ZN668_MOUSE
ID ZN668_MOUSE Reviewed; 619 AA.
AC Q8K2R5; Q3TEM2; Q3U7Y5; Q8C8B7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Zinc finger protein 668;
GN Name=Znf668; Synonyms=Zfp668;
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=Bone marrow, Cerebellum, Eye, 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].
RC STRAIN=FVB/N-3; 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).
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; AK047593; BAC33091.1; -; mRNA.
DR EMBL; AK053438; BAC35386.1; -; mRNA.
DR EMBL; AK152456; BAE31234.1; -; mRNA.
DR EMBL; AK169556; BAE41226.1; -; mRNA.
DR EMBL; BC030314; AAH30314.1; -; mRNA.
DR CCDS; CCDS21881.1; -.
DR RefSeq; NP_666371.1; NM_146259.3.
DR RefSeq; XP_006507911.1; XM_006507848.2.
DR RefSeq; XP_006507912.1; XM_006507849.1.
DR RefSeq; XP_006507913.1; XM_006507850.2.
DR RefSeq; XP_006507914.1; XM_006507851.3.
DR RefSeq; XP_017177743.1; XM_017322254.1.
DR RefSeq; XP_017177744.1; XM_017322255.1.
DR RefSeq; XP_017177745.1; XM_017322256.1.
DR AlphaFoldDB; Q8K2R5; -.
DR SMR; Q8K2R5; -.
DR IntAct; Q8K2R5; 1.
DR STRING; 10090.ENSMUSP00000056105; -.
DR iPTMnet; Q8K2R5; -.
DR PhosphoSitePlus; Q8K2R5; -.
DR EPD; Q8K2R5; -.
DR jPOST; Q8K2R5; -.
DR MaxQB; Q8K2R5; -.
DR PaxDb; Q8K2R5; -.
DR PeptideAtlas; Q8K2R5; -.
DR PRIDE; Q8K2R5; -.
DR ProteomicsDB; 275030; -.
DR Antibodypedia; 13908; 120 antibodies from 27 providers.
DR DNASU; 244219; -.
DR Ensembl; ENSMUST00000054415; ENSMUSP00000056105; ENSMUSG00000049728.
DR Ensembl; ENSMUST00000106261; ENSMUSP00000101868; ENSMUSG00000049728.
DR Ensembl; ENSMUST00000106262; ENSMUSP00000101869; ENSMUSG00000049728.
DR Ensembl; ENSMUST00000106263; ENSMUSP00000101870; ENSMUSG00000049728.
DR GeneID; 244219; -.
DR KEGG; mmu:244219; -.
DR UCSC; uc009jxa.1; mouse.
DR CTD; 244219; -.
DR MGI; MGI:2442943; Zfp668.
DR VEuPathDB; HostDB:ENSMUSG00000049728; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00920000149141; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; Q8K2R5; -.
DR OMA; WDEVQAH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8K2R5; -.
DR TreeFam; TF331849; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 244219; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q8K2R5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8K2R5; protein.
DR Bgee; ENSMUSG00000049728; Expressed in embryonic brain and 214 other tissues.
DR ExpressionAtlas; Q8K2R5; baseline and differential.
DR Genevisible; Q8K2R5; 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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; IDA:NTNU_SB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
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; 14.
DR SMART; SM00355; ZnF_C2H2; 16.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 16.
PE 2: Evidence at transcript level;
KW Acetylation; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..619
FT /note="Zinc finger protein 668"
FT /id="PRO_0000251480"
FT ZN_FING 22..44
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 84..106
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 112..134
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 140..162
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 168..190
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 196..218
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 224..246
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 252..274
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 280..302
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 308..330
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 336..358
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 364..386
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 392..414
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 516..538
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 544..566
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 572..594
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 36..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96K58"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96K58"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96K58"
FT CROSSLNK 59
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96K58"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96K58"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96K58"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96K58"
FT CROSSLNK 512
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96K58"
FT CONFLICT 86
FT /note="C -> Y (in Ref. 1; BAE41226)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="K -> R (in Ref. 1; BAE41226)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="T -> I (in Ref. 1; BAC33091)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="F -> L (in Ref. 1; BAE31234)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="R -> G (in Ref. 1; BAC33091)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="L -> I (in Ref. 1; BAC33091)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 68347 MW; A50C008267E810B5 CRC64;
MEVEATEARS PGPCYKRSGR RYKCLFCTKT FPNAPRAARH AATHTPTDCT EEVREAQPKV
DTEPKAEEAS GDKVSASVAK PRPYACPLCP KAYKTAPELR SHGRSHTGEK PFPCPECGRR
FMQPVCLRVH LASHAGELPF RCTHCPKAYG TLSKLKIHQR GHTGERPYAC PDCGKSFADP
SVFRKHRRTH AGLRPYSCER CGKAYAELKD LRNHERSHTG ERPFLCSECG KSFSRSSSLT
CHQRIHAAQK PYRCPACGKG FTQLSSYQSH ERTHSGEKPF LCPRCGRMFS DPSSFRRHQR
AHEGVKPYRC EKCGKDFRQP ADLAMHRRVH TGDRPFKCLQ CDKTFVASWD LKRHALVHSG
QRPFRCEECG RAFAERASLT KHSRMHSGER PFHCNACGKS FVVLSSLRKH ERTHRSNETT
GAAPQQELVL GLALPVGVVG EGSAAPVAGA GVGDAPAGLL GLPPESGGVV ATQWQVVGMT
VEHVECQDAG VGEAPSTLGD AGEVGGEETD EKPPQFVCRE CKETFSTLTL LRRHERSHPE
LRPFPCTQCG KSFSDRAGLR KHSRTHSSVR PYSCSQCPKA FLSASDLRKH ERTHPVPIGT
PIPLEPLVAL LGMPEEGSA
