| Tag | Content |
|---|
| CPLM ID | CPLM-014978 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3 |
Protein Synonyms/Alias | Polypeptide GalNAc transferase-like protein 3; GalNAc-T-like protein 3; pp-GaNTase-like protein 3; Protein-UDP acetylgalactosaminyltransferase-like protein 3; UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 3; Williams-Beuren syndrome chromosomal region 17 protein |
Gene Name | WBSCR17 |
Gene Synonyms/Alias | GALNTL3 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 532 | RCLVDNSKSRLPQLL | acetylation | [1] |
|
Reference | [1] Regulation of cellular metabolism by protein lysine acetylation. Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL. Science. 2010 Feb 19;327(5968):1000-4. [ PMID: 20167786] |
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 465 594 Ricin B-type lectin.
REGION 151 262 Catalytic subdomain A.
REGION 319 381 Catalytic subdomain B.
CARBOHYD 50 50 N-linked (GlcNAc...) (Potential).
CARBOHYD 461 461 N-linked (GlcNAc...) (Potential).
CARBOHYD 486 486 N-linked (GlcNAc...) (Potential).
DISULFID 478 494 By similarity.
DISULFID 526 541 By similarity.
DISULFID 568 586 By similarity. |
Keyword | Calcium; Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane; Transmembrane helix; Williams-Beuren syndrome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 598 AA |
Protein Sequence | MASLRRVKVL LVLNLIAVAG FVLFLAKCRP IAVRSGDAFH EIRPRAEVAN LSAHSASPIQ 60
DAVLKRLSLL EDIVYRQLNG LSKSLGLIEG YGGRGKGGLP ATLSPAEEEK AKGPHEKYGY 120
NSYLSEKISL DRSIPDYRPT KCKELKYSKD LPQISIIFIF VNEALSVILR SVHSAVNHTP 180
THLLKEIILV DDNSDEEELK VPLEEYVHKR YPGLVKVVRN QKREGLIRAR IEGWKVATGQ 240
VTGFFDAHVE FTAGWAEPVL SRIQENRKRV ILPSIDNIKQ DNFEVQRYEN SAHGYSWELW 300
CMYISPPKDW WDAGDPSLPI RTPAMIGCSF VVNRKFFGEI GLLDPGMDVY GGENIELGIK 360
VWLCGGSMEV LPCSRVAHIE RKKKPYNSNI GFYTKRNALR VAEVWMDDYK SHVYIAWNLP 420
LENPGIDIGD VSERRALRKS LKCKNFQWYL DHVYPEMRRY NNTVAYGELR NNKAKDVCLD 480
QGPLENHTAI LYPCHGWGPQ LARYTKEGFL HLGALGTTTL LPDTRCLVDN SKSRLPQLLD 540
CDKVKSSLYK RWNFIQNGAI MNKGTGRCLE VENRGLAGID LILRSCTGQR WTIKNSIK 598 |
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 | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |