CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008443
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Hepatoma-derived growth factor 
Protein Synonyms/Alias
 HDGF; High mobility group protein 1-like 2; HMG-1L2 
Gene Name
 HDGF 
Gene Synonyms/Alias
 HMG1L2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11SNRQKEYKCGDLVFAubiquitination[1, 2]
39EMPEAAVKSTANKYQacetylation[3]
39EMPEAAVKSTANKYQubiquitination[4, 5, 6]
44AVKSTANKYQVFFFGacetylation[7]
80FGKPNKRKGFSEGLWsumoylation[8]
80FGKPNKRKGFSEGLWubiquitination[1, 2, 4, 5, 9]
96IENNPTVKASGYQSSsumoylation[8]
96IENNPTVKASGYQSSubiquitination[5]
197PLPMEVEKNSTPSEPubiquitination[4]
226DEEEEATKEDAEAPGubiquitination[4, 5]
Reference
 [1] 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]
 [2] 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]
 [3] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [4] 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]
 [5] 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]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] SUMOylation of the hepatoma-derived growth factor negatively influences its binding to chromatin.
 Thakar K, Niedenthal R, Okaz E, Franken S, Jakobs A, Gupta S, Kelm S, Dietz F.
 FEBS J. 2008 Apr;275(7):1411-26. [PMID: 18331345]
 [9] 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
Functional Description
 Heparin-binding protein, with mitogenic activity for fibroblasts. Acts as a transcriptional repressor. 
Sequence Annotation
 DOMAIN 12 69 PWWP.
 MOTIF 75 80 Nuclear localization signal.
 MOTIF 155 170 Bipartite nuclear localization signal.
 BINDING 19 19 Heparin (Probable).
 BINDING 21 21 Heparin (Probable).
 BINDING 72 72 Heparin (Probable).
 BINDING 75 75 Heparin (Probable).
 BINDING 79 79 Heparin (Probable).
 BINDING 80 80 Heparin (Probable).
 MOD_RES 44 44 N6-acetyllysine.
 MOD_RES 132 132 Phosphoserine.
 MOD_RES 133 133 Phosphoserine.
 MOD_RES 165 165 Phosphoserine.
 MOD_RES 199 199 Phosphoserine (By similarity).
 MOD_RES 200 200 Phosphothreonine.
 MOD_RES 202 202 Phosphoserine (By similarity).
 MOD_RES 206 206 Phosphoserine.
 MOD_RES 239 239 Phosphoserine.
 CROSSLNK 80 80 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Growth factor; Heparin-binding; Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor; Transcription; Transcription regulation; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 240 AA 
Protein Sequence
MSRSNRQKEY KCGDLVFAKM KGYPHWPARI DEMPEAAVKS TANKYQVFFF GTHETAFLGP 60
KDLFPYEESK EKFGKPNKRK GFSEGLWEIE NNPTVKASGY QSSQKKSCVE EPEPEPEAAE 120
GDGDKKGNAE GSSDEEGKLV IDEPAKEKNE KGALKRRAGD LLEDSPKRPK EAENPEGEEK 180
EAATLEVERP LPMEVEKNST PSEPGSGRGP PQEEEEEEDE EEEATKEDAE APGIRDHESL 240 
Gene Ontology
 GO:0005737; C:cytoplasm; TAS:ProtInc.
 GO:0005615; C:extracellular space; IDA:BHF-UCL.
 GO:0017053; C:transcriptional repressor complex; IDA:BHF-UCL.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0008201; F:heparin binding; TAS:ProtInc.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0001106; F:RNA polymerase II transcription corepressor activity; IDA:BHF-UCL.
 GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
 GO:0008283; P:cell proliferation; TAS:ProtInc.
 GO:0044267; P:cellular protein metabolic process; TAS:Reactome. 
Interpro
 IPR000313; PWWP. 
Pfam
 PF00855; PWWP 
SMART
 SM00293; PWWP 
PROSITE
 PS50812; PWWP 
PRINTS