NAKD2_HUMAN - dbPTM
NAKD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NAKD2_HUMAN
UniProt AC Q4G0N4
Protein Name NAD kinase 2, mitochondrial
Gene Name NADK2
Organism Homo sapiens (Human).
Sequence Length 442
Subcellular Localization Mitochondrion .
Protein Description Mitochondrial NAD(+) kinase that phosphorylates NAD(+) to yield NADP(+). Can use both ATP or inorganic polyphosphate as the phosphoryl donor. Also has weak NADH kinase activity in vitro; however NADH kinase activity is much weaker than the NAD(+) kinase activity and may not be relevant in vivo..
Protein Sequence MTCYRGFLLGSCCRVAGGRAAALRGPGAGGPAARPRLGGDGGGRRHLGQGQPRELAGCGSRADGGFRPSRVVVVAKTTRYEFEQQRYRYAELSEEDLKQLLALKGSSYSGLLERHHIHTKNVEHIIDSLRNEGIEVRLVKRREYDEETVRWADAVIAAGGDGTMLLAASKVLDRLKPVIGVNTDPERSEGHLCLPVRYTHSFPEALQKFYRGEFRWLWRQRIRLYLEGTGINPVPVDLHEQQLSLNQHNRALNIERAHDERSEASGPQLLPVRALNEVFIGESLSSRASYYEISVDDGPWEKQKSSGLNLCTGTGSKAWSFNINRVATQAVEDVLNIAKRQGNLSLPLNRELVEKVTNEYNESLLYSPEEPKILFSIREPIANRVFSSSRQRCFSSKVCVRSRCWDACMVVDGGTSFEFNDGAIASMMINKEDELRTVLLEQ
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
762-HydroxyisobutyrylationSRVVVVAKTTRYEFE
CEEEEEEECCCHHHH
-
76AcetylationSRVVVVAKTTRYEFE
CEEEEEEECCCHHHH
-
76MalonylationSRVVVVAKTTRYEFE
CEEEEEEECCCHHHH
26320211
76SuccinylationSRVVVVAKTTRYEFE
CEEEEEEECCCHHHH
-
76SuccinylationSRVVVVAKTTRYEFE
CEEEEEEECCCHHHH
-
93PhosphorylationRYRYAELSEEDLKQL
HHHHHHCCHHHHHHH
-
98AcetylationELSEEDLKQLLALKG
HCCHHHHHHHHHHCC
23954790
98UbiquitinationELSEEDLKQLLALKG
HCCHHHHHHHHHHCC
-
104 (in isoform 2)Ubiquitination-21890473
104 (in isoform 1)Ubiquitination-21890473
104UbiquitinationLKQLLALKGSSYSGL
HHHHHHHCCCCHHHH
21890473
106PhosphorylationQLLALKGSSYSGLLE
HHHHHCCCCHHHHHH
24275569
109PhosphorylationALKGSSYSGLLERHH
HHCCCCHHHHHHHCC
27499020
170UbiquitinationTMLLAASKVLDRLKP
HHHHHHHHHHHHCCC
-
176 (in isoform 3)Ubiquitination-21906983
176UbiquitinationSKVLDRLKPVIGVNT
HHHHHHCCCCCCCCC
-
183PhosphorylationKPVIGVNTDPERSEG
CCCCCCCCCCCCCCC
20166139
188PhosphorylationVNTDPERSEGHLCLP
CCCCCCCCCCEEEEE
24972180
198PhosphorylationHLCLPVRYTHSFPEA
EEEEEEEEECCCHHH
24719451
201PhosphorylationLPVRYTHSFPEALQK
EEEEEECCCHHHHHH
24719451
210PhosphorylationPEALQKFYRGEFRWL
HHHHHHHHHHCHHHH
24719451
283PhosphorylationNEVFIGESLSSRASY
CEEEECCCCCCCCCE
21815630
289PhosphorylationESLSSRASYYEISVD
CCCCCCCCEEEEECC
24275569
294PhosphorylationRASYYEISVDDGPWE
CCCEEEEECCCCCHH
-
302UbiquitinationVDDGPWEKQKSSGLN
CCCCCHHHCCCCCCE
-
302SuccinylationVDDGPWEKQKSSGLN
CCCCCHHHCCCCCCE
-
302SuccinylationVDDGPWEKQKSSGLN
CCCCCHHHCCCCCCE
-
304UbiquitinationDGPWEKQKSSGLNLC
CCCHHHCCCCCCEEC
-
304SuccinylationDGPWEKQKSSGLNLC
CCCHHHCCCCCCEEC
27452117
304MalonylationDGPWEKQKSSGLNLC
CCCHHHCCCCCCEEC
26320211
307 (in isoform 2)Ubiquitination-21890473
312PhosphorylationSSGLNLCTGTGSKAW
CCCCEECCCCCCCHH
22468782
314PhosphorylationGLNLCTGTGSKAWSF
CCEECCCCCCCHHEE
22468782
316PhosphorylationNLCTGTGSKAWSFNI
EECCCCCCCHHEEEH
22468782
317UbiquitinationLCTGTGSKAWSFNIN
ECCCCCCCHHEEEHH
-
317SuccinylationLCTGTGSKAWSFNIN
ECCCCCCCHHEEEHH
-
317SuccinylationLCTGTGSKAWSFNIN
ECCCCCCCHHEEEHH
-
317AcetylationLCTGTGSKAWSFNIN
ECCCCCCCHHEEEHH
26051181
339AcetylationEDVLNIAKRQGNLSL
HHHHHHHHHCCCCCC
25953088
339 (in isoform 1)Ubiquitination-21890473
339UbiquitinationEDVLNIAKRQGNLSL
HHHHHHHHHCCCCCC
2190698
345PhosphorylationAKRQGNLSLPLNREL
HHHCCCCCCCCCHHH
24275569
355UbiquitinationLNRELVEKVTNEYNE
CCHHHHHHHHHHCCH
-
357PhosphorylationRELVEKVTNEYNESL
HHHHHHHHHHCCHHC
26074081
360PhosphorylationVEKVTNEYNESLLYS
HHHHHHHCCHHCCCC
26074081
363PhosphorylationVTNEYNESLLYSPEE
HHHHCCHHCCCCCCC
28387310
366PhosphorylationEYNESLLYSPEEPKI
HCCHHCCCCCCCCCE
26074081
367PhosphorylationYNESLLYSPEEPKIL
CCHHCCCCCCCCCEE
25159151
372UbiquitinationLYSPEEPKILFSIRE
CCCCCCCCEEEEECH
-
376PhosphorylationEEPKILFSIREPIAN
CCCCEEEEECHHHHH
-
384MethylationIREPIANRVFSSSRQ
ECHHHHHCCCCCCCC
115484427
389PhosphorylationANRVFSSSRQRCFSS
HHCCCCCCCCHHHCC
24719451
393S-nitrosocysteineFSSSRQRCFSSKVCV
CCCCCCHHHCCCCCH
-
397AcetylationRQRCFSSKVCVRSRC
CCHHHCCCCCHHHCC
25825284
431AcetylationIASMMINKEDELRTV
EEHHEECCHHHHHHH
26051181

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 NAKD2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NAKD2_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 NAKD2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NPTX1_HUMANNPTX1physical
22939629
I2BPL_HUMANIRF2BPLphysical
22939629
FERM2_HUMANFERMT2physical
22939629
THTM_HUMANMPSTphysical
22939629
TM189_HUMANTMEM189physical
22939629
DYL1_HUMANDYNLL1physical
22939629
PNPH_HUMANPNPphysical
22939629
STMN1_HUMANSTMN1physical
22939629
ERMAP_HUMANERMAPphysical
22939629
HTRA2_HUMANHTRA2physical
22939629
TIM9_HUMANTIMM9physical
22939629
TM177_HUMANTMEM177physical
22939629
VPS29_HUMANVPS29physical
22939629
DJB11_HUMANDNAJB11physical
22939629
SUCB1_HUMANSUCLA2physical
22939629

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
6160342,4-dienoyl-CoA reductase deficiency (DECRD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NAKD2_HUMAN

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Related Literatures of Post-Translational Modification

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