ZKSC5_MOUSE
ID ZKSC5_MOUSE Reviewed; 819 AA.
AC Q9Z1D8; E9QLY2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Zinc finger protein with KRAB and SCAN domains 5;
DE AltName: Full=Zinc finger protein 95;
DE Short=Zfp-95;
GN Name=Zkscan5; Synonyms=Zfp95;
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12860387; DOI=10.1016/s0014-5793(03)00669-0;
RA Weissig H., Narisawa S., Sikstrom C., Olsson P.G., McCarrey J.R.,
RA Tsonis P.A., Del Rio-Tsonis K., Millan J.L.;
RT "Three novel spermatogenesis-specific zinc finger genes.";
RL FEBS Lett. 547:61-68(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:12860387}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U62907; AAD00103.1; -; mRNA.
DR EMBL; AC127411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS39386.1; -.
DR RefSeq; NP_057892.2; NM_016683.2.
DR AlphaFoldDB; Q9Z1D8; -.
DR SMR; Q9Z1D8; -.
DR STRING; 10090.ENSMUSP00000082814; -.
DR iPTMnet; Q9Z1D8; -.
DR PhosphoSitePlus; Q9Z1D8; -.
DR jPOST; Q9Z1D8; -.
DR MaxQB; Q9Z1D8; -.
DR PaxDb; Q9Z1D8; -.
DR PRIDE; Q9Z1D8; -.
DR ProteomicsDB; 299562; -.
DR Antibodypedia; 30392; 125 antibodies from 21 providers.
DR DNASU; 22757; -.
DR Ensembl; ENSMUST00000085671; ENSMUSP00000082814; ENSMUSG00000055991.
DR GeneID; 22757; -.
DR KEGG; mmu:22757; -.
DR UCSC; uc009amn.2; mouse.
DR CTD; 23660; -.
DR MGI; MGI:107533; Zkscan5.
DR VEuPathDB; HostDB:ENSMUSG00000055991; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162299; -.
DR HOGENOM; CLU_002678_23_3_1; -.
DR InParanoid; Q9Z1D8; -.
DR OMA; TKSHQCN; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9Z1D8; -.
DR TreeFam; TF338146; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 22757; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Zkscan5; mouse.
DR PRO; PR:Q9Z1D8; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9Z1D8; protein.
DR Bgee; ENSMUSG00000055991; Expressed in secondary oocyte and 236 other tissues.
DR ExpressionAtlas; Q9Z1D8; baseline and differential.
DR Genevisible; Q9Z1D8; MM.
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; 12.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..819
FT /note="Zinc finger protein with KRAB and SCAN domains 5"
FT /id="PRO_0000047316"
FT DOMAIN 51..132
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 216..287
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 341..363
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 369..391
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 397..419
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 425..447
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 540..562
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 568..590
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 596..618
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 624..646
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 652..674
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 708..730
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 764..786
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 792..814
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 236..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L8"
FT CROSSLNK 246
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L8"
FT CROSSLNK 302
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L8"
FT CROSSLNK 700
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L8"
FT CROSSLNK 776
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L8"
FT CONFLICT 186
FT /note="V -> A (in Ref. 1; AAD00103)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="T -> I (in Ref. 1; AAD00103)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="R -> T (in Ref. 1; AAD00103)"
FT /evidence="ECO:0000305"
FT CONFLICT 792
FT /note="L -> F (in Ref. 1; AAD00103)"
FT /evidence="ECO:0000305"
FT CONFLICT 807
FT /note="L -> F (in Ref. 1; AAD00103)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 819 AA; 93788 MW; 51F5C332FBFCCB5A CRC64;
MIMTESRAVI HLEPPAETSQ EQADLLIVKV EEEDCSWMQG YNRPVLETFY QRFKHFQYHE
AAGPRDALSQ LRVLCCEWLR PELHTKEQIL ELLVLEQFLT ILPEEFQAWV REHHPESGEE
AVAVIESIQR ELEERRQQIA TSPEVLPQKM VPPGATQESF SHQCLPVEAQ PERESQNLLE
ENALPVLQVS SVPLKDSQEL TDSLLSDGPQ KLVKTEDVAD VAVSFILEEW AHLDQSQKSL
GRDSRKEDCE STTPVDYEPK EGNLEFTVQQ VSDAADPHWV AAERTEKNGV QRPESGEVSD
LKDMVPRWQV NPTSGNPRQK RPLRSGPDVN RKQKSNGERG HRCGDCGKFF LQASNFIQHR
RIHTGEKPFK CGECGKSYNQ RVHLTQHQRV HTGEKPYKCQ VCGKAFRVSS HLVQHHSVHS
GERPYGCNEC GKSFGRHSHL IEHLKRHFRE KSQRCSDRRS KNTKLNIKQI PGLSEADLEL
SGEVQRNACQ AEGHSEGCEH QDGQQGVVMK ETLGQSSSKR TDCNEFSYVH KKSSPGERPH
QCNECGKSFI QSAHLIQHRR IHTGEKPFRC EECGKSYNQR VHLTQHHRVH TGEKPYACHL
CGKAFRVRSH LVQHQSVHSR ERPFKCNECG KGFGRRSHLA GHLRLHSRDK SHQCHECGEI
FFQYVSLLEH QVLHVGQKSE KNGICEEAYS WNLTVIKDKK LELQEQPYQC DSCGKAFSYS
SDLIQHYRTH SAEKPQKCDA CRDSTCQCPH IKQQQKSCPS GKSHQCNECG RGFSLKSHLS
QHQRIHTGEK PLQCKECGMS FSWSCSLFKH LRSHERTDP
