NDKA_HUMAN - dbPTM
NDKA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NDKA_HUMAN
UniProt AC P15531
Protein Name Nucleoside diphosphate kinase A
Gene Name NME1
Organism Homo sapiens (Human).
Sequence Length 152
Subcellular Localization Cytoplasm . Nucleus . Cell-cycle dependent nuclear localization which can be induced by interaction with Epstein-barr viral proteins or by degradation of the SET complex by GzmA.
Protein Description Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein-coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination. During GZMA-mediated cell death, works in concert with TREX1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair..
Protein Sequence MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPFFAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
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
2Acetylation------MANCERTFI
------CCCCEEEEE		29.40-
5 (in isoform 2)Phosphorylation-55.3424043423
6Methylation--MANCERTFIAIKP
--CCCCEEEEEEECC		36.82115485093
6 (in isoform 2)Phosphorylation-36.8224043423
7Phosphorylation-MANCERTFIAIKPD
-CCCCEEEEEEECCC		9.3330624053
12UbiquitinationERTFIAIKPDGVQRG
EEEEEEECCCCHHCC		28.2121890473
122-HydroxyisobutyrylationERTFIAIKPDGVQRG
EEEEEEECCCCHHCC		28.21-
12AcetylationERTFIAIKPDGVQRG
EEEEEEECCCCHHCC		28.2123954790
12 (in isoform 1)Ubiquitination-28.2121890473
18MethylationIKPDGVQRGLVGEII
ECCCCHHCCHHHHHH		37.70-
19 (in isoform 2)Phosphorylation-13.9724043423
20 (in isoform 2)Phosphorylation-4.9524043423
23 (in isoform 2)Phosphorylation-33.7824043423
25 (in isoform 2)Phosphorylation-1.9724043423
26UbiquitinationGLVGEIIKRFEQKGF
CHHHHHHHHHHHCCC		57.61-
26SuccinylationGLVGEIIKRFEQKGF
CHHHHHHHHHHHCCC		57.6123954790
26AcetylationGLVGEIIKRFEQKGF
CHHHHHHHHHHHCCC		57.6123749302
26 (in isoform 1)Ubiquitination-57.6121890473
31UbiquitinationIIKRFEQKGFRLVGL
HHHHHHHCCCEEEEH		53.47-
31AcetylationIIKRFEQKGFRLVGL
HHHHHHHCCCEEEEH		53.4726051181
31 (in isoform 1)Ubiquitination-53.4721890473
32 (in isoform 2)Phosphorylation-16.7624043423
37UbiquitinationQKGFRLVGLKFMQAS
HCCCEEEEHHHHHHC		27.9519608861
37 (in isoform 2)Ubiquitination-27.9521890473
37AcetylationQKGFRLVGLKFMQAS
HCCCEEEEHHHHHHC		27.9519608861
39 (in isoform 1)Ubiquitination-32.6321890473
392-HydroxyisobutyrylationGFRLVGLKFMQASED
CCEEEEHHHHHHCHH		32.63-
39UbiquitinationGFRLVGLKFMQASED
CCEEEEHHHHHHCHH		32.6321906983
41SulfoxidationRLVGLKFMQASEDLL
EEEEHHHHHHCHHHH		2.8821406390
44PhosphorylationGLKFMQASEDLLKEH
EHHHHHHCHHHHHHH		18.1026356563
492-HydroxyisobutyrylationQASEDLLKEHYVDLK
HHCHHHHHHHCCCCC		50.14-
49 (in isoform 1)Ubiquitination-50.1421890473
49SumoylationQASEDLLKEHYVDLK
HHCHHHHHHHCCCCC		50.14-
49UbiquitinationQASEDLLKEHYVDLK
HHCHHHHHHHCCCCC		50.1421890473
49AcetylationQASEDLLKEHYVDLK
HHCHHHHHHHCCCCC		50.1423749302
51 (in isoform 2)Ubiquitination-26.7421890473
52PhosphorylationEDLLKEHYVDLKDRP
HHHHHHHCCCCCCCC		9.2128152594
56 (in isoform 2)Ubiquitination-47.4221890473
56UbiquitinationKEHYVDLKDRPFFAG
HHHCCCCCCCCCHHH		47.4219608861
56SumoylationKEHYVDLKDRPFFAG
HHHCCCCCCCCCHHH		47.4219608861
56 (in isoform 1)Ubiquitination-47.4221890473
56SuccinylationKEHYVDLKDRPFFAG
HHHCCCCCCCCCHHH		47.4223954790
56AcetylationKEHYVDLKDRPFFAG
HHHCCCCCCCCCHHH		47.4223749302
562-HydroxyisobutyrylationKEHYVDLKDRPFFAG
HHHCCCCCCCCCHHH		47.42-
58MethylationHYVDLKDRPFFAGLV
HCCCCCCCCCHHHHH		28.47115485101
64 (in isoform 2)Ubiquitination-2.4221890473
66AcetylationPFFAGLVKYMHSGPV
CCHHHHHHHHHCCCE		41.7330585599
66UbiquitinationPFFAGLVKYMHSGPV
CCHHHHHHHHHCCCE		41.73-
67PhosphorylationFFAGLVKYMHSGPVV
CHHHHHHHHHCCCEE		7.80-
74 (in isoform 2)Ubiquitination-2.9821890473
81UbiquitinationVAMVWEGLNVVKTGR
EEEEEECCCEEEECC		2.7419608861
81AcetylationVAMVWEGLNVVKTGR
EEEEEECCCEEEECC		2.7419608861
81 (in isoform 2)Ubiquitination-2.7421890473
85UbiquitinationWEGLNVVKTGRVMLG
EECCCEEEECCEEEC		40.7621906983
85AcetylationWEGLNVVKTGRVMLG
EECCCEEEECCEEEC		40.7625953088
85 (in isoform 1)Ubiquitination-40.7621890473
88MethylationLNVVKTGRVMLGETN
CCEEEECCEEECCCC		18.86-
94PhosphorylationGRVMLGETNPADSKP
CCEEECCCCCCCCCC		44.7129255136
99PhosphorylationGETNPADSKPGTIRG
CCCCCCCCCCCCCCC		42.7430266825
100 (in isoform 1)Ubiquitination-48.2721890473
100AcetylationETNPADSKPGTIRGD
CCCCCCCCCCCCCCC		48.2719608861
100MethylationETNPADSKPGTIRGD
CCCCCCCCCCCCCCC		48.277618841
100SumoylationETNPADSKPGTIRGD
CCCCCCCCCCCCCCC		48.2719608861
100UbiquitinationETNPADSKPGTIRGD
CCCCCCCCCCCCCCC		48.2719608861
103PhosphorylationPADSKPGTIRGDFCI
CCCCCCCCCCCCEEE		18.9423927012
109GlutathionylationGTIRGDFCIQVGRNI
CCCCCCEEEEECCCE		2.2422833525
109S-palmitoylationGTIRGDFCIQVGRNI
CCCCCCEEEEECCCE		2.2429575903
110 (in isoform 2)Ubiquitination-3.6221890473
118PhosphorylationQVGRNIIHGSDSVES
EECCCEECCCCCHHH		26.38-
120PhosphorylationGRNIIHGSDSVESAE
CCCEECCCCCHHHHH		16.7329255136
122PhosphorylationNIIHGSDSVESAEKE
CEECCCCCHHHHHHH		29.4930266825
125AcetylationHGSDSVESAEKEIGL
CCCCCHHHHHHHHCC		39.3019608861
125PhosphorylationHGSDSVESAEKEIGL
CCCCCHHHHHHHHCC		39.3023927012
125UbiquitinationHGSDSVESAEKEIGL
CCCCCHHHHHHHHCC		39.3019608861
125 (in isoform 2)Ubiquitination-39.3021890473
145 (in isoform 2)Phosphorylation-3.3027251275
147 (in isoform 2)Phosphorylation-50.5527251275
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
44SPhosphorylationKinaseNME1P15531
PSP
94TPhosphorylationKinaseCDK1P06493
PSP
120SPhosphorylationKinaseCDK1P06493
PSP
120SPhosphorylationKinaseNME1P15531
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NDKA_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 NDKA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NTAQ1_HUMANWDYHV1physical
16189514
NDKM_HUMANNME4physical
16189514
RPAC1_HUMANPOLR1Cphysical
16189514
GORS2_HUMANGORASP2physical
16189514
NDK3_HUMANNME3physical
16189514
NDKA_HUMANNME1physical
16189514
SET_HUMANSETphysical
12628186
AURKA_HUMANAURKAphysical
12490715
NDKA_HUMANNME1physical
11835509
TERF1_HUMANTERF1physical
9480811
TIAM1_HUMANTIAM1physical
11274357
RAC1_HUMANRAC1physical
11274357
PRUN1_HUMANPRUNEphysical
10602478
GATA1_HUMANGATA1physical
16631833
STRAP_HUMANSTRAPphysical
17314099
NDKA_HUMANNME1physical
17314099
NDKB_HUMANNME2physical
17314099
MIF_HUMANMIFphysical
18815136
NDKA_HUMANNME1physical
18815136
SODC_HUMANSOD1physical
22939629
RPAC1_HUMANPOLR1Cphysical
21988832
NDKB_HUMANNME2physical
21988832
SMRD1_HUMANSMARCD1physical
21988832
SOX30_HUMANSOX30physical
21988832
IDHC_HUMANIDH1physical
22863883
RBBP7_HUMANRBBP7physical
22863883
WDR1_HUMANWDR1physical
22863883
NDKA_HUMANNME1physical
25416956
NDK3_HUMANNME3physical
25416956
NDKM_HUMANNME4physical
25416956
RPAC1_HUMANPOLR1Cphysical
25416956
TNPO2_HUMANTNPO2physical
25416956
PCLI1_HUMANPID1physical
25416956
SR1IP_HUMANSREK1IP1physical
25416956
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
DB00718Adefovir Dipivoxil
DB00709Lamivudine
DB00300Tenofovir
Regulatory Network of NDKA_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56, AND MASS SPECTROMETRY.
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 THR-94, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry.";
Meierhofer D., Wang X., Huang L., Kaiser P.;
J. Proteome Res. 7:4566-4576(2008).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-100, AND MASSSPECTROMETRY.

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