dbPTM

NAMPT_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NAMPT_HUMAN
UniProt AC	P43490
Protein Name	Nicotinamide phosphoribosyltransferase
Gene Name	NAMPT
Organism	Homo sapiens (Human).
Sequence Length	491
Subcellular Localization	Nucleus . Cytoplasm . Secreted . Under non-inflammatory conditions, visfatin predominantly exhibits a granular pattern within the nucleus. Secreted by endothelial cells upon IL-1beta stimulation. Abundantly secreted in milk, reaching 100-fold higher
Protein 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. The secreted form behaves both as a cytokine with immunomodulating properties and an adipokine with anti-diabetic properties, it has no enzymatic activity, partly because of lack of activation by ATP, which has a low level in extracellular space and plasma. Plays a role in the modulation of circadian clock function. NAMPT-dependent oscillatory production of NAD regulates oscillation of clock target gene expression by releasing the core clock component: CLOCK-ARNTL/BMAL1 heterodimer from NAD-dependent SIRT1-mediated suppression (By similarity)..
Protein Sequence	MNPAAEAEFNILLATDSYKVTHYKQYPPNTSKVYSYFECREKKTENSKLRKVKYEETVFYGLQYILNKYLKGKVVTKEKIQEAKDVYKEHFQDDVFNEKGWNYILEKYDGHLPIEIKAVPEGFVIPRGNVLFTVENTDPECYWLTNWIETILVQSWYPITVATNSREQKKILAKYLLETSGNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDTVAGLALIKKYYGTKDPVPGYSVPAAEHSTITAWGKDHEKDAFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRHLIVSRSTQAPLIIRPDSGNPLDTVLKVLEILGKKFPVTENSKGYKLLPPYLRVIQGDGVDINTLQEIVEGMKQKMWSIENIAFGSGGGLLQKLTRDLLNCSFKCSYVVTNGLGINVFKDPVADPNKRSKKGRLSLHRTPAGNFVTLEEGKGDLEEYGQDLLHTVFKNGKVTKSYSFDEIRKNAQLNIELEAAHH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MNPAAEAE -------CCHHHHHH	14.13	22223895
15	Phosphorylation	EFNILLATDSYKVTH HHEEEEEECCEEEEE	26.00	-
17	Phosphorylation	NILLATDSYKVTHYK EEEEEECCEEEEECE	23.62	-
18	Phosphorylation	ILLATDSYKVTHYKQ EEEEECCEEEEECEE	16.58	-
23	Phosphorylation	DSYKVTHYKQYPPNT CCEEEEECEECCCCC	7.16	28857561
24	Ubiquitination	SYKVTHYKQYPPNTS CEEEEECEECCCCCC	35.43	-
26	Phosphorylation	KVTHYKQYPPNTSKV EEEECEECCCCCCHH	19.26	-
30	Phosphorylation	YKQYPPNTSKVYSYF CEECCCCCCHHEEEE	35.38	28857561
31	Phosphorylation	KQYPPNTSKVYSYFE EECCCCCCHHEEEEE	27.11	28857561
34	Phosphorylation	PPNTSKVYSYFECRE CCCCCHHEEEEECCC	11.03	25159151
35	Phosphorylation	PNTSKVYSYFECREK CCCCHHEEEEECCCC	26.74	28857561
36	Phosphorylation	NTSKVYSYFECREKK CCCHHEEEEECCCCC	5.92	-
48	Acetylation	EKKTENSKLRKVKYE CCCCCCCCCCCCCHH	64.98	25953088
48	Ubiquitination	EKKTENSKLRKVKYE CCCCCCCCCCCCCHH	64.98	-
54	Phosphorylation	SKLRKVKYEETVFYG CCCCCCCHHHHHHHH	23.22	22617229
57	Phosphorylation	RKVKYEETVFYGLQY CCCCHHHHHHHHHHH	12.18	28857561
60	Phosphorylation	KYEETVFYGLQYILN CHHHHHHHHHHHHHH	16.76	25884760
64	Phosphorylation	TVFYGLQYILNKYLK HHHHHHHHHHHHHHC	16.65	22617229
69	Phosphorylation	LQYILNKYLKGKVVT HHHHHHHHHCCCCCC	16.75	25884760
84	2-Hydroxyisobutyrylation	KEKIQEAKDVYKEHF HHHHHHHHHHHHHHH	47.15	-
84	Acetylation	KEKIQEAKDVYKEHF HHHHHHHHHHHHHHH	47.15	27452117
84	Ubiquitination	KEKIQEAKDVYKEHF HHHHHHHHHHHHHHH	47.15	-
87	Phosphorylation	IQEAKDVYKEHFQDD HHHHHHHHHHHHCHH	22.31	18083107
88	2-Hydroxyisobutyrylation	QEAKDVYKEHFQDDV HHHHHHHHHHHCHHH	44.56	-
88	Acetylation	QEAKDVYKEHFQDDV HHHHHHHHHHHCHHH	44.56	27452117
88	Ubiquitination	QEAKDVYKEHFQDDV HHHHHHHHHHHCHHH	44.56	21906983
88 (in isoform 1)	Ubiquitination	-	44.56	21906983
99	Ubiquitination	QDDVFNEKGWNYILE CHHHCCCCCHHHHHH	71.04	21890473
99 (in isoform 1)	Ubiquitination	-	71.04	21906983
107	Ubiquitination	GWNYILEKYDGHLPI CHHHHHHEECCCCCE	45.24	21906983
107 (in isoform 1)	Ubiquitination	-	45.24	21906983
117	2-Hydroxyisobutyrylation	GHLPIEIKAVPEGFV CCCCEEEEEECCCEE	30.46	-
117	Ubiquitination	GHLPIEIKAVPEGFV CCCCEEEEEECCCEE	30.46	21906983
117 (in isoform 1)	Ubiquitination	-	30.46	21906983
174	Acetylation	EQKKILAKYLLETSG HHHHHHHHHHHHHHC	32.74	25038526
174	Ubiquitination	EQKKILAKYLLETSG HHHHHHHHHHHHHHC	32.74	21906983
174 (in isoform 1)	Ubiquitination	-	32.74	21906983
175	Phosphorylation	QKKILAKYLLETSGN HHHHHHHHHHHHHCC	15.77	28152594
179	Phosphorylation	LAKYLLETSGNLDGL HHHHHHHHHCCCCCC	41.73	28857561
180	Phosphorylation	AKYLLETSGNLDGLE HHHHHHHHCCCCCCE	19.13	28857561
188	Phosphorylation	GNLDGLEYKLHDFGY CCCCCCEEEEECCCC	24.72	22817900
189	Ubiquitination	NLDGLEYKLHDFGYR CCCCCEEEEECCCCC	29.94	1890473
189 (in isoform 1)	Ubiquitination	-	29.94	21906983
195	Phosphorylation	YKLHDFGYRGVSSQE EEEECCCCCCCCCCC	12.27	29496907
196	Methylation	KLHDFGYRGVSSQET EEECCCCCCCCCCCC	39.14	115486563
199	Phosphorylation	DFGYRGVSSQETAGI CCCCCCCCCCCCCCC	29.18	28857561
200	Phosphorylation	FGYRGVSSQETAGIG CCCCCCCCCCCCCCC	29.63	28857561
209	Phosphorylation	ETAGIGASAHLVNFK CCCCCCCEEEEEECC	15.82	28857561
218	Phosphorylation	HLVNFKGTDTVAGLA EEEECCCCCCHHHHH	29.14	28857561
220	Phosphorylation	VNFKGTDTVAGLALI EECCCCCCHHHHHHH	16.46	27499020
228	Ubiquitination	VAGLALIKKYYGTKD HHHHHHHHHHHCCCC	35.26	21890473
228 (in isoform 1)	Ubiquitination	-	35.26	21906983
229	Ubiquitination	AGLALIKKYYGTKDP HHHHHHHHHHCCCCC	36.39	-
234	Ubiquitination	IKKYYGTKDPVPGYS HHHHHCCCCCCCCCC	56.52	-
241	Phosphorylation	KDPVPGYSVPAAEHS CCCCCCCCCCCCCCC	27.78	27251275
248	Phosphorylation	SVPAAEHSTITAWGK CCCCCCCCCEEECCC	17.01	28857561
249	Phosphorylation	VPAAEHSTITAWGKD CCCCCCCCEEECCCC	25.01	28857561
251	Phosphorylation	AAEHSTITAWGKDHE CCCCCCEEECCCCCH	19.22	28857561
255	Ubiquitination	STITAWGKDHEKDAF CCEEECCCCCHHHHH	45.25	-
259	Ubiquitination	AWGKDHEKDAFEHIV ECCCCCHHHHHHHHH	51.44	-
301	Phosphorylation	DLRHLIVSRSTQAPL CHHHHHHCCCCCCCE	17.33	24719451
303	Phosphorylation	RHLIVSRSTQAPLII HHHHHCCCCCCCEEE	19.84	22210691
304	Phosphorylation	HLIVSRSTQAPLIIR HHHHCCCCCCCEEEC	27.86	22210691
314	Phosphorylation	PLIIRPDSGNPLDTV CEEECCCCCCCHHHH	43.06	22210691
320	Phosphorylation	DSGNPLDTVLKVLEI CCCCCHHHHHHHHHH	35.11	28102081
330	2-Hydroxyisobutyrylation	KVLEILGKKFPVTEN HHHHHHCCCCCCCCC	48.04	-
330	Acetylation	KVLEILGKKFPVTEN HHHHHHCCCCCCCCC	48.04	25953088
330	Malonylation	KVLEILGKKFPVTEN HHHHHHCCCCCCCCC	48.04	26320211
330	Ubiquitination	KVLEILGKKFPVTEN HHHHHHCCCCCCCCC	48.04	-
331	Ubiquitination	VLEILGKKFPVTENS HHHHHCCCCCCCCCC	53.77	-
335	Phosphorylation	LGKKFPVTENSKGYK HCCCCCCCCCCCCCC	29.68	21406692
338	Phosphorylation	KFPVTENSKGYKLLP CCCCCCCCCCCCCCC	22.64	21406692
339	Ubiquitination	FPVTENSKGYKLLPP CCCCCCCCCCCCCCC	77.25	-
341	Phosphorylation	VTENSKGYKLLPPYL CCCCCCCCCCCCCCE	11.38	29496907
342	Ubiquitination	TENSKGYKLLPPYLR CCCCCCCCCCCCCEE	52.82	21890473
369	Acetylation	QEIVEGMKQKMWSIE HHHHHHHHHHCCEEE	58.59	19809495
369	Ubiquitination	QEIVEGMKQKMWSIE HHHHHHHHHHCCEEE	58.59	21906983
369 (in isoform 1)	Ubiquitination	-	58.59	21906983
371	Ubiquitination	IVEGMKQKMWSIENI HHHHHHHHCCEEEEE	36.50	21890473
372	Sulfoxidation	VEGMKQKMWSIENIA HHHHHHHCCEEEEEE	2.92	30846556
374	Phosphorylation	GMKQKMWSIENIAFG HHHHHCCEEEEEECC	19.27	25627689
382	Phosphorylation	IENIAFGSGGGLLQK EEEEECCCCCHHHHH	28.01	-
389	Ubiquitination	SGGGLLQKLTRDLLN CCCHHHHHHHHHHHC	52.36	21906983
389 (in isoform 1)	Ubiquitination	-	52.36	21906983
398	Phosphorylation	TRDLLNCSFKCSYVV HHHHHCCCCCCEEEE	27.02	25159151
403	Phosphorylation	NCSFKCSYVVTNGLG CCCCCCEEEEECCCC	14.38	24927040
415	Acetylation	GLGINVFKDPVADPN CCCCEEECCCCCCCC	57.76	7709625
423	Acetylation	DPVADPNKRSKKGRL CCCCCCCCCCCCCCC	64.53	26051181
423	Ubiquitination	DPVADPNKRSKKGRL CCCCCCCCCCCCCCC	64.53	-
431	Phosphorylation	RSKKGRLSLHRTPAG CCCCCCCCEEECCCC	22.29	20873877
435	Phosphorylation	GRLSLHRTPAGNFVT CCCCEEECCCCCEEE	13.52	21815630
447	Ubiquitination	FVTLEEGKGDLEEYG EEEECCCCCCHHHHH	53.16	2190698
447 (in isoform 1)	Ubiquitination	-	53.16	21906983
453	Phosphorylation	GKGDLEEYGQDLLHT CCCCHHHHHHHHHHH	15.65	27642862
468	Phosphorylation	VFKNGKVTKSYSFDE HHCCCEEEEEEEHHH	20.12	26074081
469	Acetylation	FKNGKVTKSYSFDEI HCCCEEEEEEEHHHH	50.84	25953088
469	Malonylation	FKNGKVTKSYSFDEI HCCCEEEEEEEHHHH	50.84	26320211
469	Ubiquitination	FKNGKVTKSYSFDEI HCCCEEEEEEEHHHH	50.84	-
470	Phosphorylation	KNGKVTKSYSFDEIR CCCEEEEEEEHHHHH	19.35	28152594
471	Phosphorylation	NGKVTKSYSFDEIRK CCEEEEEEEHHHHHH	18.21	28152594
472	Phosphorylation	GKVTKSYSFDEIRKN CEEEEEEEHHHHHHH	33.06	23401153

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 NAMPT_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NAMPT_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 NAMPT_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NU1M_HUMAN	ND1	physical	18486613
FRIL_HUMAN	FTL	physical	18486613
IFM3_HUMAN	IFITM3	physical	18486613
AA2AR_HUMAN	ADORA2A	physical	18486613
GGT1_HUMAN	GGT1	physical	18486613
ASSY_HUMAN	ASS1	physical	22863883
MVD1_HUMAN	MVD	physical	22863883
NDRG1_HUMAN	NDRG1	physical	22863883
PEPD_HUMAN	PEPD	physical	22863883
HSPB1_HUMAN	HSPB1	physical	26344197
PNCB_HUMAN	NAPRT	physical	26344197

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 NAMPT_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-34, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-188, AND MASSSPECTROMETRY.	15592455 [Abstract]