CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005308
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Growth arrest and DNA damage-inducible protein GADD45 alpha 
Protein Synonyms/Alias
 DNA damage-inducible transcript 1 protein; DDIT-1 
Gene Name
 GADD45A 
Gene Synonyms/Alias
 DDIT1; GADD45 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
12EFSAGEQKTERMDKVubiquitination[1, 2]
18QKTERMDKVGDALEEubiquitination[1, 3, 4]
29ALEEVLSKALSQRTIubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9]
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] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [7] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [8] 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]
 [9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
 In T-cells, functions as a regulator of p38 MAPKs by inhibiting p88 phosphorylation and activity (By similarity). Might affect PCNA interaction with some CDK (cell division protein kinase) complexes; stimulates DNA excision repair in vitro and inhibits entry of cells into S phase. 
Sequence Annotation
 REGION 1 16 Intrinsically disordered.
 REGION 105 118 Intrinsically disordered.  
Keyword
 3D-structure; Alternative splicing; Cell cycle; Complete proteome; DNA damage; Growth arrest; Nucleus; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 165 AA 
Protein Sequence
MTLEEFSAGE QKTERMDKVG DALEEVLSKA LSQRTITVGV YEAAKLLNVD PDNVVLCLLA 60
ADEDDDRDVA LQIHFTLIQA FCCENDINIL RVSNPGRLAE LLLLETDAGP AASEGAEQPP 120
DLHCVLVTNP HSSQWKDPAL SQLICFCRES RYMDQWVPVI NLPER 165 
Gene Ontology
 GO:0005634; C:nucleus; IDA:LIFEdb.
 GO:0006915; P:apoptotic process; TAS:ProtInc.
 GO:0007050; P:cell cycle arrest; TAS:ProtInc.
 GO:0071479; P:cellular response to ionizing radiation; IMP:BHF-UCL.
 GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
 GO:0007098; P:centrosome cycle; IEA:Compara.
 GO:0006281; P:DNA repair; TAS:ProtInc.
 GO:0006469; P:negative regulation of protein kinase activity; IEA:Compara.
 GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:BHF-UCL.
 GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc.
 GO:0042770; P:signal transduction in response to DNA damage; IMP:BHF-UCL. 
Interpro
 IPR024824; GADD45.
 IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45. 
Pfam
 PF01248; Ribosomal_L7Ae 
SMART
  
PROSITE
  
PRINTS