ZN639_BOVIN
ID ZN639_BOVIN Reviewed; 485 AA.
AC A5PK30; A9X402;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Zinc finger protein 639;
GN Name=ZNF639;
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=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 50-190.
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).
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; BC142332; AAI42333.1; -; mRNA.
DR EMBL; DQ323616; ABD27863.1; -; mRNA.
DR RefSeq; NP_001092493.1; NM_001099023.2.
DR RefSeq; XP_010799645.1; XM_010801343.2.
DR RefSeq; XP_010799646.1; XM_010801344.2.
DR AlphaFoldDB; A5PK30; -.
DR SMR; A5PK30; -.
DR STRING; 9913.ENSBTAP00000045919; -.
DR PaxDb; A5PK30; -.
DR PRIDE; A5PK30; -.
DR Ensembl; ENSBTAT00000048967; ENSBTAP00000045919; ENSBTAG00000037393.
DR GeneID; 523536; -.
DR KEGG; bta:523536; -.
DR CTD; 51193; -.
DR VEuPathDB; HostDB:ENSBTAG00000037393; -.
DR VGNC; VGNC:52853; ZNF639.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156335; -.
DR HOGENOM; CLU_569800_0_0_1; -.
DR InParanoid; A5PK30; -.
DR OMA; HLQIHET; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF335557; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000037393; Expressed in oocyte and 107 other tissues.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
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: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; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 2: Evidence at transcript 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_0000383572"
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..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..455
FT /note="Interaction with CTNNA2"
FT /evidence="ECO:0000250"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UID6"
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"
SQ SEQUENCE 485 AA; 56105 MW; D214858CF8F0AFD7 CRC64;
MNEYPKKRKR KTLHPSRYSD SSGISRIADG FNGIFSDHCY SVCSMRQPDL KYFDNKDDDS
DTETSNELPK FTDGIKARNR NQNYLVPSPV LRILDHTAFP TEKSADIEIC DEDCDSPESV
HQQTQEESPI EVHTAEDVPI AAEVHAISED YDIETENNSS ESLQDQTDEE PPAKLCKIVD
KSQALNVTAQ QKWPLLRANS SGLYKCELCE FNSKYFSDLK QHMILKHKRT DSNVCRVCKE
SFSTNMLLIE HAKLHEEDPY ICKYCDYKTV IFENLSQHIA DTHFSDHLYW CEQCDVQFSS
SSELYLHFQE HSCDEQYLCQ FCEHETNDPE DLHSHVVNEH ACKLIELSDK YNNGEHGQYS
LLSKITFDKC KNFFVCQVCG FRSRLHTNVN RHVAIEHTKI FPHVCDDCGK GFSSMLEYCK
HLNSHLSEGI YLCQYCEYST GQIEDLKIHL DFKHSADLPH KCSDCLMRFG NERELISHLP
VHETT
