VEZF1_HUMAN
ID VEZF1_HUMAN Reviewed; 521 AA.
AC Q14119;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Vascular endothelial zinc finger 1;
DE AltName: Full=Putative transcription factor DB1;
DE AltName: Full=Zinc finger protein 161;
GN Name=VEZF1; Synonyms=DB1, ZNF161;
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, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Lymphoma;
RX PubMed=8035792; DOI=10.1128/mcb.14.8.5099-5107.1994;
RA Koyano-Nakagawa N., Nishida J., Baldwin D., Arai K., Yokota T.;
RT "Molecular cloning of a novel human cDNA encoding a zinc finger protein
RT that binds to the interleukin-3 promoter.";
RL Mol. Cell. Biol. 14:5099-5107(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-362, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Possible transcription factor. Specifically binds to the
CC CT/GC-rich region of the interleukin-3 promoter and mediates tax
CC transactivation of IL-3. {ECO:0000269|PubMed:8035792}.
CC -!- SUBUNIT: Interacts with ARHGAP22. {ECO:0000250}.
CC -!- INTERACTION:
CC Q14119; O95994: AGR2; NbExp=5; IntAct=EBI-11980193, EBI-712648;
CC Q14119; O43307: ARHGEF9; NbExp=3; IntAct=EBI-11980193, EBI-3447299;
CC Q14119; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-11980193, EBI-11524452;
CC Q14119; Q5SWW7: C10orf55; NbExp=5; IntAct=EBI-11980193, EBI-12809220;
CC Q14119; P20807-4: CAPN3; NbExp=3; IntAct=EBI-11980193, EBI-11532021;
CC Q14119; P40199: CEACAM6; NbExp=3; IntAct=EBI-11980193, EBI-4314501;
CC Q14119; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-11980193, EBI-742887;
CC Q14119; Q15038: DAZAP2; NbExp=3; IntAct=EBI-11980193, EBI-724310;
CC Q14119; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-11980193, EBI-742054;
CC Q14119; Q96KQ7: EHMT2; NbExp=3; IntAct=EBI-11980193, EBI-744366;
CC Q14119; O00303: EIF3F; NbExp=3; IntAct=EBI-11980193, EBI-711990;
CC Q14119; P0C7A2-2: FAM153B; NbExp=3; IntAct=EBI-11980193, EBI-12940382;
CC Q14119; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-11980193, EBI-12193763;
CC Q14119; P53539: FOSB; NbExp=3; IntAct=EBI-11980193, EBI-2806743;
CC Q14119; A1L4K1: FSD2; NbExp=3; IntAct=EBI-11980193, EBI-5661036;
CC Q14119; Q08379: GOLGA2; NbExp=3; IntAct=EBI-11980193, EBI-618309;
CC Q14119; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-11980193, EBI-5916454;
CC Q14119; Q86YR5-3: GPSM1; NbExp=3; IntAct=EBI-11980193, EBI-10261098;
CC Q14119; O75031: HSF2BP; NbExp=3; IntAct=EBI-11980193, EBI-7116203;
CC Q14119; Q16082: HSPB2; NbExp=3; IntAct=EBI-11980193, EBI-739395;
CC Q14119; Q0VD86: INCA1; NbExp=3; IntAct=EBI-11980193, EBI-6509505;
CC Q14119; Q96MP8-2: KCTD7; NbExp=3; IntAct=EBI-11980193, EBI-11954971;
CC Q14119; A4D0Q3: KIAA1218; NbExp=3; IntAct=EBI-11980193, EBI-14308786;
CC Q14119; Q6A162: KRT40; NbExp=3; IntAct=EBI-11980193, EBI-10171697;
CC Q14119; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-11980193, EBI-10171774;
CC Q14119; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-11980193, EBI-1048945;
CC Q14119; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-11980193, EBI-10261141;
CC Q14119; Q14847-2: LASP1; NbExp=3; IntAct=EBI-11980193, EBI-9088686;
CC Q14119; P80188: LCN2; NbExp=3; IntAct=EBI-11980193, EBI-11911016;
CC Q14119; Q9UBR4-2: LHX3; NbExp=5; IntAct=EBI-11980193, EBI-12039345;
CC Q14119; P25791-3: LMO2; NbExp=3; IntAct=EBI-11980193, EBI-11959475;
CC Q14119; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-11980193, EBI-741037;
CC Q14119; Q99687-3: MEIS3; NbExp=3; IntAct=EBI-11980193, EBI-18582591;
CC Q14119; P55197-2: MLLT10; NbExp=3; IntAct=EBI-11980193, EBI-12853322;
CC Q14119; P35548: MSX2; NbExp=3; IntAct=EBI-11980193, EBI-6447480;
CC Q14119; Q9NZQ3-3: NCKIPSD; NbExp=3; IntAct=EBI-11980193, EBI-10963850;
CC Q14119; P23511-2: NFYA; NbExp=3; IntAct=EBI-11980193, EBI-11061759;
CC Q14119; Q16656-4: NRF1; NbExp=3; IntAct=EBI-11980193, EBI-11742836;
CC Q14119; Q99471: PFDN5; NbExp=3; IntAct=EBI-11980193, EBI-357275;
CC Q14119; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-11980193, EBI-79165;
CC Q14119; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-11980193, EBI-2876622;
CC Q14119; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-11980193, EBI-1389308;
CC Q14119; P78424: POU6F2; NbExp=3; IntAct=EBI-11980193, EBI-12029004;
CC Q14119; P31321: PRKAR1B; NbExp=3; IntAct=EBI-11980193, EBI-2805516;
CC Q14119; P86480: PRR20D; NbExp=3; IntAct=EBI-11980193, EBI-12754095;
CC Q14119; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-11980193, EBI-740343;
CC Q14119; Q92622: RUBCN; NbExp=3; IntAct=EBI-11980193, EBI-2952709;
CC Q14119; Q15428: SF3A2; NbExp=3; IntAct=EBI-11980193, EBI-2462271;
CC Q14119; Q9UN79: SOX13; NbExp=3; IntAct=EBI-11980193, EBI-3928516;
CC Q14119; Q02446: SP4; NbExp=3; IntAct=EBI-11980193, EBI-10198587;
CC Q14119; Q8N0X2-4: SPAG16; NbExp=3; IntAct=EBI-11980193, EBI-11946259;
CC Q14119; Q08117-2: TLE5; NbExp=3; IntAct=EBI-11980193, EBI-11741437;
CC Q14119; Q13077: TRAF1; NbExp=3; IntAct=EBI-11980193, EBI-359224;
CC Q14119; Q12933: TRAF2; NbExp=3; IntAct=EBI-11980193, EBI-355744;
CC Q14119; P14373: TRIM27; NbExp=3; IntAct=EBI-11980193, EBI-719493;
CC Q14119; Q86WV8: TSC1; NbExp=3; IntAct=EBI-11980193, EBI-12806590;
CC Q14119; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-11980193, EBI-10180829;
CC Q14119; P61758: VBP1; NbExp=3; IntAct=EBI-11980193, EBI-357430;
CC Q14119; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-11980193, EBI-2799833;
CC Q14119; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-11980193, EBI-12040603;
CC Q14119; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-11980193, EBI-12030590;
CC Q14119; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-11980193, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8035792}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highest levels in skeletal
CC muscle and kidney. {ECO:0000269|PubMed:8035792}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D28118; BAA05663.1; -; mRNA.
DR EMBL; AC015813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS32687.1; -.
DR PIR; A53772; A53772.
DR RefSeq; NP_009077.2; NM_007146.2.
DR AlphaFoldDB; Q14119; -.
DR BioGRID; 113509; 80.
DR IntAct; Q14119; 74.
DR STRING; 9606.ENSP00000462337; -.
DR GlyGen; Q14119; 20 sites, 2 O-linked glycans (20 sites).
DR iPTMnet; Q14119; -.
DR PhosphoSitePlus; Q14119; -.
DR BioMuta; VEZF1; -.
DR DMDM; 317373301; -.
DR EPD; Q14119; -.
DR jPOST; Q14119; -.
DR MassIVE; Q14119; -.
DR MaxQB; Q14119; -.
DR PaxDb; Q14119; -.
DR PeptideAtlas; Q14119; -.
DR PRIDE; Q14119; -.
DR ProteomicsDB; 59826; -.
DR Antibodypedia; 18343; 105 antibodies from 21 providers.
DR DNASU; 7716; -.
DR Ensembl; ENST00000581208.2; ENSP00000462337.1; ENSG00000136451.9.
DR GeneID; 7716; -.
DR KEGG; hsa:7716; -.
DR MANE-Select; ENST00000581208.2; ENSP00000462337.1; NM_007146.3; NP_009077.2.
DR UCSC; uc002ivf.2; human.
DR CTD; 7716; -.
DR DisGeNET; 7716; -.
DR GeneCards; VEZF1; -.
DR HGNC; HGNC:12949; VEZF1.
DR HPA; ENSG00000136451; Low tissue specificity.
DR MIM; 606747; gene.
DR neXtProt; NX_Q14119; -.
DR OpenTargets; ENSG00000136451; -.
DR PharmGKB; PA162408823; -.
DR VEuPathDB; HostDB:ENSG00000136451; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000155932; -.
DR InParanoid; Q14119; -.
DR OMA; AMNRGNN; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q14119; -.
DR TreeFam; TF331686; -.
DR PathwayCommons; Q14119; -.
DR SignaLink; Q14119; -.
DR SIGNOR; Q14119; -.
DR BioGRID-ORCS; 7716; 90 hits in 1098 CRISPR screens.
DR ChiTaRS; VEZF1; human.
DR GenomeRNAi; 7716; -.
DR Pharos; Q14119; Tbio.
DR PRO; PR:Q14119; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q14119; protein.
DR Bgee; ENSG00000136451; Expressed in buccal mucosa cell and 213 other tissues.
DR ExpressionAtlas; Q14119; baseline and differential.
DR Genevisible; Q14119; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR GO; GO:0001885; P:endothelial cell development; IEA:Ensembl.
DR GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
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; 3.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Acetylation; Activator; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..521
FT /note="Vascular endothelial zinc finger 1"
FT /id="PRO_0000047435"
FT REPEAT 394..400
FT /note="1"
FT REPEAT 445..451
FT /note="2"
FT REPEAT 457..463
FT /note="3"
FT REPEAT 479..485
FT /note="4"
FT ZN_FING 74..96
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 174..196
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 202..224
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 232..255
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 261..283
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 287..308
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 140..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..485
FT /note="4 X 7 AA repeats of P-[LV]-T-[IL]-T-[ST]-P"
FT COMPBIAS 140..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 362
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CONFLICT 350..354
FT /note="Missing (in Ref. 1; BAA05663)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="G -> E (in Ref. 1; BAA05663)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 56931 MW; B16095D95094E385 CRC64;
MEANWTAFLF QAHEASHHQQ QAAQNSLLPL LSSAVEPPDQ KPLLPIPITQ KPQGAPETLK
DAIGIKKEKP KTSFVCTYCS KAFRDSYHLR RHESCHTGIK LVSRPKKTPT TVVPLISTIA
GDSSRTSLVS TIAGILSTVT TSSSGTNPSS SASTTAMPVT QSVKKPSKPV KKNHACEMCG
KAFRDVYHLN RHKLSHSDEK PFECPICNQR FKRKDRMTYH VRSHEGGITK PYTCSVCGKG
FSRPDHLSCH VKHVHSTERP FKCQTCTAAF ATKDRLRTHM VRHEGKVSCN ICGKLLSAAY
ITSHLKTHGQ SQSINCNTCK QGISKTCMSE ETSNQKQQQQ QQQQQQQQQQ QQQQHVTSWP
GKQVETLRLW EEAVKARKKE AANLCQTSTA ATTPVTLTTP FSITSSVSSG TMSNPVTVAA
AMSMRSPVNV SSAVNITSPM NIGHPVTITS PLSMTSPLTL TTPVNLPTPV TAPVNIAHPV
TITSPMNLPT PMTLAAPLNI AMRPVESMPF LPQALPTSPP W
