ID   ZMYM3_HUMAN             Reviewed;        1370 AA.
AC   Q14202; D3DVV3; O15089; Q96E26;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 185.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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., Ropers H.-H.;
RT   "Cloning and characterization of DXS6673E, a candidate gene for X-linked
RT   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. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   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 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., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., 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., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., 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., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., 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., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., 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., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   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., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., 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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   IDENTIFICATION IN THE BHC COMPLEX WITH GSE1; GTF2I; HDAC1; HDAC2; HMG20B;
RP   KDM1A; RCOR1; PHF21A; ZNF217 AND ZMYM2.
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-267 AND SER-464, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   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., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   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 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., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; THR-795; THR-817 AND
RP   THR-826, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-817, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [16]
RP   INVOLVEMENT IN XLID112, AND VARIANT XLID112 TRP-441.
RX   PubMed=24721225; DOI=10.1186/1750-1172-9-49;
RA   Philips A.K., Siren A., Avela K., Somer M., Peippo M., Ahvenainen M.,
RA   Doagu F., Arvio M., Kaeaeriaeinen H., Van Esch H., Froyen G., Haas S.A.,
RA   Hu H., Kalscheuer V.M., Jaervelae I.;
RT   "X-exome sequencing in Finnish families with intellectual disability--four
RT   novel mutations and two novel syndromic phenotypes.";
RL   Orphanet J. Rare Dis. 9:49-49(2014).
RN   [17]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-308; LYS-320; LYS-328; LYS-778;
RP   LYS-786; LYS-804; LYS-847; LYS-861; LYS-920 AND LYS-1275, SUMOYLATION
RP   [LARGE SCALE ANALYSIS] AT LYS-786 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [18]
RP   VARIANTS XLID112 ASN-69; SER-169; LYS-241; HIS-302; SER-395; SER-398;
RP   TRP-441; GLN-441; ARG-454; HIS-688; ASP-731; CYS-752; VAL-932; GLN-1124;
RP   ASN-1137; ASN-1173; ASP-1202; THR-1213; TRP-1274; CYS-1294; TRP-1324 AND
RP   ILE-1343, AND SUBCELLULAR LOCATION.
RX   PubMed=36586412; DOI=10.1016/j.ajhg.2022.12.007;
RA   Hiatt S.M., Trajkova S., Sebastiano M.R., Partridge E.C., Abidi F.E.,
RA   Anderson A., Ansar M., Antonarakis S.E., Azadi A., Bachmann-Gagescu R.,
RA   Bartuli A., Benech C., Berkowitz J.L., Betti M.J., Brusco A., Cannon A.,
RA   Caron G., Chen Y., Cochran M.E., Coleman T.F., Crenshaw M.M., Cuisset L.,
RA   Curry C.J., Darvish H., Demirdas S., Descartes M., Douglas J., Dyment D.A.,
RA   Elloumi H.Z., Ermondi G., Faoucher M., Farrow E.G., Felker S.A., Fisher H.,
RA   Hurst A.C.E., Joset P., Kelly M.A., Kmoch S., Leadem B.R., Lyons M.J.,
RA   Macchiaiolo M., Magner M., Mandrile G., Mattioli F., McEown M.,
RA   Meadows S.K., Medne L., Meeks N.J.L., Montgomery S., Napier M.P.,
RA   Natowicz M., Newberry K.M., Niceta M., Noskova L., Nowak C.B., Noyes A.G.,
RA   Osmond M., Prijoles E.J., Pugh J., Pullano V., Quelin C.,
RA   Rahimi-Aliabadi S., Rauch A., Redon S., Reymond A., Schwager C.R.,
RA   Sellars E.A., Scheuerle A.E., Shukarova-Angelovska E., Skraban C.,
RA   Stolerman E., Sullivan B.R., Tartaglia M., Thiffault I., Uguen K.,
RA   Umana L.A., van Bever Y., van der Crabben S.N., van Slegtenhorst M.A.,
RA   Waisfisz Q., Washington C., Rodan L.H., Myers R.M., Cooper G.M.;
RT   "Deleterious, protein-altering variants in the transcriptional coregulator
RT   ZMYM3 in 27 individuals with a neurodevelopmental delay phenotype.";
RL   Am. J. Hum. Genet. 110:215-227(2023).
CC   -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC       cytoskeletal organization. {ECO:0000269|PubMed:21834987}.
CC   -!- SUBUNIT: May be a component of a BHC histone deacetylase complex that
CC       contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST,
CC       PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I.
CC       {ECO:0000269|PubMed:12493763}.
CC   -!- INTERACTION:
CC       Q14202; Q92993: KAT5; NbExp=3; IntAct=EBI-2556139, EBI-399080;
CC       Q14202; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-2556139, EBI-11742507;
CC       Q14202; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-2556139, EBI-9090795;
CC       Q14202; P61981: YWHAG; NbExp=3; IntAct=EBI-2556139, EBI-359832;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:36586412}.
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       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: Intellectual developmental disorder, X-linked 112 (XLID112)
CC       [MIM:301111]: A neurodevelopmental disorder characterized by
CC       developmental delay, impaired intellectual development, language and
CC       motor delay, autism or autistic traits, and variable dysmorphic
CC       features. {ECO:0000269|PubMed:24721225, ECO:0000269|PubMed:36586412}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- DISEASE: Note=A chromosomal aberration involving ZMYM3 may be a cause
CC       of X-linked intellectual disability in Xq13.1. Translocation
CC       t(X;13)(q13.1;q31). {ECO:0000269|PubMed:8817323}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA20839.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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   CCDS; CCDS14409.1; -. [Q14202-1]
DR   CCDS; CCDS55443.1; -. [Q14202-3]
DR   CCDS; CCDS55444.1; -. [Q14202-2]
DR   RefSeq; NP_001164633.1; NM_001171162.1. [Q14202-2]
DR   RefSeq; NP_001164634.1; NM_001171163.1. [Q14202-3]
DR   RefSeq; NP_005087.1; NM_005096.3. [Q14202-1]
DR   RefSeq; NP_963893.1; NM_201599.2. [Q14202-1]
DR   RefSeq; XP_005262366.1; XM_005262309.3. [Q14202-1]
DR   RefSeq; XP_005262367.1; XM_005262310.2. [Q14202-2]
DR   RefSeq; XP_011529364.1; XM_011531062.2. [Q14202-1]
DR   AlphaFoldDB; Q14202; -.
DR   SMR; Q14202; -.
DR   BioGRID; 114637; 136.
DR   CORUM; Q14202; -.
DR   IntAct; Q14202; 50.
DR   MINT; Q14202; -.
DR   STRING; 9606.ENSP00000322845; -.
DR   GlyGen; Q14202; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q14202; -.
DR   PhosphoSitePlus; Q14202; -.
DR   BioMuta; ZMYM3; -.
DR   DMDM; 12644413; -.
DR   EPD; Q14202; -.
DR   jPOST; Q14202; -.
DR   MassIVE; Q14202; -.
DR   MaxQB; Q14202; -.
DR   PaxDb; 9606-ENSP00000322845; -.
DR   PeptideAtlas; Q14202; -.
DR   ProteomicsDB; 59922; -. [Q14202-1]
DR   ProteomicsDB; 59923; -. [Q14202-2]
DR   ProteomicsDB; 59924; -. [Q14202-3]
DR   Pumba; Q14202; -.
DR   Antibodypedia; 524; 196 antibodies from 24 providers.
DR   DNASU; 9203; -.
DR   Ensembl; ENST00000314425.9; ENSP00000322845.5; ENSG00000147130.14. [Q14202-1]
DR   Ensembl; ENST00000373981.5; ENSP00000363093.1; ENSG00000147130.14. [Q14202-3]
DR   Ensembl; ENST00000373998.5; ENSP00000363110.1; ENSG00000147130.14. [Q14202-2]
DR   GeneID; 9203; -.
DR   KEGG; hsa:9203; -.
DR   MANE-Select; ENST00000314425.9; ENSP00000322845.5; NM_201599.3; NP_963893.1.
DR   UCSC; uc004dzh.3; human. [Q14202-1]
DR   AGR; HGNC:13054; -.
DR   CTD; 9203; -.
DR   DisGeNET; 9203; -.
DR   GeneCards; ZMYM3; -.
DR   HGNC; HGNC:13054; ZMYM3.
DR   HPA; ENSG00000147130; Low tissue specificity.
DR   MalaCards; ZMYM3; -.
DR   MIM; 300061; gene.
DR   MIM; 301111; phenotype.
DR   neXtProt; NX_Q14202; -.
DR   OpenTargets; ENSG00000147130; -.
DR   PharmGKB; PA37632; -.
DR   VEuPathDB; HostDB:ENSG00000147130; -.
DR   eggNOG; ENOG502QQQ9; Eukaryota.
DR   GeneTree; ENSGT00940000160693; -.
DR   HOGENOM; CLU_004099_1_0_1; -.
DR   InParanoid; Q14202; -.
DR   OrthoDB; 5399298at2759; -.
DR   PhylomeDB; Q14202; -.
DR   TreeFam; TF336988; -.
DR   PathwayCommons; Q14202; -.
DR   SignaLink; Q14202; -.
DR   BioGRID-ORCS; 9203; 29 hits in 790 CRISPR screens.
DR   ChiTaRS; ZMYM3; human.
DR   GeneWiki; ZMYM3; -.
DR   GenomeRNAi; 9203; -.
DR   Pharos; Q14202; Tbio.
DR   PRO; PR:Q14202; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q14202; Protein.
DR   Bgee; ENSG00000147130; Expressed in right adrenal gland and 207 other cell types or tissues.
DR   ExpressionAtlas; Q14202; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR   InterPro; IPR021893; DUF3504.
DR   InterPro; IPR011017; TRASH_dom.
DR   InterPro; IPR010507; Znf_MYM.
DR   PANTHER; PTHR45736; ZINC FINGER MYM-TYPE PROTEIN; 1.
DR   PANTHER; PTHR45736:SF3; ZINC FINGER MYM-TYPE PROTEIN 3; 1.
DR   Pfam; PF12012; DUF3504; 1.
DR   Pfam; PF06467; zf-FCS; 9.
DR   SMART; SM00746; TRASH; 10.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   Genevisible; Q14202; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Autism; Autism spectrum disorder;
KW   Chromosomal rearrangement; Disease variant; Intellectual disability;
KW   Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..1370
FT                   /note="Zinc finger MYM-type protein 3"
FT                   /id="PRO_0000191378"
FT   ZN_FING         332..366
FT                   /note="MYM-type 1"
FT   ZN_FING         378..422
FT                   /note="MYM-type 2"
FT   ZN_FING         429..464
FT                   /note="MYM-type 3"
FT   ZN_FING         477..511
FT                   /note="MYM-type 4"
FT   ZN_FING         521..559
FT                   /note="MYM-type 5"
FT   ZN_FING         567..604
FT                   /note="MYM-type 6"
FT   ZN_FING         612..646
FT                   /note="MYM-type 7"
FT   ZN_FING         653..692
FT                   /note="MYM-type 8"
FT   ZN_FING         699..733
FT                   /note="MYM-type 9"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          759..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..214
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..252
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..275
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..798
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        812..828
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         263
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648"
FT   MOD_RES         267
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648"
FT   MOD_RES         464
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         795
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         817
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         826
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CROSSLNK        308
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        320
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        328
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        778
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        786
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        804
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        847
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        861
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        920
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1275
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         491..495
FT                   /note="KNTRV -> VGPRE (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT                   /id="VSP_043262"
FT   VAR_SEQ         496..1370
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT                   /id="VSP_043263"
FT   VAR_SEQ         793..804
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8817323"
FT                   /id="VSP_004492"
FT   VARIANT         69
FT                   /note="D -> N (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088743"
FT   VARIANT         169
FT                   /note="R -> S (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088744"
FT   VARIANT         241
FT                   /note="E -> K (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088745"
FT   VARIANT         302
FT                   /note="R -> H (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088746"
FT   VARIANT         395
FT                   /note="R -> S (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088747"
FT   VARIANT         398
FT                   /note="P -> S (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088748"
FT   VARIANT         441
FT                   /note="R -> Q (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088749"
FT   VARIANT         441
FT                   /note="R -> W (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:24721225,
FT                   ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088750"
FT   VARIANT         454
FT                   /note="C -> R (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088751"
FT   VARIANT         688
FT                   /note="R -> H (in XLID112; likely benign)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088752"
FT   VARIANT         731
FT                   /note="E -> D (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088753"
FT   VARIANT         752
FT                   /note="Y -> C (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088754"
FT   VARIANT         932
FT                   /note="I -> V (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088755"
FT   VARIANT         1124
FT                   /note="R -> Q (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088756"
FT   VARIANT         1137
FT                   /note="Y -> N (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088757"
FT   VARIANT         1173
FT                   /note="S -> N (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088758"
FT   VARIANT         1202
FT                   /note="V -> D (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088759"
FT   VARIANT         1213
FT                   /note="M -> T (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088760"
FT   VARIANT         1274
FT                   /note="R -> W (in XLID112; likely pathogenic; reduced
FT                   nuclear localization)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088761"
FT   VARIANT         1294
FT                   /note="R -> C (in XLID112; likely pathogenic)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088762"
FT   VARIANT         1324
FT                   /note="R -> W (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088763"
FT   VARIANT         1343
FT                   /note="M -> I (in XLID112; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36586412"
FT                   /id="VAR_088764"
FT   CROSSLNK        Q14202-2:786
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
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
//