ZKSC5_PANTR
ID ZKSC5_PANTR Reviewed; 839 AA.
AC A2T7D2;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Zinc finger protein with KRAB and SCAN domains 5;
DE AltName: Full=Zinc finger protein 95 homolog;
DE Short=Zfp-95;
GN Name=ZKSCAN5; Synonyms=ZFP95;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nickel G.C., Tefft D.L., Trevarthen K., Funt J., Adams M.D.;
RT "Positive selection in transcription factor genes on the human lineage.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; DQ977421; ABM92087.1; -; Genomic_DNA.
DR RefSeq; NP_001138504.1; NM_001145032.1.
DR RefSeq; XP_009451526.1; XM_009453251.2.
DR RefSeq; XP_009451527.1; XM_009453252.2.
DR RefSeq; XP_009451529.1; XM_009453254.2.
DR RefSeq; XP_009451530.1; XM_009453255.2.
DR AlphaFoldDB; A2T7D2; -.
DR SMR; A2T7D2; -.
DR STRING; 9598.ENSPTRP00000033288; -.
DR PaxDb; A2T7D2; -.
DR Ensembl; ENSPTRT00000036012; ENSPTRP00000033288; ENSPTRG00000019455.
DR GeneID; 737683; -.
DR KEGG; ptr:737683; -.
DR CTD; 23660; -.
DR VGNC; VGNC:4571; ZKSCAN5.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162299; -.
DR HOGENOM; CLU_002678_23_3_1; -.
DR InParanoid; A2T7D2; -.
DR OMA; TKSHQCN; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF338146; -.
DR Proteomes; UP000002277; Chromosome 7.
DR Bgee; ENSPTRG00000019455; Expressed in fibroblast and 21 other tissues.
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: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 CDD; cd07765; KRAB_A-box; 1.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 10.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 3: Inferred from homology;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..839
FT /note="Zinc finger protein with KRAB and SCAN domains 5"
FT /id="PRO_0000285464"
FT DOMAIN 51..132
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 218..291
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 346..368
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 374..396
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 402..424
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 430..452
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 549..571
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 577..599
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 605..627
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 633..655
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 661..683
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 717..739
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 745..763
FT /note="C2H2-type 11; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 773..795
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 801..823
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 151..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L8"
FT CROSSLNK 216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L8"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L8"
FT CROSSLNK 270
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L8"
FT CROSSLNK 303
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L8"
FT CROSSLNK 317
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L8"
FT CROSSLNK 509
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L8"
FT CROSSLNK 513
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L8"
FT CROSSLNK 709
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L8"
FT CROSSLNK 785
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L8"
SQ SEQUENCE 839 AA; 96909 MW; D402EE9C1B6B2139 CRC64;
MIMTESREVI DLDPPAETSQ EQEDLFIVKV EEEDCTWMQE YNPPTFETFY QRFRHFQYHE
ASGPREALSQ LRVLCCEWLR PELHTKEQIL ELLVLEQFLT ILPEEFQPWV REHHPESGEE
AVAVIENIQR ELEERRQQIV ACPDVLPRKM APPGAVQESC SPQPLTVDTQ PEQAPQKPRL
LEENALPVLQ VPSLPLKDSQ ELTASLLSTG SQKLVKIEEV ADVAVSFILE EWGHLDQSQK
SLYRDDRKEN YGSITSMGYE SRDNMELIVK QISDDSESRW VAPEHTERSV PQDPDFAEVS
DLKGMVQRWQ VNPTVGKSRQ NPSQKRDLDA ITDISPKQST HGERGHRCSD CGKFFLQASN
FIQHRRIHTG EKPFKCGECG KSYNQRVHLT QHQRVHTGEK PYKCQVCGKA FRVSSHLVQH
HSVHSGERPY GCNECGKNFG RHSHLIEHLK RHFREKSQRC SDKRSKNTKL SVKKKISEYS
EADMELSGKT QRNVSQVQDF GEGCEFQGKL DRKQGIPMKE ILGQPSSKRM NYSEVPYVHK
KSSTGERPHK CNECGKSFIQ SAHLIQHQRI HTGEKPFRCE ECGKSYNQRV HLTQHQRVHT
GEKPYTCPLC GKAFRVRSHL VQHQSVHSGE RPFKCNECGK GFGRRSHLAG HLRLHSREKS
HQCRECGEIF FQYVSLIEHQ VLHMGQKNEK NGICEEAYSW NLTVIEDKKI ELQEQPYQCD
ICGKAFGYSS DLIQHYRTHT AEKPYQCDIC RENVGQCSHT KQHQKIYSST KSHQCHECGR
GFTLKSHLNQ HQRIHTGEKP FQCKECGMNF SWSCSLFKHL RSHERTDPIN TLSVEGSLL
