dbPTM

NDKM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NDKM_HUMAN
UniProt AC	O00746
Protein Name	Nucleoside diphosphate kinase, mitochondrial
Gene Name	NME4
Organism	Homo sapiens (Human).
Sequence Length	187
Subcellular Localization	Mitochondrion intermembrane space Peripheral membrane protein. Mitochondrion matrix . Predominantly localized in the mitochondrion intermembrane space (PubMed:18635542). Colocalizes with OPA1 in mitochondria (PubMed:24970086).
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. Through the catalyzed exchange of gamma-phosphate between di- and triphosphonucleosides participates in regulation of intracellular nucleotide homeostasis. [PubMed: 10799505 Binds to anionic phospholipids, predominantly to cardiolipin; the binding inhibits its phosphotransfer activity]
Protein Sequence	MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQRFERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRASRAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQHSSIHPA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MGGLFWRSALRGLRC CCCHHHHHHHCCCCC	23.42	28634120
21	Acetylation	RCGPRAPGPSLLVRH CCCCCCCCCCEEEEC	24.36	19608861
23	Phosphorylation	GPRAPGPSLLVRHGS CCCCCCCCEEEECCC	40.00	23403867
30	Phosphorylation	SLLVRHGSGGPSWTR CEEEECCCCCCCCCC	34.16	22496350
36	Phosphorylation	GSGGPSWTRERTLVA CCCCCCCCCEEEEEE	27.30	-
85	Phosphorylation	ESVLAEHYQDLRRKP HHHHHHHHHHHHHCC	8.67	-
91	Acetylation	HYQDLRRKPFYPALI HHHHHHHCCCHHHHH	32.80	19608861
94	Phosphorylation	DLRRKPFYPALIRYM HHHHCCCHHHHHHHH	8.98	22210691
100	Phosphorylation	FYPALIRYMSSGPVV CHHHHHHHHHCCCEE	8.38	-
102	Phosphorylation	PALIRYMSSGPVVAM HHHHHHHHCCCEEEE	24.17	-
114	Phosphorylation	VAMVWEGYNVVRASR EEEEECCHHHHHHHH	8.02	-
127	Phosphorylation	SRAMIGHTDSAEAAP HHHHHCCCCCCCCCC	26.83	20068231
129	Phosphorylation	AMIGHTDSAEAAPGT HHHCCCCCCCCCCCE	29.21	20068231
136	Phosphorylation	SAEAAPGTIRGDFSV CCCCCCCEECCCEEE	13.37	20068231
153	Phosphorylation	SRNVIHASDSVEGAQ ECCEEEEHHCHHHHH	19.09	29255136
155	Phosphorylation	NVIHASDSVEGAQRE CEEEEHHCHHHHHHH	21.41	29255136

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 NDKM_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PCH2_HUMAN	TRIP13	physical	16189514
NDKM_HUMAN	NME4	physical	10799505
SOCS3_HUMAN	SOCS3	physical	21988832
HD_HUMAN	HTT	physical	23275563
SUV92_HUMAN	SUV39H2	physical	23455924
NDKB_HUMAN	NME2	physical	27499296
NDKM_HUMAN	NME4	physical	27499296
MIPEP_HUMAN	MIPEP	physical	27499296
GOLP3_HUMAN	GOLPH3	physical	27499296
MPPA_HUMAN	PMPCA	physical	27499296
MPPB_HUMAN	PMPCB	physical	27499296
PREP_HUMAN	PITRM1	physical	27499296
CX6A1_HUMAN	COX6A1	physical	27499296
ISOC2_HUMAN	ISOC2	physical	27499296
PDIP2_HUMAN	POLDIP2	physical	27499296
NRDC_HUMAN	NRD1	physical	27499296
ECH1_HUMAN	ECH1	physical	27499296
EFTS_HUMAN	TSFM	physical	27499296
ABHDA_HUMAN	ABHD10	physical	27499296
GLRX5_HUMAN	GLRX5	physical	27499296
NDK3_HUMAN	NME3	physical	27499296
PLPHP_HUMAN	PROSC	physical	27499296
CHCH2_HUMAN	CHCHD2	physical	27499296
NT5D2_HUMAN	NT5DC2	physical	27499296
MUTYH_HUMAN	MUTYH	physical	27499296
C1QBP_HUMAN	C1QBP	physical	27499296
TIM50_HUMAN	TIMM50	physical	27499296
ATP5E_HUMAN	ATP5E	physical	27499296
CYC_HUMAN	CYCS	physical	27499296

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 NDKM_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-91, AND MASS SPECTROMETRY.	19608861 [Abstract]