| Tag | Content |
|---|
| CPLM ID | CPLM-014972 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Chondroitin sulfate synthase 2 |
Protein Synonyms/Alias | Chondroitin glucuronyltransferase 2; Chondroitin-polymerizing factor; ChPF; Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase II; N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase II; N-acetylgalactosaminyltransferase 2 |
Gene Name | Chpf |
Gene Synonyms/Alias | Css2; D1Bwg1363e |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 445 | QPALQLQKQQLVNGY | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | Has both beta-1,3-glucuronic acid and beta-1,4-N- acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer (By similarity). |
Sequence Annotation | METAL 616 616 Divalent metal cation (Potential).
CARBOHYD 138 138 N-linked (GlcNAc...) (Potential).
CARBOHYD 361 361 N-linked (GlcNAc...) (Potential). |
Keyword | Complete proteome; Glycoprotein; Golgi apparatus; Membrane; Metal-binding; Reference proteome; Signal-anchor; Transferase; Transmembrane; Transmembrane helix. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 774 AA |
Protein Sequence | MRASLLLSVL RPAGPVAVGI SLGFTLSLLS VTWVEEPCGP GPPQPGDSEL PPRGNTNAAR 60
RPNSVQPGSE RERPGAGAGT GESWEPRVLP YHPAQPGQAT KKAVRTRYIS TELGIRQKLL 120
VAVLTSQATL PTLGVAVNRT LGHRLEHVVF LTGARGRRTP SGMAVVALGE ERPIGHLHLA 180
LRHLLEQHGD DFDWFFLVPD ATYTEAHGLD RLAGHLSLAS ATHLYLGRPQ DFIGGDTTPG 240
RYCHGGFGVL LSRTLLQQLR PHLESCRNDI VSARPDEWLG RCILDATGVG CTGDHEGMHY 300
NYLELSPGEP VQEGDPRFRS ALTAHPVRDP VHMYQLHKAF ARAELDRTYQ EIQELQWEIQ 360
NTSRLAADGE RASAWPVGIP APSRPASRFE VLRWDYFTEQ YAFSCADGSP RCPLRGADQA 420
DVADVLGTAL EELNRRYQPA LQLQKQQLVN GYRRFDPARG MEYTLDLQLE ALTPQGGRWP 480
LTRRVQLLRP LSRVEILPVP YVTEASRLTV LLPLAAAERD LASGFLEAFA TAALEPGDAA 540
ALTLLLLYEP RQAQRAAHSD VFAPVKAHVA ELERRFPGAR VPWLSVQTAA PSPLRLMDLL 600
SKKHPLDTLF LLAGPDTVLT PDFLNRCRMH AISGWQAFFP MHFQAFHPAV APPQGPGPPE 660
LGRDTGHFDR QAASEACFYN SDYVAARGRL VAASEQEEEL LESLDVYELF LRFSNLHVLR 720
AVEPALLQRY RAQPCSARLS EDLYHRCRQS VLEGLGSRTQ LAMLLFEQEQ GNST 774 |
Gene Ontology | GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell. GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0047238; F:glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; IEA:EC. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0050510; F:N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity; IEA:EC. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |