ZN639_MOUSE
ID ZN639_MOUSE Reviewed; 485 AA.
AC Q99KZ6; A9X400; Q8BWU9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Zinc finger protein 639;
DE AltName: Full=Zinc finger protein ZASC1;
GN Name=Znf639; Synonyms=Zasc1, Zfp639;
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 [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16182284; DOI=10.1016/j.yexcr.2005.06.018;
RA Bogaerts S., Vanlandschoot A., van Hengel J., van Roy F.;
RT "Nuclear translocation of alphaN-catenin by the novel zinc finger
RT transcriptional repressor ZASC1.";
RL Exp. Cell Res. 311:1-13(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, Hippocampus, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 50-190.
RC STRAIN=CD-1;
RX PubMed=17623809; DOI=10.1101/gr.6320607;
RA Krull M., Petrusma M., Makalowski W., Brosius J., Schmitz J.;
RT "Functional persistence of exonized mammalian-wide interspersed repeat
RT elements (MIRs).";
RL Genome Res. 17:1139-1145(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 116-485.
RC TISSUE=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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, 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: Binds DNA and may function as a transcriptional repressor.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CTNNA2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AY736186; AAU85844.1; -; mRNA.
DR EMBL; AK049934; BAC33991.2; -; mRNA.
DR EMBL; AK076145; BAC36215.1; -; mRNA.
DR EMBL; AK076837; BAC36501.1; -; mRNA.
DR EMBL; AK078000; BAC37096.1; -; mRNA.
DR EMBL; CH466530; EDL34991.1; -; Genomic_DNA.
DR EMBL; CH466530; EDL34994.1; -; Genomic_DNA.
DR EMBL; CH466530; EDL34995.1; -; Genomic_DNA.
DR EMBL; CH466530; EDL34996.1; -; Genomic_DNA.
DR EMBL; DQ323614; ABD27861.1; -; mRNA.
DR EMBL; BC003941; AAH03941.1; -; mRNA.
DR CCDS; CCDS17295.1; -.
DR RefSeq; NP_001155290.1; NM_001161818.1.
DR RefSeq; NP_653102.1; NM_144519.4.
DR RefSeq; XP_006535590.1; XM_006535527.3.
DR RefSeq; XP_006535591.1; XM_006535528.2.
DR RefSeq; XP_006535592.1; XM_006535529.3.
DR AlphaFoldDB; Q99KZ6; -.
DR SMR; Q99KZ6; -.
DR STRING; 10090.ENSMUSP00000029203; -.
DR iPTMnet; Q99KZ6; -.
DR PhosphoSitePlus; Q99KZ6; -.
DR EPD; Q99KZ6; -.
DR jPOST; Q99KZ6; -.
DR MaxQB; Q99KZ6; -.
DR PaxDb; Q99KZ6; -.
DR PeptideAtlas; Q99KZ6; -.
DR PRIDE; Q99KZ6; -.
DR ProteomicsDB; 299593; -.
DR Antibodypedia; 46810; 79 antibodies from 19 providers.
DR DNASU; 67778; -.
DR Ensembl; ENSMUST00000029203; ENSMUSP00000029203; ENSMUSG00000027667.
DR Ensembl; ENSMUST00000191783; ENSMUSP00000141446; ENSMUSG00000027667.
DR Ensembl; ENSMUST00000193287; ENSMUSP00000141341; ENSMUSG00000027667.
DR GeneID; 67778; -.
DR KEGG; mmu:67778; -.
DR UCSC; uc008owf.2; mouse.
DR CTD; 67778; -.
DR MGI; MGI:1915028; Zfp639.
DR VEuPathDB; HostDB:ENSMUSG00000027667; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156335; -.
DR HOGENOM; CLU_569800_0_0_1; -.
DR InParanoid; Q99KZ6; -.
DR OMA; HLQIHET; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q99KZ6; -.
DR TreeFam; TF335557; -.
DR BioGRID-ORCS; 67778; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Zfp639; mouse.
DR PRO; PR:Q99KZ6; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q99KZ6; protein.
DR Bgee; ENSMUSG00000027667; Expressed in spermatocyte and 268 other tissues.
DR ExpressionAtlas; Q99KZ6; baseline and differential.
DR Genevisible; Q99KZ6; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISS:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0046718; P:viral entry into host cell; ISS:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..485
FT /note="Zinc finger protein 639"
FT /id="PRO_0000383573"
FT ZN_FING 204..227
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 233..255
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 260..283
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 289..311
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 374..397
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 403..425
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 431..454
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 460..482
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..455
FT /note="Interaction with CTNNA2"
FT /evidence="ECO:0000250"
FT COMPBIAS 115..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UID6"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UID6"
FT CROSSLNK 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UID6"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UID6"
FT CROSSLNK 226
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UID6"
FT CONFLICT 455
FT /note="S -> P (in Ref. 2; BAC33991)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 55678 MW; 5242B549C27A2E4F CRC64;
MNEYPKKRKR KTLHPSRYSD SSGISRIADG VSGIFSDHCY SVCSMRQPDL KYFDNKDDDS
DPETANDLPK FADGTKARNR NQSYLVPSPV LRILDHTVFS TEKSTEVEIC DEECASPESV
HQHTQEESPI EVHTSEDVPI AVEVHAISED YDIEAENNSS ESLQDQADEE PPAKLCKILD
KGQALNVTAQ QKWPLLRANS SGLYKCELCE FNSKYFSDLK QHVILKHKRT DSNVCRVCKE
SFSTNMLLIE HAKLHEEDPY ICKYCDYKTV IFENLSQHIA DTHFSDHLYW CEQCDVQFSS
SSELYLHFQE HSRDEQYLCQ FCEHETGDPE DLHSHVVNEH ARRLIELSDK CGSGGHGQCS
LLSKITFDKC KNFFVCQVCG FRSRLHTNVN RHVAIEHTKI FPHVCDDCGK GFSSMLEYCK
HLNSHLSEGI YLCQYCEYST GQIDDLKIHL DFKHSADLPH KCSECLMRFG NERDLLGHLQ
VHETT
