Z354C_HUMAN
ID Z354C_HUMAN Reviewed; 554 AA.
AC Q86Y25; Q6P4P9; Q8NFX1;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Zinc finger protein 354C;
DE AltName: Full=Kidney, ischemia, and developmentally-regulated protein 3;
DE Short=hKID3;
GN Name=ZNF354C; Synonyms=KID3;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Kidney;
RX PubMed=15555547; DOI=10.1016/j.bbrc.2004.10.158;
RA Gao L., Sun C., Qiu H.-L., Liu H., Shao H.-J., Wang J., Li W.-X.;
RT "Cloning and characterization of a novel human zinc finger gene, hKid3,
RT from a C2H2-ZNF enriched human embryonic cDNA library.";
RL Biochem. Biophys. Res. Commun. 325:1145-1152(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-250.
RC TISSUE=Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-554.
RA Gou D.-M., Li W.-X., Gao L., Sun Y.;
RT "A novel zinc finger gene, KID3.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-111; LYS-167; LYS-198 AND
RP LYS-531, AND 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 function as a transcription repressor. Binds to 5'-CCACA-
CC 3' core sequence. Suppresses osteogenic effects of RUNX2. May be
CC involved in osteoblastic differentiation (By similarity). Plays a role
CC in postnatal myogenesis, may be involved in the regulation of satellite
CC cells self-renewal (By similarity). {ECO:0000250|UniProtKB:Q571J5,
CC ECO:0000250|UniProtKB:Q9EPU7, ECO:0000269|PubMed:15555547}.
CC -!- SUBUNIT: Interacts with RUNX2. Binds consensus element OSE2 (By
CC similarity). {ECO:0000250|UniProtKB:Q9EPU7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15555547}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney and skeletal muscle. Very low
CC expression in brain and heart. {ECO:0000269|PubMed:15555547}.
CC -!- DEVELOPMENTAL STAGE: Expressed in brain. Very low expression in lung
CC and liver. {ECO:0000269|PubMed:15555547}.
CC -!- DOMAIN: KRAB domain is not required for nuclear targeting or for DNA
CC binding. {ECO:0000250|UniProtKB:Q9EPU7}.
CC -!- DOMAIN: Zinc finger region is involved in nuclear targeting and DNA-
CC binding. {ECO:0000250|UniProtKB:Q9EPU7}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH63312.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF525463; AAO83897.1; -; mRNA.
DR EMBL; BC063312; AAH63312.1; ALT_FRAME; mRNA.
DR EMBL; AF395540; AAM69676.1; -; mRNA.
DR CCDS; CCDS4443.1; -.
DR RefSeq; NP_055409.1; NM_014594.2.
DR RefSeq; XP_016864898.1; XM_017009409.1.
DR AlphaFoldDB; Q86Y25; -.
DR SMR; Q86Y25; -.
DR BioGRID; 119048; 27.
DR IntAct; Q86Y25; 16.
DR STRING; 9606.ENSP00000324064; -.
DR iPTMnet; Q86Y25; -.
DR PhosphoSitePlus; Q86Y25; -.
DR BioMuta; ZNF354C; -.
DR DMDM; 74762464; -.
DR EPD; Q86Y25; -.
DR jPOST; Q86Y25; -.
DR MassIVE; Q86Y25; -.
DR MaxQB; Q86Y25; -.
DR PaxDb; Q86Y25; -.
DR PeptideAtlas; Q86Y25; -.
DR PRIDE; Q86Y25; -.
DR ProteomicsDB; 70354; -.
DR Antibodypedia; 29471; 47 antibodies from 13 providers.
DR DNASU; 30832; -.
DR Ensembl; ENST00000315475.7; ENSP00000324064.6; ENSG00000177932.7.
DR GeneID; 30832; -.
DR KEGG; hsa:30832; -.
DR MANE-Select; ENST00000315475.7; ENSP00000324064.6; NM_014594.3; NP_055409.1.
DR UCSC; uc003mju.4; human.
DR CTD; 30832; -.
DR DisGeNET; 30832; -.
DR GeneCards; ZNF354C; -.
DR HGNC; HGNC:16736; ZNF354C.
DR HPA; ENSG00000177932; Low tissue specificity.
DR MIM; 619511; gene.
DR neXtProt; NX_Q86Y25; -.
DR OpenTargets; ENSG00000177932; -.
DR PharmGKB; PA38184; -.
DR VEuPathDB; HostDB:ENSG00000177932; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162715; -.
DR HOGENOM; CLU_002678_0_9_1; -.
DR InParanoid; Q86Y25; -.
DR OMA; STFIEHQ; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q86Y25; -.
DR TreeFam; TF350822; -.
DR PathwayCommons; Q86Y25; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q86Y25; -.
DR BioGRID-ORCS; 30832; 4 hits in 1085 CRISPR screens.
DR ChiTaRS; ZNF354C; human.
DR GenomeRNAi; 30832; -.
DR Pharos; Q86Y25; Tdark.
DR PRO; PR:Q86Y25; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q86Y25; protein.
DR Bgee; ENSG00000177932; Expressed in cortical plate and 155 other tissues.
DR Genevisible; Q86Y25; 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; 10.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..554
FT /note="Zinc finger protein 354C"
FT /id="PRO_0000280408"
FT DOMAIN 12..83
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 216..238
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 244..266
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 272..294
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 300..322
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 328..350
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 356..378
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 384..406
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 412..434
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 440..462
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 468..490
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 496..518
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 111
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 167
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 198
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 531
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 250
FT /note="E -> K (in dbSNP:rs17855823)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031138"
FT VARIANT 546
FT /note="F -> L (in dbSNP:rs1445846)"
FT /id="VAR_031139"
FT VARIANT 553
FT /note="E -> K (in dbSNP:rs1445845)"
FT /id="VAR_031140"
FT CONFLICT 375
FT /note="Q -> H (in Ref. 3; AAM69676)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="N -> T (in Ref. 3; AAM69676)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 554 AA; 64847 MW; 3B95DED46CCECFFC CRC64;
MAVDLLSAQE PVTFRDVAVF FSQDEWLHLD SAQRALYREV MLENYSSLVS LGIPFSMPKL
IHQLQQGEDP CMVEREVPSD TRLGFKTWLE TEALPHRQDI FIEETSQGMV KKESIKDGHW
DINFEEAVEF ESEIEEEQEK KPLRQMIDSH EKTISEDGNH TSLELGKSLF TNTALVTQQS
VPIERIPNMY YTFGKDFKQN FDLMKCFQIY PGGKPHICNE CGKSFKQNLH LIEHQRIHTG
EKPYKCNECE KTFSHRSSLL SHQRIHTGEK PYKCNECEKA FSNSSTLIKH LRVHTGEKPY
RCRECGKAFS QCSTLTVHQR IHTGEKLYKC GECEKAFNCR AKLHRHQRIH TGEKPYKCSE
CGKGYSQFTS LAEHQRFHTG EQLYTCLECG RTFTRIVTLI EHQRIHTGQK PYQCNECEKA
FNQYSSFNEH RKIHTGEKLY TCEECGKAFG CKSNLYRHQR IHTGEKPYQC NQCGKAFSQY
SFLTEHERIH TGEKLYKCME CGKAYSYRSN LCRHKKVHTK EKLYKWKEYG KPFICSSSLT
QYQRFFKGDK AYEV
