ID   MAZ_HUMAN               Reviewed;         477 AA.
AC   P56270; A8QJL9; C6G496; G5E927; H3BQD6; Q15703; Q8NFN7; Q99443;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   28-JAN-2026, entry version 207.
DE   RecName: Full=Myc-associated zinc finger protein;
DE            Short=MAZI;
DE   AltName: Full=Pur-1;
DE   AltName: Full=Purine-binding transcription factor;
DE   AltName: Full=Serum amyloid A-activating factor-1;
DE            Short=SAF-1;
DE   AltName: Full=Transcription factor Zif87;
DE   AltName: Full=ZF87;
DE   AltName: Full=Zinc finger protein 801;
GN   Name=MAZ; Synonyms=ZNF801;
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 1), FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=1502157; DOI=10.1073/pnas.89.16.7452;
RA   Bossone S.A., Asselin C., Patel A.J., Marcu K.B.;
RT   "MAZ, a zinc finger protein, binds to c-MYC and C2 gene sequences
RT   regulating transcriptional initiation and termination.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:7452-7456(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Carcinoma;
RX   PubMed=1567856; DOI=10.1021/bi00131a029;
RA   Pyrc J.J., Moberg K.H., Hall D.J.;
RT   "Isolation of a novel cDNA encoding a zinc-finger protein that binds to two
RT   sites within the c-myc promoter.";
RL   Biochemistry 31:4102-4110(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Pancreatic islet;
RX   PubMed=8831693; DOI=10.1006/bbrc.1996.1432;
RA   Tsutsui H., Sakatsume O., Itakura K., Yokoyama K.K.;
RT   "Members of the MAZ family: a novel cDNA clone for MAZ from human
RT   pancreatic islet cells.";
RL   Biochem. Biophys. Res. Commun. 226:801-809(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8626793; DOI=10.1074/jbc.271.8.4417;
RA   Parks C.L., Shenk T.;
RT   "The serotonin 1a receptor gene contains a TATA-less promoter that responds
RT   to MAZ and Sp1.";
RL   J. Biol. Chem. 271:4417-4430(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Lymphoblastoma;
RX   PubMed=9685418; DOI=10.1074/jbc.273.32.20603;
RA   Song J., Murakami H., Tsutsui H., Tang X., Matsumura M., Itakura K.,
RA   Kanazawa I., Sun K., Yokoyama K.K.;
RT   "Genomic organization and expression of a human gene for Myc-associated
RT   zinc finger protein (MAZ).";
RL   J. Biol. Chem. 273:20603-20614(1998).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, FUNCTION, AND
RP   SUBUNIT.
RX   PubMed=12270922; DOI=10.1074/jbc.m206299200;
RA   Ray B.K., Murphy R., Ray P., Ray A.;
RT   "SAF-2, a splice variant of SAF-1, acts as a negative regulator of
RT   transcription.";
RL   J. Biol. Chem. 277:46822-46830(2002).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Bae J.S., Kim S.H., Park H.S.;
RT   "Human Myc-associated zinc finger protein (MAZ).";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY, AND
RP   INDUCTION BY CYTOKINES AND GROWTH FACTORS.
RX   PubMed=19583771; DOI=10.1111/j.1742-4658.2009.07136.x;
RA   Ray A., Dhar S., Shakya A., Ray P., Okada Y., Ray B.K.;
RT   "SAF-3, a novel splice variant of the SAF-1/MAZ/Pur-1 family, is expressed
RT   during inflammation.";
RL   FEBS J. 276:4276-4286(2009).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [10]
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   [11]
RP   INTERACTION WITH BPTF, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=10727212; DOI=10.1021/bi992211q;
RA   Jordan-Sciutto K.L., Dragich J.M., Caltagarone J., Hall D.J., Bowser R.;
RT   "Fetal Alz-50 clone 1 (FAC1) protein interacts with the Myc-associated zinc
RT   finger protein (ZF87/MAZ) and alters its transcriptional activity.";
RL   Biochemistry 39:3206-3215(2000).
RN   [12]
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   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND IDENTIFICATION BY
RP   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).
CC   -!- FUNCTION: Transcriptional regulator, potentially with dual roles in
CC       transcription initiation and termination. {ECO:0000303|PubMed:1502157}.
CC   -!- FUNCTION: [Isoform 1]: Binds DNA and functions as a transcriptional
CC       activator (PubMed:12270922). Binds to two G/A-rich sites, ME1a1 and
CC       ME1a2, within the MYC promoter having greater affinity for the former
CC       (PubMed:1502157). Also binds to multiple G/C-rich sites within the
CC       promoter of the Sp1 family of transcription factors (PubMed:1502157).
CC       {ECO:0000269|PubMed:12270922, ECO:0000269|PubMed:1502157}.
CC   -!- FUNCTION: [Isoform 2]: Binds DNA and functions as a transcriptional
CC       activator (PubMed:12270922). Inhibits MAZ isoform 1-mediated
CC       transcription (PubMed:12270922). {ECO:0000269|PubMed:12270922}.
CC   -!- FUNCTION: [Isoform 3]: Binds DNA and functions as a transcriptional
CC       activator. {ECO:0000269|PubMed:19583771}.
CC   -!- SUBUNIT: Interacts with BPTF. {ECO:0000269|PubMed:10727212}.
CC   -!- SUBUNIT: [Isoform 1]: Forms a heterodimer with MAZ isoform 2; the
CC       interaction inhibits MAZ isoform 1-mediated transcription activation.
CC       {ECO:0000269|PubMed:12270922}.
CC   -!- SUBUNIT: [Isoform 2]: Forms a heterodimer with MAZ isoform 1; the
CC       interaction inhibits MAZ isoform 1-mediated transcription activation.
CC       {ECO:0000269|PubMed:12270922}.
CC   -!- INTERACTION:
CC       P56270; P05090: APOD; NbExp=2; IntAct=EBI-1809742, EBI-715495;
CC       P56270; P43146: DCC; NbExp=4; IntAct=EBI-1809742, EBI-1222919;
CC       P56270; P70211: Dcc; Xeno; NbExp=2; IntAct=EBI-1809742, EBI-1798863;
CC       P56270; Q91562: dcc.L; Xeno; NbExp=2; IntAct=EBI-1809742, EBI-1809954;
CC       P56270-2; P42858: HTT; NbExp=3; IntAct=EBI-12068586, EBI-466029;
CC       P56270-2; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-12068586, EBI-10172052;
CC       P56270-2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-12068586, EBI-79165;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:10727212}. Note=In
CC       brains of Alzheimer disease patients, present in a plaque-like
CC       structures.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=SAF-1;
CC         IsoId=P56270-1; Sequence=Displayed;
CC       Name=2; Synonyms=SAF-2;
CC         IsoId=P56270-2; Sequence=VSP_044561;
CC       Name=3; Synonyms=SAF-3;
CC         IsoId=P56270-3; Sequence=VSP_047560;
CC       Name=4;
CC         IsoId=P56270-4; Sequence=VSP_055108;
CC   -!- TISSUE SPECIFICITY: Present in kidney, liver and brain. In the brain,
CC       highest levels are found in motor cortex and midfrontal cortex (at
CC       protein level). {ECO:0000269|PubMed:10727212}.
CC   -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in the heart, brain,
CC       placenta, lung, liver, skeletal muscle and weakly expressed in the
CC       kidney (PubMed:1502157). Expressed in the joint synovium
CC       (PubMed:19583771). {ECO:0000269|PubMed:1502157,
CC       ECO:0000269|PubMed:19583771}.
CC   -!- INDUCTION: [Isoform 3]: Induced by cytokine and growth factor
CC       stimulation. {ECO:0000269|PubMed:19583771}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May act as a dominant negative of isoform
CC       1. Reduced expression during inflammatory conditions. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 3]: The transactivation potential of isoform 3
CC       is much greater than that of the predominantly expressed isoform 1.
CC       {ECO:0000269|PubMed:19583771}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB04121.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA12728.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M94046; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; M93339; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; D85131; BAA12728.1; ALT_INIT; mRNA.
DR   EMBL; U33819; AAB04121.1; ALT_INIT; mRNA.
DR   EMBL; AB017335; BAA33064.1; -; Genomic_DNA.
DR   EMBL; AF489858; AAN03800.1; -; mRNA.
DR   EMBL; EF059746; ABN80996.1; -; mRNA.
DR   EMBL; FJ532357; ACS26236.1; -; mRNA.
DR   EMBL; AC009133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471238; EAW79996.1; -; Genomic_DNA.
DR   EMBL; CH471238; EAW79997.1; -; Genomic_DNA.
DR   CCDS; CCDS42143.1; -. [P56270-1]
DR   CCDS; CCDS42144.1; -. [P56270-2]
DR   CCDS; CCDS61902.1; -. [P56270-3]
DR   CCDS; CCDS61903.1; -. [P56270-4]
DR   PIR; A42170; A42170.
DR   PIR; JC5076; JC5076.
DR   RefSeq; NP_001036004.1; NM_001042539.3. [P56270-2]
DR   RefSeq; NP_001263204.1; NM_001276275.2. [P56270-3]
DR   RefSeq; NP_001263205.1; NM_001276276.2. [P56270-4]
DR   RefSeq; NP_002374.2; NM_002383.4. [P56270-1]
DR   RefSeq; XP_047290066.1; XM_047434110.1. [P56270-2]
DR   RefSeq; XP_054236300.1; XM_054380325.1. [P56270-2]
DR   AlphaFoldDB; P56270; -.
DR   SMR; P56270; -.
DR   BioGRID; 110320; 105.
DR   CORUM; P56270; -.
DR   FunCoup; P56270; 1503.
DR   IntAct; P56270; 37.
DR   MINT; P56270; -.
DR   STRING; 9606.ENSP00000219782; -.
DR   GlyGen; P56270; 3 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P56270; -.
DR   PhosphoSitePlus; P56270; -.
DR   SwissPalm; P56270; -.
DR   BioMuta; MAZ; -.
DR   DMDM; 3024110; -.
DR   jPOST; P56270; -.
DR   MassIVE; P56270; -.
DR   PaxDb; 9606-ENSP00000219782; -.
DR   PeptideAtlas; P56270; -.
DR   ProteomicsDB; 33810; -.
DR   ProteomicsDB; 41756; -.
DR   ProteomicsDB; 56907; -. [P56270-1]
DR   ProteomicsDB; 7603; -.
DR   Pumba; P56270; -.
DR   Antibodypedia; 26824; 323 antibodies from 30 providers.
DR   DNASU; 4150; -.
DR   Ensembl; ENST00000219782.11; ENSP00000219782.6; ENSG00000103495.15. [P56270-2]
DR   Ensembl; ENST00000322945.11; ENSP00000313362.6; ENSG00000103495.15. [P56270-1]
DR   Ensembl; ENST00000545521.5; ENSP00000443956.1; ENSG00000103495.15. [P56270-3]
DR   Ensembl; ENST00000562337.5; ENSP00000455726.1; ENSG00000103495.15. [P56270-4]
DR   GeneID; 4150; -.
DR   KEGG; hsa:4150; -.
DR   MANE-Select; ENST00000322945.11; ENSP00000313362.6; NM_002383.4; NP_002374.2.
DR   UCSC; uc002dtx.5; human. [P56270-1]
DR   AGR; HGNC:6914; -.
DR   ClinPGx; PA30657; -.
DR   CTD; 4150; -.
DR   DisGeNET; 4150; -.
DR   GeneCards; MAZ; -.
DR   HGNC; HGNC:6914; MAZ.
DR   HPA; ENSG00000103495; Low tissue specificity.
DR   MIM; 600999; gene.
DR   OpenTargets; ENSG00000103495; -.
DR   VEuPathDB; HostDB:ENSG00000103495; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000158525; -.
DR   HOGENOM; CLU_042232_0_0_1; -.
DR   InParanoid; P56270; -.
DR   OMA; HVNQEGQ; -.
DR   OrthoDB; 3176202at2759; -.
DR   PAN-GO; P56270; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; P56270; -.
DR   PathwayCommons; P56270; -.
DR   SignaLink; P56270; -.
DR   SIGNOR; P56270; -.
DR   Agora; ENSG00000103495; -.
DR   BioGRID-ORCS; 4150; 30 hits in 1186 CRISPR screens.
DR   ChiTaRS; MAZ; human.
DR   GeneWiki; MAZ_(gene); -.
DR   GenomeRNAi; 4150; -.
DR   Pharos; P56270; Tbio.
DR   PRO; PR:P56270; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; P56270; protein.
DR   Bgee; ENSG00000103495; Expressed in ventricular zone and 199 other cell types or tissues.
DR   ExpressionAtlas; P56270; baseline and differential.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IDA:ARUK-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0030335; P:positive regulation of cell migration; IDA:ARUK-UCL.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:ARUK-UCL.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:ARUK-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:ARUK-UCL.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:ARUK-UCL.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006369; P:termination of RNA polymerase II transcription; IDA:UniProtKB.
DR   GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:UniProtKB.
DR   FunFam; 3.30.160.60:FF:000780; myc-associated zinc finger protein isoform X1; 1.
DR   FunFam; 3.30.160.60:FF:000859; myc-associated zinc finger protein isoform X2; 1.
DR   FunFam; 3.30.160.60:FF:000095; Vascular endothelial zinc finger 1; 1.
DR   FunFam; 3.30.160.60:FF:000108; Vascular endothelial zinc finger 1; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 5.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24394; ZINC FINGER PROTEIN; 1.
DR   PANTHER; PTHR24394:SF48; ZINC FINGER PROTEIN 771; 1.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   Pfam; PF13894; zf-C2H2_4; 1.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Proteomics identification; Reference proteome; Repeat; RNA-binding;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..477
FT                   /note="Myc-associated zinc finger protein"
FT                   /id="PRO_0000047215"
FT   ZN_FING         190..212
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         279..301
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         307..329
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         337..360
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         366..388
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         392..413
FT                   /note="C2H2-type 6; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          59..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..141
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         361
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..34
FT                   /note="MFPVFPCTLLAPPFPVLGLDSRGVGGLMNSFPPP -> MDPSNWSSFIF
FT                   (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:19583771"
FT                   /id="VSP_047560"
FT   VAR_SEQ         65..369
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_055108"
FT   VAR_SEQ         428..477
FT                   /note="TGEVCPMAAAAAAAAAAAAAAVAAPPTAVGSLSGAEGVPVSSQPLPSQPW
FT                   -> FTTAAYLRIHAVKDHGLQAPRADRILCKLCSVHCKTPAQLAGHMQTHLGGAAPPVP
FT                   GDAPQPQPTC (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12270922"
FT                   /id="VSP_044561"
FT   CONFLICT        259
FT                   /note="Missing (in Ref. 3; BAA12728)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        389
FT                   /note="E -> K (in Ref. 6; AAN03800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        395..396
FT                   /note="HV -> PW (in Ref. 6; AAN03800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        401
FT                   /note="L -> M (in Ref. 2 and 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        443..447
FT                   /note="Missing (in Ref. 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   477 AA;  48608 MW;  C04C80F32C3C6825 CRC64;
     MFPVFPCTLL APPFPVLGLD SRGVGGLMNS FPPPQGHAQN PLQVGAELQS RFFASQGCAQ
     SPFQAAPAPP PTPQAPAAEP LQVDLLPVLA AAQESAAAAA AAAAAAAAVA AAPPAPAAAS
     TVDTAALKQP PAPPPPPPPV SAPAAEAAPP ASAATIAAAA ATAVVAPTST VAVAPVASAL
     EKKTKSKGPY ICALCAKEFK NGYNLRRHEA IHTGAKAGRV PSGAMKMPTM VPLSLLSVPQ
     LSGAGGGGGE AGAGGGAAAV AAGGVVTTTA SGKRIRKNHA CEMCGKAFRD VYHLNRHKLS
     HSDEKPYQCP VCQQRFKRKD RMSYHVRSHD GAVHKPYNCS HCGKSFSRPD HLNSHVRQVH
     STERPFKCEK CEAAFATKDR LRAHTVRHEE KVPCHVCGKM LSSAYISDHM KVHSQGPHHV
     CELCNKGTGE VCPMAAAAAA AAAAAAAAVA APPTAVGSLS GAEGVPVSSQ PLPSQPW
//