NMNA2_HUMAN - dbPTM
NMNA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NMNA2_HUMAN
UniProt AC Q9BZQ4
Protein Name Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 {ECO:0000305}
Gene Name NMNAT2 {ECO:0000312|HGNC:HGNC:16789}
Organism Homo sapiens (Human).
Sequence Length 307
Subcellular Localization Golgi apparatus membrane
Lipid-anchor . Cytoplasmic vesicle membrane
Lipid-anchor . Cytoplasm . Cell projection, axon . Delivered to axons with Golgi-derived cytoplasmic vesicles.
Protein Description Nicotinamide/nicotinate-nucleotide adenylyltransferase that acts as an axon maintenance factor (By similarity). Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. [PubMed: 16118205]
Protein Sequence MTETTKTHVILLACGSFNPITKGHIQMFERARDYLHKTGRFIVIGGIVSPVHDSYGKQGLVSSRHRLIMCQLAVQNSDWIRVDPWECYQDTWQTTCSVLEHHRDLMKRVTGCILSNVNTPSMTPVIGQPQNETPQPIYQNSNVATKPTAAKILGKVGESLSRICCVRPPVERFTFVDENANLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRIMNHSSILRKYKNNIMVVKDDINHPMSVVSSTKSRLALQHGDGHVVDYLSQPVIDYILKSQLYINASG
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
7Phosphorylation-MTETTKTHVILLAC
-CCCCCCCEEEEEEC
21.20-
21PhosphorylationCGSFNPITKGHIQMF
CCCCCCCCHHHHHHH
32.03-
55PhosphorylationVSPVHDSYGKQGLVS
ECCCCCCCCCCCCCC
34.1122817900
62PhosphorylationYGKQGLVSSRHRLIM
CCCCCCCCHHHEEEE
27.0524719451
63PhosphorylationGKQGLVSSRHRLIMC
CCCCCCCHHHEEEEE
25.3226434776
150UbiquitinationVATKPTAAKILGKVG
CCCCCCHHHHHHHHH
11.2533845483
155UbiquitinationTAAKILGKVGESLSR
CHHHHHHHHHHHHHH
43.5533845483
164S-palmitoylationGESLSRICCVRPPVE
HHHHHHEECCCCCCC
1.3820943658
165S-palmitoylationESLSRICCVRPPVER
HHHHHEECCCCCCCE
2.4320943658
237PhosphorylationVPRDAADTDRIMNHS
EECCHHCCHHHHCHH
23.5825367220
245PhosphorylationDRIMNHSSILRKYKN
HHHHCHHHHHHHHCC
20.3524719451
250PhosphorylationHSSILRKYKNNIMVV
HHHHHHHHCCCEEEE
16.71-
266PhosphorylationDDINHPMSVVSSTKS
CCCCCCHHHCCCCCC
24.6627134283
267UbiquitinationDINHPMSVVSSTKSR
CCCCCHHHCCCCCCE
3.8329967540
271PhosphorylationPMSVVSSTKSRLALQ
CHHHCCCCCCEEEHH
26.0727134283
272UbiquitinationMSVVSSTKSRLALQH
HHHCCCCCCEEEHHC
35.2129967540
273PhosphorylationSVVSSTKSRLALQHG
HHCCCCCCEEEHHCC
32.3927134283
287PhosphorylationGDGHVVDYLSQPVID
CCCCHHHCCCHHHHH
9.1725884760
295PhosphorylationLSQPVIDYILKSQLY
CCHHHHHHHHHHCCE
9.3125884760

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 NMNA2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NMNA2_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 NMNA2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049

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 NMNA2_HUMAN

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Related Literatures of Post-Translational Modification

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