| Tag | Content |
|---|
| CPLM ID | CPLM-020183 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Nef-associated protein 1 |
Protein Synonyms/Alias | Thioesterase NAP1 |
Gene Name | C9orf156 |
Gene Synonyms/Alias | NAP1; HSPC219 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 363 | DVGQASFKYFQSAEE | ubiquitination | [1] | | 372 | FQSAEEAKRAIEAVL | ubiquitination | [1] | | 421 | FAEVLRIKPASEPVH | ubiquitination | [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] |
Functional Description | Hydrolyzes acyl-CoA thioesters (in vitro). Has a preference for substrates with medium chain length (C10-C14). Inactive towards substrates with C18 or C20 aliphatic chains. Its physiological substrate is not known. |
Sequence Annotation | DOMAIN 30 168 TsaA-like. |
Keyword | Complete proteome; Host-virus interaction; Hydrolase; Polymorphism; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 441 AA |
Protein Sequence | MRGLEESGPR PTATPCGCVK PALETGNLLT EPVGYLESCF SAKNGTPRQP SICSYSRACL 60
RIRKRIFNNP EHSLMGLEQF SHVWILFVFH KNGHLSCKAK VQPPRLNGAK TGVFSTRSPH 120
RPNAIGLTLA KLEKVEGGAI YLSGIDMIHG TPVLDIKPYI AEYDSPQNVM EPLADFNLQN 180
NQHTPNTVSQ SDSKTDSCDQ RQLSGCDEPQ PHHSTKRKPK CPEDRTSEEN YLTHSDTARI 240
QQAFPMHREI AVDFGLESRR DQSSSVAEEQ IGPYCPEKSF SEKGTDKKLE RVEGAAVLQG 300
SRAETQPMAP HCPAGRADGA PRSVVPAWVT EAPVATLEVR FTPHAEMDLG QLSSQDVGQA 360
SFKYFQSAEE AKRAIEAVLS ADPRSVYRRK LCQDRLFYFT VDIAHVTCWF GDGFAEVLRI 420
KPASEPVHMT GPVGSLVSLG S 441 |
Gene Ontology | GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. |
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PROSITE | |
PRINTS | |