CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009390
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Small ubiquitin-related modifier 2 
Protein Synonyms/Alias
 SUMO-2; HSMT3; SMT3 homolog 2; SUMO-3; Sentrin-2; Ubiquitin-like protein SMT3A; Smt3A 
Gene Name
 SUMO2 
Gene Synonyms/Alias
 SMT3A; SMT3H2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MADEKPKEGVKTsumoylation[1, 2]
5***MADEKPKEGVKTubiquitination[3, 4]
7*MADEKPKEGVKTENacetylation[5]
7*MADEKPKEGVKTENsumoylation[2]
7*MADEKPKEGVKTENubiquitination[3, 4]
11EKPKEGVKTENNDHIacetylation[6]
11EKPKEGVKTENNDHIsumoylation[2, 7, 8, 9]
11EKPKEGVKTENNDHIubiquitination[3, 4, 10, 11, 12]
21NNDHINLKVAGQDGSubiquitination[3, 10, 11, 12, 13]
33DGSVVQFKIKRHTPLubiquitination[3, 4, 10, 11, 12, 13]
35SVVQFKIKRHTPLSKubiquitination[4, 10, 13]
42KRHTPLSKLMKAYCEsumoylation[2, 9]
42KRHTPLSKLMKAYCEubiquitination[4, 10, 11, 12, 13]
45TPLSKLMKAYCERQGubiquitination[4, 10, 11, 12, 13]
Reference
 [1] In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy.
 Matic I, van Hagen M, Schimmel J, Macek B, Ogg SC, Tatham MH, Hay RT, Lamond AI, Mann M, Vertegaal AC.
 Mol Cell Proteomics. 2008 Jan;7(1):132-44. [PMID: 17938407]
 [2] Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions.
 Lamoliatte F, Bonneil E, Durette C, Caron-Lizotte O, Wildemann D, Zerweck J, Wenschuh H, Thibault P.
 Mol Cell Proteomics. 2013 Jun 7;. [PMID: 23750026]
 [3] 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]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] 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]
 [6] 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]
 [7] In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification.
 Blomster HA, Imanishi SY, Siimes J, Kastu J, Morrice NA, Eriksson JE, Sistonen L.
 J Biol Chem. 2010 Jun 18;285(25):19324-9. [PMID: 20388717]
 [8] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [9] A novel proteomics approach to identify SUMOylated proteins and their modification sites in human cells.
 Galisson F, Mahrouche L, Courcelles M, Bonneil E, Meloche S, Chelbi-Alix MK, Thibault P.
 Mol Cell Proteomics. 2011 Feb;10(2):M110.004796. [PMID: 21098080]
 [10] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [11] 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]
 [12] 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]
 [13] 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
Functional Description
 Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. 
Sequence Annotation
 DOMAIN 16 95 Ubiquitin-like.
 CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 93 93 Glycyl lysine isopeptide (Gly-Lys)  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Isopeptide bond; Nucleus; Polymorphism; Reference proteome; Ubl conjugation; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 95 AA 
Protein Sequence
MADEKPKEGV KTENNDHINL KVAGQDGSVV QFKIKRHTPL SKLMKAYCER QGLSMRQIRF 60
RFDGQPINET DTPAQLEMED EDTIDVFQQQ TGGVY 95 
Gene Ontology
 GO:0016605; C:PML body; IDA:UniProtKB.
 GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
 GO:0016925; P:protein sumoylation; IDA:UniProtKB. 
Interpro
 IPR022617; SUMO.
 IPR027218; SUMO_chordates.
 IPR000626; Ubiquitin.
 IPR019955; Ubiquitin_supergroup. 
Pfam
 PF11976; Rad60-SLD 
SMART
 SM00213; UBQ 
PROSITE
 PS50053; UBIQUITIN_2 
PRINTS