ZEP1_HUMAN
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 03-AUG-2022, entry version 214.
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.
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 BioGRID; 109343; 164.
DR ELM; P15822; -.
DR IntAct; P15822; 143.
DR MINT; P15822; -.
DR STRING; 9606.ENSP00000368698; -.
DR ChEMBL; CHEMBL2909; -.
DR MoonDB; P15822; Predicted.
DR GlyConnect; 2896; 1 O-Linked glycan (1 site).
DR GlyGen; P15822; 16 sites, 1 O-linked glycan (16 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; P15822; -.
DR PeptideAtlas; P15822; -.
DR PRIDE; P15822; -.
DR ProteomicsDB; 53225; -. [P15822-1]
DR ProteomicsDB; 53226; -. [P15822-2]
DR ProteomicsDB; 53227; -. [P15822-3]
DR Antibodypedia; 24904; 35 antibodies from 13 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 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 OrthoDB; 1318335at2759; -.
DR PhylomeDB; P15822; -.
DR TreeFam; TF331837; -.
DR PathwayCommons; P15822; -.
DR SignaLink; P15822; -.
DR BioGRID-ORCS; 3096; 11 hits in 1102 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 190 other tissues.
DR ExpressionAtlas; P15822; baseline and differential.
DR Genevisible; P15822; HS.
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 InterPro; IPR034729; ZF_CCHC_HIVEP.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS51811; ZF_CCHC_HIVEP; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
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
