ZFP62_MOUSE
ID ZFP62_MOUSE Reviewed; 914 AA.
AC Q8C827; Q3U3H0; Q62510; Q8BT00; Q8C2S6; Q8R5D1;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Zinc finger protein 62;
DE Short=Zfp-62;
DE AltName: Full=ZT3;
GN Name=Zfp62;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Extraembryonic tissue, Head, Placenta, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-900 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 292-914 (ISOFORM 3).
RC TISSUE=Lens;
RA Brady J.P.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 393-914, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Skeletal muscle;
RX PubMed=8808410; DOI=10.1016/0925-4773(95)00465-3;
RA Polimeni M., Giorgi S., De Gregorio L., Dragani T.A., Molinaro M.,
RA Cossu G., Bouche M.;
RT "Differentiation dependent expression in muscle cells of ZT3, a novel zinc
RT finger factor differentially expressed in embryonic and adult tissues.";
RL Mech. Dev. 54:107-117(1996).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-881, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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: May play a role in differentiating skeletal muscle.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8C827-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C827-2; Sequence=VSP_010137;
CC Name=3;
CC IsoId=Q8C827-3; Sequence=VSP_010138;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal and cardiac muscle.
CC {ECO:0000269|PubMed:8808410}.
CC -!- DEVELOPMENTAL STAGE: At 8.5 dpc, expressed predominantly in neural tube
CC and somites. At 9.5 dpc, expression is higher in the peripheral region
CC of the brain, in the dorsal region of the neural tube, in the segmental
CC plate and in the somites. In developing brain, expression is restricted
CC to regions with actively proliferating cells. At later stages,
CC expressed in many tissues of neuroectodermal and mesodermal origin. At
CC 17 dpc, expression is high in the skeletal muscle fibers, which are
CC mitotically arrested and terminally differentiated.
CC {ECO:0000269|PubMed:8808410}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22935.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC25897.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK028351; BAC25897.1; ALT_SEQ; mRNA.
DR EMBL; AK048619; BAC33395.1; -; mRNA.
DR EMBL; AK088060; BAC40122.1; -; mRNA.
DR EMBL; AK154767; BAE32816.1; -; mRNA.
DR EMBL; BC022935; AAH22935.1; ALT_SEQ; mRNA.
DR EMBL; BC065692; AAH65692.1; -; mRNA.
DR EMBL; L36315; AAA40580.1; -; mRNA.
DR EMBL; Z67747; CAA91560.1; -; mRNA.
DR CCDS; CCDS24601.1; -. [Q8C827-2]
DR RefSeq; NP_001020017.1; NM_001024846.1. [Q8C827-2]
DR RefSeq; NP_033588.2; NM_009562.2. [Q8C827-1]
DR RefSeq; XP_006533258.1; XM_006533195.2.
DR RefSeq; XP_006533261.1; XM_006533198.2.
DR RefSeq; XP_006533262.1; XM_006533199.2. [Q8C827-2]
DR RefSeq; XP_006533263.1; XM_006533200.2.
DR RefSeq; XP_006533265.1; XM_006533202.3.
DR RefSeq; XP_006533266.1; XM_006533203.2.
DR RefSeq; XP_011247278.1; XM_011248976.2.
DR RefSeq; XP_017169999.1; XM_017314510.1. [Q8C827-2]
DR AlphaFoldDB; Q8C827; -.
DR SMR; Q8C827; -.
DR BioGRID; 204675; 39.
DR IntAct; Q8C827; 1.
DR MINT; Q8C827; -.
DR STRING; 10090.ENSMUSP00000104820; -.
DR iPTMnet; Q8C827; -.
DR PhosphoSitePlus; Q8C827; -.
DR SwissPalm; Q8C827; -.
DR EPD; Q8C827; -.
DR MaxQB; Q8C827; -.
DR PaxDb; Q8C827; -.
DR PRIDE; Q8C827; -.
DR ProteomicsDB; 274985; -. [Q8C827-1]
DR ProteomicsDB; 274986; -. [Q8C827-2]
DR ProteomicsDB; 274987; -. [Q8C827-3]
DR Antibodypedia; 53012; 34 antibodies from 10 providers.
DR DNASU; 22720; -.
DR Ensembl; ENSMUST00000061757; ENSMUSP00000056226; ENSMUSG00000046311. [Q8C827-2]
DR Ensembl; ENSMUST00000109197; ENSMUSP00000104820; ENSMUSG00000046311. [Q8C827-2]
DR Ensembl; ENSMUST00000109198; ENSMUSP00000104821; ENSMUSG00000046311. [Q8C827-2]
DR Ensembl; ENSMUST00000180016; ENSMUSP00000137583; ENSMUSG00000046311. [Q8C827-2]
DR GeneID; 22720; -.
DR KEGG; mmu:22720; -.
DR UCSC; uc007ipv.1; mouse. [Q8C827-1]
DR CTD; 643836; -.
DR MGI; MGI:99662; Zfp62.
DR VEuPathDB; HostDB:ENSMUSG00000046311; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162750; -.
DR InParanoid; Q8C827; -.
DR OMA; GNTESKW; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8C827; -.
DR TreeFam; TF343410; -.
DR BioGRID-ORCS; 22720; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q8C827; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8C827; protein.
DR Bgee; ENSMUSG00000046311; Expressed in undifferentiated genital tubercle and 269 other tissues.
DR ExpressionAtlas; Q8C827; baseline and differential.
DR Genevisible; Q8C827; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 22.
DR SMART; SM00355; ZnF_C2H2; 26.
DR SUPFAM; SSF57667; SSF57667; 16.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 25.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 26.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..914
FT /note="Zinc finger protein 62"
FT /id="PRO_0000047306"
FT ZN_FING 131..153
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 159..181
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 187..209
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 215..237
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 243..265
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 271..293
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 299..321
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 327..349
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 355..377
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 383..405
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 411..433
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 439..461
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 467..489
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 495..517
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 523..545
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 551..573
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 579..601
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 607..629
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 635..657
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 663..685
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 691..713
FT /note="C2H2-type 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 719..741
FT /note="C2H2-type 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 747..769
FT /note="C2H2-type 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 775..797
FT /note="C2H2-type 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 803..824
FT /note="C2H2-type 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 830..852
FT /note="C2H2-type 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NB50"
FT CROSSLNK 57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NB50"
FT CROSSLNK 60
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NB50"
FT CROSSLNK 77
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NB50"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NB50"
FT CROSSLNK 577
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NB50"
FT CROSSLNK 738
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NB50"
FT CROSSLNK 872
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NB50"
FT VAR_SEQ 1..7
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_010137"
FT VAR_SEQ 292..304
FT /note="IHTGEKPYECDEC -> LSLSLSLSLSLSL (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_010138"
FT CONFLICT 540..541
FT /note="VH -> EN (in Ref. 1; BAC40122)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 914 AA; 104812 MW; 196A50D47205E9B9 CRC64;
MSYLKTTMED EESSKKNEND SNADSQCPSV GFFHKDHMQK SKTGDTCDLF PKWKILKEGK
SSIREMIDTH TNAANIKLEQ DDETSEKSFY PSTNTMHQTI PTEPNCTKQG EHTENINGNV
HPAHIADKKL HKCDECGKSF KYNSRLVQHK IMHTGEKRYE CDDCRGTFRS SSSLRVHKRI
HTGEKPYKCD ECGKAYMSYS SLINHKSTHS GEKNCKCDEC GKSFNYSSVL DQHKRIHTGE
KPYECGECGK AFRNSSGLRV HKRIHTGEKP YECDTCGKTF SNSSGLRVHK RIHTGEKPYE
CDECGKAFIT CRTLLNHKSI HFGDKPYKCD ECEKSFNYSS LLIQHKVIHT GEKPYECDEC
GKAFRNSSGL IVHKRIHTGE KPYKCDICGK AFSYSSGLAV HKSIHPGKKA HECKDCGKSF
SYNSLLLQHK TIHTGERPYV CDVCGKTFRN NSGLKVHRRL HTGEKPYKCD VCGKAYISRS
SLKNHKGIHM GEKPYKCSYC EKSFNYSSAL EQHKRIHTRE KPFGCDECGK AFRNNSGLKV
HKRIHTGERP YKCEECGKAY ISLSSLINHK SVHPGEKPFK CDECEKAFIT YRTLLNHKKI
HLGEKPYKCD VCEKSFNYTS LLSQHKRVHT REKPFECDRC EKVFRNNSSL KVHKRIHTGE
KPYECDICGK AYISHSSLIN HKSTHPGKTS YTCDECGKAF FSSRTLISHK RVHLGEKPFK
CVECGKSFSY SSLLSQHKRI HTGEKPYVCD WCGKAFRNSS GLTVHKRIHT GEKPYGCDEC
EKAYISHSSL INHKSVHRGK QPYNCECGKS FNYRSVLDQH KRIHTGKKPY RCNDCGKAFN
IRSNLTKHKR IHTGEESLNM ANMESHSGTF QKMIYYEGGN SLDGTRMQMP VWEAEHAKSQ
RNQIEEKLYE YNNF
