NUD12_HUMAN - dbPTM
NUD12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUD12_HUMAN
UniProt AC Q9BQG2
Protein Name Peroxisomal NADH pyrophosphatase NUDT12
Gene Name NUDT12
Organism Homo sapiens (Human).
Sequence Length 462
Subcellular Localization Peroxisome .
Protein Description Hydrolyzes NAD(P)H to NMNH and AMP (2',5'-ADP), and diadenosine diphosphate to AMP. Has also activity towards NAD(P)(+), ADP-ribose and diadenosine triphosphate. May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle..
Protein Sequence MSSVKRSLKQEIVTQFHCSAAEGDIAKLTGILSHSPSLLNETSENGWTALMYAARNGHPEIVQFLLEKGCDRSIVNKSRQTALDIAVFWGYKHIANLLATAKGGKKPWFLTNEVEECENYFSKTLLDRKSEKRNNSDWLLAKESHPATVFILFSDLNPLVTLGGNKESFQQPEVRLCQLNYTDIKDYLAQPEKITLIFLGVELEIKDKLLNYAGEVPREEEDGLVAWFALGIDPIAAEEFKQRHENCYFLHPPMPALLQLKEKEAGVVAQARSVLAWHSRYKFCPTCGNATKIEEGGYKRLCLKEDCPSLNGVHNTSYPRVDPVVIMQVIHPDGTKCLLGRQKRFPPGMFTCLAGFIEPGETIEDAVRREVEEESGVKVGHVQYVACQPWPMPSSLMIGCLALAVSTEIKVDKNEIEDARWFTREQVLDVLTKGKQQAFFVPPSRAIAHQLIKHWIRINPNL
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
84UbiquitinationKSRQTALDIAVFWGY
HHHHHHHHHHHHHHH
25.0832015554
91PhosphorylationDIAVFWGYKHIANLL
HHHHHHHHHHHHHHH
7.0326074081
100PhosphorylationHIANLLATAKGGKKP
HHHHHHHHHCCCCCC
28.9526074081
102UbiquitinationANLLATAKGGKKPWF
HHHHHHHCCCCCCEE
64.9332015554
102AcetylationANLLATAKGGKKPWF
HHHHHHHCCCCCCEE
64.9330590937
111PhosphorylationGKKPWFLTNEVEECE
CCCCEEECCCHHHHH
21.6226074081
136PhosphorylationKSEKRNNSDWLLAKE
HHHHHCCCCCHHHCC
33.4427251275
167UbiquitinationVTLGGNKESFQQPEV
EECCCCHHHHCCCCE
61.8729967540
181PhosphorylationVRLCQLNYTDIKDYL
EEEECCCCCCHHHHH
17.87-
185SuccinylationQLNYTDIKDYLAQPE
CCCCCCHHHHHCCCC
43.03-
185SuccinylationQLNYTDIKDYLAQPE
CCCCCCHHHHHCCCC
43.03-
185UbiquitinationQLNYTDIKDYLAQPE
CCCCCCHHHHHCCCC
43.0329967540
187PhosphorylationNYTDIKDYLAQPEKI
CCCCHHHHHCCCCCE
10.03-
261UbiquitinationMPALLQLKEKEAGVV
CHHHHHHHHHHHHHH
54.50-
292SuccinylationPTCGNATKIEEGGYK
CCCCCCEEEECCCEE
45.79-
292SuccinylationPTCGNATKIEEGGYK
CCCCCCEEEECCCEE
45.79-
415UbiquitinationEIKVDKNEIEDARWF
CEECCHHHHCHHCCC
54.2029967540
433UbiquitinationQVLDVLTKGKQQAFF
HHHHHHHCCCCCEEE
61.0129967540
453AcetylationAIAHQLIKHWIRINP
HHHHHHHHHHHHCCC
41.2923954790

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 NUD12_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NUD12_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 NUD12_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NCOA5_HUMANNCOA5physical
26186194
FKB15_HUMANFKBP15physical
26186194
LZTR1_HUMANLZTR1physical
26186194
VWA8_HUMANVWA8physical
26186194
BLMH_HUMANBLMHphysical
26186194
ZO2_HUMANTJP2physical
26186194
SIR2_HUMANSIRT2physical
26186194
LZTR1_HUMANLZTR1physical
28514442
NCOA5_HUMANNCOA5physical
28514442
VWA8_HUMANVWA8physical
28514442
FKB15_HUMANFKBP15physical
28514442
ZO2_HUMANTJP2physical
28514442
SIR2_HUMANSIRT2physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NUD12_HUMAN

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Related Literatures of Post-Translational Modification

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