Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O95544 (NADK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NAD kinase

EC=2.7.1.23
Alternative name(s):
Poly(P)/ATP NAD kinase
Gene names
Name:NADK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + NAD+ = ADP + NADP+. Ref.1

Cofactor

Divalent metal cations. Ref.1

Tissue specificity

Widely expressed but not detected in skeletal muscle. Ref.1

Sequence similarities

Belongs to the NAD kinase family.

Biophysicochemical properties

Kinetic parameters:

KM=3.3 mM for ATP Ref.1

KM=0.54 mM for NAD

Vmax=6.7 µmol/min/mg enzyme

pH dependence:

Optimum pH is 7.5.

Temperature dependence:

Optimum temperature is 55 degrees Celsius.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95544-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O95544-2)

The sequence of this isoform differs from the canonical sequence as follows:
     88-88: M → IATPLSLASQ...AGMGVGQATG
     131-131: E → EARGAGGKGAWGAHGVGGASIHITAPRVGSAGGMSRLALCFQ
Isoform 3 (identifier: O95544-3)

The sequence of this isoform differs from the canonical sequence as follows:
     11-87: NKELSPDAAA...ACVLQNPQTI → GRPRVRQAWP...DPTPPSNACT

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 446446NAD kinase HAMAP-Rule MF_00361
PRO_0000120713

Regions

Compositional bias326 – 3338Poly-Ala HAMAP-Rule MF_00361
Compositional bias437 – 4459Poly-Glu HAMAP-Rule MF_00361

Amino acid modifications

Modified residue461Phosphoserine Ref.7 Ref.8
Modified residue481Phosphoserine Ref.7 Ref.8
Modified residue501Phosphoserine Ref.7
Modified residue641Phosphoserine Ref.7

Natural variations

Alternative sequence11 – 8777NKELS…NPQTI → GRPRVRQAWPGCCGHTGRLP AGRGYLASHMCDPAGAELIG DGMSDPTPPSNACT in isoform 3.
VSP_047312
Alternative sequence881M → IATPLSLASQLLPSPAVSHS GQGGVTGQVHVLPQPSDQGV LSGPRAARGQTAPQEEAVTQ EEVEALVCGHTQRWVPGPVY DAAAGGSGWAQLSLRAGMGV GQATG in isoform 2.
VSP_047313
Alternative sequence1311E → EARGAGGKGAWGAHGVGGAS IHITAPRVGSAGGMSRLALC FQ in isoform 2.
VSP_047314
Natural variant2621N → K. Ref.1 Ref.6
Corresponds to variant rs4751 [ dbSNP | Ensembl ].
VAR_034119

Experimental info

Sequence conflict3631Missing in AAG44568. Ref.2
Sequence conflict4451E → EE in BAB14412. Ref.2
Sequence conflict4461G → EG in BAH12420. Ref.3

Secondary structure

........................................................................... 446
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 48CE7AF05EDD7E8B

FASTA44649,228
        10         20         30         40         50         60 
MEMEQEKMTM NKELSPDAAA YCCSACHGDE TWSYNHPIRG RAKSRSLSAS PALGSTKEFR 

        70         80         90        100        110        120 
RTRSLHGPCP VTTFGPKACV LQNPQTIMHI QDPASQRLTW NKSPKSVLVI KKMRDASLLQ 

       130        140        150        160        170        180 
PFKELCTHLM EENMIVYVEK KVLEDPAIAS DESFGAVKKK FCTFREDYDD ISNQIDFIIC 

       190        200        210        220        230        240 
LGGDGTLLYA SSLFQGSVPP VMAFHLGSLG FLTPFSFENF QSQVTQVIEG NAAVVLRSRL 

       250        260        270        280        290        300 
KVRVVKELRG KKTAVHNGLG ENGSQAAGLD MDVGKQAMQY QVLNEVVIDR GPSSYLSNVD 

       310        320        330        340        350        360 
VYLDGHLITT VQGDGVIVST PTGSTAYAAA AGASMIHPNV PAIMITPICP HSLSFRPIVV 

       370        380        390        400        410        420 
PAGVELKIML SPEARNTAWV SFDGRKRQEI RHGDSISITT SCYPLPSICV RDPVSDWFES 

       430        440 
LAQCLHWNVR KKQAHFEEEE EEEEEG 

« Hide

Isoform 2 [UniParc].

Checksum: 9F81E711739713BA
Show »

FASTA59163,456
Isoform 3 [UniParc].

Checksum: D83B07A90D5B6D0A
Show »

FASTA42346,446

References

« Hide 'large scale' references
[1]"Structural and functional characterization of human NAD kinase."
Lerner F., Niere M., Ludwig A., Ziegler M.
Biochem. Biophys. Res. Commun. 288:69-74(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, VARIANT LYS-262.
Tissue: Fibroblast.
[2]Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Hypothalamus.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: Thalamus.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LYS-262.
Tissue: Lymph.
[7]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-48; SER-50 AND SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Crystal structure of human NAD kinase."
Structural genomics consortium (SGC)
Submitted (NOV-2010) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 68-426.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY090771 mRNA. Translation: AAM01195.1.
AF250320 mRNA. Translation: AAG44568.1.
AK023114 mRNA. Translation: BAB14412.1.
AK290161 mRNA. Translation: BAF82850.1.
AK296722 mRNA. Translation: BAH12420.1.
AL031282 Genomic DNA. No translation available.
CH471183 Genomic DNA. Translation: EAW56151.1.
CH471183 Genomic DNA. Translation: EAW56152.1.
BC001709 mRNA. Translation: AAH01709.1.
CCDSCCDS30565.1. [O95544-1]
CCDS55562.1. [O95544-2]
RefSeqNP_001185922.1. NM_001198993.1. [O95544-1]
NP_001185923.1. NM_001198994.1. [O95544-2]
NP_001185924.1. NM_001198995.1.
NP_075394.3. NM_023018.4. [O95544-1]
XP_005244835.1. XM_005244778.1. [O95544-1]
XP_006710900.1. XM_006710837.1. [O95544-1]
UniGeneHs.654792.
Hs.731532.
Hs.733075.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3PFNX-ray2.70A/B/C/D68-426[»]
ProteinModelPortalO95544.
SMRO95544. Positions 72-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122408. 12 interactions.
IntActO95544. 8 interactions.
MINTMINT-3296423.
STRING9606.ENSP00000341679.

Chemistry

BindingDBO95544.
ChEMBLCHEMBL6177.

PTM databases

PhosphoSiteO95544.

Proteomic databases

MaxQBO95544.
PaxDbO95544.
PRIDEO95544.

Protocols and materials databases

DNASU65220.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341426; ENSP00000341679; ENSG00000008130. [O95544-1]
ENST00000341991; ENSP00000344340; ENSG00000008130. [O95544-1]
ENST00000344463; ENSP00000340925; ENSG00000008130. [O95544-2]
ENST00000378625; ENSP00000367890; ENSG00000008130. [O95544-2]
GeneID65220.
KEGGhsa:65220.
UCSCuc001aic.3. human. [O95544-1]

Organism-specific databases

CTD65220.
GeneCardsGC01M001682.
HGNCHGNC:29831. NADK.
HPAHPA048909.
HPA053368.
MIM611616. gene.
neXtProtNX_O95544.
PharmGKBPA142671298.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000176769.
HOVERGENHBG008249.
KOK00858.
OMASAQRENC.
OrthoDBEOG7ZPNJT.
PhylomeDBO95544.
TreeFamTF324076.

Enzyme and pathway databases

BioCycMetaCyc:HS00233-MONOMER.
BRENDA2.7.1.23. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKO95544.

Gene expression databases

ArrayExpressO95544.
BgeeO95544.
CleanExHS_NADK.
GenevestigatorO95544.

Family and domain databases

Gene3D2.60.200.30. 1 hit.
3.40.50.10330. 1 hit.
HAMAPMF_00361. NAD_kinase.
InterProIPR017438. ATP-NAD_kinase_dom_1.
IPR016064. ATP-NAD_kinase_PpnK-typ.
IPR017437. ATP-NAD_kinase_PpnK-typ_all-b.
IPR002504. PolyP/ATP_NADK.
[Graphical view]
PANTHERPTHR20275. PTHR20275. 1 hit.
PfamPF01513. NAD_kinase. 1 hit.
[Graphical view]
SUPFAMSSF111331. SSF111331. 2 hits.
ProtoNetSearch...

Other

ChiTaRSNADK. human.
EvolutionaryTraceO95544.
GeneWikiNAD%2B_kinase.
GenomeRNAi65220.
NextBio67354.
PROO95544.
SOURCESearch...

Entry information

Entry nameNADK_HUMAN
AccessionPrimary (citable) accession number: O95544
Secondary accession number(s): A6NNN3 expand/collapse secondary AC list , A8K296, B7Z434, F5GXR5, Q5QPS4, Q9H2P2, Q9H931
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM