ZNF45_HUMAN
ID ZNF45_HUMAN Reviewed; 682 AA.
AC Q02386; P17016; P78472; Q9P1U9;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Zinc finger protein 45;
DE AltName: Full=BRC1744;
DE AltName: Full=Zinc finger protein 13;
DE AltName: Full=Zinc finger protein KOX5;
GN Name=ZNF45; Synonyms=KOX5, ZNF13;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9067431; DOI=10.1159/000134490;
RA Constantinou-Deltas C.D., Bashiardes E., Patsalis P.C., Hadjimarcou M.,
RA Kroisel P.M., Ioannou P.A., Roses A.D., Lee J.E.;
RT "Complete coding sequence, exon/intron arrangement and chromosome location
RT of ZNF45, a KRAB-domain-containing gene.";
RL Cytogenet. Cell Genet. 75:230-233(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS LYS-255;
RP ALA-299; ARG-303 AND LYS-504.
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-400.
RX PubMed=1559709; DOI=10.1016/0888-7543(92)90451-w;
RA Constantinou-Deltas C.D., Gilbert J., Bartlett R.J., Herbstreith M.,
RA Roses A.D., Lee J.E.;
RT "The identification and characterization of KRAB-domain-containing zinc
RT finger proteins.";
RL Genomics 12:581-589(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 416-471.
RC TISSUE=Lymphoid tissue;
RX PubMed=2288909;
RA Thiesen H.-J.;
RT "Multiple genes encoding zinc finger domains are expressed in human T
RT cells.";
RL New Biol. 2:363-374(1990).
RN [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-117 AND LYS-249, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; L75847; AAB05653.1; -; mRNA.
DR EMBL; AC035150; AAF63030.1; -; Genomic_DNA.
DR EMBL; BC037575; AAH37575.1; -; mRNA.
DR EMBL; M67509; AAA36133.1; -; mRNA.
DR EMBL; M67509; AAA36134.1; -; mRNA.
DR EMBL; X52336; CAA36562.1; -; mRNA.
DR CCDS; CCDS12632.1; -.
DR PIR; A42177; A42177.
DR PIR; I37973; I37973.
DR RefSeq; NP_003416.1; NM_003425.3.
DR RefSeq; XP_011525569.1; XM_011527267.1.
DR RefSeq; XP_011525571.1; XM_011527269.1.
DR RefSeq; XP_011525573.1; XM_011527271.1.
DR RefSeq; XP_011525575.1; XM_011527273.1.
DR RefSeq; XP_016882706.1; XM_017027217.1.
DR RefSeq; XP_016882707.1; XM_017027218.1.
DR RefSeq; XP_016882708.1; XM_017027219.1.
DR RefSeq; XP_016882709.1; XM_017027220.1.
DR RefSeq; XP_016882710.1; XM_017027221.1.
DR RefSeq; XP_016882711.1; XM_017027222.1.
DR RefSeq; XP_016882712.1; XM_017027223.1.
DR RefSeq; XP_016882713.1; XM_017027224.1.
DR RefSeq; XP_016882714.1; XM_017027225.1.
DR RefSeq; XP_016882715.1; XM_017027226.1.
DR RefSeq; XP_016882716.1; XM_017027227.1.
DR AlphaFoldDB; Q02386; -.
DR SMR; Q02386; -.
DR BioGRID; 113421; 8.
DR IntAct; Q02386; 4.
DR STRING; 9606.ENSP00000269973; -.
DR iPTMnet; Q02386; -.
DR PhosphoSitePlus; Q02386; -.
DR BioMuta; ZNF45; -.
DR DMDM; 2507555; -.
DR EPD; Q02386; -.
DR jPOST; Q02386; -.
DR MassIVE; Q02386; -.
DR PaxDb; Q02386; -.
DR PeptideAtlas; Q02386; -.
DR PRIDE; Q02386; -.
DR ProteomicsDB; 58085; -.
DR Antibodypedia; 31139; 49 antibodies from 17 providers.
DR DNASU; 7596; -.
DR Ensembl; ENST00000269973.10; ENSP00000269973.4; ENSG00000124459.12.
DR Ensembl; ENST00000589703.5; ENSP00000468579.1; ENSG00000124459.12.
DR Ensembl; ENST00000615985.4; ENSP00000481895.1; ENSG00000124459.12.
DR GeneID; 7596; -.
DR KEGG; hsa:7596; -.
DR MANE-Select; ENST00000269973.10; ENSP00000269973.4; NM_003425.4; NP_003416.1.
DR UCSC; uc002oxu.3; human.
DR CTD; 7596; -.
DR DisGeNET; 7596; -.
DR GeneCards; ZNF45; -.
DR HGNC; HGNC:13111; ZNF45.
DR HPA; ENSG00000124459; Low tissue specificity.
DR MIM; 194554; gene.
DR neXtProt; NX_Q02386; -.
DR OpenTargets; ENSG00000124459; -.
DR PharmGKB; PA37686; -.
DR VEuPathDB; HostDB:ENSG00000124459; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162545; -.
DR HOGENOM; CLU_002678_31_6_1; -.
DR InParanoid; Q02386; -.
DR OMA; HEEPFCS; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q02386; -.
DR TreeFam; TF350845; -.
DR PathwayCommons; Q02386; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q02386; -.
DR BioGRID-ORCS; 7596; 14 hits in 1100 CRISPR screens.
DR ChiTaRS; ZNF45; human.
DR GenomeRNAi; 7596; -.
DR Pharos; Q02386; Tdark.
DR PRO; PR:Q02386; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q02386; protein.
DR Bgee; ENSG00000124459; Expressed in germinal epithelium of ovary and 179 other tissues.
DR ExpressionAtlas; Q02386; baseline and differential.
DR Genevisible; Q02386; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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 InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 15.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 10.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 15.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 18.
PE 1: Evidence at protein 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..682
FT /note="Zinc finger protein 45"
FT /id="PRO_0000047378"
FT DOMAIN 8..78
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 164..186
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 192..214
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 220..247
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 248..275
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 276..298
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 304..326
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 332..354
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 360..382
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 388..410
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 416..438
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 444..466
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 472..494
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 500..522
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 528..550
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 556..578
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 584..606
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 612..634
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 640..662
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 662..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 187
FT /note="A -> T (in dbSNP:rs1047452)"
FT /id="VAR_012019"
FT VARIANT 255
FT /note="R -> K (in dbSNP:rs399098)"
FT /evidence="ECO:0000269|PubMed:15057824"
FT /id="VAR_012020"
FT VARIANT 299
FT /note="T -> A (in dbSNP:rs388706)"
FT /evidence="ECO:0000269|PubMed:15057824"
FT /id="VAR_012021"
FT VARIANT 303
FT /note="P -> R (in dbSNP:rs388685)"
FT /evidence="ECO:0000269|PubMed:15057824"
FT /id="VAR_012022"
FT VARIANT 504
FT /note="R -> K (in dbSNP:rs407731)"
FT /evidence="ECO:0000269|PubMed:15057824"
FT /id="VAR_012023"
FT CONFLICT 455
FT /note="Q -> R (in Ref. 5; CAA36562)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 682 AA; 78242 MW; 9C8E536EB00FCE8B CRC64;
MTKSKEAVTF KDVAVVFSEE ELQLLDLAQR KLYRDVMLEN FRNVVSVGHQ STPDGLPQLE
REEKLWMMKM ATQRDNSSGA KNLKEMETLQ EVGLRYLPHE ELFCSQIWQQ ITRELIKYQD
SVVNIQRTGC QLEKRDDLHY KDEGFSNQSS HLQVHRVHTG EKPYKGEHCV KSFSWSSHLQ
INQRAHAGEK PYKCEKCDNA FRRFSSLQAH QRVHSRAKSY TNDASYRSFS QRSHLPHHQR
VPTGENPYKY EECGRNVGKS SHCQAPLIVH TGEKPYKCEE CGVGFSQRSY LQVHLKVHTG
KKPYKCEECG KSFSWRSRLQ AHERIHTGEK PYKCNACGKS FSYSSHLNIH CRIHTGEKPY
KCEECGKGFS VGSHLQAHQI SHTGEKPYKC EECGKGFCRA SNLLDHQRGH TGEKPYQCDA
CGKGFSRSSD FNIHFRVHTG EKPYKCEECG KGFSQASNLL AHQRGHTGEK PYKCGTCGKG
FSRSSDLNVH CRIHTGEKPY KCERCGKAFS QFSSLQVHQR VHTGEKPYQC AECGKGFSVG
SQLQAHQRCH TGEKPYQCEE CGKGFCRASN FLAHRGVHTG EKPYRCDVCG KRFRQRSYLQ
AHQRVHTGER PYKCEECGKV FSWSSYLQAH QRVHTGEKPY KCEECGKGFS WSSSLIIHQR
VHADDEGDKD FPSSEDSHRK TR
