ZN639_RAT
ID ZN639_RAT Reviewed; 485 AA.
AC Q5PPG4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Zinc finger protein 639;
GN Name=Znf639;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC087704; AAH87704.1; -; mRNA.
DR RefSeq; NP_001074376.1; NM_001080907.2.
DR RefSeq; XP_006232316.1; XM_006232254.2.
DR RefSeq; XP_008759164.1; XM_008760942.1.
DR RefSeq; XP_008759165.1; XM_008760943.1.
DR AlphaFoldDB; Q5PPG4; -.
DR SMR; Q5PPG4; -.
DR STRING; 10116.ENSRNOP00000062807; -.
DR iPTMnet; Q5PPG4; -.
DR PhosphoSitePlus; Q5PPG4; -.
DR PaxDb; Q5PPG4; -.
DR Ensembl; ENSRNOT00000065518; ENSRNOP00000062807; ENSRNOG00000043053.
DR GeneID; 683504; -.
DR KEGG; rno:683504; -.
DR UCSC; RGD:1585689; rat.
DR CTD; 67778; -.
DR RGD; 1585689; LOC683504.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156335; -.
DR HOGENOM; CLU_569800_0_0_1; -.
DR InParanoid; Q5PPG4; -.
DR OMA; HLQIHET; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q5PPG4; -.
DR PRO; PR:Q5PPG4; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000043053; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q5PPG4; RN.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
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:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
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:RGD.
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_0000383574"
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..82
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:0007744|PubMed:22673903"
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; 55532 MW; 08836179B00514D9 CRC64;
MSEYPKKRKR KTLHPSRYSD SSGISRIADG VSGIFSDHCY SVCSMRQPDL KYFDNKDDDS
DPETANDLPK FTDGTKARSR SQSCLVPSPV LRILEHTVFS TEKPADVEIC DEECGSPESG
HQHTHEESPI EVHTSEDVPI AVEVHAISED YDIEAENNSS ESLLDQTDEE PPAKLCKILD
KSQASNVTAQ 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 GQIEDLKIHL DFKHSADLPH KCSDCLMRFG NERELISHLP
VHETT
