CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018909
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Exostosin-2 
Protein Synonyms/Alias
 Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase; Multiple exostoses protein 2; Putative tumor suppressor protein EXT2 
Gene Name
 EXT2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
101YRCGFNPKNKIKVYIubiquitination[1]
113VYIYALKKYVDDFGVubiquitination[1]
168NQNTLRIKETAQAMAubiquitination[1, 2, 3, 4, 5]
245AEVDLPEKGPGPRQYubiquitination[1, 2, 3, 5, 6]
275DLEALQVKHGESVLVubiquitination[1, 2]
285ESVLVLDKCTNLSEGubiquitination[1]
369SVVVPEEKMSDVYSIubiquitination[1, 2, 3, 5]
478RVITEVSKVPSLSKLubiquitination[1, 2, 5]
484SKVPSLSKLLVVWNNubiquitination[2]
494VVWNNQNKNPPEDSLubiquitination[1, 2, 5]
510PKIRVPLKVVRTAENubiquitination[1]
518VVRTAENKLSNRFFPubiquitination[1, 2]
579LWDHEMNKWKYESEWubiquitination[1]
581DHEMNKWKYESEWTNubiquitination[1]
645VTGKAVIKVTPRKKFubiquitination[1]
653VTPRKKFKCPECTAIubiquitination[1]
679ERSECINKFASVFGTubiquitination[1, 3, 4]
690VFGTMPLKVVEHRADubiquitination[1, 7, 8]
708YKDDFPEKLKSFPNIubiquitination[1]
710DDFPEKLKSFPNIGSubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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] 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]
 [7] 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]
 [8] 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
 Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a tumor suppressor. 
Sequence Annotation
 CARBOHYD 288 288 N-linked (GlcNAc...) (Potential).
 CARBOHYD 637 637 N-linked (GlcNAc...) (Potential).  
Keyword
 Alternative splicing; Complete proteome; Disease mutation; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Golgi apparatus; Hereditary multiple exostoses; Membrane; Polymorphism; Reference proteome; Signal-anchor; Transferase; Transmembrane; Transmembrane helix; Tumor suppressor. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 718 AA 
Protein Sequence
MCASVKYNIR GPALIPRMKT KHRIYYITLF SIVLLGLIAT GMFQFWPHSI ESSNDWNVEK 60
RSIRDVPVVR LPADSPIPER GDLSCRMHTC FDVYRCGFNP KNKIKVYIYA LKKYVDDFGV 120
SVSNTISREY NELLMAISDS DYYTDDINRA CLFVPSIDVL NQNTLRIKET AQAMAQLSRW 180
DRGTNHLLFN MLPGGPPDYN TALDVPRDRA LLAGGGFSTW TYRQGYDVSI PVYSPLSAEV 240
DLPEKGPGPR QYFLLSSQVG LHPEYREDLE ALQVKHGESV LVLDKCTNLS EGVLSVRKRC 300
HKHQVFDYPQ VLQEATFCVV LRGARLGQAV LSDVLQAGCV PVVIADSYIL PFSEVLDWKR 360
ASVVVPEEKM SDVYSILQSI PQRQIEEMQR QARWFWEAYF QSIKAIALAT LQIINDRIYP 420
YAAISYEEWN DPPAVKWGSV SNPLFLPLIP PQSQGFTAIV LTYDRVESLF RVITEVSKVP 480
SLSKLLVVWN NQNKNPPEDS LWPKIRVPLK VVRTAENKLS NRFFPYDEIE TEAVLAIDDD 540
IIMLTSDELQ FGYEVWREFP DRLVGYPGRL HLWDHEMNKW KYESEWTNEV SMVLTGAAFY 600
HKYFNYLYTY KMPGDIKNWV DAHMNCEDIA MNFLVANVTG KAVIKVTPRK KFKCPECTAI 660
DGLSLDQTHM VERSECINKF ASVFGTMPLK VVEHRADPVL YKDDFPEKLK SFPNIGSL 718 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; TAS:ProtInc.
 GO:0000139; C:Golgi membrane; TAS:Reactome.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0031227; C:intrinsic to endoplasmic reticulum membrane; IEA:InterPro.
 GO:0050508; F:glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity; IEA:EC.
 GO:0042328; F:heparan sulfate N-acetylglucosaminyltransferase activity; NAS:BHF-UCL.
 GO:0050509; F:N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity; NAS:BHF-UCL.
 GO:0006024; P:glycosaminoglycan biosynthetic process; IDA:BHF-UCL.
 GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; IMP:BHF-UCL.
 GO:0001503; P:ossification; IMP:BHF-UCL.
 GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
 GO:0007165; P:signal transduction; TAS:ProtInc. 
Interpro
 IPR004263; Exostosin.
 IPR015338; HexNAc_Trfase_a. 
Pfam
 PF03016; Exostosin
 PF09258; Glyco_transf_64 
SMART
  
PROSITE
  
PRINTS