ZN580_HUMAN
ID ZN580_HUMAN Reviewed; 172 AA.
AC Q9UK33; B2RC05; Q9NPP7;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Zinc finger protein 580;
DE AltName: Full=LDL-induced EC protein;
GN Name=ZNF580;
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=Vascular endothelial cell;
RA Zhang W.C., Zhang K.M., Chen B.S.;
RT "A novel gene associated with LDL stimulation in vascular endothelial
RT cells.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG The European IMAGE consortium;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION BY SPHINGOSINE-1-PHOSPHATE.
RX PubMed=20382120; DOI=10.1016/j.bbrc.2010.04.019;
RA Sun H.Y., Wei S.P., Xu R.C., Xu P.X., Zhang W.C.;
RT "Sphingosine-1-phosphate induces human endothelial VEGF and MMP-2
RT production via transcription factor ZNF580: novel insights into
RT angiogenesis.";
RL Biochem. Biophys. Res. Commun. 395:361-366(2010).
RN [7]
RP INTERACTION WITH SMAD2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21599657; DOI=10.1042/cbi20110050;
RA Luo Y., Hu W., Xu R., Hou B., Zhang L., Zhang W.;
RT "ZNF580, a novel C2H2 zinc-finger transcription factor, interacts with the
RT TGF-beta signal molecule Smad2.";
RL Cell Biol. Int. 35:1153-1157(2011).
RN [8]
RP FUNCTION, AND INDUCTION BY REACTIVE OXYGEN SPECIES.
RX PubMed=21830064; DOI=10.1007/s11010-011-1013-0;
RA DangLi R., HeKong W., JiQin L., MingHua Z., WenCheng Z.;
RT "ROS-induced ZNF580 expression: a key role for H2O2/NF-kappaB signaling
RT pathway in vascular endothelial inflammation.";
RL Mol. Cell. Biochem. 359:183-191(2012).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-31 AND LYS-118, 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: Involved in the regulation of endothelial cell proliferation
CC and migration. Mediates H(2)O(2)-induced leukocyte chemotaxis by
CC elevating interleukin-8 production and may play a role in inflammation.
CC May be involved in transcriptional regulation.
CC {ECO:0000269|PubMed:20382120, ECO:0000269|PubMed:21830064}.
CC -!- SUBUNIT: Interacts with SMAD2. {ECO:0000269|PubMed:21599657}.
CC -!- INTERACTION:
CC Q9UK33; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-746277, EBI-11524452;
CC Q9UK33; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-746277, EBI-3867333;
CC Q9UK33; A1L4K1: FSD2; NbExp=3; IntAct=EBI-746277, EBI-5661036;
CC Q9UK33; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-746277, EBI-5916454;
CC Q9UK33; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-746277, EBI-11522367;
CC Q9UK33; O75525: KHDRBS3; NbExp=3; IntAct=EBI-746277, EBI-722504;
CC Q9UK33; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-746277, EBI-3044087;
CC Q9UK33; O76011: KRT34; NbExp=3; IntAct=EBI-746277, EBI-1047093;
CC Q9UK33; Q6A162: KRT40; NbExp=3; IntAct=EBI-746277, EBI-10171697;
CC Q9UK33; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-746277, EBI-10172290;
CC Q9UK33; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-746277, EBI-10171774;
CC Q9UK33; Q99750: MDFI; NbExp=3; IntAct=EBI-746277, EBI-724076;
CC Q9UK33; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-746277, EBI-11522433;
CC Q9UK33; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-746277, EBI-22310682;
CC Q9UK33; O43586: PSTPIP1; NbExp=3; IntAct=EBI-746277, EBI-1050964;
CC Q9UK33; P14373: TRIM27; NbExp=3; IntAct=EBI-746277, EBI-719493;
CC Q9UK33; Q15654: TRIP6; NbExp=3; IntAct=EBI-746277, EBI-742327;
CC Q9UK33; Q9C0F3: ZNF436; NbExp=3; IntAct=EBI-746277, EBI-8489702;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20382120,
CC ECO:0000269|PubMed:21599657}. Note=Colocalized with SMAD2 in the
CC nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in endothelial cells.
CC {ECO:0000269|PubMed:21599657}.
CC -!- INDUCTION: Up-regulated in presence of reactive oxygen species (ROS),
CC like H(2)O(2), through the NF-kappaB signaling pathway. Up-regulated by
CC sphingosine-1-phosphate (SP1) through the p38 MAPK signaling pathway
CC (at protein level). {ECO:0000269|PubMed:20382120,
CC ECO:0000269|PubMed:21830064}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB94389.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF184939; AAD56549.1; -; mRNA.
DR EMBL; AL359054; CAB94389.1; ALT_INIT; mRNA.
DR EMBL; AK314888; BAG37402.1; -; mRNA.
DR EMBL; BC017698; AAH17698.1; -; mRNA.
DR CCDS; CCDS12931.1; -.
DR RefSeq; NP_001156895.1; NM_001163423.1.
DR RefSeq; NP_057286.1; NM_016202.2.
DR RefSeq; NP_996998.1; NM_207115.1.
DR AlphaFoldDB; Q9UK33; -.
DR SMR; Q9UK33; -.
DR BioGRID; 119340; 29.
DR IntAct; Q9UK33; 25.
DR MINT; Q9UK33; -.
DR STRING; 9606.ENSP00000443957; -.
DR iPTMnet; Q9UK33; -.
DR PhosphoSitePlus; Q9UK33; -.
DR BioMuta; ZNF580; -.
DR DMDM; 55976777; -.
DR EPD; Q9UK33; -.
DR jPOST; Q9UK33; -.
DR MassIVE; Q9UK33; -.
DR MaxQB; Q9UK33; -.
DR PaxDb; Q9UK33; -.
DR PeptideAtlas; Q9UK33; -.
DR PRIDE; Q9UK33; -.
DR ProteomicsDB; 84713; -.
DR Antibodypedia; 19580; 87 antibodies from 15 providers.
DR DNASU; 51157; -.
DR Ensembl; ENST00000325333.10; ENSP00000320050.4; ENSG00000213015.9.
DR Ensembl; ENST00000543039.2; ENSP00000443957.1; ENSG00000213015.9.
DR Ensembl; ENST00000545125.1; ENSP00000446126.1; ENSG00000213015.9.
DR GeneID; 51157; -.
DR KEGG; hsa:51157; -.
DR MANE-Select; ENST00000325333.10; ENSP00000320050.4; NM_207115.2; NP_996998.1.
DR UCSC; uc002qlo.4; human.
DR CTD; 51157; -.
DR DisGeNET; 51157; -.
DR GeneCards; ZNF580; -.
DR HGNC; HGNC:29473; ZNF580.
DR HPA; ENSG00000213015; Low tissue specificity.
DR MIM; 617888; gene.
DR neXtProt; NX_Q9UK33; -.
DR OpenTargets; ENSG00000213015; -.
DR PharmGKB; PA134867016; -.
DR VEuPathDB; HostDB:ENSG00000213015; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163086; -.
DR HOGENOM; CLU_002678_42_5_1; -.
DR InParanoid; Q9UK33; -.
DR OMA; VWPRVGF; -.
DR PhylomeDB; Q9UK33; -.
DR TreeFam; TF338348; -.
DR PathwayCommons; Q9UK33; -.
DR SignaLink; Q9UK33; -.
DR BioGRID-ORCS; 51157; 30 hits in 1105 CRISPR screens.
DR ChiTaRS; ZNF580; human.
DR GenomeRNAi; 51157; -.
DR Pharos; Q9UK33; Tbio.
DR PRO; PR:Q9UK33; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9UK33; protein.
DR Bgee; ENSG00000213015; Expressed in adenohypophysis and 177 other tissues.
DR ExpressionAtlas; Q9UK33; baseline and differential.
DR Genevisible; Q9UK33; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
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:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:UniProtKB.
DR GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IDA:UniProtKB.
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; 2.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Chemotaxis; DNA-binding; Inflammatory response; Isopeptide bond;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..172
FT /note="Zinc finger protein 580"
FT /id="PRO_0000047671"
FT ZN_FING 92..114
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 120..142
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 150..172
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 31
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 118
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 172 AA; 18756 MW; 55A89DD94E0440A8 CRC64;
MLLLPPRPPH PRSSSPEAMD PPPPKAPPFP KAEGPSSTPS SAAGPRPPRL GRHLLIDANG
VPYTYTVQLE EEPRGPPQRE APPGEPGPRK GYSCPECARV FASPLRLQSH RVSHSDLKPF
TCGACGKAFK RSSHLSRHRA THRARAGPPH TCPLCPRRFQ DAAELAQHVR LH
