MZF1_HUMAN
ID MZF1_HUMAN Reviewed; 734 AA.
AC P28698; M0QXU0; Q7Z729; Q96I71; Q9NRY0; Q9UBW2;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Myeloid zinc finger 1;
DE Short=MZF-1;
DE AltName: Full=Zinc finger and SCAN domain-containing protein 6;
DE AltName: Full=Zinc finger protein 42;
GN Name=MZF1; Synonyms=MZF, ZNF42, ZSCAN6;
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] (ISOFORM MZF1A).
RX PubMed=1860835; DOI=10.1016/s0021-9258(18)98664-3;
RA Hromas R., Collins S.J., Hickstein D., Raskind W., Deaven L.L., O'Hara P.,
RA Hagen F.S., Kaushansky K.;
RT "A retinoic acid-responsive human zinc finger gene, MZF-1, preferentially
RT expressed in myeloid cells.";
RL J. Biol. Chem. 266:14183-14187(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS MZF1A AND MZF1B-C), AND
RP VARIANT HIS-51.
RC TISSUE=Bone marrow;
RX PubMed=10974541; DOI=10.1016/s0378-1119(00)00281-x;
RA Peterson M.J., Morris J.F.;
RT "Human myeloid zinc finger gene MZF produces multiple transcripts and
RT encodes a SCAN box protein.";
RL Gene 254:105-118(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS MZF1A AND 3), AND VARIANT
RP HIS-51.
RC TISSUE=Skin, and Uterus;
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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15541732; DOI=10.1016/j.yexcr.2004.08.028;
RA Le Mee S., Fromigue O., Marie P.J.;
RT "Sp1/Sp3 and the myeloid zinc finger gene MZF1 regulate the human N-
RT cadherin promoter in osteoblasts.";
RL Exp. Cell Res. 302:129-142(2005).
RN [7]
RP FUNCTION.
RX PubMed=17851584; DOI=10.1038/sj.jid.5701048;
RA Dong S., Ying S., Kojima T., Shiraiwa M., Kawada A., Mechin M.C., Adoue V.,
RA Chavanas S., Serre G., Simon M., Takahara H.;
RT "Crucial roles of MZF1 and Sp1 in the transcriptional regulation of the
RT peptidylarginine deiminase type I gene (PADI1) in human keratinocytes.";
RL J. Invest. Dermatol. 128:549-557(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND IDENTIFICATION BY
RP 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).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-723, AND IDENTIFICATION BY MASS
RP 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).
RN [10]
RP STRUCTURE BY NMR OF 37-128, AND SUBUNIT.
RX PubMed=16950398; DOI=10.1016/j.jmb.2006.07.063;
RA Peterson F.C., Hayes P.L., Waltner J.K., Heisner A.K., Jensen D.R.,
RA Sander T.L., Volkman B.F.;
RT "Structure of the SCAN domain from the tumor suppressor protein MZF1.";
RL J. Mol. Biol. 363:137-147(2006).
CC -!- FUNCTION: Binds to target promoter DNA and functions as transcription
CC regulator. Regulates transcription from the PADI1 and CDH2 promoter.
CC May be one regulator of transcriptional events during hemopoietic
CC development. {ECO:0000269|PubMed:15541732,
CC ECO:0000269|PubMed:17851584}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16950398}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=MZF1A; Synonyms=MZF1B;
CC IsoId=P28698-1; Sequence=Displayed;
CC Name=MZF1B-C;
CC IsoId=P28698-2; Sequence=VSP_006889, VSP_006890;
CC Name=3;
CC IsoId=P28698-3; Sequence=VSP_047013, VSP_047014;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in differentiating myeloid
CC cells. Detected in osteoblasts. {ECO:0000269|PubMed:15541732}.
CC -!- INDUCTION: By retinoic acid.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; M58297; AAA59898.1; -; mRNA.
DR EMBL; AF055077; AAD55809.1; -; mRNA.
DR EMBL; AF055078; AAD55810.1; -; mRNA.
DR EMBL; AF161886; AAF80465.1; -; Genomic_DNA.
DR EMBL; AF161886; AAF80466.1; -; Genomic_DNA.
DR EMBL; AC016629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW72617.1; -; Genomic_DNA.
DR EMBL; BC007777; AAH07777.1; -; mRNA.
DR EMBL; BC053316; AAH53316.1; -; mRNA.
DR CCDS; CCDS12988.1; -. [P28698-1]
DR CCDS; CCDS59427.1; -. [P28698-3]
DR PIR; A40751; A40751.
DR RefSeq; NP_001253962.1; NM_001267033.1. [P28698-3]
DR RefSeq; NP_003413.2; NM_003422.2. [P28698-1]
DR RefSeq; NP_932172.1; NM_198055.1. [P28698-1]
DR PDB; 2FI2; NMR; -; A/B=37-128.
DR PDBsum; 2FI2; -.
DR AlphaFoldDB; P28698; -.
DR BMRB; P28698; -.
DR SMR; P28698; -.
DR BioGRID; 113419; 29.
DR IntAct; P28698; 5.
DR STRING; 9606.ENSP00000215057; -.
DR iPTMnet; P28698; -.
DR PhosphoSitePlus; P28698; -.
DR BioMuta; MZF1; -.
DR DMDM; 215274121; -.
DR jPOST; P28698; -.
DR MassIVE; P28698; -.
DR MaxQB; P28698; -.
DR PaxDb; P28698; -.
DR PeptideAtlas; P28698; -.
DR PRIDE; P28698; -.
DR ProteomicsDB; 54492; -. [P28698-1]
DR ProteomicsDB; 54493; -. [P28698-2]
DR ABCD; P28698; 3 sequenced antibodies.
DR Antibodypedia; 914; 171 antibodies from 26 providers.
DR DNASU; 7593; -.
DR Ensembl; ENST00000215057.7; ENSP00000215057.1; ENSG00000099326.9. [P28698-1]
DR Ensembl; ENST00000594234.5; ENSP00000469378.1; ENSG00000099326.9. [P28698-3]
DR Ensembl; ENST00000599369.5; ENSP00000469493.1; ENSG00000099326.9. [P28698-1]
DR GeneID; 7593; -.
DR KEGG; hsa:7593; -.
DR MANE-Select; ENST00000215057.7; ENSP00000215057.1; NM_198055.2; NP_932172.1.
DR UCSC; uc002qtn.4; human. [P28698-1]
DR CTD; 7593; -.
DR DisGeNET; 7593; -.
DR GeneCards; MZF1; -.
DR HGNC; HGNC:13108; MZF1.
DR HPA; ENSG00000099326; Low tissue specificity.
DR MIM; 194550; gene.
DR neXtProt; NX_P28698; -.
DR OpenTargets; ENSG00000099326; -.
DR PharmGKB; PA37683; -.
DR VEuPathDB; HostDB:ENSG00000099326; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00950000182890; -.
DR HOGENOM; CLU_002678_49_8_1; -.
DR InParanoid; P28698; -.
DR OMA; FCYEEAV; -.
DR PhylomeDB; P28698; -.
DR TreeFam; TF337913; -.
DR PathwayCommons; P28698; -.
DR SignaLink; P28698; -.
DR SIGNOR; P28698; -.
DR BioGRID-ORCS; 7593; 96 hits in 1101 CRISPR screens.
DR ChiTaRS; MZF1; human.
DR EvolutionaryTrace; P28698; -.
DR GeneWiki; MZF1; -.
DR GenomeRNAi; 7593; -.
DR Pharos; P28698; Tbio.
DR PRO; PR:P28698; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P28698; protein.
DR Bgee; ENSG00000099326; Expressed in pancreatic ductal cell and 197 other tissues.
DR ExpressionAtlas; P28698; baseline and differential.
DR Genevisible; P28698; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR CDD; cd07936; SCAN; 1.
DR DisProt; DP02096; -.
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; 11.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 1: Evidence at protein level;
KW 3D-structure; 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..734
FT /note="Myeloid zinc finger 1"
FT /id="PRO_0000047375"
FT DOMAIN 44..125
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 356..378
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 384..406
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 412..434
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 440..462
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 485..507
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 513..535
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 541..563
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 569..591
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 597..619
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 625..647
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 653..675
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 681..703
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 709..731
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 144..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..172
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..485
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 723
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..249
FT /note="Missing (in isoform MZF1B-C)"
FT /evidence="ECO:0000303|PubMed:10974541"
FT /id="VSP_006889"
FT VAR_SEQ 250..257
FT /note="EAGGIFSP -> MNGPLVYA (in isoform MZF1B-C)"
FT /evidence="ECO:0000303|PubMed:10974541"
FT /id="VSP_006890"
FT VAR_SEQ 259..290
FT /note="FALQLGSISAGPGSVSPHLHVPWDLGMAGLSG -> AGAGAAPALGAGWLGA
FT AVAMYVARCSANAATC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047013"
FT VAR_SEQ 291..734
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047014"
FT VARIANT 51
FT /note="R -> H (in dbSNP:rs3752109)"
FT /evidence="ECO:0000269|PubMed:10974541,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_047677"
FT VARIANT 103
FT /note="R -> H (in dbSNP:rs3752110)"
FT /id="VAR_047678"
FT VARIANT 130
FT /note="R -> Q (in dbSNP:rs3752111)"
FT /id="VAR_047679"
FT VARIANT 331
FT /note="I -> V (in dbSNP:rs4756)"
FT /id="VAR_014826"
FT VARIANT 441
FT /note="R -> P (in dbSNP:rs2229255)"
FT /id="VAR_047680"
FT CONFLICT 304..305
FT /note="AL -> RV (in Ref. 1; AAA59898)"
FT /evidence="ECO:0000305"
FT HELIX 40..48
FT /evidence="ECO:0007829|PDB:2FI2"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:2FI2"
FT HELIX 58..73
FT /evidence="ECO:0007829|PDB:2FI2"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:2FI2"
FT HELIX 80..95
FT /evidence="ECO:0007829|PDB:2FI2"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:2FI2"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:2FI2"
FT TURN 123..127
FT /evidence="ECO:0007829|PDB:2FI2"
SQ SEQUENCE 734 AA; 82055 MW; B804766A0B008048 CRC64;
MRPAVLGSPD RAPPEDEGPV MVKLEDSEEE GEAALWDPGP EAARLRFRCF RYEEATGPQE
ALAQLRELCR QWLRPEVRSK EQMLELLVLE QFLGALPPEI QARVQGQRPG SPEEAAALVD
GLRREPGGPR RWVTVQVQGQ EVLSEKMEPS SFQPLPETEP PTPEPGPKTP PRTMQESPLG
LQVKEESEVT EDSDFLESGP LAATQESVPT LLPEEAQRCG TVLDQIFPHS KTGPEGPSWR
EHPRALWHEE AGGIFSPGFA LQLGSISAGP GSVSPHLHVP WDLGMAGLSG QIQSPSREGG
FAHALLLPSD LRSEQDPTDE DPCRGVGPAL ITTRWRSPRG RSRGRPSTGG GVVRGGRCDV
CGKVFSQRSN LLRHQKIHTG ERPFVCSECG RSFSRSSHLL RHQLTHTEER PFVCGDCGQG
FVRSARLEEH RRVHTGEQPF RCAECGQSFR QRSNLLQHQR IHGDPPGPGA KPPAPPGAPE
PPGPFPCSEC RESFARRAVL LEHQAVHTGD KSFGCVECGE RFGRRSVLLQ HRRVHSGERP
FACAECGQSF RQRSNLTQHR RIHTGERPFA CAECGKAFRQ RPTLTQHLRV HTGEKPFACP
ECGQRFSQRL KLTRHQRTHT GEKPYHCGEC GLGFTQVSRL TEHQRIHTGE RPFACPECGQ
SFRQHANLTQ HRRIHTGERP YACPECGKAF RQRPTLTQHL RTHRREKPFA CQDCGRRFHQ
STKLIQHQRV HSAE
