JUND_HUMAN
ID JUND_HUMAN Reviewed; 347 AA.
AC P17535; Q53EK9;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Transcription factor JunD {ECO:0000305};
DE AltName: Full=Transcription factor AP-1 subunit JunD {ECO:0000305};
GN Name=JUND;
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=1903194;
RA Berger I., Shaul Y.;
RT "Structure and function of human jun-D.";
RL Oncogene 6:561-566(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-20.
RG NIEHS SNPs program;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-347.
RX PubMed=2112242; DOI=10.1093/nar/18.10.3047;
RA Nomura N., Ide M., Sasamoto S., Matsui M., Date T., Ishizaki R.;
RT "Isolation of human cDNA clones of jun-related genes, jun-B and jun-D.";
RL Nucleic Acids Res. 18:3047-3048(1990).
RN [6]
RP FUNCTION, AND INTERACTION WITH MEN1.
RX PubMed=9989505; DOI=10.1016/s0092-8674(00)80967-8;
RA Agarwal S.K., Guru S.C., Heppner C., Erdos M.R., Collins R.M., Park S.Y.,
RA Saggar S., Chandrasekharappa S.C., Collins F.S., Spiegel A.M., Marx S.J.,
RA Burns A.L.;
RT "Menin interacts with the AP1 transcription factor JunD and represses JunD-
RT activated transcription.";
RL Cell 96:143-152(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; SER-255 AND SER-259, AND
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-259, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-259, AND
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [12] {ECO:0007744|PDB:3U86}
RP X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) OF 27-39 IN COMPLEX WITH MEN1,
RP INTERACTION WITH MEN1 AND MAPK10, DOMAIN MENIN-BINDING AND MAP KINASE
RP DOCKING MOTIFS, MUTAGENESIS OF ARG-30; LEU-31; PHE-32; PRO-33; GLY-34;
RP ALA-35; PRO-36; PRO-37; LYS-46; LYS-47; LEU-52 AND LEU-54, AND
RP PHOSPHORYLATION AT SER-90; SER-100 AND THR-117.
RX PubMed=22327296; DOI=10.1038/nature10806;
RA Huang J., Gurung B., Wan B., Matkar S., Veniaminova N.A., Wan K.,
RA Merchant J.L., Hua X., Lei M.;
RT "The same pocket in menin binds both MLL and JUND but has opposite effects
RT on transcription.";
RL Nature 482:542-546(2012).
RN [13] {ECO:0007744|PDB:5VPA, ECO:0007744|PDB:5VPB, ECO:0007744|PDB:5VPC, ECO:0007744|PDB:5VPD, ECO:0007744|PDB:5VPE, ECO:0007744|PDB:5VPF}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 266-332 IN COMPLEX WITH FOSB AND
RP DNA, FUNCTION, SUBUNIT, INTERACTION WITH FOSB, DOMAIN, AND DISULFIDE BOND.
RX PubMed=28981703; DOI=10.1093/nar/gkx795;
RA Yin Z., Machius M., Nestler E.J., Rudenko G.;
RT "Activator Protein-1: redox switch controlling structure and DNA-binding.";
RL Nucleic Acids Res. 45:11425-11436(2017).
CC -!- FUNCTION: Transcription factor binding AP-1 sites (PubMed:9989505).
CC Heterodimerizes with proteins of the FOS family to form an AP-1
CC transcription factor complex, thereby enhancing their DNA binding
CC activity to an AP-1 consensus sequence 3'-TGA[GC]TCA-5' and enhancing
CC their transcriptional activity (PubMed:9989505, PubMed:28981703).
CC {ECO:0000269|PubMed:28981703, ECO:0000269|PubMed:9989505}.
CC -!- SUBUNIT: Heterodimer; binds DNA as a heterodimer (PubMed:28981703).
CC Component of an AP-1 transcription factor complex composed of JUN-FOS
CC heterodimers (By similarity). As part of the AP-1 transcription factor
CC complex, forms heterodimers with FOS proteins, thereby binding to the
CC AP-1 consensus sequence and stimulating transcription (By similarity).
CC Forms heterodimers with FOSB; thereby binding to the AP-1 consensus
CC sequence (PubMed:28981703). Interacts (via MBM motif) with MEN1; this
CC interaction represses transcriptional activation (PubMed:9989505,
CC PubMed:22327296). Interacts with MAPK10; this interaction is inhibited
CC in the presence of MEN1 (PubMed:22327296).
CC {ECO:0000250|UniProtKB:P13346, ECO:0000269|PubMed:22327296,
CC ECO:0000269|PubMed:28981703, ECO:0000269|PubMed:9989505}.
CC -!- INTERACTION:
CC P17535; P61158: ACTR3; NbExp=2; IntAct=EBI-2682803, EBI-351428;
CC P17535; P05067: APP; NbExp=3; IntAct=EBI-2682803, EBI-77613;
CC P17535; P15336: ATF2; NbExp=3; IntAct=EBI-2682803, EBI-1170906;
CC P17535; P18847: ATF3; NbExp=3; IntAct=EBI-2682803, EBI-712767;
CC P17535; P17544: ATF7; NbExp=2; IntAct=EBI-2682803, EBI-765623;
CC P17535; Q16520: BATF; NbExp=2; IntAct=EBI-2682803, EBI-749503;
CC P17535; Q9NR55: BATF3; NbExp=3; IntAct=EBI-2682803, EBI-10312707;
CC P17535; P01100: FOS; NbExp=12; IntAct=EBI-2682803, EBI-852851;
CC P17535; P15408: FOSL2; NbExp=4; IntAct=EBI-2682803, EBI-3893419;
CC P17535; P53779: MAPK10; NbExp=2; IntAct=EBI-2682803, EBI-713543;
CC P17535; Q00987: MDM2; NbExp=3; IntAct=EBI-2682803, EBI-389668;
CC P17535; O00255-2: MEN1; NbExp=6; IntAct=EBI-2682803, EBI-9869387;
CC P17535; P0C746: HBZ; Xeno; NbExp=2; IntAct=EBI-2682803, EBI-10890294;
CC P17535; Q9DGW5: MDV005; Xeno; NbExp=2; IntAct=EBI-2682803, EBI-10889526;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: Binds DNA via bZIP domain; DNA-binding is under control of
CC cellular redox homeostasis (in vitro) (PubMed:28981703). To enable DNA
CC binding, the bZIP domain must undergo a conformational rearrangement
CC which requires the reduction of the interchain disulfide bond between
CC FosB and JunD (in vitro) (PubMed:28981703).
CC {ECO:0000269|PubMed:28981703}.
CC -!- PTM: Phosphorylated by MAP kinases MAPK8 and MAPK10; phosphorylation is
CC inhibited in the presence of MEN1. {ECO:0000269|PubMed:22327296}.
CC -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA40010.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/tnfrsf1b/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/JUNDID179.html";
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DR EMBL; X56681; CAA40010.1; ALT_FRAME; mRNA.
DR EMBL; EF044249; ABJ53425.1; -; Genomic_DNA.
DR EMBL; AK223630; BAD97350.1; -; mRNA.
DR EMBL; CH471106; EAW84684.1; -; Genomic_DNA.
DR EMBL; X51346; CAA35739.1; -; mRNA.
DR CCDS; CCDS32959.1; -.
DR PIR; A43815; A43815.
DR PIR; S10184; TVHUJD.
DR RefSeq; NP_001273897.1; NM_001286968.1.
DR RefSeq; NP_005345.3; NM_005354.5.
DR PDB; 3U86; X-ray; 2.84 A; B=27-39.
DR PDB; 5VPA; X-ray; 2.83 A; B=266-332.
DR PDB; 5VPB; X-ray; 2.69 A; B/D=266-332.
DR PDB; 5VPC; X-ray; 2.50 A; B/D=266-332.
DR PDB; 5VPD; X-ray; 2.79 A; B/D=266-332.
DR PDB; 5VPE; X-ray; 2.05 A; B/D=266-332.
DR PDB; 5VPF; X-ray; 2.69 A; B/D=266-332.
DR PDBsum; 3U86; -.
DR PDBsum; 5VPA; -.
DR PDBsum; 5VPB; -.
DR PDBsum; 5VPC; -.
DR PDBsum; 5VPD; -.
DR PDBsum; 5VPE; -.
DR PDBsum; 5VPF; -.
DR AlphaFoldDB; P17535; -.
DR SMR; P17535; -.
DR BioGRID; 109930; 66.
DR ComplexPortal; CPX-497; Menin-JUND transcription inhibition complex.
DR ComplexPortal; CPX-6422; bZIP transcription factor complex, ATF2-JUND.
DR ComplexPortal; CPX-6788; bZIP transcription factor complex, ATF7-JUND.
DR ComplexPortal; CPX-7013; bZIP transcription factor complex, BATF-JUND.
DR ComplexPortal; CPX-7102; bZIP transcription factor complex, BATF3-JUND.
DR CORUM; P17535; -.
DR DIP; DIP-1053N; -.
DR IntAct; P17535; 36.
DR MINT; P17535; -.
DR STRING; 9606.ENSP00000252818; -.
DR BindingDB; P17535; -.
DR ChEMBL; CHEMBL4630755; -.
DR GlyGen; P17535; 4 sites, 2 O-linked glycans (4 sites).
DR iPTMnet; P17535; -.
DR PhosphoSitePlus; P17535; -.
DR BioMuta; JUND; -.
DR DMDM; 229462969; -.
DR EPD; P17535; -.
DR jPOST; P17535; -.
DR MassIVE; P17535; -.
DR MaxQB; P17535; -.
DR PaxDb; P17535; -.
DR PeptideAtlas; P17535; -.
DR PRIDE; P17535; -.
DR ProteomicsDB; 53481; -.
DR Antibodypedia; 3936; 662 antibodies from 41 providers.
DR DNASU; 3727; -.
DR Ensembl; ENST00000252818.5; ENSP00000252818.3; ENSG00000130522.6.
DR GeneID; 3727; -.
DR KEGG; hsa:3727; -.
DR MANE-Select; ENST00000252818.5; ENSP00000252818.3; NM_005354.6; NP_005345.3.
DR UCSC; uc002nip.4; human.
DR CTD; 3727; -.
DR DisGeNET; 3727; -.
DR GeneCards; JUND; -.
DR HGNC; HGNC:6206; JUND.
DR HPA; ENSG00000130522; Low tissue specificity.
DR MIM; 165162; gene.
DR neXtProt; NX_P17535; -.
DR OpenTargets; ENSG00000130522; -.
DR PharmGKB; PA30008; -.
DR VEuPathDB; HostDB:ENSG00000130522; -.
DR eggNOG; KOG0837; Eukaryota.
DR GeneTree; ENSGT00940000162806; -.
DR HOGENOM; CLU_057007_0_0_1; -.
DR InParanoid; P17535; -.
DR OMA; PHEVQVH; -.
DR OrthoDB; 1090460at2759; -.
DR PhylomeDB; P17535; -.
DR TreeFam; TF323952; -.
DR PathwayCommons; P17535; -.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR SignaLink; P17535; -.
DR SIGNOR; P17535; -.
DR BioGRID-ORCS; 3727; 26 hits in 1107 CRISPR screens.
DR ChiTaRS; JUND; human.
DR GeneWiki; JunD; -.
DR GenomeRNAi; 3727; -.
DR Pharos; P17535; Tbio.
DR PRO; PR:P17535; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P17535; protein.
DR Bgee; ENSG00000130522; Expressed in cardia of stomach and 205 other tissues.
DR ExpressionAtlas; P17535; baseline and differential.
DR Genevisible; P17535; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0032993; C:protein-DNA complex; IEA:Ensembl.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0035976; C:transcription factor AP-1 complex; IDA:CAFA.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0017053; C:transcription repressor complex; IPI:ComplexPortal.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0016922; F:nuclear receptor binding; IEA:Ensembl.
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:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0001221; F:transcription coregulator binding; IEA:Ensembl.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
DR GO; GO:0043032; P:positive regulation of macrophage activation; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:CAFA.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR IDEAL; IID00542; -.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR005643; JNK.
DR InterPro; IPR029823; JunD.
DR InterPro; IPR002112; Leuzip_Jun.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR PANTHER; PTHR11462:SF7; PTHR11462:SF7; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF03957; Jun; 1.
DR PRINTS; PR00043; LEUZIPPRJUN.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF47454; SSF47454; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Disulfide bond; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..347
FT /note="Transcription factor JunD"
FT /id="PRO_0000076442"
FT DOMAIN 268..331
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..295
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 296..324
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOTIF 27..39
FT /note="Menin-binding motif (MBM)"
FT /evidence="ECO:0000269|PubMed:22327296"
FT MOTIF 46..55
FT /note="MAP kinase docking motif; essential for its
FT phosphorylation"
FT /evidence="ECO:0000269|PubMed:22327296"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22327296"
FT MOD_RES 100
FT /note="Phosphoserine; by MAPK8"
FT /evidence="ECO:0000269|PubMed:22327296"
FT MOD_RES 117
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22327296"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT DISULFID 285
FT /note="Interchain (with C-172 in FOSB)"
FT /evidence="ECO:0000269|PubMed:28981703,
FT ECO:0007744|PDB:5VPA, ECO:0007744|PDB:5VPB,
FT ECO:0007744|PDB:5VPC, ECO:0007744|PDB:5VPD"
FT VARIANT 20
FT /note="G -> V (in dbSNP:rs41478151)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_055247"
FT MUTAGEN 30
FT /note="R->A: Reduced interaction with MEN1."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 31
FT /note="L->A: Reduced interaction with MEN1."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 32
FT /note="F->A: Loss of interaction with MEN1."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 33
FT /note="P->A: Loss of interaction with MEN1."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 34
FT /note="G->R: Loss of interaction with MEN1."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 35
FT /note="A->R: Reduced interaction with MEN1."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 36
FT /note="P->A: Reduced interaction with MEN1."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 37
FT /note="P->A: Reduced interaction with MEN1."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 46
FT /note="K->A: Loss of phosphorylation; when associated with
FT A-47."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 46
FT /note="K->E: Reduced interaction with MEN1; when associated
FT with E-47."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 47
FT /note="K->A: Loss of phosphorylation; when associated with
FT A-46."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 47
FT /note="K->E: Reduced interaction with MEN1; when associated
FT with E-46."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 52
FT /note="L->A: Loss of phosphorylation; when associated with
FT A-54."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 54
FT /note="L->A: Loss of phosphorylation; when associated with
FT A-52."
FT /evidence="ECO:0000269|PubMed:22327296"
FT CONFLICT 24
FT /note="S -> T (in Ref. 1; CAA40010)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="A -> R (in Ref. 1; CAA40010)"
FT /evidence="ECO:0000305"
FT HELIX 266..329
FT /evidence="ECO:0007829|PDB:5VPE"
SQ SEQUENCE 347 AA; 35174 MW; FE85A1AA2B5B9597 CRC64;
METPFYGDEA LSGLGGGASG SGGSFASPGR LFPGAPPTAA AGSMMKKDAL TLSLSEQVAA
ALKPAAAPPP TPLRADGAPS AAPPDGLLAS PDLGLLKLAS PELERLIIQS NGLVTTTPTS
SQFLYPKVAA SEEQEFAEGF VKALEDLHKQ NQLGAGAAAA AAAAAAGGPS GTATGSAPPG
ELAPAAAAPE APVYANLSSY AGGAGGAGGA ATVAFAAEPV PFPPPPPPGA LGPPRLAALK
DEPQTVPDVP SFGESPPLSP IDMDTQERIK AERKRLRNRI AASKCRKRKL ERISRLEEKV
KTLKSQNTEL ASTASLLREQ VAQLKQKVLS HVNSGCQLLP QHQVPAY
