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O95544

- NADK_HUMAN

UniProt

O95544 - NADK_HUMAN

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Protein

NAD kinase

Gene

NADK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Divalent metal cations.1 Publication

Kineticsi

  1. KM=3.3 mM for ATP1 Publication
  2. KM=0.54 mM for NAD1 Publication

Vmax=6.7 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 7.5.1 Publication

Temperature dependencei

Optimum temperature is 55 degrees Celsius.1 Publication

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. NAD+ kinase activity Source: UniProtKB

GO - Biological processi

  1. ATP metabolic process Source: UniProtKB
  2. NAD metabolic process Source: Reactome
  3. NADP biosynthetic process Source: InterPro
  4. phosphorylation Source: UniProtKB
  5. small molecule metabolic process Source: Reactome
  6. vitamin metabolic process Source: Reactome
  7. water-soluble vitamin metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Metal-binding, NAD, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS00233-MONOMER.
BRENDAi2.7.1.23. 2681.
ReactomeiREACT_11088. Nicotinate metabolism.
SABIO-RKO95544.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD kinase (EC:2.7.1.23)
Alternative name(s):
Poly(P)/ATP NAD kinase
Gene namesi
Name:NADK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:29831. NADK.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671298.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446NAD kinasePRO_0000120713Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461Phosphoserine2 Publications
Modified residuei48 – 481Phosphoserine2 Publications
Modified residuei50 – 501Phosphoserine1 Publication
Modified residuei64 – 641Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO95544.
PaxDbiO95544.
PRIDEiO95544.

PTM databases

PhosphoSiteiO95544.

Expressioni

Tissue specificityi

Widely expressed but not detected in skeletal muscle.1 Publication

Gene expression databases

BgeeiO95544.
CleanExiHS_NADK.
ExpressionAtlasiO95544. baseline and differential.
GenevestigatoriO95544.

Organism-specific databases

HPAiHPA048909.
HPA053368.

Interactioni

Protein-protein interaction databases

BioGridi122408. 12 interactions.
IntActiO95544. 8 interactions.
MINTiMINT-3296423.
STRINGi9606.ENSP00000341679.

Structurei

Secondary structure

1
446
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni75 – 773
Beta strandi78 – 803
Turni84 – 863
Beta strandi87 – 915
Turni93 – 953
Beta strandi97 – 1026
Beta strandi106 – 1116
Helixi116 – 1183
Helixi119 – 13113
Beta strandi135 – 1395
Helixi140 – 1445
Helixi146 – 1505
Helixi155 – 1606
Beta strandi162 – 1643
Turni166 – 1683
Turni172 – 1743
Beta strandi176 – 1838
Helixi186 – 1938
Beta strandi195 – 1973
Beta strandi201 – 2088
Turni210 – 2123
Beta strandi215 – 2173
Helixi220 – 22910
Beta strandi233 – 2375
Beta strandi240 – 2456
Beta strandi277 – 28913
Beta strandi299 – 3035
Beta strandi306 – 3116
Beta strandi313 – 3197
Helixi321 – 3255
Helixi327 – 3304
Beta strandi343 – 3497
Beta strandi358 – 3603
Beta strandi366 – 3705
Beta strandi378 – 3825
Beta strandi385 – 3906
Beta strandi395 – 4006
Beta strandi405 – 4084
Helixi413 – 42412

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PFNX-ray2.70A/B/C/D68-426[»]
ProteinModelPortaliO95544.
SMRiO95544. Positions 72-426.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95544.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi326 – 3338Poly-Ala
Compositional biasi437 – 4459Poly-Glu

Sequence similaritiesi

Belongs to the NAD kinase family.Curated

Phylogenomic databases

eggNOGiCOG0061.
GeneTreeiENSGT00390000013792.
HOGENOMiHOG000176769.
HOVERGENiHBG008249.
InParanoidiO95544.
KOiK00858.
OMAiSAQRENC.
OrthoDBiEOG7ZPNJT.
PhylomeDBiO95544.
TreeFamiTF324076.

Family and domain databases

Gene3Di2.60.200.30. 1 hit.
3.40.50.10330. 1 hit.
HAMAPiMF_00361. NAD_kinase.
InterProiIPR017438. 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]
PANTHERiPTHR20275. PTHR20275. 1 hit.
PfamiPF01513. NAD_kinase. 1 hit.
[Graphical view]
SUPFAMiSSF111331. SSF111331. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O95544) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MEMEQEKMTM NKELSPDAAA YCCSACHGDE TWSYNHPIRG RAKSRSLSAS
60 70 80 90 100
PALGSTKEFR RTRSLHGPCP VTTFGPKACV LQNPQTIMHI QDPASQRLTW
110 120 130 140 150
NKSPKSVLVI KKMRDASLLQ PFKELCTHLM EENMIVYVEK KVLEDPAIAS
160 170 180 190 200
DESFGAVKKK FCTFREDYDD ISNQIDFIIC LGGDGTLLYA SSLFQGSVPP
210 220 230 240 250
VMAFHLGSLG FLTPFSFENF QSQVTQVIEG NAAVVLRSRL KVRVVKELRG
260 270 280 290 300
KKTAVHNGLG ENGSQAAGLD MDVGKQAMQY QVLNEVVIDR GPSSYLSNVD
310 320 330 340 350
VYLDGHLITT VQGDGVIVST PTGSTAYAAA AGASMIHPNV PAIMITPICP
360 370 380 390 400
HSLSFRPIVV PAGVELKIML SPEARNTAWV SFDGRKRQEI RHGDSISITT
410 420 430 440
SCYPLPSICV RDPVSDWFES LAQCLHWNVR KKQAHFEEEE EEEEEG
Length:446
Mass (Da):49,228
Last modified:May 1, 1999 - v1
Checksum:i48CE7AF05EDD7E8B
GO
Isoform 2 (identifier: O95544-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     88-88: M → IATPLSLASQ...AGMGVGQATG
     131-131: E → EARGAGGKGAWGAHGVGGASIHITAPRVGSAGGMSRLALCFQ

Show »
Length:591
Mass (Da):63,456
Checksum:i9F81E711739713BA
GO
Isoform 3 (identifier: O95544-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:423
Mass (Da):46,446
Checksum:iD83B07A90D5B6D0A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti363 – 3631Missing in AAG44568. 1 PublicationCurated
Sequence conflicti445 – 4451E → EE in BAB14412. 1 PublicationCurated
Sequence conflicti446 – 4461G → EG in BAH12420. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti262 – 2621N → K.2 Publications
Corresponds to variant rs4751 [ dbSNP | Ensembl ].
VAR_034119

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei11 – 8777NKELS…NPQTI → GRPRVRQAWPGCCGHTGRLP AGRGYLASHMCDPAGAELIG DGMSDPTPPSNACT in isoform 3. 1 PublicationVSP_047312Add
BLAST
Alternative sequencei88 – 881M → IATPLSLASQLLPSPAVSHS GQGGVTGQVHVLPQPSDQGV LSGPRAARGQTAPQEEAVTQ EEVEALVCGHTQRWVPGPVY DAAAGGSGWAQLSLRAGMGV GQATG in isoform 2. 1 PublicationVSP_047313
Alternative sequencei131 – 1311E → EARGAGGKGAWGAHGVGGAS IHITAPRVGSAGGMSRLALC FQ in isoform 2. 1 PublicationVSP_047314

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS30565.1. [O95544-1]
CCDS55562.1. [O95544-2]
RefSeqiNP_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]
UniGeneiHs.654792.
Hs.731532.
Hs.733075.

Genome annotation databases

EnsembliENST00000341426; ENSP00000341679; ENSG00000008130. [O95544-1]
ENST00000341991; ENSP00000344340; ENSG00000008130. [O95544-1]
ENST00000378625; ENSP00000367890; ENSG00000008130. [O95544-2]
GeneIDi65220.
KEGGihsa:65220.
UCSCiuc001aic.3. human. [O95544-1]
uc001aie.3. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS30565.1. [O95544-1 ]
CCDS55562.1. [O95544-2 ]
RefSeqi NP_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 ]
UniGenei Hs.654792.
Hs.731532.
Hs.733075.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3PFN X-ray 2.70 A/B/C/D 68-426 [» ]
ProteinModelPortali O95544.
SMRi O95544. Positions 72-426.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122408. 12 interactions.
IntActi O95544. 8 interactions.
MINTi MINT-3296423.
STRINGi 9606.ENSP00000341679.

Chemistry

BindingDBi O95544.
ChEMBLi CHEMBL6177.

PTM databases

PhosphoSitei O95544.

Proteomic databases

MaxQBi O95544.
PaxDbi O95544.
PRIDEi O95544.

Protocols and materials databases

DNASUi 65220.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000341426 ; ENSP00000341679 ; ENSG00000008130 . [O95544-1 ]
ENST00000341991 ; ENSP00000344340 ; ENSG00000008130 . [O95544-1 ]
ENST00000378625 ; ENSP00000367890 ; ENSG00000008130 . [O95544-2 ]
GeneIDi 65220.
KEGGi hsa:65220.
UCSCi uc001aic.3. human. [O95544-1 ]
uc001aie.3. human.

Organism-specific databases

CTDi 65220.
GeneCardsi GC01M001682.
HGNCi HGNC:29831. NADK.
HPAi HPA048909.
HPA053368.
MIMi 611616. gene.
neXtProti NX_O95544.
PharmGKBi PA142671298.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0061.
GeneTreei ENSGT00390000013792.
HOGENOMi HOG000176769.
HOVERGENi HBG008249.
InParanoidi O95544.
KOi K00858.
OMAi SAQRENC.
OrthoDBi EOG7ZPNJT.
PhylomeDBi O95544.
TreeFami TF324076.

Enzyme and pathway databases

BioCyci MetaCyc:HS00233-MONOMER.
BRENDAi 2.7.1.23. 2681.
Reactomei REACT_11088. Nicotinate metabolism.
SABIO-RK O95544.

Miscellaneous databases

ChiTaRSi NADK. human.
EvolutionaryTracei O95544.
GeneWikii NAD%2B_kinase.
GenomeRNAii 65220.
NextBioi 67354.
PROi O95544.
SOURCEi Search...

Gene expression databases

Bgeei O95544.
CleanExi HS_NADK.
ExpressionAtlasi O95544. baseline and differential.
Genevestigatori O95544.

Family and domain databases

Gene3Di 2.60.200.30. 1 hit.
3.40.50.10330. 1 hit.
HAMAPi MF_00361. NAD_kinase.
InterProi IPR017438. 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 ]
PANTHERi PTHR20275. PTHR20275. 1 hit.
Pfami PF01513. NAD_kinase. 1 hit.
[Graphical view ]
SUPFAMi SSF111331. SSF111331. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiNADK_HUMAN
AccessioniPrimary (citable) accession number: O95544
Secondary accession number(s): A6NNN3
, A8K296, B7Z434, F5GXR5, Q5QPS4, Q9H2P2, Q9H931
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: October 29, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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