ZFP30_HUMAN
ID ZFP30_HUMAN Reviewed; 519 AA.
AC Q9Y2G7; Q58EY8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Zinc finger protein 30 homolog;
DE Short=Zfp-30;
DE AltName: Full=Zinc finger protein 745;
GN Name=ZFP30; Synonyms=KIAA0961, ZNF745;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-110 AND LYS-141, 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 {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76805.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB023178; BAA76805.2; ALT_INIT; mRNA.
DR EMBL; BC041087; AAH41087.1; -; mRNA.
DR CCDS; CCDS33005.1; -.
DR RefSeq; NP_001307595.1; NM_001320666.1.
DR RefSeq; NP_001307596.1; NM_001320667.1.
DR RefSeq; NP_001307597.1; NM_001320668.1.
DR RefSeq; NP_001307598.1; NM_001320669.1.
DR RefSeq; NP_055713.1; NM_014898.2.
DR AlphaFoldDB; Q9Y2G7; -.
DR SMR; Q9Y2G7; -.
DR BioGRID; 116509; 14.
DR IntAct; Q9Y2G7; 4.
DR STRING; 9606.ENSP00000343581; -.
DR iPTMnet; Q9Y2G7; -.
DR PhosphoSitePlus; Q9Y2G7; -.
DR BioMuta; ZFP30; -.
DR DMDM; 6686181; -.
DR EPD; Q9Y2G7; -.
DR jPOST; Q9Y2G7; -.
DR MassIVE; Q9Y2G7; -.
DR MaxQB; Q9Y2G7; -.
DR PaxDb; Q9Y2G7; -.
DR PeptideAtlas; Q9Y2G7; -.
DR PRIDE; Q9Y2G7; -.
DR ProteomicsDB; 85772; -.
DR Antibodypedia; 29933; 86 antibodies from 17 providers.
DR DNASU; 22835; -.
DR Ensembl; ENST00000351218.6; ENSP00000343581.1; ENSG00000120784.17.
DR Ensembl; ENST00000514101.6; ENSP00000422930.2; ENSG00000120784.17.
DR Ensembl; ENST00000684514.1; ENSP00000508019.1; ENSG00000120784.17.
DR GeneID; 22835; -.
DR KEGG; hsa:22835; -.
DR MANE-Select; ENST00000684514.1; ENSP00000508019.1; NM_001320669.3; NP_001307598.1.
DR UCSC; uc002ogx.2; human.
DR CTD; 22835; -.
DR DisGeNET; 22835; -.
DR GeneCards; ZFP30; -.
DR HGNC; HGNC:29555; ZFP30.
DR HPA; ENSG00000120784; Low tissue specificity.
DR MIM; 617317; gene.
DR neXtProt; NX_Q9Y2G7; -.
DR OpenTargets; ENSG00000120784; -.
DR PharmGKB; PA143485675; -.
DR VEuPathDB; HostDB:ENSG00000120784; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162363; -.
DR HOGENOM; CLU_002678_44_0_1; -.
DR InParanoid; Q9Y2G7; -.
DR OMA; YQRIHNR; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9Y2G7; -.
DR TreeFam; TF341817; -.
DR PathwayCommons; Q9Y2G7; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q9Y2G7; -.
DR BioGRID-ORCS; 22835; 7 hits in 1065 CRISPR screens.
DR ChiTaRS; ZFP30; human.
DR GenomeRNAi; 22835; -.
DR Pharos; Q9Y2G7; Tdark.
DR PRO; PR:Q9Y2G7; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9Y2G7; protein.
DR Bgee; ENSG00000120784; Expressed in cortical plate and 148 other tissues.
DR ExpressionAtlas; Q9Y2G7; baseline and differential.
DR Genevisible; Q9Y2G7; HS.
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; 12.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Methylation; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..519
FT /note="Zinc finger protein 30 homolog"
FT /id="PRO_0000047291"
FT DOMAIN 6..78
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 158..180
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 186..208
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 214..236
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 242..264
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 270..292
FT /note="C2H2-type 5; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 298..320
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 326..348
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 354..376
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 382..404
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 410..432
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 438..460
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 466..488
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 494..516
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT MOD_RES 75
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q60585"
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 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 519 AA; 61558 MW; A0903F75E3B1C320 CRC64;
MARDLVMFRD VAVDFSQEEW ECLNSYQRNL YRDVILENYS NLVSLAGCSI SKPDVITLLE
QGKEPWMVVR DEKRRWTLDL ESRYDTKKLF QGKDIYEMNL SQWKVMERIK SCGLEEQESP
HEVCFRQVTK TTSEKMPTYR KLTSLPLYQK SHNREKPYEC GECGKAFRVR QQLTFHQRIH
TGEKPYECKE CGKAFRQCAH LSRHQRIHTS DKLYECKKCG KIFTCGSDLR VHQRIHIGEK
PYECKECGKA FRVRGQLNLH QRIHTGEKPY ECKECGKAFR QYAHLTRHQR LNIAEKCYEC
KECGQAFLCS TGLRLHHKLH TGEKPYECKE CGKAFRVRQQ LTLHQRIHTG EKPYDCKECG
KTFSRGYHLT LHQRIHTGEK PYECKECQKF FRRYSELISH QGIHIGEKPY ECKECGKAFR
LFSQLTQHQS IHFGEKPFKC KECEKTFRLL SQLTQHQSIH TGEKPYDCKE CGKAFRLHSS
LIQHQRIHSG EKPYKCKECK KAFRQHSHLT YHQRIHNVT
