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Q96EZ8

- MCRS1_HUMAN

UniProt

Q96EZ8 - MCRS1_HUMAN

Protein

Microspherule protein 1

Gene

MCRS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    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.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular protein modification process Source: ProtInc
    2. chromatin organization Source: Reactome
    3. DNA recombination Source: UniProtKB-KW
    4. DNA repair Source: UniProtKB-KW
    5. histone H4-K16 acetylation Source: UniProtKB
    6. histone H4-K5 acetylation Source: UniProtKB
    7. histone H4-K8 acetylation Source: UniProtKB
    8. regulation of transcription, DNA-templated Source: UniProtKB-KW
    9. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Microspherule protein 1
    Alternative name(s):
    58 kDa microspherule protein
    Cell cycle-regulated factor p78
    INO80 complex subunit J
    MCRS2
    Gene namesi
    Name:MCRS1
    Synonyms:INO80Q, MSP58
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:6960. MCRS1.

    Subcellular locationi

    Nucleus. Nucleusnucleolus
    Note: In microspherules in the nucleolus.

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. histone acetyltransferase complex Source: UniProtKB
    3. Ino80 complex Source: UniProtKB
    4. MLL1 complex Source: UniProtKB
    5. nucleoplasm Source: Reactome
    6. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30708.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 462462Microspherule protein 1PRO_0000096305Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei22 – 221Phosphoserine1 Publication
    Modified residuei103 – 1031Phosphothreonine1 Publication
    Modified residuei108 – 1081Phosphoserine4 Publications
    Modified residuei123 – 1231N6-acetyllysine1 Publication
    Modified residuei130 – 1301N6-acetyllysine1 Publication
    Modified residuei282 – 2821Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96EZ8.
    PaxDbiQ96EZ8.
    PRIDEiQ96EZ8.

    PTM databases

    PhosphoSiteiQ96EZ8.

    Expressioni

    Tissue specificityi

    Detected in testis, and at lower levels in spleen, thymus, prostate, uterus, small intestine, colon and leukocytes.

    Developmental stagei

    Cell-cycle regulated: levels are highest early in S phase; not detectable in G2.

    Gene expression databases

    ArrayExpressiQ96EZ8.
    BgeeiQ96EZ8.
    CleanExiHS_MCRS1.
    GenevestigatoriQ96EZ8.

    Organism-specific databases

    HPAiHPA039057.

    Interactioni

    Subunit structurei

    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 HCFC1.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCDC53Q9Y3C03EBI-348259,EBI-712969
    DAXXQ9UER78EBI-348259,EBI-77321
    MAP3K5Q996833EBI-348259,EBI-476263
    PHC2Q8IXK02EBI-348259,EBI-713786

    Protein-protein interaction databases

    BioGridi115710. 52 interactions.
    IntActiQ96EZ8. 38 interactions.
    MINTiMINT-1033866.
    STRINGi9606.ENSP00000349640.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96EZ8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini363 – 41957FHAPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili301 – 33535Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi113 – 12311Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi11 – 10292Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 FHA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG287326.
    HOGENOMiHOG000007227.
    HOVERGENiHBG052434.
    KOiK11674.
    OMAiNKWKLNN.
    PhylomeDBiQ96EZ8.
    TreeFamiTF318119.

    Family and domain databases

    Gene3Di2.60.200.20. 1 hit.
    InterProiIPR000253. FHA_dom.
    IPR025999. MCRS_N.
    IPR008984. SMAD_FHA_domain.
    [Graphical view]
    PfamiPF00498. FHA. 1 hit.
    PF13325. MCRS_N. 1 hit.
    [Graphical view]
    SMARTiSM00240. FHA. 1 hit.
    [Graphical view]
    SUPFAMiSSF49879. SSF49879. 1 hit.
    PROSITEiPS50006. FHA_DOMAIN. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96EZ8-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MDKDSQGLLD SSLMASGTAS RSEDEESLAG QKRASSQALG TIPKRRSSSR    50
    FIKRKKFDDE LVESSLAKSS TRAKGASGVE PGRCSGSEPS SSEKKKVSKA 100
    PSTPVPPSPA PAPGLTKRVK KSKQPLQVTK DLGRWKPADD LLLINAVLQT 150
    NDLTSVHLGV KFSCRFTLRE VQERWYALLY DPVISKLACQ AMRQLHPEAI 200
    AAIQSKALFS KAEEQLLSKV GSTSQPTLET FQDLLHRHPD AFYLARTAKA 250
    LQAHWQLMKQ YYLLEDQTVQ PLPKGDQVLN FSDAEDLIDD SKLKDMRDEV 300
    LEHELMVADR RQKREIRQLE QELHKWQVLV DSITGMSSPD FDNQTLAVLR 350
    GRMVRYLMRS REITLGRATK DNQIDVDLSL EGPAWKISRK QGVIKLKNNG 400
    DFFIANEGRR PIYIDGRPVL CGSKWRLSNN SVVEIASLRF VFLINQDLIA 450
    LIRAEAAKIT PQ 462
    Length:462
    Mass (Da):51,803
    Last modified:December 1, 2001 - v1
    Checksum:iF6B7CC8A2AAF16BC
    GO
    Isoform 2 (identifier: Q96EZ8-2) [UniParc]FASTAAdd to Basket

    Also known as: MCRS2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3: MDK → MTRGTGGTAQRGRSGP

    Show »
    Length:475
    Mass (Da):53,001
    Checksum:i5ABAFCB412408F76
    GO
    Isoform 3 (identifier: Q96EZ8-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:449
    Mass (Da):50,413
    Checksum:i46DB62C0D3158EC1
    GO
    Isoform 4 (identifier: Q96EZ8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-191: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:271
    Mass (Da):31,134
    Checksum:i9B6338AC1B6BAF5E
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti245 – 2451A → G in AAC52086. (PubMed:9654073)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti441 – 4411V → I in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035473

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 191191Missing in isoform 4. CuratedVSP_054571Add
    BLAST
    Alternative sequencei1 – 1313Missing in isoform 3. 1 PublicationVSP_016259Add
    BLAST
    Alternative sequencei1 – 33MDK → MTRGTGGTAQRGRSGP in isoform 2. 1 PublicationVSP_016260

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF015308 mRNA. Translation: AAC52086.1.
    AF068007 mRNA. Translation: AAC68599.1. Frameshift.
    AY336730 mRNA. Translation: AAQ84517.1.
    BX538079 mRNA. Translation: CAD98003.1.
    AC020612 Genomic DNA. No translation available.
    CH471111 Genomic DNA. Translation: EAW58078.1.
    BC011794 mRNA. Translation: AAH11794.1.
    CCDSiCCDS31795.1. [Q96EZ8-2]
    CCDS61118.1. [Q96EZ8-4]
    CCDS8787.1. [Q96EZ8-1]
    RefSeqiNP_001012300.1. NM_001012300.1. [Q96EZ8-2]
    NP_001265270.1. NM_001278341.1. [Q96EZ8-4]
    NP_006328.2. NM_006337.4. [Q96EZ8-1]
    XP_005268629.1. XM_005268572.1. [Q96EZ8-1]
    UniGeneiHs.25313.

    Genome annotation databases

    EnsembliENST00000343810; ENSP00000345358; ENSG00000187778. [Q96EZ8-1]
    ENST00000357123; ENSP00000349640; ENSG00000187778. [Q96EZ8-2]
    ENST00000546244; ENSP00000444982; ENSG00000187778. [Q96EZ8-4]
    ENST00000550165; ENSP00000448056; ENSG00000187778. [Q96EZ8-1]
    GeneIDi10445.
    KEGGihsa:10445.
    UCSCiuc001rui.1. human. [Q96EZ8-2]
    uc001ruj.2. human. [Q96EZ8-1]

    Polymorphism databases

    DMDMi24638035.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF015308 mRNA. Translation: AAC52086.1 .
    AF068007 mRNA. Translation: AAC68599.1 . Frameshift.
    AY336730 mRNA. Translation: AAQ84517.1 .
    BX538079 mRNA. Translation: CAD98003.1 .
    AC020612 Genomic DNA. No translation available.
    CH471111 Genomic DNA. Translation: EAW58078.1 .
    BC011794 mRNA. Translation: AAH11794.1 .
    CCDSi CCDS31795.1. [Q96EZ8-2 ]
    CCDS61118.1. [Q96EZ8-4 ]
    CCDS8787.1. [Q96EZ8-1 ]
    RefSeqi NP_001012300.1. NM_001012300.1. [Q96EZ8-2 ]
    NP_001265270.1. NM_001278341.1. [Q96EZ8-4 ]
    NP_006328.2. NM_006337.4. [Q96EZ8-1 ]
    XP_005268629.1. XM_005268572.1. [Q96EZ8-1 ]
    UniGenei Hs.25313.

    3D structure databases

    ProteinModelPortali Q96EZ8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115710. 52 interactions.
    IntActi Q96EZ8. 38 interactions.
    MINTi MINT-1033866.
    STRINGi 9606.ENSP00000349640.

    PTM databases

    PhosphoSitei Q96EZ8.

    Polymorphism databases

    DMDMi 24638035.

    Proteomic databases

    MaxQBi Q96EZ8.
    PaxDbi Q96EZ8.
    PRIDEi Q96EZ8.

    Protocols and materials databases

    DNASUi 10445.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343810 ; ENSP00000345358 ; ENSG00000187778 . [Q96EZ8-1 ]
    ENST00000357123 ; ENSP00000349640 ; ENSG00000187778 . [Q96EZ8-2 ]
    ENST00000546244 ; ENSP00000444982 ; ENSG00000187778 . [Q96EZ8-4 ]
    ENST00000550165 ; ENSP00000448056 ; ENSG00000187778 . [Q96EZ8-1 ]
    GeneIDi 10445.
    KEGGi hsa:10445.
    UCSCi uc001rui.1. human. [Q96EZ8-2 ]
    uc001ruj.2. human. [Q96EZ8-1 ]

    Organism-specific databases

    CTDi 10445.
    GeneCardsi GC12M049952.
    HGNCi HGNC:6960. MCRS1.
    HPAi HPA039057.
    MIMi 609504. gene.
    neXtProti NX_Q96EZ8.
    PharmGKBi PA30708.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG287326.
    HOGENOMi HOG000007227.
    HOVERGENi HBG052434.
    KOi K11674.
    OMAi NKWKLNN.
    PhylomeDBi Q96EZ8.
    TreeFami TF318119.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi MCRS1. human.
    GeneWikii MCRS1.
    GenomeRNAii 10445.
    NextBioi 39587.
    PROi Q96EZ8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96EZ8.
    Bgeei Q96EZ8.
    CleanExi HS_MCRS1.
    Genevestigatori Q96EZ8.

    Family and domain databases

    Gene3Di 2.60.200.20. 1 hit.
    InterProi IPR000253. FHA_dom.
    IPR025999. MCRS_N.
    IPR008984. SMAD_FHA_domain.
    [Graphical view ]
    Pfami PF00498. FHA. 1 hit.
    PF13325. MCRS_N. 1 hit.
    [Graphical view ]
    SMARTi SM00240. FHA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49879. SSF49879. 1 hit.
    PROSITEi PS50006. FHA_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Rectum tumor.
    5. "The finished DNA sequence of human chromosome 12."
      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.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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.
    8. "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.
    9. "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.
    10. Cited for: IDENTIFICATION IN INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "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.
    12. "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.
    13. "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.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-282, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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].
    16. "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.
    17. "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].
    18. "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.
    19. "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.
    20. "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.
    21. "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].
    22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-441.

    Entry informationi

    Entry nameiMCRS1_HUMAN
    AccessioniPrimary (citable) accession number: Q96EZ8
    Secondary accession number(s): O14742
    , O75497, Q6VN53, Q7Z372
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 2002
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3