ZN444_HUMAN
ID ZN444_HUMAN Reviewed; 327 AA.
AC Q8N0Y2; Q8TEQ9; Q8WU35; Q9NUU1;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Zinc finger protein 444;
DE AltName: Full=Endothelial zinc finger protein 2;
DE Short=EZF-2;
DE AltName: Full=Zinc finger and SCAN domain-containing protein 17;
GN Name=ZNF444; Synonyms=EZF2, ZSCAN17;
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] (ISOFORMS 1 AND 2).
RX PubMed=11978792; DOI=10.1074/jbc.m201854200;
RA Adachi H., Tsujimoto M.;
RT "Characterization of the human gene encoding the scavenger receptor
RT expressed by endothelial cell and its regulation by a novel transcription
RT factor, endothelial zinc finger protein-2.";
RL J. Biol. Chem. 277:24014-24021(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND IDENTIFICATION BY
RP 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-18, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-8 AND LYS-190, AND IDENTIFICATION
RP 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: Transcriptional regulator. Binds to the 5'-flanking critical
CC region of the SCARF1 promoter.
CC -!- INTERACTION:
CC Q8N0Y2-2; Q86V38: ATN1; NbExp=3; IntAct=EBI-12010736, EBI-11954292;
CC Q8N0Y2-2; P02489: CRYAA; NbExp=3; IntAct=EBI-12010736, EBI-6875961;
CC Q8N0Y2-2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-12010736, EBI-10976677;
CC Q8N0Y2-2; Q92997: DVL3; NbExp=3; IntAct=EBI-12010736, EBI-739789;
CC Q8N0Y2-2; P14136: GFAP; NbExp=3; IntAct=EBI-12010736, EBI-744302;
CC Q8N0Y2-2; O14908-2: GIPC1; NbExp=3; IntAct=EBI-12010736, EBI-25913156;
CC Q8N0Y2-2; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-12010736, EBI-5916454;
CC Q8N0Y2-2; P28799: GRN; NbExp=3; IntAct=EBI-12010736, EBI-747754;
CC Q8N0Y2-2; O15499: GSC2; NbExp=3; IntAct=EBI-12010736, EBI-19954058;
CC Q8N0Y2-2; O43464: HTRA2; NbExp=3; IntAct=EBI-12010736, EBI-517086;
CC Q8N0Y2-2; P42858: HTT; NbExp=9; IntAct=EBI-12010736, EBI-466029;
CC Q8N0Y2-2; Q92993: KAT5; NbExp=3; IntAct=EBI-12010736, EBI-399080;
CC Q8N0Y2-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-12010736, EBI-10975473;
CC Q8N0Y2-2; Q92876: KLK6; NbExp=3; IntAct=EBI-12010736, EBI-2432309;
CC Q8N0Y2-2; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-12010736, EBI-10172290;
CC Q8N0Y2-2; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-12010736, EBI-10171774;
CC Q8N0Y2-2; P02545: LMNA; NbExp=3; IntAct=EBI-12010736, EBI-351935;
CC Q8N0Y2-2; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-12010736, EBI-11742507;
CC Q8N0Y2-2; P19404: NDUFV2; NbExp=3; IntAct=EBI-12010736, EBI-713665;
CC Q8N0Y2-2; Q96CV9: OPTN; NbExp=3; IntAct=EBI-12010736, EBI-748974;
CC Q8N0Y2-2; Q13153: PAK1; NbExp=3; IntAct=EBI-12010736, EBI-1307;
CC Q8N0Y2-2; D3DTS7: PMP22; NbExp=3; IntAct=EBI-12010736, EBI-25882629;
CC Q8N0Y2-2; P62937-2: PPIA; NbExp=3; IntAct=EBI-12010736, EBI-25884072;
CC Q8N0Y2-2; P17252: PRKCA; NbExp=3; IntAct=EBI-12010736, EBI-1383528;
CC Q8N0Y2-2; P41219: PRPH; NbExp=3; IntAct=EBI-12010736, EBI-752074;
CC Q8N0Y2-2; P60891: PRPS1; NbExp=3; IntAct=EBI-12010736, EBI-749195;
CC Q8N0Y2-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-12010736, EBI-396669;
CC Q8N0Y2-2; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-12010736, EBI-9090795;
CC Q8N0Y2-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-12010736, EBI-5235340;
CC Q8N0Y2-2; Q86WV8: TSC1; NbExp=3; IntAct=EBI-12010736, EBI-12806590;
CC Q8N0Y2-2; O76024: WFS1; NbExp=3; IntAct=EBI-12010736, EBI-720609;
CC Q8N0Y2-2; P61981: YWHAG; NbExp=3; IntAct=EBI-12010736, EBI-359832;
CC Q8N0Y2-2; Q15776: ZKSCAN8; NbExp=4; IntAct=EBI-12010736, EBI-2602314;
CC Q8N0Y2-2; P17028: ZNF24; NbExp=6; IntAct=EBI-12010736, EBI-707773;
CC Q8N0Y2-2; P10073: ZSCAN22; NbExp=3; IntAct=EBI-12010736, EBI-10178224;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N0Y2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N0Y2-2; Sequence=VSP_008798;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB84889.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB052955; BAC02698.1; -; mRNA.
DR EMBL; AB052954; BAC02697.1; -; mRNA.
DR EMBL; AL834130; CAD38847.1; -; mRNA.
DR EMBL; AK074063; BAB84889.1; ALT_FRAME; mRNA.
DR EMBL; AK001999; BAA92028.1; -; mRNA.
DR EMBL; BC021282; AAH21282.1; -; mRNA.
DR CCDS; CCDS12939.1; -. [Q8N0Y2-1]
DR CCDS; CCDS59426.1; -. [Q8N0Y2-2]
DR RefSeq; NP_001240721.1; NM_001253792.1. [Q8N0Y2-2]
DR RefSeq; NP_060807.2; NM_018337.3. [Q8N0Y2-1]
DR RefSeq; XP_005259091.1; XM_005259034.2. [Q8N0Y2-1]
DR RefSeq; XP_005259092.1; XM_005259035.1. [Q8N0Y2-1]
DR RefSeq; XP_005259093.1; XM_005259036.1. [Q8N0Y2-1]
DR RefSeq; XP_011525370.1; XM_011527068.1. [Q8N0Y2-1]
DR AlphaFoldDB; Q8N0Y2; -.
DR SMR; Q8N0Y2; -.
DR BioGRID; 120593; 116.
DR IntAct; Q8N0Y2; 65.
DR STRING; 9606.ENSP00000338860; -.
DR iPTMnet; Q8N0Y2; -.
DR PhosphoSitePlus; Q8N0Y2; -.
DR BioMuta; ZNF444; -.
DR DMDM; 38258800; -.
DR EPD; Q8N0Y2; -.
DR jPOST; Q8N0Y2; -.
DR MassIVE; Q8N0Y2; -.
DR MaxQB; Q8N0Y2; -.
DR PaxDb; Q8N0Y2; -.
DR PeptideAtlas; Q8N0Y2; -.
DR PRIDE; Q8N0Y2; -.
DR ProteomicsDB; 71486; -. [Q8N0Y2-1]
DR ProteomicsDB; 71487; -. [Q8N0Y2-2]
DR Antibodypedia; 19607; 92 antibodies from 18 providers.
DR DNASU; 55311; -.
DR Ensembl; ENST00000337080.8; ENSP00000338860.3; ENSG00000167685.15. [Q8N0Y2-1]
DR Ensembl; ENST00000592949.5; ENSP00000468069.1; ENSG00000167685.15. [Q8N0Y2-2]
DR GeneID; 55311; -.
DR KEGG; hsa:55311; -.
DR MANE-Select; ENST00000337080.8; ENSP00000338860.3; NM_018337.4; NP_060807.2.
DR UCSC; uc002qmm.4; human. [Q8N0Y2-1]
DR CTD; 55311; -.
DR DisGeNET; 55311; -.
DR GeneCards; ZNF444; -.
DR HGNC; HGNC:16052; ZNF444.
DR HPA; ENSG00000167685; Low tissue specificity.
DR MIM; 607874; gene.
DR neXtProt; NX_Q8N0Y2; -.
DR OpenTargets; ENSG00000167685; -.
DR PharmGKB; PA134984823; -.
DR VEuPathDB; HostDB:ENSG00000167685; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162893; -.
DR HOGENOM; CLU_002678_49_3_1; -.
DR InParanoid; Q8N0Y2; -.
DR OMA; ADSPWHR; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8N0Y2; -.
DR TreeFam; TF337369; -.
DR PathwayCommons; Q8N0Y2; -.
DR SignaLink; Q8N0Y2; -.
DR BioGRID-ORCS; 55311; 9 hits in 1094 CRISPR screens.
DR ChiTaRS; ZNF444; human.
DR GenomeRNAi; 55311; -.
DR Pharos; Q8N0Y2; Tdark.
DR PRO; PR:Q8N0Y2; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8N0Y2; protein.
DR Bgee; ENSG00000167685; Expressed in type B pancreatic cell and 202 other tissues.
DR ExpressionAtlas; Q8N0Y2; baseline and differential.
DR Genevisible; Q8N0Y2; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..327
FT /note="Zinc finger protein 444"
FT /id="PRO_0000047593"
FT DOMAIN 20..104
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 179..201
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 207..229
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 250..272
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 278..300
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 101..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 190
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 136
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11978792,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_008798"
FT CONFLICT 49
FT /note="L -> P (in Ref. 4; BAA92028)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 35204 MW; C7C812DC8FC6D706 CRC64;
MEVAVPVKQE AEGLALDSPW HRFRRFHLGD APGPREALGL LRALCRDWLR PEVHTKEQML
ELLVLEQFLS ALPADTQAWV CSRQPQSGEE AVALLEELWG PAASPDGSSA TRVPQDVTQG
PGATGGKEDS GMIPLAGTAP GAEGPAPGDS QAVRPYKQEP SSPPLAPGLP AFLAAPGTTS
CPECGKTSLK PAHLLRHRQS HSGEKPHACP ECGKAFRRKE HLRRHRDTHP GSPGSPGPAL
RPLPAREKPH ACCECGKTFY WREHLVRHRK THSGARPFAC WECGKGFGRR EHVLRHQRIH
GRAAASAQGA VAPGPDGGGP FPPWPLG
