ZMYM4_MOUSE
ID ZMYM4_MOUSE Reviewed; 1549 AA.
AC A2A791; Q3UFQ2; Q6ZQB9; Q80X47; Q8K1H5;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Zinc finger MYM-type protein 4;
DE AltName: Full=Zinc finger protein 262;
GN Name=Zmym4; Synonyms=Kiaa0425, Zfp262, Znf262;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-218.
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 253-1549 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND SER-1548, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC cytoskeletal organization. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2A791-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2A791-2; Sequence=VSP_027515;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97947.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAM19273.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK129137; BAC97947.1; ALT_INIT; mRNA.
DR EMBL; AL606985; CAM15585.1; -; Genomic_DNA.
DR EMBL; AL606908; CAM15585.1; JOINED; Genomic_DNA.
DR EMBL; AL606908; CAM19271.1; -; Genomic_DNA.
DR EMBL; AL606985; CAM19271.1; JOINED; Genomic_DNA.
DR EMBL; AL606908; CAM19273.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK148366; BAE28508.1; -; mRNA.
DR EMBL; BC029670; AAH29670.1; -; mRNA.
DR EMBL; BC050924; AAH50924.1; -; mRNA.
DR CCDS; CCDS51303.1; -. [A2A791-1]
DR RefSeq; NP_001107871.1; NM_001114399.1. [A2A791-1]
DR RefSeq; XP_006503407.1; XM_006503344.3. [A2A791-2]
DR AlphaFoldDB; A2A791; -.
DR SMR; A2A791; -.
DR BioGRID; 212440; 12.
DR IntAct; A2A791; 2.
DR MINT; A2A791; -.
DR STRING; 10090.ENSMUSP00000101714; -.
DR iPTMnet; A2A791; -.
DR PhosphoSitePlus; A2A791; -.
DR EPD; A2A791; -.
DR jPOST; A2A791; -.
DR MaxQB; A2A791; -.
DR PaxDb; A2A791; -.
DR PeptideAtlas; A2A791; -.
DR PRIDE; A2A791; -.
DR ProteomicsDB; 302067; -. [A2A791-1]
DR ProteomicsDB; 302068; -. [A2A791-2]
DR Antibodypedia; 31536; 118 antibodies from 28 providers.
DR Ensembl; ENSMUST00000106108; ENSMUSP00000101714; ENSMUSG00000042446. [A2A791-1]
DR GeneID; 67785; -.
DR KEGG; mmu:67785; -.
DR UCSC; uc008uty.3; mouse. [A2A791-1]
DR CTD; 9202; -.
DR MGI; MGI:1915035; Zmym4.
DR VEuPathDB; HostDB:ENSMUSG00000042446; -.
DR eggNOG; ENOG502QQQ9; Eukaryota.
DR GeneTree; ENSGT00940000159550; -.
DR InParanoid; A2A791; -.
DR OMA; CLLQFCC; -.
DR OrthoDB; 587724at2759; -.
DR PhylomeDB; A2A791; -.
DR TreeFam; TF336988; -.
DR BioGRID-ORCS; 67785; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Zmym4; mouse.
DR PRO; PR:A2A791; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2A791; protein.
DR Bgee; ENSMUSG00000042446; Expressed in undifferentiated genital tubercle and 256 other tissues.
DR ExpressionAtlas; A2A791; baseline and differential.
DR Genevisible; A2A791; MM.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS: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:0000250|UniProtKB:Q5VZL5"
FT CHAIN 2..1549
FT /note="Zinc finger MYM-type protein 4"
FT /id="PRO_0000299018"
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 83..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1179
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT MOD_RES 1065
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT MOD_RES 1072
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT MOD_RES 1182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT MOD_RES 1257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT MOD_RES 1540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT MOD_RES 1543
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT MOD_RES 1548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT CROSSLNK 148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT CROSSLNK 195
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT CROSSLNK 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT CROSSLNK 232
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT CROSSLNK 273
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT CROSSLNK 289
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT CROSSLNK 327
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT CROSSLNK 400
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT CROSSLNK 428
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT CROSSLNK 430
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT CROSSLNK 1035
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT CROSSLNK 1062
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT CROSSLNK 1081
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT CROSSLNK 1128
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT CROSSLNK 1432
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VZL5"
FT VAR_SEQ 524..612
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027515"
FT CONFLICT 1357
FT /note="M -> V (in Ref. 1; BAC97947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1549 AA; 172438 MW; 644AF24B4FEB0A62 CRC64;
MAEREVETGP RKRFEQKSDA VFDEIVENCG VMDTEMSEDT DHNLTPTLAS MSYGMPNQTG
SENSLLDEDD YFLNSGDLAG IPVVSSDNED EQDCSSKDNL VSSVHTDGSL EVERRAAHQE
SDNENEIQIQ NQLKKDFPKQ FDQVSVFKSI RKDFCLVREN SKETFSGKEK NRDLTYHERE
KRLDKPHKGL DSRLKSSFFD KAANQVEETL HTHLPQNPET NFRDSSYPFA SKESIGSELG
NSFASNIRIK EEPLDDEYDR AVAPQQGLLD RVKDEPDNAQ EYSHGQQQKT QEGELKISAV
FSVSGSPLAP QLTTGFQPSL ASPGMNKMLP SVPATAVRVS CSGCKKILQK GQTAYQRKGS
TQLFCSTLCL TGYTVPPARP PPPLTKKTCS SCSKDILNPK DVISAQFENS TTSKDFCSQS
CLSTYELKKK PIVTINTNSI STKCSMCQKN AVIRHEVNYQ NVVHKLCSDA CFSKFRSANN
LTMNCCENCG GYCYSGSGQC HVLQIEGQSK KFCSSMCVTS YKQKSAKITP CALCKSLRSS
AEMIENTNSL GKTELFCSVN CLSAYRVKMV TSAGVQVQCN SCKTSAIPQY HLAMSDGSIR
NFCSYSCVVA FQNLFNKPTG MNSSVVPLSQ GQVIVSIPTG SSASAGGGST PAVSPTSINS
SAAAGLQRLA AQSQHVGFAR SVVKLRCQHC NRLFATKPEL LDYKGKMFQF CGKNCCDEYK
KINNVMAMCE YCKIEKIIKE TVRFSGADKS FCSEGCKLLY KHDLGKRWGS HCKMCSYCLQ
TSPKLIQNNL GGKVEDFCCE ECMSKYTVLF YQMAKCDGCK RQGKLSESLK WRGDIKHFCN
LLCILMFCHQ QTVCDPPLQN NAVASISMVQ AASAGPPSLR KDSTPVIANV VSLASAPAAQ
PTANTNSVLQ GAVPTVTAKI IGDASTQTDA LKLPPSQPPR LLKNKALLCK PITQTKATSC
KPHTQNKECQ TDTPSEPQVM VVPVPVPVFV PIPLHLYTQY TPVPFGIPVP MPVPMFIPSS
MDNDEKATEG IEDIKEKLAT HPFEADLLEM AEMIAEDEEK EKTLSQGESQ TSEQELFLDT
KIFEKDQGST YSGDLESEAV STPHSWEEEL NHYALKSNAV QDADSELKPF SKGETEQDLE
ADFPSESFDP LNKGQGIQAR SRTRRRHRDG FPQPRRRGRK KSVVPVEPRS LIQGALQGCS
VSGMTLKYMY GVNAWKNWVQ WKNAKDEQGD LKCGGGELAS ASPCSDSLGS AQDHALSQES
SEQGCKARSV KLKEDILSCT FSELSLGLCQ FIQEVRRPNG EKYDPDSILY LCLGIQQYLF
ENGRIDNIFT EPYSRFMIEL TKLLKIWEPT ILPNGYMFSR IEEEHLWECK QLGAYSPIVL
LNTLLFFNTK YFQLRNVTEH LKLSFAHVMR RTRTLKYSTK MTYLRFFPPL QKPESEPDKV
TIGKRKRNED DEAPVGVEMA ENTDNPLRCP VRLYEFYLSK CSESVKQRSD VFYLQPERSC
VPNSPMWYST FPIDPGTLDT MLTRILMVRE VHEELAKAKS EDSDAELSD
