ZN250_MOUSE
ID ZN250_MOUSE Reviewed; 535 AA.
AC Q7TNU6; Q8BJ57;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Zinc finger protein 250;
DE AltName: Full=Zinc finger protein 647;
GN Name=Znf250; Synonyms=Zfp647, Znf647;
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 STRAIN=C57BL/6J; TISSUE=Embryonic 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK031543; BAC27443.1; -; mRNA.
DR EMBL; BC055686; AAH55686.1; -; mRNA.
DR CCDS; CCDS27596.1; -.
DR RefSeq; NP_001161748.1; NM_001168276.1.
DR RefSeq; NP_766405.2; NM_172817.3.
DR RefSeq; XP_006520991.1; XM_006520928.3.
DR RefSeq; XP_006520992.1; XM_006520929.3.
DR RefSeq; XP_011243919.1; XM_011245617.2.
DR AlphaFoldDB; Q7TNU6; -.
DR SMR; Q7TNU6; -.
DR STRING; 10090.ENSMUSP00000041575; -.
DR iPTMnet; Q7TNU6; -.
DR PhosphoSitePlus; Q7TNU6; -.
DR MaxQB; Q7TNU6; -.
DR PaxDb; Q7TNU6; -.
DR PRIDE; Q7TNU6; -.
DR ProteomicsDB; 275068; -.
DR Antibodypedia; 15013; 10 antibodies from 8 providers.
DR DNASU; 239546; -.
DR Ensembl; ENSMUST00000048854; ENSMUSP00000041575; ENSMUSG00000054967.
DR Ensembl; ENSMUST00000229055; ENSMUSP00000155685; ENSMUSG00000054967.
DR GeneID; 239546; -.
DR KEGG; mmu:239546; -.
DR UCSC; uc007wmu.2; mouse.
DR CTD; 239546; -.
DR MGI; MGI:3052806; Zfp647.
DR VEuPathDB; HostDB:ENSMUSG00000054967; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162306; -.
DR HOGENOM; CLU_002678_0_5_1; -.
DR InParanoid; Q7TNU6; -.
DR OMA; CMQQDSL; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q7TNU6; -.
DR TreeFam; TF341817; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 239546; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Zfp647; mouse.
DR PRO; PR:Q7TNU6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q7TNU6; protein.
DR Bgee; ENSMUSG00000054967; Expressed in manus and 215 other tissues.
DR ExpressionAtlas; Q7TNU6; baseline and differential.
DR Genevisible; Q7TNU6; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 13.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..535
FT /note="Zinc finger protein 250"
FT /id="PRO_0000047484"
FT DOMAIN 17..88
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 174..196
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 202..224
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 230..252
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 258..280
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 286..308
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 314..336
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 342..364
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 370..392
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 398..420
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 426..448
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 454..476
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 482..504
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 510..532
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P15622"
FT CROSSLNK 200
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P15622"
FT CROSSLNK 396
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P15622"
FT CONFLICT 171
FT /note="E -> A (in Ref. 1; BAC27443)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="K -> E (in Ref. 1; BAC27443)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 59873 MW; EB8EDABBE2716CBF CRC64;
MAAAGLLPLP AAPQAKVTFE DVAVLLSQEE WARLGPAQRG LYRHVMMETY GNVVSLGLPG
SKPVVISQLE RGEDPWVLDG QGTELSQSLG SDHSECKAKE ENQNTDLNVP PLISDEASAT
LTETPLRKVA EERYKTEPKV CPSPKPIGPQ NAHGLNPSVP VARPQTAPSV ERPYICIECG
KCFGRSSHLL QHQRIHTGEK PYVCHVCGKA FSQSSVLSKH RRIHTGEKPY ECNECGKAFR
VSSDLAQHHK IHTGEKPHEC LECGKAFTQL SHLIQHQRIH TGERPYVCPL CGKAFNHSTV
LRSHQRVHTG EKPHGCSECG KTFSVKRTLL QHQRVHTGEK PYTCSECGKA FSDRSVLIQH
HNVHTGEKPY ECSECGKTFS HRSTLMNHER IHTQEKPYAC YECGKAFVQH SHLIQHQRVH
TGEKPYVCGE CGHAFSARRS LIQHERIHTG EKPFQCTECG KAFSLKATLI VHLRTHTGEK
PYECNSCGKA FSQYSVLIQH QRIHTGEKPY ECGECGRAFN QHGHLIQHQK VHKKL
