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Protein data for EMSY_MOUSE:

Description:
Protein EMSY.

Molecular weight: 1352

View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )


Important dates:
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
24-MAY-2004, sequence version 2.
07-FEB-2006, entry version 24.

Phylogenetic order:
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Sciurognathi Muroidea Muridae Murinae Mus.

To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html

Links to references in other databases for protein EMSY_MOUSE:

DatabasePointerAdd. info#1Add. info#2
EMBLBC020109AAH20109.1ALT_INIT
EMBLBC039956AAH39956.1ALT_FRAME
EMBLAK032985BAC28113.1-
EnsemblENSMUSG00000035401Mus musculus.1
MGIMGI:19242032210018M11Rik.1
InterProIPR005491ENT.
PfamPF03735ENT1.
PROSITEPS51138ENT1.

General information about the databases mentioned above

Keywords:
Alternative splicing; Chromatin regulator; DNA damage; DNA repair; Nuclear protein; Phosphorylation; Repressor; Transcription; Transcription regulation.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 790-1265 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney;
RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-749 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Mesonephros;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schonbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH BRCA2.
RX PubMed=14651845; DOI=10.1016/S0092-8674(03)00930-9;
RA Hughes-Davies L., Huntsman D., Ruas M., Fuks F., Bye J., Chin S.-F.,
RA Milner J., Brown L.A., Hsu F., Gilks B., Nielsen T., Schulzer M.,
RA Chia S., Ragaz J., Cahn A., Linger L., Ozdag H., Cattaneo E.,
RA Jordanova E.S., Schuuring E., Yu D.S., Venkitaraman A., Ponder B.,
RA Doherty A., Aparicio S., Bentley D., Theillet C., Ponting C.P.,
RA Caldas C., Kouzarides T.;
RT "EMSY links the BRCA2 pathway to sporadic breast and ovarian cancer.";
RL Cell 115:523-535(2003).

Feature:
CHAIN 1 1264 Protein EMSY.
/FTId=PRO_0000086969.
DOMAIN 16 114 ENT.
REGION 1 442 Interaction with BRCA2 (By similarity).
REGION 118 122 Interaction with ZMYND11 (By similarity).
COMPBIAS 173 177 Poly-Ser.
COMPBIAS 290 355 Ser-rich.
COMPBIAS 359 428 Gln-rich.
COMPBIAS 460 600 Thr-rich.
COMPBIAS 683 687 Poly-Ser.
COMPBIAS 895 1048 Gln-rich.
MOD_RES 173 173 Phosphoserine (By similarity).
MOD_RES 202 202 Phosphoserine (By similarity).
MOD_RES 1085 1085 Phosphoserine (By similarity).
VARSPLIC 82 96 KMNLSLYLGERPSYS -> N (in isoform 3).
/FTId=VSP_010432.
VARSPLIC 802 802 T -> TERTDEGTEVAFPLL (in isoform 2).
/FTId=VSP_010433.
VARSPLIC 1040 1199 Missing (in isoform 2).
/FTId=VSP_010434.
CONFLICT 975 975 V -> A (in Ref. 1; AAH39956).

Comments:
-!- FUNCTION: 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).
-!- SUBUNIT: Interacts with the transactivation domain of BRCA2.
Interacts with CBX1 and ZMYND11. Does not interact with CBX3 or
CBX5 (By similarity).
-!- SUBCELLULAR LOCATION: Nuclear. Localizes to DNA damage markers in
irradiated cells; suggesting that it participates in DNA repair
process.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8BMB0-1; Sequence=Displayed;
Name=2;
IsoId=Q8BMB0-2; Sequence=VSP_010433, VSP_010434;
Note=No experimental confirmation available;
Name=3;
IsoId=Q8BMB0-3; Sequence=VSP_010432;
Note=No experimental confirmation available;
-!- SIMILARITY: Contains 1 ENT (EMSY N-terminal) domain.
-!- CAUTION: Ref.1 sequence differs from that shown due to a
frameshift in position 569.
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Sequence length: 1264

     MPVVWPTLLD LSRDECKRIL RKLELEAYAG VISALRAQGD LTKEKKDLLG ELSKVLSIST
     ERHRAEVRRA VNDERLTTIA HKMNLSLYLG ERPSYSMSGP NSSSEWSIEG RRLVPLMPRL
     VPQTAFTVTA NAVANAAVQH NASLPVPAET ASKDGVSCSD EDEKPRKRRR TNSSSSSPVV
     LKEVPKAVVP VSKTITVPVS GSPKMSNIMQ SIANSLPPHM SPVKITFTKP STQTTNTTTQ
     KVIIVTTSPS STFVPNILSK SHNYAAVTKL VPTSVIASTT QKPPVVITAS QASLVTSSSN
     GNSSSTSSPI SSTVAVTTVV SSTPSVVMST VAQGVSTSAI KVASTRLPSP KSLVSGPTQI
     LAQFPKQHQQ SPKQQLQQVQ QQTQQPVAQP SSVSQQQQPQ QSALPPGIKP TIQIKQESGV
     KIITQQVQPS KILPKPVTAT LPTSSNSPIM VVSSNGAIMT TKLVTTPTGT QATYTRPTVS
     PSLGRVATTP GAATYVKTTS GSIITVVPKS LATLGGKIIS SNIVSGTTTK ITTIPMTSKP
     NVIVVQKTTG KGTTIQGLPG KNVVTTLLNA GGEKTLQTVP AGAKPAIITA TRPITKMIVT
     QPKGIGSAVQ PAAKIIPTKI VYGQQGKTQV LIKPKPVTFQ ATVVSEQTRQ LVTETLQQAS
     RVADASNSSA QEGKEEPQGY TDSSSSSTES SQSSQDSQPV VHVIASRRQD WSEHEIAMET
     SPTIIYQDVS SESQSATSTI KALLELQQTT VKEKLESKPR QPTIDLSQMA VPIQMTQEKR
     HSPESPSIAV VESELVAEYI TTVSHRSQPQ QPSQPQRTLL QHVAQSQTAT QTSVVVKSIP
     ASSPGAITHI MQQALSSHTA FTKHSEELGT EEGEVEEMDT LDPQTGLFYR SALTQSQSTK
     QQKLSQPQLE QTQLQVKTLQ CFQTKQKQTI HLQADQLQHK LTQMPQLSIR HQKLNPLQQE
     QAQPKPDAQH TQHTVVAKDR QLPTLMAQPP QTVVQVLAVK TTQQLPKLQQ APNQPKIYVQ
     PQTPQSQMAL PSSEKQPASQ VEQPIITQGS SVTKITFEGR QPPTVTKITG GSSVPKLTSP
     VTSISPIQAS EKTAVSDILQ MSLMEAQIDT NVEHMVVDPP KKALATNVLT GEAGALPSTH
     VVVAGMTKCR ESCSSPSAVG PPLTTRKIEA AGVPTTGQFM RIQNVGQKKA EESPTEIIIQ
     AIPQYAIPCH SSSNVVVEPS GLLELNNFTS QQLDDDETAM EQDIDSSTED GTEPSPSQSA
     VERS

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