CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017314
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Spartin 
Protein Synonyms/Alias
 Spastic paraplegia 20 protein; Trans-activated by hepatitis C virus core protein 1 
Gene Name
 SPG20 
Gene Synonyms/Alias
 KIAA0610; TAHCCP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
29KAFLFVNKGLNTDELubiquitination[1, 2]
47EEAKNYYKQGIGHLLubiquitination[1, 2]
62RGISISSKESEHTGPubiquitination[1, 2]
82RQMQQKMKETLQNVRubiquitination[1, 2, 3]
97TRLEILEKGLATSLQubiquitination[4]
362RPSSDQLKEASGTDVubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13]
370EASGTDVKQLDQGNKubiquitination[1, 2, 3, 4, 7, 8, 9, 12, 13]
377KQLDQGNKDVRHKGKubiquitination[1, 2, 3, 7, 8, 13]
390GKRGKRAKDTSSEEVubiquitination[3]
412CEPVPEEKPKELPEWubiquitination[3, 8]
440WVSWGLVKGAEITGKubiquitination[7, 8, 13]
447KGAEITGKAIQKGASubiquitination[1, 2, 3, 8, 10, 12, 13]
465ERIQPEEKPVEVSPAubiquitination[1, 2, 3, 12, 13]
475EVSPAVTKGLYIAKQubiquitination[1, 2, 3, 7, 8, 12, 13]
481TKGLYIAKQATGGAAubiquitination[3, 8, 10, 12, 13]
489QATGGAAKVSQFLVDubiquitination[3, 8, 13]
507TVANCVGKELAPHVKubiquitination[1, 2, 3, 8]
515ELAPHVKKHGSKLVPubiquitination[3]
519HVKKHGSKLVPESLKubiquitination[3, 12, 13]
526KLVPESLKKDKDGKSubiquitination[13]
527LVPESLKKDKDGKSPubiquitination[3]
578TVQTVRYKYGYNAGEubiquitination[1, 2, 3, 4]
610NINNIGIKAMVKKTAubiquitination[8]
615GIKAMVKKTATQTGHubiquitination[3, 4, 13]
656GEKDEQTKEVKEAKKubiquitination[7]
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] 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]
 [4] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [5] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
 Meierhofer D, Wang X, Huang L, Kaiser P.
 J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797]
 [6] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [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] 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] 
Functional Description
 May be implicated in endosomal trafficking, or microtubule dynamics, or both. 
Sequence Annotation
 DOMAIN 16 94 MIT.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 470 470 Phosphoserine.
 CROSSLNK 362 362 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Hereditary spastic paraplegia; Isopeptide bond; Neurodegeneration; Phosphoprotein; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 666 AA 
Protein Sequence
MEQEPQNGEP AEIKIIREAY KKAFLFVNKG LNTDELGQKE EAKNYYKQGI GHLLRGISIS 60
SKESEHTGPG WESARQMQQK MKETLQNVRT RLEILEKGLA TSLQNDLQEV PKLYPEFPPK 120
DMCEKLPEPQ SFSSAPQHAE VNGNTSTPSA GAVAAPASLS LPSQSCPAEA PPAYTPQAAE 180
GHYTVSYGTD SGEFSSVGEE FYRNHSQPPP LETLGLDADE LILIPNGVQI FFVNPAGEVS 240
APSYPGYLRI VRFLDNSLDT VLNRPPGFLQ VCDWLYPLVP DRSPVLKCTA GAYMFPDTML 300
QAAGCFVGVV LSSELPEDDR ELFEDLLRQM SDLRLQANWN RAEEENEFQI PGRTRPSSDQ 360
LKEASGTDVK QLDQGNKDVR HKGKRGKRAK DTSSEEVNLS HIVPCEPVPE EKPKELPEWS 420
EKVAHNILSG ASWVSWGLVK GAEITGKAIQ KGASKLRERI QPEEKPVEVS PAVTKGLYIA 480
KQATGGAAKV SQFLVDGVCT VANCVGKELA PHVKKHGSKL VPESLKKDKD GKSPLDGAMV 540
VAASSVQGFS TVWQGLECAA KCIVNNVSAE TVQTVRYKYG YNAGEATHHA VDSAVNVGVT 600
AYNINNIGIK AMVKKTATQT GHTLLEDYQI VDNSQRENQE GAANVNVRGE KDEQTKEVKE 660
AKKKDK 666 
Gene Ontology
 GO:0005811; C:lipid particle; IEA:Compara.
 GO:0030496; C:midbody; IDA:UniProtKB.
 GO:0005741; C:mitochondrial outer membrane; IDA:MGI.
 GO:0045202; C:synapse; IEA:Compara.
 GO:0009838; P:abscission; IMP:UniProtKB.
 GO:0060612; P:adipose tissue development; IEA:Compara.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IMP:UniProtKB.
 GO:0000910; P:cytokinesis; IEA:Compara.
 GO:0034389; P:lipid particle organization; IEA:Compara.
 GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Compara.
 GO:0048698; P:negative regulation of collateral sprouting in absence of injury; IEA:Compara.
 GO:0050905; P:neuromuscular process; IEA:Compara.
 GO:0051881; P:regulation of mitochondrial membrane potential; IMP:MGI. 
Interpro
 IPR007330; MIT.
 IPR009686; Senescence/spartin. 
Pfam
 PF04212; MIT
 PF06911; Senescence 
SMART
 SM00745; MIT 
PROSITE
  
PRINTS