ID ZHX3_HUMAN Reviewed; 956 AA.
AC Q9H4I2; E1P5W5; F5H820; O43145; Q6NUJ7;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 3.
DT 27-MAR-2024, entry version 194.
DE RecName: Full=Zinc fingers and homeoboxes protein 3;
DE AltName: Full=Triple homeobox protein 1;
DE AltName: Full=Zinc finger and homeodomain protein 3;
GN Name=ZHX3; Synonyms=KIAA0395, TIX1;
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, SUBUNIT, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH NFYA.
RC TISSUE=Testis;
RX PubMed=12659632; DOI=10.1042/bj20021866;
RA Yamada K., Kawata H., Shou Z., Hirano S., Mizutani T., Yazawa T.,
RA Sekiguchi T., Yoshino M., Kajitani T., Miyamoto K.;
RT "Analysis of zinc-fingers and homeoboxes (ZHX)-1-interacting proteins:
RT molecular cloning and characterization of a member of the ZHX family,
RT ZHX3.";
RL Biochem. J. 373:167-178(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [8]
RP SUBUNIT.
RX PubMed=14659886; DOI=10.1016/j.gene.2003.09.013;
RA Kawata H., Yamada K., Shou Z., Mizutani T., Miyamoto K.;
RT "The mouse zinc-fingers and homeoboxes (ZHX) family: ZHX2 forms a
RT heterodimer with ZHX3.";
RL Gene 323:133-140(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-946, AND IDENTIFICATION BY
RP 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 [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 FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=21174497; DOI=10.1089/scd.2010.0279;
RA Suehiro F., Nishimura M., Kawamoto T., Kanawa M., Yoshizawa Y., Murata H.,
RA Kato Y.;
RT "Impact of zinc fingers and homeoboxes 3 on the regulation of mesenchymal
RT stem cell osteogenic differentiation.";
RL Stem Cells Dev. 20:1539-1547(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599; SER-604; SER-680 AND
RP SER-723, AND 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-927 AND SER-946, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP STRUCTURE BY NMR OF 494-675.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the homeobox domain of zinc fingers and homeoboxes
RT protein 3 (triple homeobox 1 protein).";
RL Submitted (JUN-2006) to the PDB data bank.
RN [17]
RP STRUCTURE BY NMR OF 494-556.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the second homeobox domain of human zinc fingers and
RT homeoboxes protein 3.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Acts as a transcriptional repressor. Involved in the early
CC stages of mesenchymal stem cell (MSC) osteogenic differentiation. Is a
CC regulator of podocyte gene expression during primary glomerula disease.
CC Binds to promoter DNA. {ECO:0000269|PubMed:12659632,
CC ECO:0000269|PubMed:21174497}.
CC -!- SUBUNIT: Homodimer (via homeobox domain 1) (PubMed:12659632,
CC PubMed:14659886). Heterodimer with ZHX1 (via homeobox domain 1)
CC (PubMed:12659632). Heterodimer with ZHX2 (via homeobox domain 1)
CC (PubMed:14659886). Heterodimerization with ZHX1 is a prerequisite for
CC repressor activity (PubMed:12659632). Interacts with NFYA
CC (PubMed:12659632). {ECO:0000269|PubMed:12659632,
CC ECO:0000269|PubMed:14659886}.
CC -!- INTERACTION:
CC Q9H4I2; Q9UBE8: NLK; NbExp=4; IntAct=EBI-948582, EBI-366978;
CC Q9H4I2-2; P54253: ATXN1; NbExp=6; IntAct=EBI-10693326, EBI-930964;
CC Q9H4I2-2; P54252: ATXN3; NbExp=3; IntAct=EBI-10693326, EBI-946046;
CC Q9H4I2-2; P46379-2: BAG6; NbExp=3; IntAct=EBI-10693326, EBI-10988864;
CC Q9H4I2-2; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-10693326, EBI-21553822;
CC Q9H4I2-2; P14136: GFAP; NbExp=3; IntAct=EBI-10693326, EBI-744302;
CC Q9H4I2-2; O14901: KLF11; NbExp=3; IntAct=EBI-10693326, EBI-948266;
CC Q9H4I2-2; Q9UBE8: NLK; NbExp=3; IntAct=EBI-10693326, EBI-366978;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC ECO:0000269|PubMed:12659632}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H4I2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H4I2-2; Sequence=VSP_054307;
CC -!- TISSUE SPECIFICITY: Widely expressed. High expression in kidney.
CC Expressed during osteogenic differentiation.
CC {ECO:0000269|PubMed:12659632, ECO:0000269|PubMed:21174497}.
CC -!- INDUCTION: Up-regulated during osteogenic differentiation of
CC mesenchymal stem cells. {ECO:0000269|PubMed:21174497}.
CC -!- SIMILARITY: Belongs to the ZHX family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA23691.3; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB081948; BAC65211.1; -; mRNA.
DR EMBL; AB007855; BAA23691.3; ALT_INIT; mRNA.
DR EMBL; AL022394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75987.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75988.1; -; Genomic_DNA.
DR EMBL; BC068569; AAH68569.1; -; mRNA.
DR CCDS; CCDS13315.1; -. [Q9H4I2-1]
DR CCDS; CCDS93040.1; -. [Q9H4I2-2]
DR RefSeq; NP_055850.1; NM_015035.3. [Q9H4I2-1]
DR RefSeq; XP_005260398.1; XM_005260341.3. [Q9H4I2-2]
DR RefSeq; XP_011527022.1; XM_011528720.1.
DR RefSeq; XP_016883226.1; XM_017027737.1.
DR RefSeq; XP_016883227.1; XM_017027738.1.
DR PDB; 2DA5; NMR; -; A=613-674.
DR PDB; 2DN0; NMR; -; A=494-556.
DR PDBsum; 2DA5; -.
DR PDBsum; 2DN0; -.
DR AlphaFoldDB; Q9H4I2; -.
DR SMR; Q9H4I2; -.
DR BioGRID; 116688; 36.
DR IntAct; Q9H4I2; 24.
DR MINT; Q9H4I2; -.
DR STRING; 9606.ENSP00000312222; -.
DR GlyCosmos; Q9H4I2; 4 sites, 1 glycan.
DR GlyGen; Q9H4I2; 13 sites, 1 O-linked glycan (13 sites).
DR iPTMnet; Q9H4I2; -.
DR PhosphoSitePlus; Q9H4I2; -.
DR BioMuta; ZHX3; -.
DR DMDM; 44889075; -.
DR EPD; Q9H4I2; -.
DR jPOST; Q9H4I2; -.
DR MassIVE; Q9H4I2; -.
DR MaxQB; Q9H4I2; -.
DR PaxDb; 9606-ENSP00000312222; -.
DR PeptideAtlas; Q9H4I2; -.
DR ProteomicsDB; 27656; -.
DR ProteomicsDB; 80842; -. [Q9H4I2-1]
DR Pumba; Q9H4I2; -.
DR Antibodypedia; 1834; 187 antibodies from 21 providers.
DR DNASU; 23051; -.
DR Ensembl; ENST00000309060.7; ENSP00000312222.4; ENSG00000174306.22. [Q9H4I2-1]
DR Ensembl; ENST00000432768.6; ENSP00000415498.3; ENSG00000174306.22. [Q9H4I2-1]
DR Ensembl; ENST00000544979.6; ENSP00000443783.2; ENSG00000174306.22. [Q9H4I2-2]
DR Ensembl; ENST00000559234.5; ENSP00000452965.1; ENSG00000174306.22. [Q9H4I2-1]
DR Ensembl; ENST00000560361.5; ENSP00000454006.1; ENSG00000174306.22. [Q9H4I2-1]
DR Ensembl; ENST00000683867.1; ENSP00000506788.1; ENSG00000174306.22. [Q9H4I2-1]
DR GeneID; 23051; -.
DR KEGG; hsa:23051; -.
DR MANE-Select; ENST00000683867.1; ENSP00000506788.1; NM_001384317.1; NP_001371246.1.
DR UCSC; uc002xjr.2; human. [Q9H4I2-1]
DR AGR; HGNC:15935; -.
DR CTD; 23051; -.
DR DisGeNET; 23051; -.
DR GeneCards; ZHX3; -.
DR HGNC; HGNC:15935; ZHX3.
DR HPA; ENSG00000174306; Low tissue specificity.
DR MIM; 609598; gene.
DR neXtProt; NX_Q9H4I2; -.
DR OpenTargets; ENSG00000174306; -.
DR PharmGKB; PA38056; -.
DR VEuPathDB; HostDB:ENSG00000174306; -.
DR eggNOG; ENOG502RC6G; Eukaryota.
DR GeneTree; ENSGT00950000182893; -.
DR HOGENOM; CLU_009147_1_0_1; -.
DR InParanoid; Q9H4I2; -.
DR OMA; YYVTHKM; -.
DR OrthoDB; 5350395at2759; -.
DR PhylomeDB; Q9H4I2; -.
DR TreeFam; TF333363; -.
DR PathwayCommons; Q9H4I2; -.
DR SignaLink; Q9H4I2; -.
DR BioGRID-ORCS; 23051; 9 hits in 1176 CRISPR screens.
DR ChiTaRS; ZHX3; human.
DR EvolutionaryTrace; Q9H4I2; -.
DR GeneWiki; ZHX3; -.
DR GenomeRNAi; 23051; -.
DR Pharos; Q9H4I2; Tbio.
DR PRO; PR:Q9H4I2; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H4I2; Protein.
DR Bgee; ENSG00000174306; Expressed in sural nerve and 204 other cell types or tissues.
DR ExpressionAtlas; Q9H4I2; baseline and differential.
DR Genevisible; Q9H4I2; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 4.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 5.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR024578; Homez_homeobox_dom.
DR InterPro; IPR041057; ZHX_Znf_C2H2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15467:SF6; ZINC FINGERS AND HOMEOBOXES PROTEIN 3; 1.
DR PANTHER; PTHR15467; ZINC-FINGERS AND HOMEOBOXES RELATED; 1.
DR Pfam; PF00046; Homeodomain; 3.
DR Pfam; PF11569; Homez; 1.
DR Pfam; PF18387; zf_C2H2_ZHX; 1.
DR SMART; SM00389; HOX; 4.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 5.
DR PROSITE; PS50071; HOMEOBOX_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Differentiation; DNA-binding; Homeobox;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..956
FT /note="Zinc fingers and homeoboxes protein 3"
FT /id="PRO_0000049395"
FT ZN_FING 77..100
FT /note="C2H2-type 1"
FT ZN_FING 109..132
FT /note="C2H2-type 2"
FT DNA_BIND 304..363
FT /note="Homeobox 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 494..553
FT /note="Homeobox 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 612..671
FT /note="Homeobox 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 764..823
FT /note="Homeobox 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 835..894
FT /note="Homeobox 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..107
FT /note="Required for nuclear localization"
FT REGION 22..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..488
FT /note="Required for homodimerization and interaction with
FT NFYA"
FT /evidence="ECO:0000269|PubMed:12659632"
FT REGION 303..502
FT /note="Required for repressor activity"
FT REGION 497..555
FT /note="Required for nuclear localization"
FT REGION 598..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..695
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0Q2"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 927
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 946
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 879..956
FT /note="VKQWFAEKMGEETRAVADTGSEDQGPGTGELTAVHKGMGDTYSEVSENSESW
FT EPRVPEASSEPFDTSSPQAGRQLETD -> KQTEFDLINVKDWPVWETACHVEEPNPTL
FT CCHMPFPCPAAGHLGELPESSQTAQSLPLPSACPPPSKQQARWGSHQFFLPQCRTFPLP
FT SNG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054307"
FT VARIANT 310
FT /note="N -> S (in dbSNP:rs17265513)"
FT /id="VAR_049597"
FT CONFLICT 642
FT /note="L -> M (in Ref. 7; AAH68569)"
FT /evidence="ECO:0000305"
FT CONFLICT 907
FT /note="G -> T (in Ref. 2; BAA23691)"
FT /evidence="ECO:0000305"
FT HELIX 503..515
FT /evidence="ECO:0007829|PDB:2DN0"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:2DN0"
FT HELIX 522..531
FT /evidence="ECO:0007829|PDB:2DN0"
FT HELIX 535..548
FT /evidence="ECO:0007829|PDB:2DN0"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:2DN0"
FT STRAND 554..556
FT /evidence="ECO:0007829|PDB:2DN0"
FT HELIX 621..633
FT /evidence="ECO:0007829|PDB:2DA5"
FT HELIX 639..649
FT /evidence="ECO:0007829|PDB:2DA5"
FT HELIX 653..663
FT /evidence="ECO:0007829|PDB:2DA5"
FT HELIX 666..669
FT /evidence="ECO:0007829|PDB:2DA5"
SQ SEQUENCE 956 AA; 104658 MW; B3DB35CFC1781A3A CRC64;
MASKRKSTTP CMIPVKTVVL QDASMEAQPA ETLPEGPQQD LPPEASAASS EAAQNPSSTD
GSTLANGHRS TLDGYLYSCK YCDFRSHDMT QFVGHMNSEH TDFNKDPTFV CSGCSFLAKT
PEGLSLHNAT CHSGEASFVW NVAKPDNHVV VEQSIPESTS TPDLAGEPSA EGADGQAEII
ITKTPIMKIM KGKAEAKKIH TLKENVPSQP VGEALPKLST GEMEVREGDH SFINGAVPVS
QASASSAKNP HAANGPLIGT VPVLPAGIAQ FLSLQQQPPV HAQHHVHQPL PTAKALPKVM
IPLSSIPTYN AAMDSNSFLK NSFHKFPYPT KAELCYLTVV TKYPEEQLKI WFTAQRLKQG
ISWSPEEIED ARKKMFNTVI QSVPQPTITV LNTPLVASAG NVQHLIQAAL PGHVVGQPEG
TGGGLLVTQP LMANGLQATS SPLPLTVTSV PKQPGVAPIN TVCSNTTSAV KVVNAAQSLL
TACPSITSQA FLDASIYKNK KSHEQLSALK GSFCRNQFPG QSEVEHLTKV TGLSTREVRK
WFSDRRYHCR NLKGSRAMIP GDHSSIIIDS VPEVSFSPSS KVPEVTCIPT TATLATHPSA
KRQSWHQTPD FTPTKYKERA PEQLRALESS FAQNPLPLDE ELDRLRSETK MTRREIDSWF
SERRKKVNAE ETKKAEENAS QEEEEAAEDE GGEEDLASEL RVSGENGSLE MPSSHILAER
KVSPIKINLK NLRVTEANGR NEIPGLGACD PEDDESNKLA EQLPGKVSCK KTAQQRHLLR
QLFVQTQWPS NQDYDSIMAQ TGLPRPEVVR WFGDSRYALK NGQLKWYEDY KRGNFPPGLL
VIAPGNRELL QDYYMTHKML YEEDLQNLCD KTQMSSQQVK QWFAEKMGEE TRAVADTGSE
DQGPGTGELT AVHKGMGDTY SEVSENSESW EPRVPEASSE PFDTSSPQAG RQLETD
//
