CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004575
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcription factor jun-D 
Protein Synonyms/Alias
  
Gene Name
 JUND 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
97SPDLGLLKLASPELEubiquitination[1]
327QVAQLKQKVLSHVNSubiquitination[2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
 Transcription factor binding AP-1 sites. 
Sequence Annotation
 DOMAIN 268 331 bZIP.
 REGION 268 295 Basic motif (By similarity).
 REGION 296 324 Leucine-zipper (By similarity).
 MOD_RES 251 251 Phosphoserine.
 MOD_RES 255 255 Phosphoserine.
 MOD_RES 259 259 Phosphoserine.  
Keyword
 3D-structure; Activator; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 347 AA 
Protein Sequence
METPFYGDEA LSGLGGGASG SGGSFASPGR LFPGAPPTAA AGSMMKKDAL TLSLSEQVAA 60
ALKPAAAPPP TPLRADGAPS AAPPDGLLAS PDLGLLKLAS PELERLIIQS NGLVTTTPTS 120
SQFLYPKVAA SEEQEFAEGF VKALEDLHKQ NQLGAGAAAA AAAAAAGGPS GTATGSAPPG 180
ELAPAAAAPE APVYANLSSY AGGAGGAGGA ATVAFAAEPV PFPPPPPPGA LGPPRLAALK 240
DEPQTVPDVP SFGESPPLSP IDMDTQERIK AERKRLRNRI AASKCRKRKL ERISRLEEKV 300
KTLKSQNTEL ASTASLLREQ VAQLKQKVLS HVNSGCQLLP QHQVPAY 347 
Gene Ontology
 GO:0000785; C:chromatin; TAS:ProtInc.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0003690; F:double-stranded DNA binding; IEA:Compara.
 GO:0043565; F:sequence-specific DNA binding; IEA:Compara.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:Compara.
 GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
 GO:0007568; P:aging; IEA:Compara.
 GO:0071277; P:cellular response to calcium ion; IEA:Compara.
 GO:0007623; P:circadian rhythm; IEA:Compara.
 GO:0002076; P:osteoblast development; IEA:Compara.
 GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Compara.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
 GO:0009416; P:response to light stimulus; IEA:Compara.
 GO:0032496; P:response to lipopolysaccharide; IEA:Compara.
 GO:0009612; P:response to mechanical stimulus; IEA:Compara.
 GO:0014070; P:response to organic cyclic compound; IEA:Compara.
 GO:0043434; P:response to peptide hormone stimulus; IEA:Compara.
 GO:0006366; P:transcription from RNA polymerase II promoter; IEA:Compara. 
Interpro
 IPR004827; bZIP.
 IPR008917; Euk_TF_DNA-bd.
 IPR005643; JNK.
 IPR002112; Leuzip_Jun. 
Pfam
 PF00170; bZIP_1
 PF03957; Jun 
SMART
 SM00338; BRLZ 
PROSITE
 PS50217; BZIP
 PS00036; BZIP_BASIC 
PRINTS
 PR00043; LEUZIPPRJUN.