ZN467_HUMAN
ID ZN467_HUMAN Reviewed; 595 AA.
AC Q7Z7K2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Zinc finger protein 467;
GN Name=ZNF467;
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=Mammary gland;
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 [2]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-97 AND LYS-368, 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: Transcription factor that promotes adipocyte differentiation
CC and suppresses osteoblast differentiation in the bone marrow. Enhances
CC the osteoclast-supporting ability of stromal cells. Binds with STAT3
CC the consensus sequence 5'-CTTCTGGGAAGA-3' of the acute phase response
CC element (APRE). Transactivates several promoters including FOS, OSM and
CC PPARG. Recruits a histone deacetylase complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with STAT3. Enhances STAT3 activity by keeping it in
CC the nucleus (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q7Z7K2; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-11986485, EBI-11953334;
CC Q7Z7K2; Q969R5: L3MBTL2; NbExp=3; IntAct=EBI-11986485, EBI-739909;
CC Q7Z7K2; P61968: LMO4; NbExp=3; IntAct=EBI-11986485, EBI-2798728;
CC Q7Z7K2; Q08117-2: TLE5; NbExp=3; IntAct=EBI-11986485, EBI-11741437;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; BC052625; AAH52625.1; -; mRNA.
DR CCDS; CCDS5899.1; -.
DR RefSeq; NP_997219.1; NM_207336.2.
DR RefSeq; XP_005250016.1; XM_005249959.4.
DR RefSeq; XP_005250017.1; XM_005249960.4.
DR RefSeq; XP_005250018.1; XM_005249961.4.
DR RefSeq; XP_011514160.1; XM_011515858.1.
DR AlphaFoldDB; Q7Z7K2; -.
DR SMR; Q7Z7K2; -.
DR BioGRID; 127969; 299.
DR IntAct; Q7Z7K2; 4.
DR STRING; 9606.ENSP00000304769; -.
DR iPTMnet; Q7Z7K2; -.
DR PhosphoSitePlus; Q7Z7K2; -.
DR BioMuta; ZNF467; -.
DR DMDM; 74762444; -.
DR MassIVE; Q7Z7K2; -.
DR PaxDb; Q7Z7K2; -.
DR PeptideAtlas; Q7Z7K2; -.
DR PRIDE; Q7Z7K2; -.
DR ProteomicsDB; 69556; -.
DR TopDownProteomics; Q7Z7K2; -.
DR Antibodypedia; 51657; 13 antibodies from 8 providers.
DR DNASU; 168544; -.
DR Ensembl; ENST00000302017.4; ENSP00000304769.3; ENSG00000181444.13.
DR GeneID; 168544; -.
DR KEGG; hsa:168544; -.
DR MANE-Select; ENST00000302017.4; ENSP00000304769.3; NM_207336.3; NP_997219.1.
DR UCSC; uc003wgd.3; human.
DR CTD; 168544; -.
DR GeneCards; ZNF467; -.
DR HGNC; HGNC:23154; ZNF467.
DR HPA; ENSG00000181444; Low tissue specificity.
DR MIM; 614040; gene.
DR neXtProt; NX_Q7Z7K2; -.
DR OpenTargets; ENSG00000181444; -.
DR PharmGKB; PA134886769; -.
DR VEuPathDB; HostDB:ENSG00000181444; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162497; -.
DR HOGENOM; CLU_002678_73_2_1; -.
DR InParanoid; Q7Z7K2; -.
DR OMA; CSGDEWM; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q7Z7K2; -.
DR TreeFam; TF326846; -.
DR PathwayCommons; Q7Z7K2; -.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; Q7Z7K2; -.
DR BioGRID-ORCS; 168544; 12 hits in 1102 CRISPR screens.
DR GenomeRNAi; 168544; -.
DR Pharos; Q7Z7K2; Tdark.
DR PRO; PR:Q7Z7K2; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q7Z7K2; protein.
DR Bgee; ENSG00000181444; Expressed in monocyte and 116 other tissues.
DR ExpressionAtlas; Q7Z7K2; baseline and differential.
DR Genevisible; Q7Z7K2; 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 InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 8.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
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..595
FT /note="Zinc finger protein 467"
FT /id="PRO_0000247517"
FT ZN_FING 160..182
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 188..210
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 216..238
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 244..266
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 272..294
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 300..322
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 355..377
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 431..453
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 459..481
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 487..509
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 515..537
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 543..565
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 368
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 324
FT /note="T -> A (in dbSNP:rs6965332)"
FT /id="VAR_052835"
SQ SEQUENCE 595 AA; 65124 MW; 8D0C6EEE42310BF6 CRC64;
MRETLEALSS LGFSVGQPEM APQSEPREGS HNAQEQMSSS REERALGVCS GHEAPTPEEG
AHTEQAEAPC RGQACSAQKA QPVGTCPGEE WMIRKVKVED EDQEAEEEVE WPQHLSLLPS
PFPAPDLGHL AAAYKLEPGA PGALSGLALS GWGPMPEKPY GCGECERRFR DQLTLRLHQR
LHRGEGPCAC PDCGRSFTQR AHMLLHQRSH RGERPFPCSE CDKRFSKKAH LTRHLRTHTG
ERPYPCAECG KRFSQKIHLG SHQKTHTGER PFPCTECEKR FRKKTHLIRH QRIHTGERPY
QCAQCARSFT HKQHLVRHQR VHQTAGPARP SPDSSASPHS TAPSPTPSFP GPKPFACSDC
GLSFGWKKNL ATHQCLHRSE GRPFGCDECA LGATVDAPAA KPLASAPGGP GCGPGSDPVV
PQRAPSGERS FFCPDCGRGF SHGQHLARHP RVHTGERPFA CTQCDRRFGS RPNLVAHSRA
HSGARPFACA QCGRRFSRKS HLGRHQAVHT GSRPHACAVC ARSFSSKTNL VRHQAIHTGS
RPFSCPQCGK SFSRKTHLVR HQLIHGEAAH AAPDAALAAP AWSAPPEVAP PPLFF
