Z354A_HUMAN
ID Z354A_HUMAN Reviewed; 605 AA.
AC O60765; Q9UNJ8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Zinc finger protein 354A;
DE AltName: Full=Transcription factor 17;
DE Short=TCF-17;
DE AltName: Full=Zinc finger protein eZNF;
GN Name=ZNF354A; Synonyms=EZNF, HKL1, TCF17;
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].
RC TISSUE=Fetal brain;
RX PubMed=9465904; DOI=10.1159/000134673;
RA Omori Y., Kyushiki H., Takeda S., Suzuki M., Kawai A., Fujiwara T.,
RA Takahashi E., Nakamura Y.;
RT "Cloning, expression and mapping of a novel human zinc-finger gene TCF17
RT homologous to rodent Kid1.";
RL Cytogenet. Cell Genet. 78:285-288(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Inner ear;
RX PubMed=9919311; DOI=10.1023/b:scam.0000007114.14371.f4;
RA Jacob A.N., Manjunath N.A., Bray-Ward P., Kandpal R.P.;
RT "Molecular cloning of a zinc finger gene eZNF from a human inner ear cDNA
RT library, and in situ expression pattern of its mouse homologue in mouse
RT inner ear.";
RL Somat. Cell Mol. Genet. 24:121-129(1998).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=23665872; DOI=10.1007/s00018-013-1359-4;
RA Wang W., Cai J., Wu Y., Hu L., Chen Z., Hu J., Chen Z., Li W., Guo M.,
RA Huang Z.;
RT "Novel activity of KRAB domain that functions to reinforce nuclear
RT localization of KRAB-containing zinc finger proteins by interacting with
RT KAP1.";
RL Cell. Mol. Life Sci. 70:3947-3958(2013).
RN [4]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-110; LYS-121; LYS-139; LYS-171
RP AND LYS-268, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23665872}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney and inner ear.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; D89928; BAA25182.1; -; mRNA.
DR EMBL; AF116030; AAD05335.1; -; mRNA.
DR CCDS; CCDS4438.1; -.
DR RefSeq; NP_005640.2; NM_005649.2.
DR RefSeq; XP_016865280.1; XM_017009791.1.
DR AlphaFoldDB; O60765; -.
DR SMR; O60765; -.
DR BioGRID; 112800; 45.
DR IntAct; O60765; 11.
DR STRING; 9606.ENSP00000337122; -.
DR GlyGen; O60765; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60765; -.
DR PhosphoSitePlus; O60765; -.
DR BioMuta; ZNF354A; -.
DR EPD; O60765; -.
DR jPOST; O60765; -.
DR MassIVE; O60765; -.
DR PaxDb; O60765; -.
DR PeptideAtlas; O60765; -.
DR PRIDE; O60765; -.
DR ProteomicsDB; 49592; -.
DR Antibodypedia; 17609; 61 antibodies from 23 providers.
DR DNASU; 6940; -.
DR Ensembl; ENST00000335815.7; ENSP00000337122.2; ENSG00000169131.13.
DR GeneID; 6940; -.
DR KEGG; hsa:6940; -.
DR MANE-Select; ENST00000335815.7; ENSP00000337122.2; NM_005649.3; NP_005640.2.
DR CTD; 6940; -.
DR DisGeNET; 6940; -.
DR GeneCards; ZNF354A; -.
DR HGNC; HGNC:11628; ZNF354A.
DR HPA; ENSG00000169131; Low tissue specificity.
DR MIM; 602444; gene.
DR neXtProt; NX_O60765; -.
DR OpenTargets; ENSG00000169131; -.
DR PharmGKB; PA36383; -.
DR VEuPathDB; HostDB:ENSG00000169131; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161487; -.
DR HOGENOM; CLU_002678_57_1_1; -.
DR InParanoid; O60765; -.
DR OMA; TNHYKTH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O60765; -.
DR TreeFam; TF350822; -.
DR PathwayCommons; O60765; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; O60765; -.
DR BioGRID-ORCS; 6940; 12 hits in 1058 CRISPR screens.
DR GenomeRNAi; 6940; -.
DR Pharos; O60765; Tbio.
DR PRO; PR:O60765; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O60765; protein.
DR Bgee; ENSG00000169131; Expressed in secondary oocyte and 169 other tissues.
DR ExpressionAtlas; O60765; baseline and differential.
DR Genevisible; O60765; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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 GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc.
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; 13.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..605
FT /note="Zinc finger protein 354A"
FT /id="PRO_0000047238"
FT DOMAIN 14..85
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 214..236
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 242..264
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 270..292
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 298..320
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 354..376
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 382..404
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 410..432
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 438..460
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 464..488
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 494..516
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 522..544
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 550..572
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 578..600
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 74..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 110
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 268
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 437
FT /note="F -> Y (in Ref. 1; BAA25182)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 605 AA; 69237 MW; 464D20BBD9045AF9 CRC64;
MAAGQREARP QVSLTFEDVA VLFTRDEWRK LAPSQRNLYR DVMLENYRNL VSLGLPFTKP
KVISLLQQGE DPWEVEKDGS GVSSLGSKSS HKTTKSTQTQ DSSFQGLILK RSNRNVPWDL
KLEKPYIYEG RLEKKQDKKG SFQIVSATHK KIPTIERSHK NTELSQNFSP KSVLIRQQIL
PREKTPPKCE IQGNSLKQNS QLLNQPKITA DKRYKCSLCE KTFINTSSLR KHEKNHSGEK
LFKCKECSKA FSQSSALIQH QITHTGEKPY ICKECGKAFT LSTSLYKHLR THTVEKSYRC
KECGKSFSRR SGLFIHQKIH AEENPCKYNP GRKASSCSTS LSGCQRIHSR KKSYLCNECG
NTFKSSSSLR YHQRIHTGEK PFKCSECGRA FSQSASLIQH ERIHTGEKPY RCNECGKGFT
SISRLNRHRI IHTGEKFYNC NECGKALSSH STLIIHERIH TGEKPCKCKV CGKAFRQSSA
LIQHQRMHTG ERPYKCNECG KTFRCNSSLS NHQRIHTGEK PYRCEECGIS FGQSSALIQH
RRIHTGEKPF KCNTCGKTFR QSSSRIAHQR IHTGEKPYEC NTCGKLFNHR SSLTNHYKIH
IEEDP
