| Tag | Content |
|---|
| CPLM ID | CPLM-016117 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Nicotinamide phosphoribosyltransferase |
Protein Synonyms/Alias | NAmPRTase; Nampt; Pre-B-cell colony-enhancing factor 1 homolog; PBEF; Visfatin |
Gene Name | Nampt |
Gene Synonyms/Alias | Pbef1 |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 469 | FKNGKVTKSYSFDEV | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Catalyzes the condensation of nicotinamide with 5- phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway (By similarity). |
Sequence Annotation | REGION 311 313 Nicotinamide ribonucleotide binding.
REGION 353 354 Nicotinamide ribonucleotide binding.
BINDING 196 196 Diphosphate (By similarity).
BINDING 219 219 Nicotinamide ribonucleotide (By
BINDING 247 247 Diphosphate (By similarity).
BINDING 311 311 Diphosphate (By similarity).
BINDING 384 384 Nicotinamide ribonucleotide; via amide
BINDING 392 392 Nicotinamide ribonucleotide. |
Keyword | 3D-structure; Complete proteome; Cytoplasm; Glycosyltransferase; Nucleus; Pyridine nucleotide biosynthesis; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 491 AA |
Protein Sequence | MNAAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECR EKKTENSKVR KVKYEETVFY 60
GLQYILNKYL KGKVVTKEKI QEAKEVYREH FQDDVFNERG WNYILEKYDG HLPIEVKAVP 120
EGSVIPRGNV LFTVENTDPE CYWLTNWIET ILVQSWYPIT VATNSREQKK ILAKYLLETS 180
GNLDGLEYKL HDFGYRGVSS QETAGIGASA HLVNFKGTDT VAGIALIKKY YGTKDPVPGY 240
SVPAAEHSTI TAWGKDHEKD AFEHIVTQFS SVPVSVVSDS YDIYNACEKI WGEDLRHLIV 300
SRSTEAPLII RPDSGNPLDT VLKVLDILGK KFPVSENSKG YKLLPPYLRV IQGDGVDINT 360
LQEIVEGMKQ KKWSIENVSF GSGGALLQKL TRDLLNCSFK CSYVVTNGLG VNVFKDPVAD 420
PNKRSKKGRL SLHRTPAGTF VTLEEGKGDL EEYGHDLLHT VFKNGKVTKS YSFDEVRKNA 480
QLNMEQDVAP H 491 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:RGD. GO:0005634; C:nucleus; IDA:RGD. GO:0005125; F:cytokine activity; IDA:RGD. GO:0008144; F:drug binding; IDA:RGD. GO:0047280; F:nicotinamide phosphoribosyltransferase activity; IDA:RGD. GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:InterPro. GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro. GO:0042803; F:protein homodimerization activity; IDA:RGD. GO:0007565; P:female pregnancy; IEP:RGD. GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway. GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD. GO:0014070; P:response to organic cyclic compound; IEP:RGD. |
Interpro | |
Pfam | |
SMART | |
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PRINTS | |