ZMYM4_HUMAN
ID ZMYM4_HUMAN Reviewed; 1548 AA.
AC Q5VZL5; A0JP19; A0JP20; O43308; Q5T5E1; Q5T5E2; Q7L3Q4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Zinc finger MYM-type protein 4;
DE AltName: Full=Zinc finger protein 262;
GN Name=ZMYM4; Synonyms=KIAA0425, ZNF262;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
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 (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Placenta;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 279-1548, AND VARIANT ILE-452.
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [5]
RP IDENTIFICATION.
RX PubMed=10449923; DOI=10.1159/000015282;
RA Sohal J., Chase A., Goldman J.M., Cross N.C.P.;
RT "Assignment of ZNF262 to human chromosome band 1p34-->p32 by in situ
RT hybridization.";
RL Cytogenet. Cell Genet. 85:306-307(1999).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=10486218; DOI=10.1006/geno.1999.5918;
RA Smedley D., Hamoudi R., Lu Y.-J., Cooper C., Shipley J.;
RT "Cloning and mapping of members of the MYM family.";
RL Genomics 60:244-247(1999).
RN [7]
RP IDENTIFICATION OF UTR.
RX PubMed=12356764; DOI=10.1074/jbc.m202272200;
RA Shchors K., Yehiely F., Kular R.K., Kotlo K.U., Brewer G., Deiss L.P.;
RT "Cell death inhibiting RNA (CDIR) derived from a 3'-untranslated region
RT binds AUF1 and heat shock protein 27.";
RL J. Biol. Chem. 277:47061-47072(2002).
RN [8]
RP IDENTIFICATION OF UTR.
RX PubMed=15611657; DOI=10.4161/cc.3.12.1295;
RA Shchors K., Yehiely F., Deiss L.P.;
RT "Cell death inhibiting RNA (CDIR) modulates IFN-gamma-stimulated
RT sensitization to Fas/CD95/Apo-1 and TRAIL/Apo-2L-induced apoptosis.";
RL Cell Cycle 3:1606-1611(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-162, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1256, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107; SER-110; SER-122 AND
RP SER-1030, AND 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 [14]
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122; SER-1181; SER-1539;
RP SER-1542 AND SER-1547, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-122; SER-162;
RP SER-197; SER-242; SER-1064; SER-1071 AND SER-1181, AND IDENTIFICATION BY
RP 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 [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-250; LYS-273 AND LYS-430, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-250 AND LYS-273, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-149; LYS-250; LYS-273 AND
RP LYS-430, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-250 AND LYS-273, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-140; LYS-149; LYS-195; LYS-201;
RP LYS-232; LYS-250; LYS-260; LYS-271; LYS-273; LYS-289; LYS-327; LYS-400;
RP LYS-428; LYS-430; LYS-1035; LYS-1061; LYS-1080; LYS-1127 AND LYS-1431, AND
RP IDENTIFICATION BY MASS 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 [23]
RP VARIANT [LARGE SCALE ANALYSIS] TRP-1410.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC cytoskeletal organization. {ECO:0000269|PubMed:21834987}.
CC -!- INTERACTION:
CC Q5VZL5; P49711: CTCF; NbExp=3; IntAct=EBI-2514659, EBI-932887;
CC Q5VZL5; Q14192: FHL2; NbExp=3; IntAct=EBI-2514659, EBI-701903;
CC Q5VZL5; A1L4F5: ROR2; NbExp=3; IntAct=EBI-2514659, EBI-10172778;
CC Q5VZL5; Q06455-4: RUNX1T1; NbExp=3; IntAct=EBI-2514659, EBI-10224192;
CC Q5VZL5; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-2514659, EBI-741480;
CC Q5VZL5; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-2514659, EBI-10173939;
CC Q5VZL5-4; Q96CV9: OPTN; NbExp=3; IntAct=EBI-10984536, EBI-748974;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5VZL5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VZL5-2; Sequence=VSP_027514;
CC Name=3;
CC IsoId=Q5VZL5-3; Sequence=VSP_027512;
CC Name=4;
CC IsoId=Q5VZL5-4; Sequence=VSP_027513;
CC -!- TISSUE SPECIFICITY: Expressed at higher level in heart, skeletal
CC muscle, kidney and liver. {ECO:0000269|PubMed:10486218}.
CC -!- MISCELLANEOUS: The 3'-UTR region of the mRNA encoding this protein
CC contains a motif called CDIR (for cell death inhibiting RNA) that binds
CC HNRPD/AUF1 and HSPB1/HSP27. It is able to inhibit interferon-gamma
CC induced apoptosis.
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DR EMBL; AL160000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590434; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07417.1; -; Genomic_DNA.
DR EMBL; BC012093; AAH12093.2; -; mRNA.
DR EMBL; BC127113; AAI27114.1; -; mRNA.
DR EMBL; BC127114; AAI27115.1; -; mRNA.
DR EMBL; AB007885; BAA24855.2; -; mRNA.
DR CCDS; CCDS389.1; -. [Q5VZL5-1]
DR PIR; T00059; T00059.
DR RefSeq; NP_005086.2; NM_005095.2. [Q5VZL5-1]
DR RefSeq; XP_005271388.1; XM_005271331.2. [Q5VZL5-3]
DR RefSeq; XP_011540725.1; XM_011542423.2.
DR RefSeq; XP_011540727.1; XM_011542425.2.
DR RefSeq; XP_016858292.1; XM_017002803.1. [Q5VZL5-4]
DR RefSeq; XP_016858293.1; XM_017002804.1.
DR AlphaFoldDB; Q5VZL5; -.
DR SMR; Q5VZL5; -.
DR BioGRID; 114636; 145.
DR IntAct; Q5VZL5; 78.
DR MINT; Q5VZL5; -.
DR STRING; 9606.ENSP00000322915; -.
DR GlyGen; Q5VZL5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5VZL5; -.
DR PhosphoSitePlus; Q5VZL5; -.
DR BioMuta; ZMYM4; -.
DR DMDM; 74762280; -.
DR EPD; Q5VZL5; -.
DR jPOST; Q5VZL5; -.
DR MassIVE; Q5VZL5; -.
DR MaxQB; Q5VZL5; -.
DR PaxDb; Q5VZL5; -.
DR PeptideAtlas; Q5VZL5; -.
DR PRIDE; Q5VZL5; -.
DR ProteomicsDB; 65706; -. [Q5VZL5-1]
DR ProteomicsDB; 65707; -. [Q5VZL5-2]
DR ProteomicsDB; 65708; -. [Q5VZL5-3]
DR ProteomicsDB; 65709; -. [Q5VZL5-4]
DR Antibodypedia; 31536; 118 antibodies from 28 providers.
DR DNASU; 9202; -.
DR Ensembl; ENST00000314607.11; ENSP00000322915.6; ENSG00000146463.12. [Q5VZL5-1]
DR GeneID; 9202; -.
DR KEGG; hsa:9202; -.
DR MANE-Select; ENST00000314607.11; ENSP00000322915.6; NM_005095.3; NP_005086.2.
DR UCSC; uc001byt.3; human. [Q5VZL5-1]
DR CTD; 9202; -.
DR DisGeNET; 9202; -.
DR GeneCards; ZMYM4; -.
DR HGNC; HGNC:13055; ZMYM4.
DR HPA; ENSG00000146463; Low tissue specificity.
DR MIM; 613568; gene.
DR neXtProt; NX_Q5VZL5; -.
DR OpenTargets; ENSG00000146463; -.
DR PharmGKB; PA37633; -.
DR VEuPathDB; HostDB:ENSG00000146463; -.
DR eggNOG; ENOG502QQQ9; Eukaryota.
DR GeneTree; ENSGT00940000159550; -.
DR InParanoid; Q5VZL5; -.
DR OMA; CLLQFCC; -.
DR OrthoDB; 587724at2759; -.
DR PhylomeDB; Q5VZL5; -.
DR TreeFam; TF336988; -.
DR PathwayCommons; Q5VZL5; -.
DR SignaLink; Q5VZL5; -.
DR BioGRID-ORCS; 9202; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; ZMYM4; human.
DR GenomeRNAi; 9202; -.
DR Pharos; Q5VZL5; Tbio.
DR PRO; PR:Q5VZL5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5VZL5; protein.
DR Bgee; ENSG00000146463; Expressed in calcaneal tendon and 208 other tissues.
DR ExpressionAtlas; Q5VZL5; baseline and differential.
DR Genevisible; Q5VZL5; HS.
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 Pfam; PF12012; DUF3504; 1.
DR Pfam; PF06467; zf-FCS; 5.
DR SMART; SM00746; TRASH; 10.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Isopeptide bond; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..1548
FT /note="Zinc finger MYM-type protein 4"
FT /id="PRO_0000299017"
FT ZN_FING 362..402
FT /note="MYM-type 1"
FT ZN_FING 414..457
FT /note="MYM-type 2"
FT ZN_FING 464..499
FT /note="MYM-type 3"
FT ZN_FING 510..544
FT /note="MYM-type 4"
FT ZN_FING 554..592
FT /note="MYM-type 5"
FT ZN_FING 600..631
FT /note="MYM-type 6"
FT ZN_FING 708..742
FT /note="MYM-type 7"
FT ZN_FING 749..788
FT /note="MYM-type 8"
FT ZN_FING 795..829
FT /note="MYM-type 9"
FT REGION 162..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1178
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 107
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1030
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1064
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1071
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 1539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 195
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 232
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 260
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 273
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 289
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 327
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 400
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 428
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 430
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 1035
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1061
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1080
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1431
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..324
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027512"
FT VAR_SEQ 1..32
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027513"
FT VAR_SEQ 524..612
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_027514"
FT VARIANT 452
FT /note="V -> I (in dbSNP:rs34924462)"
FT /evidence="ECO:0000269|PubMed:9455477"
FT /id="VAR_034764"
FT VARIANT 1410
FT /note="R -> W (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs191217255)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035672"
FT CONFLICT 279..280
FT /note="AQ -> RT (in Ref. 4; BAA24855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1548 AA; 172788 MW; 3B5B730EA9B9882B CRC64;
MAEREVESGP RKRFEQKSGA VFDEIVENCG GIMDTEMSED IDHNLTPTLD SMSYGMPNQT
GSENSLLDED DYFLNSGDLA GIPVVGSDNE DEQDFSSKDN LVSSIHTDDS LEVERRVTQH
ESDNENEIQI QNKLKKDFPK QFDQVSVFKS IRKDFSLVRE NSKETFSGKE KNRDLTYERE
KRLDKPHKDL DSRLKSSFFD KAANQVEETL HTHLPQTPET NFRDSSYPFA NKESIGSELG
NSFASNIRIK EEPLDDEYDK AMAPQQGLLD KIKDEPDNAQ EYSHGQQQKT QEGELKISAV
FSVSGSPLAP QLTTGFQPSL ASSGMNKMLP SVPATAVRVS CSGCKKILQK GQTAYQRKGS
TQLFCSTLCL TGYTVPPARP PPPLTKKTCS SCSKDILNPK DVISAQFENT TTSKDFCSQS
CLSTYELKKK PIVTINTNSI STKCSMCQKN AVIRHEVNYQ NVVHKLCSDA CFSKFRSANN
LTMNCCENCG GYCYSGSGQC HMLQIEGQSK KFCSSSCITA YKQKSAKITP CALCKSLRSS
AEMIENTNSL GKTELFCSVN CLSAYRVKMV TSAGVQVQCN SCKTSAIPQY HLAMSDGSIR
NFCSYSCVVA FQNLFNKPTG MNSSVVPLSQ GQVIVSIPTG STVSAGGGST SAVSPTSISS
SAAAGLQRLA AQSQHVGFAR SVVKLKCQHC NRLFATKPEL LDYKGKMFQF CGKNCSDEYK
KINNVMAMCE YCKIEKIVKE TVRFSGADKS FCSEGCKLLY KHDLAKRWGN HCKMCSYCLQ
TSPKLVQNNL GGKVEEFCCE ECMSKYTVLF YQMAKCDACK RQGKLSESLK WRGEMKHFCN
LLCILMFCNQ QSVCDPPSQN NAANISMVQA ASAGPPSLRK DSTPVIANVV SLASAPAAQP
TVNSNSVLQG AVPTVTAKII GDASTQTDAL KLPPSQPPRL LKNKALLCKP ITQTKATSCK
PHTQNKECQT EDTPSQPQII VVPVPVPVFV PIPLHLYTQY APVPFGIPVP MPVPMLIPSS
MDSEDKVTES IEDIKEKLPT HPFEADLLEM AEMIAEDEEK KTLSQGESQT SEHELFLDTK
IFEKDQGSTY SGDLESEAVS TPHSWEEELN HYALKSNAVQ EADSELKQFS KGETEQDLEA
DFPSDSFDPL NKGQGIQARS RTRRRHRDGF PQPRRRGRKK SIVAVEPRSL IQGAFQGCSV
SGMTLKYMYG VNAWKNWVQW KNAKEEQGDL KCGGVEQASS SPRSDPLGST QDHALSQESS
EPGCRVRSIK LKEDILSCTF AELSLGLCQF IQEVRRPNGE KYDPDSILYL CLGIQQYLFE
NGRIDNIFTE PYSRFMIELT KLLKIWEPTI LPNGYMFSRI EEEHLWECKQ LGAYSPIVLL
NTLLFFNTKY FQLKNVTEHL KLSFAHVMRR TRTLKYSTKM TYLRFFPPLQ KQESEPDKLT
VGKRKRNEDD EVPVGVEMAE NTDNPLRCPV RLYEFYLSKC SESVKQRNDV FYLQPERSCV
PNSPMWYSTF PIDPGTLDTM LTRILMVREV HEELAKAKSE DSDVELSD
