CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015219
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Polypeptide N-acetylgalactosaminyltransferase 18 
Protein Synonyms/Alias
 Polypeptide GalNAc transferase-like protein 4; GalNAc-T-like protein 4; pp-GaNTase-like protein 4; Polypeptide N-acetylgalactosaminyltransferase-like protein 4; Protein-UDP acetylgalactosaminyltransferase-like protein 4; UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 4 
Gene Name
 GALNT18 
Gene Synonyms/Alias
 GALNTL4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
284SPSFDNIKYDNFEIEubiquitination[1]
Reference
 [1] 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 catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor (By similarity). 
Sequence Annotation
 DOMAIN 469 599 Ricin B-type lectin.
 REGION 153 267 Catalytic subdomain A.
 REGION 324 385 Catalytic subdomain B.
 CARBOHYD 146 146 N-linked (GlcNAc...) (Potential).
 CARBOHYD 195 195 N-linked (GlcNAc...) (Potential).
 CARBOHYD 320 320 N-linked (GlcNAc...) (Potential).
 DISULFID 482 498 By similarity.
 DISULFID 530 543 By similarity.
 DISULFID 571 591 By similarity.  
Keyword
 Alternative splicing; Calcium; Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 607 AA 
Protein Sequence
MVCTRKTKTL VSTCVILSGM TNIICLLYVG WVTNYIASVY VRGQEPAPDK KLEEDKGDTL 60
KIIERLDHLE NVIKQHIQEA PAKPEEAEAE PFTDSSLFAH WGQELSPEGR RVALKQFQYY 120
GYNAYLSDRL PLDRPLPDLR PSGCRNLSFP DSLPEVSIVF IFVNEALSVL LRSIHSAMER 180
TPPHLLKEII LVDDNSSNEE LKEKLTEYVD KVNSQKPGFI KVVRHSKQEG LIRSRVSGWR 240
AATAPVVALF DAHVEFNVGW AEPVLTRIKE NRKRIISPSF DNIKYDNFEI EEYPLAAQGF 300
DWELWCRYLN PPKAWWKLEN STAPIRSPAL IGCFIVDRQY FQEIGLLDEG MEVYGGENVE 360
LGIRVWQCGG SVEVLPCSRI AHIERAHKPY TEDLTAHVRR NALRVAEVWM DEFKSHVYMA 420
WNIPQEDSGI DIGDITARKA LRKQLQCKTF RWYLVSVYPE MRMYSDIIAY GVLQNSLKTD 480
LCLDQGPDTE NVPIMYICHG MTPQNVYYTS SQQIHVGILS PTVDDDDNRC LVDVNSRPRL 540
IECSYAKAKR MKLHWQFSQG GPIQNRKSKR CLELQENSDL EFGFQLVLQK CSGQHWSITN 600
VLRSLAS 607 
Gene Ontology
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IEA:EC.
 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