ID   ZEP1_HUMAN              Reviewed;        2718 AA.
AC   P15822; B2RTU3; Q14122; Q5MPB1; Q5VW60;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 4.
DT   27-MAR-2024, entry version 223.
DE   RecName: Full=Zinc finger protein 40;
DE   AltName: Full=Cirhin interaction protein;
DE            Short=CIRIP;
DE   AltName: Full=Gate keeper of apoptosis-activating protein;
DE            Short=GAAP;
DE   AltName: Full=Human immunodeficiency virus type I enhancer-binding protein 1;
DE            Short=HIV-EP1;
DE   AltName: Full=Major histocompatibility complex-binding protein 1;
DE            Short=MBP-1;
DE   AltName: Full=Positive regulatory domain II-binding factor 1;
DE            Short=PRDII-BF1;
GN   Name=HIVEP1; Synonyms=ZNF40;
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), AND VARIANTS SER-1074; ASN-1170;
RP   ARG-1915 AND GLY-2692.
RX   PubMed=2106471; DOI=10.1101/gad.4.1.29;
RA   Fan C.M., Maniatis T.;
RT   "A DNA-binding protein containing two widely separated zinc finger motifs
RT   that recognize the same DNA sequence.";
RL   Genes Dev. 4:29-42(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION (ISOFORMS 2 AND 3),
RP   AND SUBCELLULAR LOCATION (ISOFORMS 2 AND 3).
RA   Tovey M.;
RT   "Transcriptional regulator of genes involved in the control of cell growth
RT   or cell proliferation. Use of said regulator as a therapeutic or diagnostic
RT   agent.";
RL   Patent number CA2448384, 12-DEC-2002.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-1520.
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   NUCLEOTIDE SEQUENCE [MRNA] OF 817-2718 (ISOFORM 1), AND VARIANTS ILE-1609
RP   AND GLY-2692.
RX   PubMed=2108316; DOI=10.1128/mcb.10.4.1406-1414.1990;
RA   Baldwin A.S. Jr., LeClair K.P., Singh H., Sharp P.A.;
RT   "A large protein containing zinc finger domains binds to related sequence
RT   elements in the enhancers of the class I major histocompatibility complex
RT   and kappa immunoglobulin genes.";
RL   Mol. Cell. Biol. 10:1406-1414(1990).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2035-2718 (ISOFORM 1).
RC   TISSUE=Liver;
RA   Yu B., Mitchell G.A., Richter A.;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   FUNCTION (ISOFORM 2), AND ALTERNATIVE SPLICING.
RX   PubMed=1727488; DOI=10.1128/jvi.66.1.244-250.1992;
RA   Muchardt C., Seeler J.S., Nirula A., Shurland D.L., Gaynor R.B.;
RT   "Regulation of human immunodeficiency virus enhancer function by PRDII-BF1
RT   and c-rel gene products.";
RL   J. Virol. 66:244-250(1992).
RN   [8]
RP   FUNCTION (ISOFORM 1).
RX   PubMed=8289330; DOI=10.1128/jvi.68.2.1002-1009.1994;
RA   Seeler J.S., Muchardt C., Suessle A., Gaynor R.B.;
RT   "Transcription factor PRDII-BF1 activates human immunodeficiency virus type
RT   1 gene expression.";
RL   J. Virol. 68:1002-1009(1994).
RN   [9]
RP   FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), AND ALTERNATIVE
RP   SPLICING.
RX   PubMed=11818340; DOI=10.1093/embo-reports/kvf032;
RA   Lallemand C., Palmieri M., Blanchard B., Meritet J.F., Tovey M.G.;
RT   "GAAP-1: a transcriptional activator of p53 and IRF-1 possesses pro-
RT   apoptotic activity.";
RL   EMBO Rep. 3:153-158(2002).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-429; SER-1036 AND SER-1735,
RP   AND 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   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [13]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH UTP4.
RX   PubMed=19732766; DOI=10.1016/j.yexcr.2009.08.017;
RA   Yu B., Mitchell G.A., Richter A.;
RT   "Cirhin up-regulates a canonical NF-kappaB element through strong
RT   interaction with Cirip/HIVEP1.";
RL   Exp. Cell Res. 315:3086-3098(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492; SER-495 AND SER-1749,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1749 AND SER-1753, AND
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   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-476; SER-479;
RP   SER-571; SER-577; SER-670; SER-681; SER-1036; SER-1051; SER-1091; SER-1158;
RP   SER-1161; SER-1180; THR-1268; SER-1735; SER-1740; SER-1749; SER-1753;
RP   SER-1884; SER-2033; SER-2327; SER-2599; SER-2669 AND SER-2682, AND
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   [17]
RP   STRUCTURE BY NMR OF 2114-2143.
RX   PubMed=2248949; DOI=10.1021/bi00492a004;
RA   Omichinski J.G., Clore G.M., Appella E., Sakaguchi K., Gronenborn A.M.;
RT   "High-resolution three-dimensional structure of a single zinc finger from a
RT   human enhancer binding protein in solution.";
RL   Biochemistry 29:9324-9334(1990).
RN   [18]
RP   STRUCTURE BY NMR OF 2088-2143.
RX   PubMed=1567844; DOI=10.1021/bi00131a004;
RA   Omichinski J.G., Clore G.M., Robien M., Sakaguchi K., Appella E.,
RA   Gronenborn A.M.;
RT   "High-resolution solution structure of the double Cys2His2 zinc finger from
RT   the human enhancer binding protein MBP-1.";
RL   Biochemistry 31:3907-3917(1992).
CC   -!- FUNCTION: This protein specifically binds to the DNA sequence 5'-
CC       GGGACTTTCC-3' which is found in the enhancer elements of numerous viral
CC       promoters such as those of SV40, CMV, or HIV-1. In addition, related
CC       sequences are found in the enhancer elements of a number of cellular
CC       promoters, including those of the class I MHC, interleukin-2 receptor,
CC       and interferon-beta genes. It may act in T-cell activation. Involved in
CC       activating HIV-1 gene expression. Isoform 2 and isoform 3 also bind to
CC       the IPCS (IRF1 and p53 common sequence) DNA sequence in the promoter
CC       region of interferon regulatory factor 1 and p53 genes and are involved
CC       in transcription regulation of these genes. Isoform 2 does not activate
CC       HIV-1 gene expression. Isoform 2 and isoform 3 may be involved in
CC       apoptosis.
CC   -!- SUBUNIT: Interacts with UTP4. {ECO:0000269|PubMed:19732766}.
CC   -!- INTERACTION:
CC       P15822; P54253: ATXN1; NbExp=6; IntAct=EBI-722264, EBI-930964;
CC       P15822; O00555: CACNA1A; NbExp=2; IntAct=EBI-722264, EBI-766279;
CC       P15822; Q969X6: UTP4; NbExp=3; IntAct=EBI-722264, EBI-2602591;
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus.
CC   -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|Ref.2}.
CC       Nucleus {ECO:0000269|Ref.2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P15822-1; Sequence=Displayed;
CC       Name=2; Synonyms=Delta 2, GAAP-1;
CC         IsoId=P15822-2; Sequence=VSP_037714, VSP_037717;
CC       Name=3; Synonyms=GAAP-2;
CC         IsoId=P15822-3; Sequence=VSP_037715, VSP_037716;
CC   -!- INDUCTION: By mitogens and phorbol ester.
CC   -!- DOMAIN: Contains two sets of 2 zinc-fingers, which are widely separated
CC       and recognize the same DNA sequence. There is a fifth zinc-finger in-
CC       between.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA35798.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X51435; CAA35798.1; ALT_FRAME; mRNA.
DR   EMBL; AL137221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL157373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL391828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z98050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC140816; AAI40817.1; -; mRNA.
DR   EMBL; M32019; AAA17534.1; -; mRNA.
DR   EMBL; AY673640; AAV85766.1; -; mRNA.
DR   CCDS; CCDS43426.1; -. [P15822-1]
DR   PIR; A34203; A34203.
DR   RefSeq; NP_002105.3; NM_002114.3. [P15822-1]
DR   RefSeq; XP_011512853.1; XM_011514551.2.
DR   RefSeq; XP_011512854.1; XM_011514552.2. [P15822-1]
DR   RefSeq; XP_011512855.1; XM_011514553.1. [P15822-1]
DR   PDB; 1BBO; NMR; -; A=2087-2143.
DR   PDB; 3ZNF; NMR; -; A=2114-2143.
DR   PDB; 4ZNF; NMR; -; A=2114-2143.
DR   PDBsum; 1BBO; -.
DR   PDBsum; 3ZNF; -.
DR   PDBsum; 4ZNF; -.
DR   SMR; P15822; -.
DR   BioGRID; 109343; 178.
DR   ELM; P15822; -.
DR   IntAct; P15822; 144.
DR   MINT; P15822; -.
DR   STRING; 9606.ENSP00000368698; -.
DR   ChEMBL; CHEMBL2909; -.
DR   MoonDB; P15822; Predicted.
DR   GlyConnect; 2896; 1 O-GlcNAc glycan (1 site).
DR   GlyCosmos; P15822; 16 sites, 1 glycan.
DR   GlyGen; P15822; 48 sites, 1 O-linked glycan (48 sites).
DR   iPTMnet; P15822; -.
DR   PhosphoSitePlus; P15822; -.
DR   BioMuta; HIVEP1; -.
DR   DMDM; 254763385; -.
DR   EPD; P15822; -.
DR   jPOST; P15822; -.
DR   MassIVE; P15822; -.
DR   MaxQB; P15822; -.
DR   PaxDb; 9606-ENSP00000368698; -.
DR   PeptideAtlas; P15822; -.
DR   ProteomicsDB; 53225; -. [P15822-1]
DR   ProteomicsDB; 53226; -. [P15822-2]
DR   ProteomicsDB; 53227; -. [P15822-3]
DR   Pumba; P15822; -.
DR   Antibodypedia; 24904; 49 antibodies from 14 providers.
DR   DNASU; 3096; -.
DR   Ensembl; ENST00000379388.7; ENSP00000368698.2; ENSG00000095951.17. [P15822-1]
DR   GeneID; 3096; -.
DR   KEGG; hsa:3096; -.
DR   MANE-Select; ENST00000379388.7; ENSP00000368698.2; NM_002114.4; NP_002105.3.
DR   UCSC; uc003nac.4; human. [P15822-1]
DR   AGR; HGNC:4920; -.
DR   CTD; 3096; -.
DR   DisGeNET; 3096; -.
DR   GeneCards; HIVEP1; -.
DR   HGNC; HGNC:4920; HIVEP1.
DR   HPA; ENSG00000095951; Low tissue specificity.
DR   MalaCards; HIVEP1; -.
DR   MIM; 194540; gene.
DR   neXtProt; NX_P15822; -.
DR   OpenTargets; ENSG00000095951; -.
DR   PharmGKB; PA29297; -.
DR   VEuPathDB; HostDB:ENSG00000095951; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000158242; -.
DR   HOGENOM; CLU_000719_2_1_1; -.
DR   InParanoid; P15822; -.
DR   OMA; EGKQDCH; -.
DR   OrthoDB; 3353821at2759; -.
DR   PhylomeDB; P15822; -.
DR   TreeFam; TF331837; -.
DR   PathwayCommons; P15822; -.
DR   SignaLink; P15822; -.
DR   BioGRID-ORCS; 3096; 13 hits in 1180 CRISPR screens.
DR   ChiTaRS; HIVEP1; human.
DR   EvolutionaryTrace; P15822; -.
DR   GeneWiki; HIVEP1; -.
DR   GenomeRNAi; 3096; -.
DR   Pharos; P15822; Tbio.
DR   PRO; PR:P15822; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; P15822; Protein.
DR   Bgee; ENSG00000095951; Expressed in calcaneal tendon and 192 other cell types or tissues.
DR   ExpressionAtlas; P15822; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IEA:Ensembl.
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:0030509; P:BMP signaling pathway; IDA:FlyBase.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 4.
DR   InterPro; IPR034729; ZF_CCHC_HIVEP.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR45944; SCHNURRI, ISOFORM F; 1.
DR   PANTHER; PTHR45944:SF3; ZINC FINGER PROTEIN 40; 1.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   PROSITE; PS51811; ZF_CCHC_HIVEP; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
DR   Genevisible; P15822; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Cytoplasm; DNA-binding;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..2718
FT                   /note="Zinc finger protein 40"
FT                   /id="PRO_0000047369"
FT   ZN_FING         406..428
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         434..456
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         956..986
FT                   /note="CCHC HIVEP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01154"
FT   ZN_FING         2088..2110
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         2116..2140
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          58..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          484..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1022..1062
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1138..1169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1202..1282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1384..1414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1523..1548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1871..1911
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2155..2228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2265..2303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2327..2381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2572..2718
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..159
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..723
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1026..1042
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1043..1062
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1239..1262
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1384..1412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2160..2177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2178..2199
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2200..2228
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2356..2375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2575..2606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2627..2643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2647..2686
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2702..2718
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         141
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         429
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         476
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         479
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         492
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         495
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         571
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         577
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         670
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         681
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1036
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1051
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1091
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1158
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1180
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1268
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1735
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1740
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1749
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         1753
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1884
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         2033
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         2327
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         2599
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         2669
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         2682
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..2017
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_037714"
FT   VAR_SEQ         1..2002
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_037715"
FT   VAR_SEQ         2003..2024
FT                   /note="AITTHSKSDLLVYSSKWKSSLS -> MGQKFQKKSYRLVLKELRNPLL (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_037716"
FT   VAR_SEQ         2018..2024
FT                   /note="KWKSSLS -> MGQKFQK (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_037717"
FT   VARIANT         187
FT                   /note="T -> M (in dbSNP:rs2228209)"
FT                   /id="VAR_057383"
FT   VARIANT         362
FT                   /note="P -> L (in dbSNP:rs34221818)"
FT                   /id="VAR_057384"
FT   VARIANT         716
FT                   /note="T -> A (in dbSNP:rs2228210)"
FT                   /id="VAR_057385"
FT   VARIANT         828
FT                   /note="V -> I (in dbSNP:rs2228218)"
FT                   /id="VAR_057386"
FT   VARIANT         873
FT                   /note="A -> T (in dbSNP:rs6900196)"
FT                   /id="VAR_057387"
FT   VARIANT         1074
FT                   /note="N -> S (in dbSNP:rs2228220)"
FT                   /evidence="ECO:0000269|PubMed:2106471"
FT                   /id="VAR_057388"
FT   VARIANT         1170
FT                   /note="K -> N (in dbSNP:rs34258344)"
FT                   /evidence="ECO:0000269|PubMed:2106471"
FT                   /id="VAR_057389"
FT   VARIANT         1520
FT                   /note="A -> G (in dbSNP:rs2228212)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_057390"
FT   VARIANT         1609
FT                   /note="M -> I (in dbSNP:rs2228213)"
FT                   /evidence="ECO:0000269|PubMed:2108316"
FT                   /id="VAR_057391"
FT   VARIANT         1915
FT                   /note="Q -> R (in dbSNP:rs1126472)"
FT                   /evidence="ECO:0000269|PubMed:2106471"
FT                   /id="VAR_057392"
FT   VARIANT         2444
FT                   /note="T -> M (in dbSNP:rs2228214)"
FT                   /id="VAR_059892"
FT   VARIANT         2692
FT                   /note="A -> G (in dbSNP:rs1042054)"
FT                   /evidence="ECO:0000269|PubMed:2106471,
FT                   ECO:0000269|PubMed:2108316"
FT                   /id="VAR_059893"
FT   CONFLICT        515
FT                   /note="P -> N (in Ref. 1; CAA35798)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1227
FT                   /note="V -> I (in Ref. 1; CAA35798)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1436
FT                   /note="N -> G (in Ref. 1; CAA35798)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1660
FT                   /note="V -> E (in Ref. 5; AAA17534)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1883
FT                   /note="I -> L (in Ref. 1; CAA35798)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2067
FT                   /note="F -> C (in Ref. 6; AAV85766)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2080
FT                   /note="V -> I (in Ref. 1; CAA35798)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2149
FT                   /note="V -> I (in Ref. 1; CAA35798)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2388
FT                   /note="S -> P (in Ref. 6; AAV85766)"
FT                   /evidence="ECO:0000305"
FT   TURN            2091..2093
FT                   /evidence="ECO:0007829|PDB:1BBO"
FT   HELIX           2100..2109
FT                   /evidence="ECO:0007829|PDB:1BBO"
FT   STRAND          2119..2122
FT                   /evidence="ECO:0007829|PDB:1BBO"
FT   STRAND          2124..2127
FT                   /evidence="ECO:0007829|PDB:1BBO"
FT   HELIX           2128..2136
FT                   /evidence="ECO:0007829|PDB:1BBO"
FT   STRAND          2137..2140
FT                   /evidence="ECO:0007829|PDB:1BBO"
SQ   SEQUENCE   2718 AA;  296835 MW;  27AD2BB4E9484033 CRC64;
     MPRTKQIHPR NLRDKIEEAQ KELNGAEVSK KEILQAGVKG TSESLKGVKR KKIVAENHLK
     KIPKSPLRNP LQAKHKQNTE ESSFAVLHSA SESHKKQNYI PVKNGKQFTK QNGETPGIIA
     EASKSEESVS PKKPLFLQQP SELRRWRSEG ADPAKFSDLD EQCDSSSLSS KTRTDNSECI
     SSHCGTTSPS YTNTAFDVLL KAMEPELSTL SQKGSPCAIK TEKLRPNKTA RSPPKLKNSS
     MDAPNQTSQE LVAESQSSCT SYTVHMSAAQ KNEQGAMQSA SHLYHQHEHF VPKSNQHNQQ
     LPGCSGFTGS LTNLQNQENA KLEQVYNIAV TSSVGLTSPS SRSQVTPQNQ QMDSASPLSI
     SPANSTQSPP MPIYNSTHVA SVVNQSVEQM CNLLLKDQKP KKQGKYICEY CNRACAKPSV
     LLKHIRSHTG ERPYPCVTCG FSFKTKSNLY KHKKSHAHTI KLGLVLQPDA GGLFLSHESP
     KALSIHSDVE DSGESEEEGA TDERQHDLGA MELQPVHIIK RMSNAETLLK SSFTPSSPEN
     VIGDFLLQDR SAESQAVTEL PKVVVHHVTV SPLRTDSPKA MDPKPELSSA QKQKDLQVTN
     VQPLSANMSQ GGVSRLETNE NSHQKGDMNP LEGKQDSHVG TVHAQLQRQQ ATDYSQEQQG
     KLLSPRSLGS TDSGYFSRSE SADQTVSPPT PFARRLPSTE QDSGRSNGPS AALVTTSTPS
     ALPTGEKALL LPGQMRPPLA TKTLEERISK LISDNEALVD DKQLDSVKPR RTSLSRRGSI
     DSPKSYIFKD SFQFDLKPVG RRTSSSSDIP KSPFTPTEKS KQVFLLSVPS LDCLPITRSN
     SMPTTGYSAV PANIIPPPHP LRGSQSFDDK IGAFYDDVFV SGPNAPVPQS GHPRTLVRQA
     AIEDSSANES HVLGTGQSLD ESHQGCHAAG EAMSVRSKAL AQGPHIEKKK SHQGRGTMFE
     CETCRNRYRK LENFENHKKF YCSELHGPKT KVAMREPEHS PVPGGLQPQI LHYRVAGSSG
     IWEQTPQIRK RRKMKSVGDD EELQQNESGT SPKSSEGLQF QNALGCNPSL PKHNVTIRSD
     QQHKNIQLQN SHIHLVARGP EQTMDPKLST IMEQQISSAA QDKIELQRHG TGISVIQHTN
     SLSRPNSFDK PEPFERASPV SFQELNRTGK SGSLKVIGIS QEESHPSRDG SHPHQLALSD
     ALRGELQESS RKSPSERHVL GQPSRLVRQH NIQVPEILVT EEPDRDLEAQ CHDQEKSEKF
     SWPQRSETLS KLPTEKLPPK KKRLRLAEIE HSSTESSFDS TLSRSLSRES SLSHTSSFSA
     SLDIEDVSKT EASPKIDFLN KAEFLMIPAG LNTLNVPGCH REMRRTASEQ INCTQTSMEV
     SDLRSKSFDC GSITPPQTTP LTELQPPSSP SRVGVTGHVP LLERRRGPLV RQISLNIAPD
     SHLSPVHPTS FQNTALPSVN AVPYQGPQLT STSLAEFSAN TLHSQTQVKD LQAETSNSSS
     TNVFPVQQLC DINLLNQIHA PPSHQSTQLS LQVSTQGSKP DKNSVLSGSS KSEDCFAPKY
     QLHCQVFTSG PSCSSNPVHS LPNQVISDPV GTDHCVTSAT LPTKLIDSMS NSHPLLPPEL
     RPLGSQVQKV PSSFMLPIRL QSSVPAYCFA TLTSLPQILV TQDLPNQPIC QTNHSVVPIS
     EEQNSVPTLQ KGHQNALPNP EKEFLCENVF SEMSQNSSLS ESLPITQKIS VGRLSPQQES
     SASSKRMLSP ANSLDIAMEK HQKRAKDENG AVCATDVRPL EALSSRVNEA SKQKKPILVR
     QVCTTEPLDG VMLEKDVFSQ PEISNEAVNL TNVLPADNSS TGCSKFVVIE PISELQEFEN
     IKSSTSLTLT VRSSPAPSEN THISPLKCTD NNQERKSPGV KNQGDKVNIQ EQSQQPVTSL
     SLFNIKDTQQ LAFPSLKTTT NFTWCYLLRQ KSLHLPQKDQ KTSAYTDWTV SASNPNPLGL
     PTKVALALLN SKQNTGKSLY CQAITTHSKS DLLVYSSKWK SSLSKRALGN QKSTVVEFSN
     KDASEINSEQ DKENSLIKSE PRRIKIFDGG YKSNEEYVYV RGRGRGKYIC EECGIRCKKP
     SMLKKHIRTH TDVRPYHCTY CNFSFKTKGN LTKHMKSKAH SKKCVDLGVS VGLIDEQDTE
     ESDEKQRFSY ERSGYDLEES DGPDEDDNEN EDDDEDSQAE SVLSATPSVT ASPQHLPSRS
     SLQDPVSTDE DVRITDCFSG VHTDPMDVLP RALLTRMTVL STAQSDYNRK TLSPGKARQR
     AARDENDTIP SVDTSRSPCH QMSVDYPESE EILRSSMAGK AVAITQSPSS VRLPPAAAEH
     SPQTAAGMPS VASPHPDPQE QKQQITLQPT PGLPSPHTHL FSHLPLHSQQ QSRTPYNMVP
     VGGIHVVPAG LTYSTFVPLQ AGPVQLTIPA VSVVHRTLGT HRNTVTEVSG TTNPAGVAEL
     SSVVPCIPIG QIRVPGLQNL STPGLQSLPS LSMETVNIVG LANTNMAPQV HPPGLALNAV
     GLQVLTANPS SQSSPAPQAH IPGLQILNIA LPTLIPSVSQ VAVDAQGAPE MPASQSKACE
     TQPKQTSVAS ANQVSRTESP QGLPTVQREN AKKVLNPPAP AGDHARLDGL SKMDTEKAAS
     ANHVKPKPEL TSIQGQPAST SQPLLKAHSE VFTKPSGQQT LSPDRQVPRP TALPRRQPTV
     HFSDVSSDDD EDRLVIAT
//