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Q96EZ8

- MCRS1_HUMAN

UniProt

Q96EZ8 - MCRS1_HUMAN

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Protein

Microspherule protein 1

Gene

MCRS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 - 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ96EZ8.
CleanExiHS_MCRS1.
ExpressionAtlasiQ96EZ8. baseline and differential.
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. 53 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.
GeneTreeiENSGT00390000005536.
HOGENOMiHOG000007227.
HOVERGENiHBG052434.
InParanoidiQ96EZ8.
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

        10         20         30         40         50
MDKDSQGLLD SSLMASGTAS RSEDEESLAG QKRASSQALG TIPKRRSSSR
60 70 80 90 100
FIKRKKFDDE LVESSLAKSS TRAKGASGVE PGRCSGSEPS SSEKKKVSKA
110 120 130 140 150
PSTPVPPSPA PAPGLTKRVK KSKQPLQVTK DLGRWKPADD LLLINAVLQT
160 170 180 190 200
NDLTSVHLGV KFSCRFTLRE VQERWYALLY DPVISKLACQ AMRQLHPEAI
210 220 230 240 250
AAIQSKALFS KAEEQLLSKV GSTSQPTLET FQDLLHRHPD AFYLARTAKA
260 270 280 290 300
LQAHWQLMKQ YYLLEDQTVQ PLPKGDQVLN FSDAEDLIDD SKLKDMRDEV
310 320 330 340 350
LEHELMVADR RQKREIRQLE QELHKWQVLV DSITGMSSPD FDNQTLAVLR
360 370 380 390 400
GRMVRYLMRS REITLGRATK DNQIDVDLSL EGPAWKISRK QGVIKLKNNG
410 420 430 440 450
DFFIANEGRR PIYIDGRPVL CGSKWRLSNN SVVEIASLRF VFLINQDLIA
460
LIRAEAAKIT PQ
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. 53 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.
GeneTreei ENSGT00390000005536.
HOGENOMi HOG000007227.
HOVERGENi HBG052434.
InParanoidi Q96EZ8.
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

Bgeei Q96EZ8.
CleanExi HS_MCRS1.
ExpressionAtlasi Q96EZ8. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 126 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