ID ZKSC1_RAT Reviewed; 562 AA.
AC Q4KLI1;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 24-JAN-2024, entry version 129.
DE RecName: Full=Zinc finger protein with KRAB and SCAN domains 1;
GN Name=Zkscan1;
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=Thymus;
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-13, 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: 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; BC099191; AAH99191.1; -; mRNA.
DR RefSeq; NP_001020931.1; NM_001025760.1.
DR AlphaFoldDB; Q4KLI1; -.
DR SMR; Q4KLI1; -.
DR STRING; 10116.ENSRNOP00000051042; -.
DR iPTMnet; Q4KLI1; -.
DR PhosphoSitePlus; Q4KLI1; -.
DR PaxDb; 10116-ENSRNOP00000051042; -.
DR Ensembl; ENSRNOT00000045379.4; ENSRNOP00000051042.3; ENSRNOG00000001335.7.
DR Ensembl; ENSRNOT00055019269; ENSRNOP00055015541; ENSRNOG00055011357.
DR Ensembl; ENSRNOT00060045689; ENSRNOP00060037914; ENSRNOG00060026363.
DR Ensembl; ENSRNOT00065000064; ENSRNOP00065000064; ENSRNOG00065000043.
DR GeneID; 498160; -.
DR KEGG; rno:498160; -.
DR UCSC; RGD:1560616; rat.
DR AGR; RGD:1560616; -.
DR CTD; 7586; -.
DR RGD; 1560616; Zkscan1.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161592; -.
DR HOGENOM; CLU_002678_49_8_1; -.
DR InParanoid; Q4KLI1; -.
DR OMA; HRIHNRE; -.
DR OrthoDB; 4682389at2759; -.
DR PhylomeDB; Q4KLI1; -.
DR TreeFam; TF350830; -.
DR Reactome; R-RNO-212436; Generic Transcription Pathway.
DR PRO; PR:Q4KLI1; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001335; Expressed in stomach and 19 other cell types or tissues.
DR Genevisible; Q4KLI1; RN.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 6.10.140.140; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 6.
DR Gene3D; 1.10.4020.10; DNA breaking-rejoining enzymes; 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 PANTHER; PTHR23226; ZINC FINGER AND SCAN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23226:SF94; ZINC FINGER PROTEIN WITH KRAB AND SCAN DOMAINS 1; 1.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
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..562
FT /note="Zinc finger protein with KRAB and SCAN domains 1"
FT /id="PRO_0000047756"
FT DOMAIN 56..138
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 226..305
FT /note="KRAB"
FT ZN_FING 376..398
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 404..426
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 432..454
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 460..482
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 488..510
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 516..538
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 180
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 227
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 278
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 302
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 337
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 374
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 411
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 439
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 477
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 559
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
SQ SEQUENCE 562 AA; 63365 MW; 06DE99D78EBB4572 CRC64;
MMTAESREAT GLSPQAAQEK DGIVIVKVEE EDEEDHMWGQ DASLQETPPP DPEVFRQRFR
RFCYQNTFGP REALNRLKEL CHQWLRPEVN TKEQILELLV LEQFLSILPK ELQVWLQEYR
PDSGEEAVTL LEDLELDLSG QQVPGQVHGP EMLARGVVPL DPVQESSSFD HHEAAQSHFK
HSSRKPRLLS PRALPATHVP APQHEGNPRD QAMASALLTA DSQAMVKIED MAVSLILEEW
GCQNLARRNL NRDSRQMNLG TVFSQGSENR NGSESTSKAE VKGDSTSHGE IAGRFQKEFG
EKREQQGRVI ERQQKNPEEK TGKEKKAPGP PTAKEKKPTT GERGPREKGK GLGRSFSLSA
NFNNTPEEIP SGAKTHRCDE CGKCFTRSSS LIRHKIIHTG EKPYECNECG KAFSLNSNLV
LHQRIHTGEK PHECNECGKA FSHSSNLILH QRIHSGEKPY ECNECGKAFS QSSDLTKHQR
IHTGEKPYEC SECGKAFNRN SYLILHRRIH TREKPYKCTK CGKAFTRSST LTLHHRIHAR
ERASEYSPAS LDTFGAFLKS CV
//
