ZN668_BOVIN
ID ZN668_BOVIN Reviewed; 619 AA.
AC Q2TA17; Q1JPF5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Zinc finger protein 668;
GN Name=ZNF668;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-116.
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI11166.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC111165; AAI11166.1; ALT_SEQ; mRNA.
DR EMBL; BT025398; ABF57354.1; -; mRNA.
DR RefSeq; NP_001070421.1; NM_001076953.1.
DR RefSeq; XP_005225022.1; XM_005224965.3.
DR RefSeq; XP_015315872.1; XM_015460386.1.
DR AlphaFoldDB; Q2TA17; -.
DR SMR; Q2TA17; -.
DR STRING; 9913.ENSBTAP00000008736; -.
DR PaxDb; Q2TA17; -.
DR PRIDE; Q2TA17; -.
DR Ensembl; ENSBTAT00000008736; ENSBTAP00000008736; ENSBTAG00000006650.
DR GeneID; 767831; -.
DR KEGG; bta:767831; -.
DR CTD; 79759; -.
DR VEuPathDB; HostDB:ENSBTAG00000006650; -.
DR VGNC; VGNC:37326; ZNF668.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00920000149141; -.
DR HOGENOM; CLU_002678_44_10_1; -.
DR InParanoid; Q2TA17; -.
DR OMA; WDEVQAH; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF331849; -.
DR Reactome; R-BTA-212436; Generic Transcription Pathway.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000006650; Expressed in laryngeal cartilage and 102 other tissues.
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; IEA:Ensembl.
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; 12.
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_0000251477"
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 52..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..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 57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
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"
SQ SEQUENCE 619 AA; 68095 MW; 56EB28883E1C4FEC CRC64;
MEVESPEERS PAPGYKRSGR RYKCLSCTKT FPNAPRAARH AATHGLADCT EEMAEAKLKP
ETDPKAEDAS GDKVSGAAAK PRPYACPLCP KAYKTAPELR SHGRSHTGEK PFPCPECGRR
FMQPVCLRVH LASHAGELPF RCAHCPKAYG ALSKLKIHQR GHTGERPYTC ADCGKSFADP
SVFRKHRRTH AGLRPYSCER CGKAYAELKD LRNHERSHTG ERPFLCSECG KSFSRSSSLT
CHQRIHAAQK PYRCPACGKG FTQLSSYQSH ERTHSGEKPF LCPRCGRMFS DPSSFRRHQR
AHEGVKPYRC EKCGKDFRQP ADLAMHRRVH TGDRPFKCLQ CDKTFVASWD LKRHALVHSG
QRPFRCEECG RAFAERASLT KHSRVHSGER PFHCNACGKS FVVSSSLRKH ERTHRSSEAT
GAPPQQELVV GLALPVSMAG EGPAAPASGA ALGDPPAGLL GLPSESGGVM ATQWQVVGMT
VEHVECQDAG VGEAPGPLGA AGEVGGEEVD EKPPQFVCRE CKETFSTLTL LRRHERSHPE
LRPFHCTQCG KSFSDRAGLR KHSRTHSSVR PYTCPHCPKA FLSASDLRKH ERTHPVPIGT
PTPLEPLVAL LGMPEEGPA
