Reviewed, UniProtKB/Swiss-Prot O60361 (NDK8_HUMAN)

Names and origin

Protein names

Recommended name:
    Putative nucleoside diphosphate kinase
      Short name=NDP kinase
      Short name=NDK
    EC=2.7.4.6

Gene names

Name:

NME2P1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	137 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Uncertain.

General annotation (Comments)

Function	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 By similarity.
Catalytic activity	ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.
Cofactor	Magnesium By similarity.
Sequence similarities	Belongs to the NDK family.
Caution	Could be the product of a pseudogene.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	CTP biosynthetic process Inferred from electronic annotation. Source: InterPro GTP biosynthetic process Inferred from electronic annotation. Source: InterPro UTP biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside diphosphate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 137	137	Putative nucleoside diphosphate kinase		PRO_0000137133
Sites
	Active site	103	1	Pros-phosphohistidine intermediate By similarity
	Binding site	45	1	ATP By similarity
	Binding site	73	1	ATP By similarity
	Binding site	79	1	ATP By similarity
	Binding site	90	1	ATP By similarity
	Binding site	100	1	ATP By similarity
Amino acid modifications
	Modified residue	105	1	Phosphoserine Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O60361-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 92671EB92FE23167	FASTA	137	15,529
	10 20 30 40 50 60 MQCGLVGKII KRFEQKGFRL VAMKFLPASE EHLKQHYIDL KDRPFFPGLV KYMNSGPVVA 70 80 90 100 110 120 MVWEGLNVVK TGRVMLGETN PADSKPGTIR GDFCIQVGRN IIHGSDSVKS AEKEISLRFK 130 PEELVDYKSC AHDWVYE

References

[1]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed: 16541075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, MASS SPECTROMETRY. Tissue: Epithelium.
[3]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC004263 Genomic DNA. Translation: AAC05177.1.
IPI	IPI00029091.
3D structure databases
HSSP	HSSP built from PDB template 1NUE based on UniProtKB P22392.
SMR	O60361. Positions 1-137.
ModBase	Search...
Protein-protein interaction databases
STRING	O60361.
PTM databases
PhosphoSite	O60361.
Proteomic databases
PRIDE	O60361.
Genome annotation databases
Ensembl	ENST00000242630; ENSP00000242630; ENSG00000123009; Homo sapiens. [Genome view]
NMPDR	fig|9606.3.peg.8354.
Organism-specific databases
GeneCards	GC12P119182.
HGNC	HGNC:31358. NME2P1.
PharmGKB	PA134929506.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	O60361.
HOVERGEN	O60361.
OMA	WFKADEI.
Enzyme and pathway databases
BRENDA	2.7.4.6. 247.
Gene expression databases
Genevestigator	O60361.
GermOnline	ENSG00000123009. Homo sapiens.
Family and domain databases
InterPro	IPR001564. Nuc_diP_kinase_core. [Graphical view]
Gene3D	G3DSA:3.30.70.141. NDK. 1 hit.
PANTHER	PTHR11349. Nuc_diP_kinase_core. 1 hit.
Pfam	PF00334. NDK. 1 hit. [Graphical view]
PRINTS	PR01243. NUCDPKINASE.
ProDom	PD001018. NDK. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00562. NDK. 1 hit. [Graphical view]
PROSITE	PS00469. NDP_KINASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NDK8_HUMAN

Accession

Primary (citable) accession number: O60361

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	August 1, 1998
Last modified:	November 3, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.