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Protein

BRCA2-interacting transcriptional repressor EMSY

Gene

Emsy

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Regulator which is able to repress transcription, possibly via its interaction with a multiprotein chromatin remodeling complex that modifies the chromatin. Its interaction with BRCA2 suggests that it may play a central role in the DNA repair function of BRCA2 (By similarity). As part of a H3-specific methyltransferase complex may mediate ligand-dependent transcriptional activation by nuclear hormone receptors (By similarity).By similarity

GO - Molecular functioni

  • protein homodimerization activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
BRCA2-interacting transcriptional repressor EMSYBy similarity
Gene namesi
Name:EmsyBy similarity
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1924203. Emsy.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12641264BRCA2-interacting transcriptional repressor EMSYPRO_0000086969Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei171 – 1711PhosphothreonineBy similarity
Modified residuei173 – 1731PhosphoserineCombined sources
Modified residuei177 – 1771PhosphoserineCombined sources
Glycosylationi192 – 1921O-linked (GlcNAc)1 Publication
Glycosylationi200 – 2001O-linked (GlcNAc)By similarity
Modified residuei202 – 2021PhosphoserineBy similarity
Glycosylationi235 – 2351O-linked (GlcNAc)By similarity
Glycosylationi465 – 4651O-linked (GlcNAc)By similarity
Glycosylationi470 – 4701O-linked (GlcNAc)By similarity
Glycosylationi521 – 5211O-linked (GlcNAc)By similarity
Modified residuei782 – 7821PhosphoserineCombined sources
Modified residuei785 – 7851PhosphoserineCombined sources
Glycosylationi1069 – 10691O-linked (GlcNAc)By similarity
Modified residuei1085 – 10851PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ8BMB0.
MaxQBiQ8BMB0.
PaxDbiQ8BMB0.
PeptideAtlasiQ8BMB0.
PRIDEiQ8BMB0.

PTM databases

iPTMnetiQ8BMB0.
PhosphoSiteiQ8BMB0.

Expressioni

Gene expression databases

BgeeiQ8BMB0.
CleanExiMM_2210018M11RIK.
GenevisibleiQ8BMB0. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with the transactivation domain of BRCA2. Interacts with the chromoshadow domain of CBX1 and with HCFC1. Interacts with the viral transactivator protein VP16. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with ZMYND11.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi231423. 5 interactions.
IntActiQ8BMB0. 2 interactions.
STRINGi10090.ENSMUSP00000038216.

Structurei

3D structure databases

ProteinModelPortaliQ8BMB0.
SMRiQ8BMB0. Positions 9-126.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 11499ENTPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 442442Interaction with BRCA2By similarityAdd
BLAST
Regioni118 – 1225Interaction with ZMYND11By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi173 – 1775Poly-Ser
Compositional biasi290 – 35566Ser-richAdd
BLAST
Compositional biasi359 – 42870Gln-richAdd
BLAST
Compositional biasi460 – 600141Thr-richAdd
BLAST
Compositional biasi683 – 6875Poly-Ser
Compositional biasi895 – 1048154Gln-richAdd
BLAST

Sequence similaritiesi

Contains 1 ENT (EMSY N-terminal) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4675. Eukaryota.
ENOG410YF3T. LUCA.
GeneTreeiENSGT00390000009554.
HOGENOMiHOG000112366.
HOVERGENiHBG051476.
InParanoidiQ8BMB0.
OMAiKISMMEA.
OrthoDBiEOG7NGQBP.
PhylomeDBiQ8BMB0.
TreeFamiTF332401.

Family and domain databases

InterProiIPR033482. EMSY.
IPR005491. ENT_dom.
[Graphical view]
PANTHERiPTHR16500. PTHR16500. 1 hit.
PfamiPF03735. ENT. 1 hit.
[Graphical view]
SMARTiSM01191. ENT. 1 hit.
[Graphical view]
SUPFAMiSSF158639. SSF158639. 1 hit.
PROSITEiPS51138. ENT. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8BMB0-1) [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
MPVVWPTLLD LSRDECKRIL RKLELEAYAG VISALRAQGD LTKEKKDLLG
60 70 80 90 100
ELSKVLSIST ERHRAEVRRA VNDERLTTIA HKMNLSLYLG ERPSYSMSGP
110 120 130 140 150
NSSSEWSIEG RRLVPLMPRL VPQTAFTVTA NAVANAAVQH NASLPVPAET
160 170 180 190 200
ASKDGVSCSD EDEKPRKRRR TNSSSSSPVV LKEVPKAVVP VSKTITVPVS
210 220 230 240 250
GSPKMSNIMQ SIANSLPPHM SPVKITFTKP STQTTNTTTQ KVIIVTTSPS
260 270 280 290 300
STFVPNILSK SHNYAAVTKL VPTSVIASTT QKPPVVITAS QASLVTSSSN
310 320 330 340 350
GNSSSTSSPI SSTVAVTTVV SSTPSVVMST VAQGVSTSAI KVASTRLPSP
360 370 380 390 400
KSLVSGPTQI LAQFPKQHQQ SPKQQLQQVQ QQTQQPVAQP SSVSQQQQPQ
410 420 430 440 450
QSALPPGIKP TIQIKQESGV KIITQQVQPS KILPKPVTAT LPTSSNSPIM
460 470 480 490 500
VVSSNGAIMT TKLVTTPTGT QATYTRPTVS PSLGRVATTP GAATYVKTTS
510 520 530 540 550
GSIITVVPKS LATLGGKIIS SNIVSGTTTK ITTIPMTSKP NVIVVQKTTG
560 570 580 590 600
KGTTIQGLPG KNVVTTLLNA GGEKTLQTVP AGAKPAIITA TRPITKMIVT
610 620 630 640 650
QPKGIGSAVQ PAAKIIPTKI VYGQQGKTQV LIKPKPVTFQ ATVVSEQTRQ
660 670 680 690 700
LVTETLQQAS RVADASNSSA QEGKEEPQGY TDSSSSSTES SQSSQDSQPV
710 720 730 740 750
VHVIASRRQD WSEHEIAMET SPTIIYQDVS SESQSATSTI KALLELQQTT
760 770 780 790 800
VKEKLESKPR QPTIDLSQMA VPIQMTQEKR HSPESPSIAV VESELVAEYI
810 820 830 840 850
TTVSHRSQPQ QPSQPQRTLL QHVAQSQTAT QTSVVVKSIP ASSPGAITHI
860 870 880 890 900
MQQALSSHTA FTKHSEELGT EEGEVEEMDT LDPQTGLFYR SALTQSQSTK
910 920 930 940 950
QQKLSQPQLE QTQLQVKTLQ CFQTKQKQTI HLQADQLQHK LTQMPQLSIR
960 970 980 990 1000
HQKLNPLQQE QAQPKPDAQH TQHTVVAKDR QLPTLMAQPP QTVVQVLAVK
1010 1020 1030 1040 1050
TTQQLPKLQQ APNQPKIYVQ PQTPQSQMAL PSSEKQPASQ VEQPIITQGS
1060 1070 1080 1090 1100
SVTKITFEGR QPPTVTKITG GSSVPKLTSP VTSISPIQAS EKTAVSDILQ
1110 1120 1130 1140 1150
MSLMEAQIDT NVEHMVVDPP KKALATNVLT GEAGALPSTH VVVAGMTKCR
1160 1170 1180 1190 1200
ESCSSPSAVG PPLTTRKIEA AGVPTTGQFM RIQNVGQKKA EESPTEIIIQ
1210 1220 1230 1240 1250
AIPQYAIPCH SSSNVVVEPS GLLELNNFTS QQLDDDETAM EQDIDSSTED
1260
GTEPSPSQSA VERS
Length:1,264
Mass (Da):135,291
Last modified:May 24, 2004 - v2
Checksum:iF4BA591D43912B2A
GO
Isoform 2 (identifier: Q8BMB0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     802-802: T → TERTDEGTEVAFPLL
     1040-1199: Missing.

Note: No experimental confirmation available.
Show »
Length:1,118
Mass (Da):120,119
Checksum:iCA649C85E97E26E4
GO
Isoform 3 (identifier: Q8BMB0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     82-96: KMNLSLYLGERPSYS → N

Note: No experimental confirmation available.
Show »
Length:1,250
Mass (Da):133,665
Checksum:iCAB7FCE9DFC838FD
GO

Sequence cautioni

The sequence AAH20109.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BC039956 differs from that shown. Reason: Frameshift at position 569. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti975 – 9751V → A in BC039956 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei82 – 9615KMNLS…RPSYS → N in isoform 3. 1 PublicationVSP_010432Add
BLAST
Alternative sequencei802 – 8021T → TERTDEGTEVAFPLL in isoform 2. 1 PublicationVSP_010433
Alternative sequencei1040 – 1199160Missing in isoform 2. 1 PublicationVSP_010434Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC020109 mRNA. Translation: AAH20109.1. Different initiation.
BC039956 mRNA. No translation available.
BC089304 mRNA. Translation: AAH89304.1.
AK032985 mRNA. Translation: BAC28113.2.
CCDSiCCDS40028.1. [Q8BMB0-1]
RefSeqiNP_758484.2. NM_172280.2. [Q8BMB0-1]
XP_006507693.1. XM_006507630.2. [Q8BMB0-2]
UniGeneiMm.387819.

Genome annotation databases

EnsembliENSMUST00000038359; ENSMUSP00000038216; ENSMUSG00000035401. [Q8BMB0-2]
ENSMUST00000205276; ENSMUSP00000145858; ENSMUSG00000035401. [Q8BMB0-1]
GeneIDi233545.
KEGGimmu:233545.
UCSCiuc009iko.1. mouse. [Q8BMB0-1]
uc009ikp.1. mouse. [Q8BMB0-2]
uc009ikr.1. mouse. [Q8BMB0-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC020109 mRNA. Translation: AAH20109.1. Different initiation.
BC039956 mRNA. No translation available.
BC089304 mRNA. Translation: AAH89304.1.
AK032985 mRNA. Translation: BAC28113.2.
CCDSiCCDS40028.1. [Q8BMB0-1]
RefSeqiNP_758484.2. NM_172280.2. [Q8BMB0-1]
XP_006507693.1. XM_006507630.2. [Q8BMB0-2]
UniGeneiMm.387819.

3D structure databases

ProteinModelPortaliQ8BMB0.
SMRiQ8BMB0. Positions 9-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231423. 5 interactions.
IntActiQ8BMB0. 2 interactions.
STRINGi10090.ENSMUSP00000038216.

PTM databases

iPTMnetiQ8BMB0.
PhosphoSiteiQ8BMB0.

Proteomic databases

EPDiQ8BMB0.
MaxQBiQ8BMB0.
PaxDbiQ8BMB0.
PeptideAtlasiQ8BMB0.
PRIDEiQ8BMB0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038359; ENSMUSP00000038216; ENSMUSG00000035401. [Q8BMB0-2]
ENSMUST00000205276; ENSMUSP00000145858; ENSMUSG00000035401. [Q8BMB0-1]
GeneIDi233545.
KEGGimmu:233545.
UCSCiuc009iko.1. mouse. [Q8BMB0-1]
uc009ikp.1. mouse. [Q8BMB0-2]
uc009ikr.1. mouse. [Q8BMB0-3]

Organism-specific databases

CTDi56946.
MGIiMGI:1924203. Emsy.

Phylogenomic databases

eggNOGiKOG4675. Eukaryota.
ENOG410YF3T. LUCA.
GeneTreeiENSGT00390000009554.
HOGENOMiHOG000112366.
HOVERGENiHBG051476.
InParanoidiQ8BMB0.
OMAiKISMMEA.
OrthoDBiEOG7NGQBP.
PhylomeDBiQ8BMB0.
TreeFamiTF332401.

Miscellaneous databases

PROiQ8BMB0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BMB0.
CleanExiMM_2210018M11RIK.
GenevisibleiQ8BMB0. MM.

Family and domain databases

InterProiIPR033482. EMSY.
IPR005491. ENT_dom.
[Graphical view]
PANTHERiPTHR16500. PTHR16500. 1 hit.
PfamiPF03735. ENT. 1 hit.
[Graphical view]
SMARTiSM01191. ENT. 1 hit.
[Graphical view]
SUPFAMiSSF158639. SSF158639. 1 hit.
PROSITEiPS51138. ENT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J, Czech II and FVB/N.
    Tissue: Brain, Kidney and Mammary gland.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-750 (ISOFORM 3).
    Strain: C57BL/6J.
    Tissue: Mesonephros.
  3. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BRCA2.
  4. "O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry."
    Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:923-934(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT SER-192.
    Tissue: Brain.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-177; SER-782 AND SER-785, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Lung, Spleen and Testis.

Entry informationi

Entry nameiEMSY_MOUSE
AccessioniPrimary (citable) accession number: Q8BMB0
Secondary accession number(s): Q5FWK5, Q80XU1, Q8VDW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: July 6, 2016
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.