SMAD5_HUMAN
ID SMAD5_HUMAN Reviewed; 465 AA.
AC Q99717; O14688; Q15798; Q9UQA1;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Mothers against decapentaplegic homolog 5;
DE Short=MAD homolog 5;
DE Short=Mothers against DPP homolog 5;
DE AltName: Full=JV5-1;
DE AltName: Full=SMAD family member 5;
DE Short=SMAD 5;
DE Short=Smad5;
DE Short=hSmad5;
GN Name=SMAD5; Synonyms=MADH5;
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].
RX PubMed=8673135; DOI=10.1038/ng0796-347;
RA Riggins G.J., Thiagalingam S., Rosenblum E., Weinstein C.L., Kern S.E.,
RA Hamilton S.R., Willson J.K.V., Markowitz S.D., Kinzler K.W.,
RA Vogelstein B.V.;
RT "Mad-related genes in the human.";
RL Nat. Genet. 13:347-349(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=9288787;
RA Hejlik D.P., Kottickal L.V., Liang H., Fairman J., Davis T., Janecki T.,
RA Sexton D., Perry W. III, Tavtigian S.V., Teng D.H., Nagarajan L.;
RT "Localization of SMAD5 and its evaluation as a candidate myeloid tumor
RT suppressor.";
RL Cancer Res. 57:3779-3783(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9264367; DOI=10.1038/sj.leu.2400750;
RA Zavadil J., Brezinova J., Svoboda P., Zemanova Z., Michalova K.;
RT "Smad5, a tumor suppressor candidate at 5q31.1, is hemizygously lost and
RT not mutated in the retained allele in human leukemia cell line HL60.";
RL Leukemia 11:1187-1192(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9484787; DOI=10.1038/sj.onc.1201614;
RA Gemma A., Hagiwara K., Vincent F., Ke Y., Hancock A.R., Nagashima M.,
RA Bennett W.P., Harris C.C.;
RT "hSmad5 gene, a human hSmad family member: its full length cDNA, genomic
RT structure, promoter region and mutation analysis in human tumors.";
RL Oncogene 16:951-956(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF GLY-419.
RX PubMed=9442019; DOI=10.1074/jbc.273.4.1872;
RA Nishimura R., Kato Y., Chen D., Harris S.E., Mundy G.R., Yoneda T.;
RT "Smad5 and DPC4 are key molecules in mediating BMP-2-induced osteoblastic
RT differentiation of the pluripotent mesenchymal precursor cell line C2C12.";
RL J. Biol. Chem. 273:1872-1879(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-16; 34-40; 130-158; 283-306 AND 309-319, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lempens A., Norman J.C.;
RL Submitted (OCT-2009) to UniProtKB.
RN [8]
RP REVIEW.
RX PubMed=9759503; DOI=10.1146/annurev.biochem.67.1.753;
RA Massague J.;
RT "TGF-beta signal transduction.";
RL Annu. Rev. Biochem. 67:753-791(1998).
RN [9]
RP REVIEW.
RX PubMed=10647776; DOI=10.1016/s1359-6101(99)00012-x;
RA Verschueren K., Huylebroeck D.;
RT "Remarkable versatility of Smad proteins in the nucleus of transforming
RT growth factor-beta activated cells.";
RL Cytokine Growth Factor Rev. 10:187-199(1999).
RN [10]
RP REVIEW.
RX PubMed=10708948; DOI=10.1016/s1359-6101(99)00024-6;
RA Wrana J.L., Attisano L.;
RT "The Smad pathway.";
RL Cytokine Growth Factor Rev. 11:5-13(2000).
RN [11]
RP REVIEW.
RX PubMed=10708949; DOI=10.1016/s1359-6101(99)00025-8;
RA Miyazono K.;
RT "TGF-beta signaling by Smad proteins.";
RL Cytokine Growth Factor Rev. 11:15-22(2000).
RN [12]
RP INTERACTION WITH ZNF8.
RX PubMed=12370310; DOI=10.1128/mcb.22.21.7633-7644.2002;
RA Jiao K., Zhou Y., Hogan B.L.M.;
RT "Identification of mZnf8, a mouse Kruppel-like transcriptional repressor,
RT as a novel nuclear interaction partner of Smad1.";
RL Mol. Cell. Biol. 22:7633-7644(2002).
RN [13]
RP INTERACTION WITH SUV39H1 AND SUV39H2.
RX PubMed=15107829; DOI=10.1038/sj.onc.1207660;
RA Frontelo P., Leader J.E., Yoo N., Potocki A.C., Crawford M., Kulik M.,
RA Lechleider R.J.;
RT "Suv39h histone methyltransferases interact with Smads and cooperate in
RT BMP-induced repression.";
RL Oncogene 23:5242-5251(2004).
RN [14]
RP INTERACTION WITH LEMD3.
RX PubMed=15647271; DOI=10.1074/jbc.m411234200;
RA Pan D., Estevez-Salmeron L.D., Stroschein S.L., Zhu X., He J., Zhou S.,
RA Luo K.;
RT "The integral inner nuclear membrane protein MAN1 physically interacts with
RT the R-Smad proteins to repress signaling by the transforming growth
RT factor-{beta} superfamily of cytokines.";
RL J. Biol. Chem. 280:15992-16001(2005).
RN [15]
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 [16]
RP 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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 AND SER-465, 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 [19]
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 [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [22]
RP INTERACTION WITH RANBP3L.
RX PubMed=25755279; DOI=10.1128/mcb.00121-15;
RA Chen F., Lin X., Xu P., Zhang Z., Chen Y., Wang C., Han J., Zhao B.,
RA Xiao M., Feng X.H.;
RT "Nuclear export of Smads by RanBP3L regulates bone morphogenetic protein
RT signaling and mesenchymal stem cell differentiation.";
RL Mol. Cell. Biol. 35:1700-1711(2015).
CC -!- FUNCTION: Transcriptional modulator activated by BMP (bone
CC morphogenetic proteins) type 1 receptor kinase. SMAD5 is a receptor-
CC regulated SMAD (R-SMAD).
CC -!- SUBUNIT: May form trimers with the co-SMAD SMAD4. Interacts with PEBP2-
CC alpha subunit and SMURF1. Interacts with SUV39H1 and SUV39H2. Interacts
CC (via MH2 domain) with LEMD3. Interacts with WWP1. Interacts with
CC TMEM119 (By similarity). Interacts with ZNF8 (PubMed:12370310).
CC Interacts with RANBP3L (PubMed:25755279).
CC {ECO:0000250|UniProtKB:P97454, ECO:0000269|PubMed:12370310,
CC ECO:0000269|PubMed:15107829, ECO:0000269|PubMed:15647271,
CC ECO:0000269|PubMed:25755279}.
CC -!- INTERACTION:
CC Q99717; P17844: DDX5; NbExp=3; IntAct=EBI-6391136, EBI-351962;
CC Q99717; Q92876: KLK6; NbExp=3; IntAct=EBI-6391136, EBI-2432309;
CC Q99717; Q99732: LITAF; NbExp=3; IntAct=EBI-6391136, EBI-725647;
CC Q99717; P78424: POU6F2; NbExp=3; IntAct=EBI-6391136, EBI-12029004;
CC Q99717; Q969T9: WBP2; NbExp=3; IntAct=EBI-6391136, EBI-727055;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic in the
CC absence of ligand. Migrates to the nucleus when complexed with SMAD4.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Phosphorylated on serine by BMP (bone morphogenetic proteins) type
CC 1 receptor kinase.
CC -!- PTM: Ubiquitin-mediated proteolysis by SMAD-specific E3 ubiquitin
CC ligase SMURF1.
CC -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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DR EMBL; U59913; AAC50791.1; -; mRNA.
DR EMBL; AF010601; AAB66353.1; -; mRNA.
DR EMBL; AF010607; AAB92396.1; -; Genomic_DNA.
DR EMBL; AF010602; AAB92396.1; JOINED; Genomic_DNA.
DR EMBL; AF010603; AAB92396.1; JOINED; Genomic_DNA.
DR EMBL; AF010604; AAB92396.1; JOINED; Genomic_DNA.
DR EMBL; AF010605; AAB92396.1; JOINED; Genomic_DNA.
DR EMBL; AF010606; AAB92396.1; JOINED; Genomic_DNA.
DR EMBL; U73825; AAB95090.1; -; mRNA.
DR EMBL; AF009744; AAB82655.1; -; Genomic_DNA.
DR EMBL; AF009739; AAB82655.1; JOINED; Genomic_DNA.
DR EMBL; AF009740; AAB82655.1; JOINED; Genomic_DNA.
DR EMBL; AF009741; AAB82655.1; JOINED; Genomic_DNA.
DR EMBL; AF009742; AAB82655.1; JOINED; Genomic_DNA.
DR EMBL; AF009743; AAB82655.1; JOINED; Genomic_DNA.
DR EMBL; AF009678; AAB72180.1; -; mRNA.
DR EMBL; BC009682; AAH09682.1; -; mRNA.
DR CCDS; CCDS75308.1; -.
DR RefSeq; NP_001001419.1; NM_001001419.2.
DR RefSeq; NP_001001420.1; NM_001001420.2.
DR RefSeq; NP_005894.3; NM_005903.6.
DR RefSeq; XP_016864959.1; XM_017009470.1.
DR PDB; 6FZS; X-ray; 2.31 A; A/B=9-138.
DR PDB; 6TCE; X-ray; 2.92 A; A=9-138.
DR PDBsum; 6FZS; -.
DR PDBsum; 6TCE; -.
DR AlphaFoldDB; Q99717; -.
DR SASBDB; Q99717; -.
DR SMR; Q99717; -.
DR BioGRID; 110265; 82.
DR DIP; DIP-57571N; -.
DR IntAct; Q99717; 43.
DR MINT; Q99717; -.
DR STRING; 9606.ENSP00000441954; -.
DR iPTMnet; Q99717; -.
DR PhosphoSitePlus; Q99717; -.
DR BioMuta; SMAD5; -.
DR DMDM; 13959566; -.
DR EPD; Q99717; -.
DR jPOST; Q99717; -.
DR MassIVE; Q99717; -.
DR MaxQB; Q99717; -.
DR PaxDb; Q99717; -.
DR PeptideAtlas; Q99717; -.
DR PRIDE; Q99717; -.
DR ProteomicsDB; 78432; -.
DR Antibodypedia; 7303; 616 antibodies from 41 providers.
DR DNASU; 4090; -.
DR Ensembl; ENST00000509297.6; ENSP00000426696.2; ENSG00000113658.18.
DR Ensembl; ENST00000545279.6; ENSP00000441954.2; ENSG00000113658.18.
DR Ensembl; ENST00000545620.5; ENSP00000446474.2; ENSG00000113658.18.
DR GeneID; 4090; -.
DR KEGG; hsa:4090; -.
DR MANE-Select; ENST00000545279.6; ENSP00000441954.2; NM_005903.7; NP_005894.3.
DR UCSC; uc032vlw.2; human.
DR CTD; 4090; -.
DR DisGeNET; 4090; -.
DR GeneCards; SMAD5; -.
DR HGNC; HGNC:6771; SMAD5.
DR HPA; ENSG00000113658; Low tissue specificity.
DR MIM; 603110; gene.
DR neXtProt; NX_Q99717; -.
DR OpenTargets; ENSG00000113658; -.
DR PharmGKB; PA30528; -.
DR VEuPathDB; HostDB:ENSG00000113658; -.
DR eggNOG; KOG3701; Eukaryota.
DR GeneTree; ENSGT00940000155437; -.
DR HOGENOM; CLU_026736_0_2_1; -.
DR InParanoid; Q99717; -.
DR OMA; PPEEQMG; -.
DR OrthoDB; 608001at2759; -.
DR PhylomeDB; Q99717; -.
DR PathwayCommons; Q99717; -.
DR Reactome; R-HSA-201451; Signaling by BMP.
DR SignaLink; Q99717; -.
DR SIGNOR; Q99717; -.
DR BioGRID-ORCS; 4090; 11 hits in 290 CRISPR screens.
DR ChiTaRS; SMAD5; human.
DR GeneWiki; Mothers_against_decapentaplegic_homolog_5; -.
DR GenomeRNAi; 4090; -.
DR Pharos; Q99717; Tbio.
DR PRO; PR:Q99717; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q99717; protein.
DR Bgee; ENSG00000113658; Expressed in mucosa of paranasal sinus and 199 other tissues.
DR ExpressionAtlas; Q99717; baseline and differential.
DR Genevisible; Q99717; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0071144; C:heteromeric SMAD protein complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0071141; C:SMAD protein complex; NAS:BHF-UCL.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0070411; F:I-SMAD binding; IBA:GO_Central.
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; IDA:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0003161; P:cardiac conduction system development; NAS:BHF-UCL.
DR GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0009880; P:embryonic pattern specification; ISS:UniProtKB.
DR GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0007281; P:germ cell development; IEA:Ensembl.
DR GO; GO:0001880; P:Mullerian duct regression; IEA:Ensembl.
DR GO; GO:0002051; P:osteoblast fate commitment; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; ISS:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISS:BHF-UCL.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
DR Gene3D; 2.60.200.10; -; 1.
DR Gene3D; 3.90.520.10; -; 1.
DR InterPro; IPR013790; Dwarfin.
DR InterPro; IPR003619; MAD_homology1_Dwarfin-type.
DR InterPro; IPR013019; MAD_homology_MH1.
DR InterPro; IPR017855; SMAD-like_dom_sf.
DR InterPro; IPR001132; SMAD_dom_Dwarfin-type.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR036578; SMAD_MH1_sf.
DR PANTHER; PTHR13703; PTHR13703; 1.
DR Pfam; PF03165; MH1; 1.
DR Pfam; PF03166; MH2; 1.
DR SMART; SM00523; DWA; 1.
DR SMART; SM00524; DWB; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF56366; SSF56366; 1.
DR PROSITE; PS51075; MH1; 1.
DR PROSITE; PS51076; MH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:22223895"
FT CHAIN 2..465
FT /note="Mothers against decapentaplegic homolog 5"
FT /id="PRO_0000090865"
FT DOMAIN 13..137
FT /note="MH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
FT DOMAIN 271..465
FT /note="MH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
FT REGION 163..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..201
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:22223895"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MUTAGEN 419
FT /note="G->S: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:9442019"
FT CONFLICT 175
FT /note="D -> H (in Ref. 1; AAC50791)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="N -> P (in Ref. 1; AAC50791)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="S -> R (in Ref. 1; AAC50791)"
FT /evidence="ECO:0000305"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:6FZS"
FT HELIX 26..42
FT /evidence="ECO:0007829|PDB:6FZS"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:6FZS"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6FZS"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6FZS"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6FZS"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6FZS"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:6FZS"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:6FZS"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:6FZS"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6FZS"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:6FZS"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6FZS"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6FZS"
SQ SEQUENCE 465 AA; 52258 MW; 4A1FD7EC7BD06728 CRC64;
MTSMASLFSF TSPAVKRLLG WKQGDEEEKW AEKAVDALVK KLKKKKGAME ELEKALSSPG
QPSKCVTIPR SLDGRLQVSH RKGLPHVIYC RVWRWPDLQS HHELKPLDIC EFPFGSKQKE
VCINPYHYKR VESPVLPPVL VPRHNEFNPQ HSLLVQFRNL SHNEPHMPQN ATFPDSFHQP
NNTPFPLSPN SPYPPSPASS TYPNSPASSG PGSPFQLPAD TPPPAYMPPD DQMGQDNSQP
MDTSNNMIPQ IMPSISSRDV QPVAYEEPKH WCSIVYYELN NRVGEAFHAS STSVLVDGFT
DPSNNKSRFC LGLLSNVNRN STIENTRRHI GKGVHLYYVG GEVYAECLSD SSIFVQSRNC
NFHHGFHPTT VCKIPSSCSL KIFNNQEFAQ LLAQSVNHGF EAVYELTKMC TIRMSFVKGW
GAEYHRQDVT STPCWIEIHL HGPLQWLDKV LTQMGSPLNP ISSVS
