 Ref.8 Ref.10 Ref.15 Ref.17

Subcellular location

Nucleus. Nucleusnucleolus. Note: In microspherules in the nucleolus. Ref.1 Ref.3 Ref.10 Ref.15

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 similarities

Contains 1 FHA domain.

Sequence caution

The sequence AAC68599.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   Molecular functionChromatin regulator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

DNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

cellular protein modification process

Traceable author statement Ref.2. Source: ProtInc

chromatin organization

Traceable author statement. Source: Reactome

histone H4-K16 acetylation

Inferred from direct assay Ref.15. Source: UniProtKB

histone H4-K5 acetylation

Inferred from direct assay Ref.15. Source: UniProtKB

histone H4-K8 acetylation

Inferred from direct assay Ref.15. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentIno80 complex

Inferred from direct assay Ref.17. Source: UniProtKB

MLL1 complex

Inferred from direct assay Ref.6. Source: UniProtKB

cytoplasm

Traceable author statement Ref.2. Source: ProtInc

histone acetyltransferase complex

Inferred from direct assay Ref.15. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96EZ8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q96EZ8-2)

Also known as: MCRS2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MDK → MTRGTGGTAQRGRSGP
Isoform 3 (identifier: Q96EZ8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: Missing.
Note: No experimental confirmation available. May be due to intron retention.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462Microspherule protein 1
PRO_0000096305

Regions

Domain363 – 41957FHA
Coiled coil301 – 33535 Potential
Motif113 – 12311Nuclear localization signal Potential
Compositional bias11 – 10292Ser-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.19
Modified residue221Phosphoserine Ref.16
Modified residue1031Phosphothreonine Ref.9
Modified residue1081Phosphoserine Ref.9 Ref.11 Ref.13 Ref.16
Modified residue1231N6-acetyllysine Ref.14
Modified residue1301N6-acetyllysine Ref.14
Modified residue2821Phosphoserine Ref.11 Ref.13 Ref.16 Ref.18

Natural variations

Alternative sequence1 – 1313Missing in isoform 3.
VSP_016259
Alternative sequence1 – 33MDK → MTRGTGGTAQRGRSGP in isoform 2.
VSP_016260
Natural variant4411V → I in a colorectal cancer sample; somatic mutation. Ref.20
VAR_035473

Experimental info

Sequence conflict2451A → G in AAC52086. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: F6B7CC8A2AAF16BC

FASTA46251,803
        10         20         30         40         50         60 
MDKDSQGLLD SSLMASGTAS RSEDEESLAG QKRASSQALG TIPKRRSSSR FIKRKKFDDE 

        70         80         90        100        110        120 
LVESSLAKSS TRAKGASGVE PGRCSGSEPS SSEKKKVSKA PSTPVPPSPA PAPGLTKRVK 

       130        140        150        160        170        180 
KSKQPLQVTK DLGRWKPADD LLLINAVLQT NDLTSVHLGV KFSCRFTLRE VQERWYALLY 

       190        200        210        220        230        240 
DPVISKLACQ AMRQLHPEAI AAIQSKALFS KAEEQLLSKV GSTSQPTLET FQDLLHRHPD 

       250        260        270        280        290        300 
AFYLARTAKA LQAHWQLMKQ YYLLEDQTVQ PLPKGDQVLN FSDAEDLIDD SKLKDMRDEV 

       310        320        330        340        350        360 
LEHELMVADR RQKREIRQLE QELHKWQVLV DSITGMSSPD FDNQTLAVLR GRMVRYLMRS 

       370        380        390        400        410        420 
REITLGRATK DNQIDVDLSL EGPAWKISRK QGVIKLKNNG DFFIANEGRR PIYIDGRPVL 

       430        440        450        460 
CGSKWRLSNN SVVEIASLRF VFLINQDLIA LIRAEAAKIT PQ 

« Hide

Isoform 2 (MCRS2) [UniParc].

Checksum: 5ABAFCB412408F76
Show »

FASTA47553,001
Isoform 3 [UniParc].

Checksum: 46DB62C0D3158EC1
Show »

FASTA44950,413

References

« Hide 'large scale' references
[1]"The 58-kDa microspherule protein (MSP58), a nucleolar protein, interacts with nucleolar protein p120."
Ren Y., Busch R.K., Perlaky L., Busch H.
Eur. J. Biochem. 253:734-742(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH NOP2, SUBCELLULAR LOCATION.
Tissue: Cervix carcinoma.
[2]"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."
Bruni R., Roizman B.
J. Virol. 72:8525-8531(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH ICP22.
Tissue: Cervix carcinoma.
[3]"Human MCRS2, a cell-cycle-dependent protein, associates with LPTS/PinX1 and reduces the telomere length."
Song H., Li Y., Chen G., Xing Z., Zhao J., Yokoyama K.K., Li T., Zhao M.
Biochem. Biophys. Res. Commun. 316:1116-1123(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, INTERACTION WITH PINX1 AND TERT, FUNCTION.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Uterus.
[5]"Essential role of the 58-kDa microspherule protein in the modulation of Daxx-dependent transcriptional repression as revealed by nucleolar sequestration."
Lin D.-Y., Shih H.-M.
J. Biol. Chem. 277:25446-25456(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
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.
Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
[7]"A mammalian chromatin remodeling complex with similarities to the yeast INO80 complex."
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.
J. Biol. Chem. 280:41207-41212(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"DIPA, which can localize to the centrosome, associates with p78/MCRS1/MSP58 and acts as a repressor of gene transcription."
Du X., Wang Q., Hirohashi Y., Greene M.I.
Exp. Mol. Pathol. 81:184-190(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CCDC85B.
[9]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-103 AND SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complex."
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.
Mol. Cell 31:909-917(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE INO80 COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-282, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-282, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123 AND LYS-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex."
Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L., Washburn M.P., Conaway J.W., Conaway R.C.
J. Biol. Chem. 285:4268-4272(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, SUBCELLULAR LOCATION.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-108 AND SER-282, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Subunit organization of the human INO80 chromatin remodeling complex: An evolutionarily conserved core complex catalyzes ATP-dependent nucleosome remodeling."
Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P., Conaway J.W., Conaway R.C.
J. Biol. Chem. 286:11283-11289(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE INO80 COMPLEX.
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"The consensus coding sequences of human breast and colorectal cancers."
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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-441.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF015308 mRNA. Translation: AAC52086.1.
AF068007 mRNA. Translation: AAC68599.1. Frameshift.
AY336730 mRNA. Translation: AAQ84517.1.
BC011794 mRNA. Translation: AAH11794.1.
RefSeqNP_001012300.1. NM_001012300.1.
NP_001265270.1. NM_001278341.1.
NP_006328.2. NM_006337.4.
XP_005268629.1. XM_005268572.1.
UniGeneHs.25313.

3D structure databases

ProteinModelPortalQ96EZ8.
SMRQ96EZ8. Positions 345-444.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115710. 52 interactions.
IntActQ96EZ8. 38 interactions.
MINTMINT-1033866.
STRING9606.ENSP00000349640.

PTM databases

PhosphoSiteQ96EZ8.

Polymorphism databases

DMDM24638035.

Proteomic databases

PaxDbQ96EZ8.
PRIDEQ96EZ8.

Protocols and materials databases

DNASU10445.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343810; ENSP00000345358; ENSG00000187778. [Q96EZ8-1]
ENST00000357123; ENSP00000349640; ENSG00000187778. [Q96EZ8-2]
ENST00000550165; ENSP00000448056; ENSG00000187778. [Q96EZ8-1]
GeneID10445.
KEGGhsa:10445.
UCSCuc001rui.1. human. [Q96EZ8-2]
uc001ruj.2. human. [Q96EZ8-1]

Organism-specific databases

CTD10445.
GeneCardsGC12M049952.
HGNCHGNC:6960. MCRS1.
HPAHPA039057.
MIM609504. gene.
neXtProtNX_Q96EZ8.
PharmGKBPA30708.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG287326.
HOGENOMHOG000007227.
HOVERGENHBG052434.
KOK11674.
OMANKWKLNN.
PhylomeDBQ96EZ8.
TreeFamTF318119.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.

Gene expression databases

ArrayExpressQ96EZ8.
BgeeQ96EZ8.
CleanExHS_MCRS1.
GenevestigatorQ96EZ8.

Family and domain databases

Gene3D2.60.200.20. 1 hit.
InterProIPR000253. FHA_dom.
IPR025999. MCRS_N.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamPF00498. FHA. 1 hit.
PF13325. MCRS_N. 1 hit.
[Graphical view]
SMARTSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
PROSITEPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMCRS1. human.
GeneWikiMCRS1.
GenomeRNAi10445.
NextBio39587.
PROQ96EZ8.
SOURCESearch...

Entry information

Entry nameMCRS1_HUMAN
AccessionPrimary (citable) accession number: Q96EZ8
Secondary accession number(s): O14742, O75497, Q6VN53
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM