ZKSC1_MOUSE
ID ZKSC1_MOUSE Reviewed; 561 AA.
AC Q8BGS3; Q7TS88; Q8BJ55; Q9CRN6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Zinc finger protein with KRAB and SCAN domains 1;
GN Name=Zkscan1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Egg, Ovary, Skin, and Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; 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).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BGS3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BGS3-2; Sequence=VSP_016958;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27539.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK131148; BAD21398.1; -; mRNA.
DR EMBL; AK020039; BAB31975.1; -; mRNA.
DR EMBL; AK028932; BAC26200.1; -; mRNA.
DR EMBL; AK031759; BAC27539.1; ALT_FRAME; mRNA.
DR EMBL; AK036807; BAC29584.1; -; mRNA.
DR EMBL; AK054323; BAC35730.1; -; mRNA.
DR EMBL; AK135999; BAE22767.1; -; mRNA.
DR EMBL; BC052441; AAH52441.1; -; mRNA.
DR CCDS; CCDS19788.1; -. [Q8BGS3-2]
DR CCDS; CCDS19789.1; -. [Q8BGS3-1]
DR RefSeq; NP_084145.1; NM_029869.1. [Q8BGS3-2]
DR RefSeq; NP_598667.2; NM_133906.4. [Q8BGS3-1]
DR RefSeq; XP_006504691.1; XM_006504628.3. [Q8BGS3-2]
DR AlphaFoldDB; Q8BGS3; -.
DR SMR; Q8BGS3; -.
DR BioGRID; 216852; 2.
DR IntAct; Q8BGS3; 1.
DR STRING; 10090.ENSMUSP00000019660; -.
DR iPTMnet; Q8BGS3; -.
DR PhosphoSitePlus; Q8BGS3; -.
DR EPD; Q8BGS3; -.
DR MaxQB; Q8BGS3; -.
DR PaxDb; Q8BGS3; -.
DR PeptideAtlas; Q8BGS3; -.
DR PRIDE; Q8BGS3; -.
DR ProteomicsDB; 275372; -. [Q8BGS3-1]
DR ProteomicsDB; 275373; -. [Q8BGS3-2]
DR Antibodypedia; 1764; 174 antibodies from 22 providers.
DR Ensembl; ENSMUST00000019660; ENSMUSP00000019660; ENSMUSG00000029729. [Q8BGS3-1]
DR Ensembl; ENSMUST00000066617; ENSMUSP00000068480; ENSMUSG00000029729. [Q8BGS3-2]
DR Ensembl; ENSMUST00000110962; ENSMUSP00000106587; ENSMUSG00000029729. [Q8BGS3-2]
DR Ensembl; ENSMUST00000110963; ENSMUSP00000106588; ENSMUSG00000029729. [Q8BGS3-2]
DR GeneID; 74570; -.
DR KEGG; mmu:74570; -.
DR UCSC; uc009aej.1; mouse. [Q8BGS3-1]
DR UCSC; uc009aek.1; mouse. [Q8BGS3-2]
DR CTD; 7586; -.
DR MGI; MGI:1921820; Zkscan1.
DR VEuPathDB; HostDB:ENSMUSG00000029729; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161592; -.
DR HOGENOM; CLU_002678_49_8_1; -.
DR InParanoid; Q8BGS3; -.
DR OMA; HRIHNRE; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8BGS3; -.
DR TreeFam; TF350830; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 74570; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Zkscan1; mouse.
DR PRO; PR:Q8BGS3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BGS3; protein.
DR Bgee; ENSMUSG00000029729; Expressed in metanephric cortical collecting duct and 229 other tissues.
DR Genevisible; Q8BGS3; MM.
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; 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; 4.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..561
FT /note="Zinc finger protein with KRAB and SCAN domains 1"
FT /id="PRO_0000047754"
FT DOMAIN 56..138
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 225..304
FT /note="KRAB"
FT ZN_FING 375..397
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 403..425
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 431..453
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 459..481
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 487..509
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 515..537
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
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 274..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17029"
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 226
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 277
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 296
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 301
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 336
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 373
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 410
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 438
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 476
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT CROSSLNK 558
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17029"
FT VAR_SEQ 192..264
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15449545,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016958"
FT CONFLICT 244
FT /note="L -> M (in Ref. 2; BAC27539)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 63439 MW; 757C4FD2CFB28DDB CRC64;
MMTAESRETT GLSPQAAQEK DGIVIVKVEE EDEEDHMWGQ DSSLQETPPP DPEVFRQRFR
RFCYQNTFGP REALNRLKEL CHQWLRPEVN SKEQILELLV LEQFLSILPK ELQVWLQEYR
PDSGEEAVTL LEDLELDLSG QQVPGQVHGP EMLARGVVPL DPVQESSSFD HHETAQSHFK
HSSRKPRLLS RALPATHVPA PHHEGNPRDQ AMASALLTAD SQAMVKIEDM AVSLILEEWG
CQNLARRNLN RDSRQMNLGN VFSQGSENRN GNESTSKAEV KEDSTSHGEI AGRFQKEFGE
KREQQGRVVE RQQKNPEEKT GKEKKEPGPP TAKEKKPSTG ERGPREKGKG LGRSFSLSAN
FNNTPEEAPS GAKTHRCDEC GKCFTRSSSL IRHKIIHTGE KPYECNECGK AFSLNSNLVL
HQRIHTGEKP HECNECGKAF SHSSNLILHQ RIHSGEKPYE CNECGKAFSQ SSDLTKHQRI
HTGEKPYECS ECGKAFNRNS YLILHRRIHT REKPYKCTKC GKAFTRSSTL TLHHRIHARE
RTSEYSPASL DAFGAFLKSC V
