PNCB_HUMAN - dbPTM
PNCB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PNCB_HUMAN
UniProt AC Q6XQN6
Protein Name Nicotinate phosphoribosyltransferase
Gene Name NAPRT
Organism Homo sapiens (Human).
Sequence Length 538
Subcellular Localization Cytoplasm, cytosol .
Protein Description Catalyzes the conversion of nicotinic acid (NA) to NA mononucleotide (NaMN). Essential for NA to increase cellular NAD levels and prevent oxidative stress of the cells.; Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP..
Protein Sequence MAAEQDPEARAAARPLLTDLYQATMALGYWRAGRARDAAEFELFFRRCPFGGAFALAAGLRDCVRFLRAFRLRDADVQFLASVLPPDTDPAFFEHLRALDCSEVTVRALPEGSLAFPGVPLLQVSGPLLVVQLLETPLLCLVSYASLVATNAARLRLIAGPEKRLLEMGLRRAQGPDGGLTASTYSYLGGFDSSSNVLAGQLRGVPVAGTLAHSFVTSFSGSEVPPDPMLAPAAGEGPGVDLAAKAQVWLEQVCAHLGLGVQEPHPGERAAFVAYALAFPRAFQGLLDTYSVWRSGLPNFLAVALALGELGYRAVGVRLDSGDLLQQAQEIRKVFRAAAAQFQVPWLESVLIVVSNNIDEEALARLAQEGSEVNVIGIGTSVVTCPQQPSLGGVYKLVAVGGQPRMKLTEDPEKQTLPGSKAAFRLLGSDGSPLMDMLQLAEEPVPQAGQELRVWPPGAQEPCTVRPAQVEPLLRLCLQQGQLCEPLPSLAESRALAQLSLSRLSPEHRRLRSPAQYQVVLSERLQALVNSLCAGQSP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
18PhosphorylationAAARPLLTDLYQATM
HHHHHHHHHHHHHHH		31.4722673903
21PhosphorylationRPLLTDLYQATMALG
HHHHHHHHHHHHHHC		10.0227259358
24PhosphorylationLTDLYQATMALGYWR
HHHHHHHHHHHCCHH		6.3522673903
163UbiquitinationRLIAGPEKRLLEMGL
HHHHCHHHHHHHHHH		52.0221906983
163 (in isoform 3)Ubiquitination-52.0221906983
163 (in isoform 2)Ubiquitination-52.0221906983
163 (in isoform 1)Ubiquitination-52.0221906983
1632-HydroxyisobutyrylationRLIAGPEKRLLEMGL
HHHHCHHHHHHHHHH		52.02-
179UbiquitinationRAQGPDGGLTASTYS
HHCCCCCCCCHHCEE		27.5127667366
186UbiquitinationGLTASTYSYLGGFDS
CCCHHCEEECCCCCC		17.6124816145
193UbiquitinationSYLGGFDSSSNVLAG
EECCCCCCCCCCCCH		33.1421963094
213PhosphorylationPVAGTLAHSFVTSFS
CCCHHHCCCHHHCCC		25.53-
380UbiquitinationVNVIGIGTSVVTCPQ
EEEEEECCCEEECCC		19.2127667366
387UbiquitinationTSVVTCPQQPSLGGV
CCEEECCCCCCCCCE		70.7124816145
394UbiquitinationQQPSLGGVYKLVAVG
CCCCCCCEEEEEEEC		3.4621963094
396UbiquitinationPSLGGVYKLVAVGGQ
CCCCCEEEEEEECCC		33.79-
405MethylationVAVGGQPRMKLTEDP
EEECCCCCCCCCCCC		27.29115484459
407 (in isoform 1)Ubiquitination-54.2421906983
407UbiquitinationVGGQPRMKLTEDPEK
ECCCCCCCCCCCCCC		54.2421906983
407 (in isoform 3)Ubiquitination-54.2421906983
407 (in isoform 2)Ubiquitination-54.2421906983
414UbiquitinationKLTEDPEKQTLPGSK
CCCCCCCCCCCCCCH		54.7121906983
414 (in isoform 1)Ubiquitination-54.7121906983
414 (in isoform 2)Ubiquitination-54.7121906983
414 (in isoform 3)Ubiquitination-54.7121906983
416PhosphorylationTEDPEKQTLPGSKAA
CCCCCCCCCCCCHHH		46.09-
420PhosphorylationEKQTLPGSKAAFRLL
CCCCCCCCHHHHHHH		19.7220068231
421 (in isoform 2)Ubiquitination-50.0421906983
421 (in isoform 1)Ubiquitination-50.0421906983
421 (in isoform 3)Ubiquitination-50.0421906983
421UbiquitinationKQTLPGSKAAFRLLG
CCCCCCCHHHHHHHC		50.0427667366
429PhosphorylationAAFRLLGSDGSPLMD
HHHHHHCCCCCCHHH		38.4724719451
432PhosphorylationRLLGSDGSPLMDMLQ
HHHCCCCCCHHHHHH		21.6128348404
480UbiquitinationLLRLCLQQGQLCEPL
HHHHHHHCCCCCCCC		28.7527667366
487UbiquitinationQGQLCEPLPSLAESR
CCCCCCCCCCHHHHH		1.7824816145
494UbiquitinationLPSLAESRALAQLSL
CCCHHHHHHHHHHHH		25.7321963094
500PhosphorylationSRALAQLSLSRLSPE
HHHHHHHHHHHCCHH		16.5420068231
502PhosphorylationALAQLSLSRLSPEHR
HHHHHHHHHCCHHHH		28.0020068231
505PhosphorylationQLSLSRLSPEHRRLR
HHHHHHCCHHHHHCC		27.4223186163
513PhosphorylationPEHRRLRSPAQYQVV
HHHHHCCCHHHHHHH		29.2228450419
517PhosphorylationRLRSPAQYQVVLSER
HCCCHHHHHHHHHHH		12.8428857561
522PhosphorylationAQYQVVLSERLQALV
HHHHHHHHHHHHHHH		14.7324719451
531PhosphorylationRLQALVNSLCAGQSP
HHHHHHHHHHCCCCC		19.8323403867
537PhosphorylationNSLCAGQSP------
HHHHCCCCC------		31.4923927012
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PNCB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PNCB_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PNCB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP7C_HUMANHSPA8physical
22863883
NOL3_HUMANNOL3physical
22863883
PA1B2_HUMANPAFAH1B2physical
22863883
RASL1_HUMANRASAL1physical
22863883
K1C40_HUMANKRT40physical
25416956
CCD57_HUMANCCDC57physical
25416956
ARMT1_HUMANC6orf211physical
26344197
EF1A1_HUMANEEF1A1physical
26344197
NIF3L_HUMANNIF3L1physical
26344197
SEC13_HUMANSEC13physical
26344197
SC31A_HUMANSEC31Aphysical
26344197
TCEA1_HUMANTCEA1physical
26344197
TNR6C_HUMANTNRC6Cphysical
26344197
TR112_HUMANTRMT112physical
26344197
EKI1_HUMANETNK1physical
28514442
LCAP_HUMANLNPEPphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PNCB_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND MASSSPECTROMETRY.

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