ZN652_MOUSE
ID ZN652_MOUSE Reviewed; 608 AA.
AC Q5DU09; A2A617; Q7TNT4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Zinc finger protein 652;
GN Name=Znf652; Synonyms=Kiaa0924, Zfp652;
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] (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Kidney;
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: Functions as a transcriptional repressor. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CBFA2T3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5DU09-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5DU09-2; Sequence=VSP_023669, VSP_023670;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK220361; BAD90422.1; -; mRNA.
DR EMBL; AL593858; CAM15507.1; -; Genomic_DNA.
DR EMBL; BC055752; AAH55752.1; -; mRNA.
DR CCDS; CCDS36287.1; -. [Q5DU09-1]
DR RefSeq; NP_963903.2; NM_201609.2. [Q5DU09-1]
DR AlphaFoldDB; Q5DU09; -.
DR SMR; Q5DU09; -.
DR BioGRID; 234503; 30.
DR STRING; 10090.ENSMUSP00000103345; -.
DR iPTMnet; Q5DU09; -.
DR PhosphoSitePlus; Q5DU09; -.
DR EPD; Q5DU09; -.
DR jPOST; Q5DU09; -.
DR MaxQB; Q5DU09; -.
DR PaxDb; Q5DU09; -.
DR PRIDE; Q5DU09; -.
DR Antibodypedia; 30374; 71 antibodies from 21 providers.
DR DNASU; 268469; -.
DR Ensembl; ENSMUST00000091565; ENSMUSP00000089153; ENSMUSG00000075595. [Q5DU09-1]
DR Ensembl; ENSMUST00000107717; ENSMUSP00000103345; ENSMUSG00000075595. [Q5DU09-1]
DR GeneID; 268469; -.
DR KEGG; mmu:268469; -.
DR UCSC; uc007laq.1; mouse. [Q5DU09-1]
DR CTD; 268469; -.
DR MGI; MGI:2442221; Zfp652.
DR VEuPathDB; HostDB:ENSMUSG00000075595; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157416; -.
DR HOGENOM; CLU_002678_74_2_1; -.
DR InParanoid; Q5DU09; -.
DR OMA; VENCAAH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q5DU09; -.
DR TreeFam; TF332655; -.
DR BioGRID-ORCS; 268469; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Zfp652; mouse.
DR PRO; PR:Q5DU09; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5DU09; protein.
DR Bgee; ENSMUSG00000075595; Expressed in hindlimb stylopod muscle and 213 other tissues.
DR ExpressionAtlas; Q5DU09; baseline and differential.
DR Genevisible; Q5DU09; MM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; 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; 4.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..608
FT /note="Zinc finger protein 652"
FT /id="PRO_0000280429"
FT ZN_FING 244..267
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 271..293
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 298..321
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 328..350
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 356..378
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 384..406
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 412..434
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 440..462
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 468..491
FT /note="C2H2-type 9; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 61..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..608
FT /note="Mediates interaction with CBFA2T3"
FT /evidence="ECO:0000250"
FT COMPBIAS 67..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..165
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D9"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1L1J6"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A1L1J6"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D9"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D9"
FT VAR_SEQ 300..350
FT /note="CVSCNKSFKKLWSLHEHIKIVHGYAEKKFACEICEKKFYTMAHVRKHMVAH
FT -> VGLTSGGQSFQARTWLFRVIWCLPKRIEAEGTDFTNYHFRLCCLGLFKTKA (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023669"
FT VAR_SEQ 351..608
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023670"
SQ SEQUENCE 608 AA; 69441 MW; 501DA89A7E92289F CRC64;
MSYTASPCPE LVEPCAVHAE GMAQEESHRS QAPPTFYHGA SQELDLSTKV YKRESGSPYS
VLADTKMSKP HLHETEEQPY FREPRAVSDV HTVKEDRENS DDTEEEEEVS YKREQIIVEV
NLNNQTLNVS KGEKGVSSQS KETPVLKTSS EEDEEETEEE ATDNSSDYGE NGRQKKKEKQ
VERVRVTQRR TRRAASAAAA TTSPAPRTTR GRRKSAELPK RKKRATKEAK APVQKAKCEE
KETLTCEKCP RVFNTRWYLE KHMNVTHRRM QICDKCGKKF VLESELSLHQ QTDCEKNIQC
VSCNKSFKKL WSLHEHIKIV HGYAEKKFAC EICEKKFYTM AHVRKHMVAH TKDMPFTCET
CGKSFKRSMS LKVHSLQHSG EKPFRCENCD ERFQYKYQLR SHMSIHIGHK QFMCQWCGKD
FNMKQYFDEH MKTHTGEKPF ICEICGKSFT SRPNMKRHRR THTGEKPYPC DVCGQRFRFS
NMLKAHKEKC FRVTSPVNVP PAVQIPLASA PAAPAPAVAN TPTSPAPAVS MSPVGAVLPS
RPVPHPFSHL HIHTHPHHAH HLPIPPVPHL PPPPALFKSE PLNHRSQSED TFLRHLAEKN
SAAPAQHH
