CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-041305
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Polypeptide N-acetylgalactosaminyltransferase 2 soluble form 
Protein Synonyms/Alias
 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2), isoform CRA_b 
Gene Name
 GALNT2 
Gene Synonyms/Alias
 hCG_15927 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
264GNPVAPIKTPMIAGGubiquitination[1]
325RVGHVFRKQHPYTFPubiquitination[1, 2]
355EVWMDEYKNFYYAAVubiquitination[1, 3]
471RAPGSLIKLQGCRENubiquitination[1, 3]
483RENDSRQKWEQIEGNubiquitination[1]
492EQIEGNSKLRHVGSNubiquitination[1]
508CLDSRTAKSGGLSVEubiquitination[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] 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]
 [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
Functional Description
  
Sequence Annotation
  
Keyword
 Calcium; Complete proteome; Disulfide bond; Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane; Reference proteome; Transferase; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 533 AA 
Protein Sequence
MADREDWNEI DPIKKKDLHH SNGEEKAQSM ETLPPGKVRW PDFNQEAYVG GTMVRSGQDP 60
YARNKFNQVE SDKLRMDRAI PDTRHDQCQR KQWRVDLPAT SVVITFHNEA RSALLRTVVS 120
VLKKSPPHLI KEIILVDDYS NDPEDGALLG KIEKVRVLRN DRREGLMRSR VRGADAAQAK 180
VLTFLDSHCE CNEHWLEPLL ERVAEDRTRV VSPIIDVINM DNFQYVGASA DLKGGFDWNL 240
VFKWDYMTPE QRRSRQGNPV APIKTPMIAG GLFVMDKFYF EELGKYDMMM DVWGGENLEI 300
SFRVWQCGGS LEIIPCSRVG HVFRKQHPYT FPGGSGTVFA RNTRRAAEVW MDEYKNFYYA 360
AVPSARNVPY GNIQSRLELR KKLSCKPFKW YLENVYPELR VPDHQDIAFG ALQQGTNCLD 420
TLGHFADGVV GVYECHNAGG NQEWALTKEK SVKHMDLCLT VVDRAPGSLI KLQGCRENDS 480
RQKWEQIEGN SKLRHVGSNL CLDSRTAKSG GLSVEVCGPA LSQQWKFTLN LQQ 533 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW.
 GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway. 
Interpro
 IPR001173; Glyco_trans_2.
 IPR000772; Ricin_B_lectin. 
Pfam
 PF00535; Glycos_transf_2
 PF00652; Ricin_B_lectin 
SMART
 SM00458; RICIN 
PROSITE
 PS50231; RICIN_B_LECTIN 
PRINTS