Full text data of ZMYM3
ZMYM3
(DXS6673E, KIAA0385, ZNF261)
[Confidence: low (only semi-automatic identification from reviews)]
Zinc finger MYM-type protein 3 (Zinc finger protein 261)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Zinc finger MYM-type protein 3 (Zinc finger protein 261)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q14202
ID ZMYM3_HUMAN Reviewed; 1370 AA.
AC Q14202; D3DVV3; O15089; Q96E26;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2000, sequence version 2.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Zinc finger MYM-type protein 3;
DE AltName: Full=Zinc finger protein 261;
GN Name=ZMYM3; Synonyms=DXS6673E, KIAA0385, ZNF261;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RX PubMed=8817323; DOI=10.1093/hmg/5.7.887;
RA van der Maarel S.M., Scholten I.H.G.M., Huber I., Phillippe C.,
RA Suijkerbuijk R.F., Gilgenkrantz S., Kere J., Cremers F.P.M.,
RA Ropers H.-H.;
RT "Cloning and characterization of DXS6673E, a candidate gene for X-
RT linked mental retardation in Xq13.1.";
RL Hum. Mol. Genet. 5:887-897(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Lymph, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION IN THE BHC COMPLEX WITH HDAC1; HDAC2; HMG20B; KDM1A;
RP RCOR1; PHF21A; ZMYM2; ZNF217; KIAA0182 AND GTF2I.
RX PubMed=12493763; DOI=10.1074/jbc.M208992200;
RA Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.;
RT "A candidate X-linked mental retardation gene is a component of a new
RT family of histone deacetylase-containing complexes.";
RL J. Biol. Chem. 278:7234-7239(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-267, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-267 AND
RP SER-464, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and
RT migration.";
RL BMC Biol. 9:54-54(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC cytoskeletal organization.
CC -!- SUBUNIT: May be a component of a BHC histone deacetylase complex
CC that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST,
CC PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I.
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q14202-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14202-2; Sequence=VSP_004492;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q14202-3; Sequence=VSP_043262, VSP_043263;
CC -!- TISSUE SPECIFICITY: Most abundant in brain, moderate in muscle and
CC heart, low in other tissues except placenta.
CC -!- DISEASE: Note=A chromosomal aberration involving ZMYM3 may be a
CC cause of X-linked mental retardation in Xq13.1. Translocation
CC t(X;13)(q13.1;?).
CC -!- SIMILARITY: Contains 9 MYM-type zinc fingers.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20839.2; Type=Erroneous initiation;
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DR EMBL; X95808; CAA65075.1; -; mRNA.
DR EMBL; AB002383; BAA20839.2; ALT_INIT; mRNA.
DR EMBL; BT007095; AAP35759.1; -; mRNA.
DR EMBL; AL590762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471132; EAX05302.1; -; Genomic_DNA.
DR EMBL; CH471132; EAX05303.1; -; Genomic_DNA.
DR EMBL; BC069057; AAH69057.1; -; mRNA.
DR EMBL; BC013009; AAH13009.1; -; mRNA.
DR RefSeq; NP_001164633.1; NM_001171162.1.
DR RefSeq; NP_001164634.1; NM_001171163.1.
DR RefSeq; NP_005087.1; NM_005096.3.
DR RefSeq; NP_963893.1; NM_201599.2.
DR RefSeq; XP_005262366.1; XM_005262309.1.
DR RefSeq; XP_005262367.1; XM_005262310.1.
DR UniGene; Hs.522684; -.
DR ProteinModelPortal; Q14202; -.
DR SMR; Q14202; 308-340.
DR IntAct; Q14202; 8.
DR MINT; MINT-7969582; -.
DR STRING; 9606.ENSP00000322845; -.
DR PhosphoSite; Q14202; -.
DR DMDM; 12644413; -.
DR PaxDb; Q14202; -.
DR PRIDE; Q14202; -.
DR DNASU; 9203; -.
DR Ensembl; ENST00000314425; ENSP00000322845; ENSG00000147130.
DR Ensembl; ENST00000353904; ENSP00000343909; ENSG00000147130.
DR Ensembl; ENST00000373981; ENSP00000363093; ENSG00000147130.
DR Ensembl; ENST00000373998; ENSP00000363110; ENSG00000147130.
DR GeneID; 9203; -.
DR KEGG; hsa:9203; -.
DR UCSC; uc004dzh.2; human.
DR CTD; 9203; -.
DR GeneCards; GC0XM070459; -.
DR HGNC; HGNC:13054; ZMYM3.
DR HPA; HPA003211; -.
DR MIM; 300061; gene.
DR neXtProt; NX_Q14202; -.
DR PharmGKB; PA37632; -.
DR eggNOG; NOG86062; -.
DR HOGENOM; HOG000293258; -.
DR HOVERGEN; HBG057545; -.
DR OrthoDB; EOG7JT6VN; -.
DR PhylomeDB; Q14202; -.
DR GeneWiki; ZMYM3; -.
DR GenomeRNAi; 9203; -.
DR NextBio; 34497; -.
DR PRO; PR:Q14202; -.
DR ArrayExpress; Q14202; -.
DR Bgee; Q14202; -.
DR CleanEx; HS_ZMYM3; -.
DR Genevestigator; Q14202; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0007275; P:multicellular organismal development; TAS:ProtInc.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR InterPro; IPR021893; DUF3504.
DR InterPro; IPR011017; TRASH_dom.
DR InterPro; IPR010507; Znf_MYM.
DR Pfam; PF12012; DUF3504; 1.
DR Pfam; PF06467; zf-FCS; 10.
DR SMART; SM00746; TRASH; 10.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosomal rearrangement; Complete proteome;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1 1370 Zinc finger MYM-type protein 3.
FT /FTId=PRO_0000191378.
FT ZN_FING 332 366 MYM-type 1.
FT ZN_FING 378 422 MYM-type 2.
FT ZN_FING 429 464 MYM-type 3.
FT ZN_FING 477 511 MYM-type 4.
FT ZN_FING 521 559 MYM-type 5.
FT ZN_FING 567 604 MYM-type 6.
FT ZN_FING 612 646 MYM-type 7.
FT ZN_FING 653 692 MYM-type 8.
FT ZN_FING 699 733 MYM-type 9.
FT MOD_RES 263 263 Phosphoserine.
FT MOD_RES 267 267 Phosphoserine.
FT MOD_RES 464 464 Phosphoserine.
FT VAR_SEQ 491 495 KNTRV -> VGPRE (in isoform 3).
FT /FTId=VSP_043262.
FT VAR_SEQ 496 1370 Missing (in isoform 3).
FT /FTId=VSP_043263.
FT VAR_SEQ 793 804 Missing (in isoform 2).
FT /FTId=VSP_004492.
SQ SEQUENCE 1370 AA; 152379 MW; 088B5E01E7EE9C30 CRC64;
MDPSDFPSPF DPLTLPEKPL AGDLPVDMEF GEDLLESQTA PTRGWAPPGP SPSSGALDLL
DTPAGLEKDP GVLDGATELL GLGGLLYKAP SPPEVDHGPE GTLAWDAGDQ TLEPGPGGQT
PEVVPPDPGA GANSCSPEGL LEPLAPDSPI TLQSPHIEEE ETTSIATARR GSPGQEEELP
QGQPQSPNAP PSPSVGETLG DGINSSQTKP GGSSPPAHPS LPGDGLTAKA SEKPPERKRS
ERVRRAEPPK PEVVDSTESI PVSDEDSDAM VDDPNDEDFV PFRPRRSPRM SLRSSVSQRA
GRSAVGTKMT CAHCRTPLQK GQTAYQRKGL PQLFCSSSCL TTFSKKPSGK KTCTFCKKEI
WNTKDSVVAQ TGSGGSFHEF CTSVCLSLYE AQQQRPIPQS GDPADATRCS ICQKTGEVLH
EVSNGSVVHR LCSDSCFSKF RANKGLKTNC CDQCGAYIYT KTGSPGPELL FHEGQQKRFC
NTTCLGAYKK KNTRVYPCVW CKTLCKNFEM LSHVDRNGKT SLFCSLCCTT SYKVKQAGLT
GPPRPCSFCR RSLSDPCYYN KVDRTVYQFC SPSCWTKFQR TSPEGGIHLS CHYCHSLFSG
KPEVLDWQDQ VFQFCCRDCC EDFKRLRGVV SQCEHCRQEK LLHEKLRFSG VEKSFCSEGC
VLLYKQDFTK KLGLCCITCT YCSQTCQRGV TEQLDGSTWD FCSEDCKSKY LLWYCKAARC
HACKRQGKLL ETIHWRGQIR HFCNQQCLLR FYSQQNQPNL DTQSGPESLL NSQSPESKPQ
TPSQTKVENS NTVRTPEENG NLGKIPVKTR SAPTAPTPPP PPPPATPRKN KAAMCKPLMQ
NRGVSCKVEM KSKGSQTEEW KPQVIVLPIP VPIFVPVPMH LYCQKVPVPF SMPIPVPVPM
FLPTTLESTD KIVETIEELK VKIPSNPLEA DILAMAEMIA EAEELDKASS DLCDLVSNQS
AEGLLEDCDL FGPARDDVLA MAVKMANVLD EPGQDLEADF PKNPLDINPS VDFLFDCGLV
GPEDVSTEQD LPRTMRKGQK RLVLSESCSR DSMSSQPSCT GLNYSYGVNA WKCWVQSKYA
NGETSKGDEL RFGPKPMRIK EDILACSAAE LNYGLAQFVR EITRPNGERY EPDSIYYLCL
GIQQYLLENN RMVNIFTDLY YLTFVQELNK SLSTWQPTLL PNNTVFSRVE EEHLWECKQL
GVYSPFVLLN TLMFFNTKFF GLQTAEEHMQ LSFTNVVRQS RKCTTPRGTT KVVSIRYYAP
VRQRKGRDTG PGKRKREDEA PILEQRENRM NPLRCPVKFY EFYLSKCPES LRTRNDVFYL
QPERSCIAES PLWYSVIPMD RSMLESMLNR ILAVREIYEE LGRPGEEDLD
//
ID ZMYM3_HUMAN Reviewed; 1370 AA.
AC Q14202; D3DVV3; O15089; Q96E26;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2000, sequence version 2.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Zinc finger MYM-type protein 3;
DE AltName: Full=Zinc finger protein 261;
GN Name=ZMYM3; Synonyms=DXS6673E, KIAA0385, ZNF261;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RX PubMed=8817323; DOI=10.1093/hmg/5.7.887;
RA van der Maarel S.M., Scholten I.H.G.M., Huber I., Phillippe C.,
RA Suijkerbuijk R.F., Gilgenkrantz S., Kere J., Cremers F.P.M.,
RA Ropers H.-H.;
RT "Cloning and characterization of DXS6673E, a candidate gene for X-
RT linked mental retardation in Xq13.1.";
RL Hum. Mol. Genet. 5:887-897(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Lymph, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION IN THE BHC COMPLEX WITH HDAC1; HDAC2; HMG20B; KDM1A;
RP RCOR1; PHF21A; ZMYM2; ZNF217; KIAA0182 AND GTF2I.
RX PubMed=12493763; DOI=10.1074/jbc.M208992200;
RA Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.;
RT "A candidate X-linked mental retardation gene is a component of a new
RT family of histone deacetylase-containing complexes.";
RL J. Biol. Chem. 278:7234-7239(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-267, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-267 AND
RP SER-464, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and
RT migration.";
RL BMC Biol. 9:54-54(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC cytoskeletal organization.
CC -!- SUBUNIT: May be a component of a BHC histone deacetylase complex
CC that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST,
CC PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I.
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q14202-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14202-2; Sequence=VSP_004492;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q14202-3; Sequence=VSP_043262, VSP_043263;
CC -!- TISSUE SPECIFICITY: Most abundant in brain, moderate in muscle and
CC heart, low in other tissues except placenta.
CC -!- DISEASE: Note=A chromosomal aberration involving ZMYM3 may be a
CC cause of X-linked mental retardation in Xq13.1. Translocation
CC t(X;13)(q13.1;?).
CC -!- SIMILARITY: Contains 9 MYM-type zinc fingers.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20839.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; X95808; CAA65075.1; -; mRNA.
DR EMBL; AB002383; BAA20839.2; ALT_INIT; mRNA.
DR EMBL; BT007095; AAP35759.1; -; mRNA.
DR EMBL; AL590762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471132; EAX05302.1; -; Genomic_DNA.
DR EMBL; CH471132; EAX05303.1; -; Genomic_DNA.
DR EMBL; BC069057; AAH69057.1; -; mRNA.
DR EMBL; BC013009; AAH13009.1; -; mRNA.
DR RefSeq; NP_001164633.1; NM_001171162.1.
DR RefSeq; NP_001164634.1; NM_001171163.1.
DR RefSeq; NP_005087.1; NM_005096.3.
DR RefSeq; NP_963893.1; NM_201599.2.
DR RefSeq; XP_005262366.1; XM_005262309.1.
DR RefSeq; XP_005262367.1; XM_005262310.1.
DR UniGene; Hs.522684; -.
DR ProteinModelPortal; Q14202; -.
DR SMR; Q14202; 308-340.
DR IntAct; Q14202; 8.
DR MINT; MINT-7969582; -.
DR STRING; 9606.ENSP00000322845; -.
DR PhosphoSite; Q14202; -.
DR DMDM; 12644413; -.
DR PaxDb; Q14202; -.
DR PRIDE; Q14202; -.
DR DNASU; 9203; -.
DR Ensembl; ENST00000314425; ENSP00000322845; ENSG00000147130.
DR Ensembl; ENST00000353904; ENSP00000343909; ENSG00000147130.
DR Ensembl; ENST00000373981; ENSP00000363093; ENSG00000147130.
DR Ensembl; ENST00000373998; ENSP00000363110; ENSG00000147130.
DR GeneID; 9203; -.
DR KEGG; hsa:9203; -.
DR UCSC; uc004dzh.2; human.
DR CTD; 9203; -.
DR GeneCards; GC0XM070459; -.
DR HGNC; HGNC:13054; ZMYM3.
DR HPA; HPA003211; -.
DR MIM; 300061; gene.
DR neXtProt; NX_Q14202; -.
DR PharmGKB; PA37632; -.
DR eggNOG; NOG86062; -.
DR HOGENOM; HOG000293258; -.
DR HOVERGEN; HBG057545; -.
DR OrthoDB; EOG7JT6VN; -.
DR PhylomeDB; Q14202; -.
DR GeneWiki; ZMYM3; -.
DR GenomeRNAi; 9203; -.
DR NextBio; 34497; -.
DR PRO; PR:Q14202; -.
DR ArrayExpress; Q14202; -.
DR Bgee; Q14202; -.
DR CleanEx; HS_ZMYM3; -.
DR Genevestigator; Q14202; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0007275; P:multicellular organismal development; TAS:ProtInc.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR InterPro; IPR021893; DUF3504.
DR InterPro; IPR011017; TRASH_dom.
DR InterPro; IPR010507; Znf_MYM.
DR Pfam; PF12012; DUF3504; 1.
DR Pfam; PF06467; zf-FCS; 10.
DR SMART; SM00746; TRASH; 10.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosomal rearrangement; Complete proteome;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1 1370 Zinc finger MYM-type protein 3.
FT /FTId=PRO_0000191378.
FT ZN_FING 332 366 MYM-type 1.
FT ZN_FING 378 422 MYM-type 2.
FT ZN_FING 429 464 MYM-type 3.
FT ZN_FING 477 511 MYM-type 4.
FT ZN_FING 521 559 MYM-type 5.
FT ZN_FING 567 604 MYM-type 6.
FT ZN_FING 612 646 MYM-type 7.
FT ZN_FING 653 692 MYM-type 8.
FT ZN_FING 699 733 MYM-type 9.
FT MOD_RES 263 263 Phosphoserine.
FT MOD_RES 267 267 Phosphoserine.
FT MOD_RES 464 464 Phosphoserine.
FT VAR_SEQ 491 495 KNTRV -> VGPRE (in isoform 3).
FT /FTId=VSP_043262.
FT VAR_SEQ 496 1370 Missing (in isoform 3).
FT /FTId=VSP_043263.
FT VAR_SEQ 793 804 Missing (in isoform 2).
FT /FTId=VSP_004492.
SQ SEQUENCE 1370 AA; 152379 MW; 088B5E01E7EE9C30 CRC64;
MDPSDFPSPF DPLTLPEKPL AGDLPVDMEF GEDLLESQTA PTRGWAPPGP SPSSGALDLL
DTPAGLEKDP GVLDGATELL GLGGLLYKAP SPPEVDHGPE GTLAWDAGDQ TLEPGPGGQT
PEVVPPDPGA GANSCSPEGL LEPLAPDSPI TLQSPHIEEE ETTSIATARR GSPGQEEELP
QGQPQSPNAP PSPSVGETLG DGINSSQTKP GGSSPPAHPS LPGDGLTAKA SEKPPERKRS
ERVRRAEPPK PEVVDSTESI PVSDEDSDAM VDDPNDEDFV PFRPRRSPRM SLRSSVSQRA
GRSAVGTKMT CAHCRTPLQK GQTAYQRKGL PQLFCSSSCL TTFSKKPSGK KTCTFCKKEI
WNTKDSVVAQ TGSGGSFHEF CTSVCLSLYE AQQQRPIPQS GDPADATRCS ICQKTGEVLH
EVSNGSVVHR LCSDSCFSKF RANKGLKTNC CDQCGAYIYT KTGSPGPELL FHEGQQKRFC
NTTCLGAYKK KNTRVYPCVW CKTLCKNFEM LSHVDRNGKT SLFCSLCCTT SYKVKQAGLT
GPPRPCSFCR RSLSDPCYYN KVDRTVYQFC SPSCWTKFQR TSPEGGIHLS CHYCHSLFSG
KPEVLDWQDQ VFQFCCRDCC EDFKRLRGVV SQCEHCRQEK LLHEKLRFSG VEKSFCSEGC
VLLYKQDFTK KLGLCCITCT YCSQTCQRGV TEQLDGSTWD FCSEDCKSKY LLWYCKAARC
HACKRQGKLL ETIHWRGQIR HFCNQQCLLR FYSQQNQPNL DTQSGPESLL NSQSPESKPQ
TPSQTKVENS NTVRTPEENG NLGKIPVKTR SAPTAPTPPP PPPPATPRKN KAAMCKPLMQ
NRGVSCKVEM KSKGSQTEEW KPQVIVLPIP VPIFVPVPMH LYCQKVPVPF SMPIPVPVPM
FLPTTLESTD KIVETIEELK VKIPSNPLEA DILAMAEMIA EAEELDKASS DLCDLVSNQS
AEGLLEDCDL FGPARDDVLA MAVKMANVLD EPGQDLEADF PKNPLDINPS VDFLFDCGLV
GPEDVSTEQD LPRTMRKGQK RLVLSESCSR DSMSSQPSCT GLNYSYGVNA WKCWVQSKYA
NGETSKGDEL RFGPKPMRIK EDILACSAAE LNYGLAQFVR EITRPNGERY EPDSIYYLCL
GIQQYLLENN RMVNIFTDLY YLTFVQELNK SLSTWQPTLL PNNTVFSRVE EEHLWECKQL
GVYSPFVLLN TLMFFNTKFF GLQTAEEHMQ LSFTNVVRQS RKCTTPRGTT KVVSIRYYAP
VRQRKGRDTG PGKRKREDEA PILEQRENRM NPLRCPVKFY EFYLSKCPES LRTRNDVFYL
QPERSCIAES PLWYSVIPMD RSMLESMLNR ILAVREIYEE LGRPGEEDLD
//
MIM
300061
*RECORD*
*FIELD* NO
300061
*FIELD* TI
*300061 ZINC FINGER, MYM-TYPE 3; ZMYM3
;;ZINC FINGER PROTEIN 261; ZNF261;;
DXS6673E
read more*FIELD* TX
CLONING
Van der Maarel et al. (1996) reported the cloning and characterization
of the ZNF261 gene, which the called DXS6673E. ZNF261 maps to the X
chromosome, is subject to X inactivation, and was disrupted in the
5-prime untranslated region by a balanced X;13 translocation in a
mentally retarded female. They identified a YAC clone that spanned the
breakpoint and used this YAC to isolate a cDNA from a fetal brain
library. The cDNA contains a 4,074-bp ORF encoding a predicted
1,358-amino acid polypeptide. By Northern analysis, van der Maarel et
al. (1996) showed that the DXS6673E gene is highly conserved among
vertebrates and that its expression is most abundant in brain.
GENE FUNCTION
Hakimi et al. (2003) identified a family of multiprotein corepressor
complexes that function through modifying chromatin structure to keep
genes silent. The polypeptide composition of these complexes includes a
common core of 2 subunits, HDAC1 (601241)/HDAC2 (605164) and the
FAD-binding protein BHC110 (AOF2; 609132). Other subunits of these
complexes include ZNF261, GTF2I (601679), and polypeptides associated
with cancer-causing chromosomal translocations.
GENE STRUCTURE
Van der Maarel et al. (1996) reported that the ZNF261 gene contains 25
exons, including 2 putative alternatively spliced noncoding exons (1A
and 1B).
MAPPING
Van der Maarel et al. (1996) mapped the ZNF261 gene to chromosome
Xq13.1.
CYTOGENETICS
Van der Maarel et al. (1996) reported a mentally retarded female whose
ZNF261 gene was disrupted in the 5-prime UTR by a balanced X;13
translocation. They noted that apart from mental retardation, the only
conspicuous clinical features in this patient were scoliosis and spotty
abdominal hypopigmentation.
*FIELD* RF
1. Hakimi, M.-A.; Dong, Y.; Lane, W. S.; Speicher, D. W.; Shiekhattar,
R.: A candidate X-linked mental retardation gene is a component of
a new family of histone deacetylase-containing complexes. J. Biol.
Chem. 278: 7234-7239, 2003.
2. van der Maarel, S. M.; Scholten, I. H. J. M.; Huber, I.; Philippe,
C.; Suijkerbuijk, R. F.; Gilgenkrantz, S.; Kere, J.; Cremers, F. P.
M.; Ropers, H.-H.: Cloning and characterization of DXS6673E, a candidate
gene for X-linked mental retardation in Xq13.1. Hum. Molec. Genet. 5:
887-897, 1996.
*FIELD* CN
Stylianos E. Antonarakis - updated: 1/3/2005
*FIELD* CD
Moyra Smith: 8/8/1996
*FIELD* ED
carol: 09/02/2010
mgross: 1/3/2005
alopez: 10/12/1999
terry: 8/15/1996
mark: 8/15/1996
marlene: 8/9/1996
mark: 8/8/1996
*RECORD*
*FIELD* NO
300061
*FIELD* TI
*300061 ZINC FINGER, MYM-TYPE 3; ZMYM3
;;ZINC FINGER PROTEIN 261; ZNF261;;
DXS6673E
read more*FIELD* TX
CLONING
Van der Maarel et al. (1996) reported the cloning and characterization
of the ZNF261 gene, which the called DXS6673E. ZNF261 maps to the X
chromosome, is subject to X inactivation, and was disrupted in the
5-prime untranslated region by a balanced X;13 translocation in a
mentally retarded female. They identified a YAC clone that spanned the
breakpoint and used this YAC to isolate a cDNA from a fetal brain
library. The cDNA contains a 4,074-bp ORF encoding a predicted
1,358-amino acid polypeptide. By Northern analysis, van der Maarel et
al. (1996) showed that the DXS6673E gene is highly conserved among
vertebrates and that its expression is most abundant in brain.
GENE FUNCTION
Hakimi et al. (2003) identified a family of multiprotein corepressor
complexes that function through modifying chromatin structure to keep
genes silent. The polypeptide composition of these complexes includes a
common core of 2 subunits, HDAC1 (601241)/HDAC2 (605164) and the
FAD-binding protein BHC110 (AOF2; 609132). Other subunits of these
complexes include ZNF261, GTF2I (601679), and polypeptides associated
with cancer-causing chromosomal translocations.
GENE STRUCTURE
Van der Maarel et al. (1996) reported that the ZNF261 gene contains 25
exons, including 2 putative alternatively spliced noncoding exons (1A
and 1B).
MAPPING
Van der Maarel et al. (1996) mapped the ZNF261 gene to chromosome
Xq13.1.
CYTOGENETICS
Van der Maarel et al. (1996) reported a mentally retarded female whose
ZNF261 gene was disrupted in the 5-prime UTR by a balanced X;13
translocation. They noted that apart from mental retardation, the only
conspicuous clinical features in this patient were scoliosis and spotty
abdominal hypopigmentation.
*FIELD* RF
1. Hakimi, M.-A.; Dong, Y.; Lane, W. S.; Speicher, D. W.; Shiekhattar,
R.: A candidate X-linked mental retardation gene is a component of
a new family of histone deacetylase-containing complexes. J. Biol.
Chem. 278: 7234-7239, 2003.
2. van der Maarel, S. M.; Scholten, I. H. J. M.; Huber, I.; Philippe,
C.; Suijkerbuijk, R. F.; Gilgenkrantz, S.; Kere, J.; Cremers, F. P.
M.; Ropers, H.-H.: Cloning and characterization of DXS6673E, a candidate
gene for X-linked mental retardation in Xq13.1. Hum. Molec. Genet. 5:
887-897, 1996.
*FIELD* CN
Stylianos E. Antonarakis - updated: 1/3/2005
*FIELD* CD
Moyra Smith: 8/8/1996
*FIELD* ED
carol: 09/02/2010
mgross: 1/3/2005
alopez: 10/12/1999
terry: 8/15/1996
mark: 8/15/1996
marlene: 8/9/1996
mark: 8/8/1996