SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P23743

- DGKA_HUMAN

UniProt

P23743 - DGKA_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Diacylglycerol kinase alpha

Gene
DGKA, DAGK, DAGK1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity.

Catalytic activityi

ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate.

Enzyme regulationi

Stimulated by calcium and phosphatidylserine. Phosphorylated by protein kinase C.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi123 – 134121 InferredAdd
BLAST
Calcium bindingi168 – 179122 InferredAdd
BLAST
Zinc fingeri205 – 25349Phorbol-ester/DAG-type 1Add
BLAST
Zinc fingeri269 – 31951Phorbol-ester/DAG-type 2Add
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium ion binding Source: InterPro
  3. diacylglycerol kinase activity Source: ProtInc
  4. NAD+ kinase activity Source: InterPro
  5. phospholipid binding Source: Ensembl

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. intracellular signal transduction Source: ProtInc
  3. platelet activation Source: Reactome
  4. protein kinase C-activating G-protein coupled receptor signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Calcium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_2202. Effects of PIP2 hydrolysis.
SABIO-RKP23743.

Names & Taxonomyi

Protein namesi
Recommended name:
Diacylglycerol kinase alpha (EC:2.7.1.107)
Short name:
DAG kinase alpha
Alternative name(s):
80 kDa diacylglycerol kinase
Diglyceride kinase alpha
Short name:
DGK-alpha
Gene namesi
Name:DGKA
Synonyms:DAGK, DAGK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:2849. DGKA.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. plasma membrane Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27310.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 735735Diacylglycerol kinase alphaPRO_0000218453Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei484 – 4841N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP23743.
PaxDbiP23743.
PRIDEiP23743.

PTM databases

PhosphoSiteiP23743.

Expressioni

Tissue specificityi

Lymphocytes and oligodendroglial cells.

Gene expression databases

ArrayExpressiP23743.
BgeeiP23743.
CleanExiHS_DGKA.
GenevestigatoriP23743.

Organism-specific databases

HPAiHPA041645.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi107976. 5 interactions.
IntActiP23743. 3 interactions.
MINTiMINT-8020268.
STRINGi9606.ENSP00000328405.

Structurei

Secondary structure

1
735
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2213
Helixi27 – 359
Helixi38 – 425
Helixi50 – 6011
Helixi68 – 7710
Helixi96 – 10712

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TUZNMR-A1-116[»]
ProteinModelPortaliP23743.
SMRiP23743. Positions 1-198.

Miscellaneous databases

EvolutionaryTraceiP23743.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini110 – 14536EF-hand 1Add
BLAST
Domaini155 – 19036EF-hand 2Add
BLAST
Domaini372 – 506135DAGKcAdd
BLAST

Sequence similaritiesi

Contains 1 DAGKc domain.
Contains 2 EF-hand domains.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG47311.
HOVERGENiHBG051345.
InParanoidiP23743.
KOiK00901.
OMAiLVGLHCV.
OrthoDBiEOG75XGK8.
PhylomeDBiP23743.
TreeFamiTF313104.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.238.110. 1 hit.
InterProiIPR016064. ATP-NAD_kinase_PpnK-typ.
IPR029477. DAG_kinase_typeI_N.
IPR000756. Diacylglycerol_kin_accessory.
IPR001206. Diacylglycerol_kinase_cat_dom.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF14513. DAG_kinase_N. 2 hits.
PF00609. DAGK_acc. 1 hit.
PF00781. DAGK_cat. 1 hit.
PF13405. EF-hand_6. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 2 hits.
SM00045. DAGKa. 1 hit.
SM00046. DAGKc. 1 hit.
SM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF111331. SSF111331. 2 hits.
PROSITEiPS50146. DAGK. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P23743-1) [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

MAKERGLISP SDFAQLQKYM EYSTKKVSDV LKLFEDGEMA KYVQGDAIGY    50
EGFQQFLKIY LEVDNVPRHL SLALFQSFET GHCLNETNVT KDVVCLNDVS 100
CYFSLLEGGR PEDKLEFTFK LYDTDRNGIL DSSEVDKIIL QMMRVAEYLD 150
WDVSELRPIL QEMMKEIDYD GSGSVSQAEW VRAGATTVPL LVLLGLEMTL 200
KDDGQHMWRP KRFPRPVYCN LCESSIGLGK QGLSCNLCKY TVHDQCAMKA 250
LPCEVSTYAK SRKDIGVQSH VWVRGGCESG RCDRCQKKIR IYHSLTGLHC 300
VWCHLEIHDD CLQAVGHECD CGLLRDHILP PSSIYPSVLA SGPDRKNSKT 350
SQKTMDDLNL STSEALRIDP VPNTHPLLVF VNPKSGGKQG QRVLWKFQYI 400
LNPRQVFNLL KDGPEIGLRL FKDVPDSRIL VCGGDGTVGW ILETIDKANL 450
PVLPPVAVLP LGTGNDLARC LRWGGGYEGQ NLAKILKDLE MSKVVHMDRW 500
SVEVIPQQTE EKSDPVPFQI INNYFSIGVD ASIAHRFHIM REKYPEKFNS 550
RMKNKLWYFE FATSESIFST CKKLEESLTV EICGKPLDLS NLSLEGIAVL 600
NIPSMHGGSN LWGDTRRPHG DIYGINQALG ATAKVITDPD ILKTCVPDLS 650
DKRLEVVGLE GAIEMGQIYT KLKNAGRRLA KCSEITFHTT KTLPMQIDGE 700
PWMQTPCTIK ITHKNQMPML MGPPPRSTNF FGFLS 735
Length:735
Mass (Da):82,630
Last modified:December 15, 2009 - v3
Checksum:iACAA0AD186EE64A0
GO
Isoform 2 (identifier: P23743-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     117-118: FT → WS
     119-735: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:118
Mass (Da):13,486
Checksum:iDC47336F5D8B584F
GO
Isoform 3 (identifier: P23743-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     237-247: LCKYTVHDQCA → RPITCVGARRL
     248-735: Missing.

Show »
Length:247
Mass (Da):28,094
Checksum:i8B502053A1906FB4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti538 – 5381H → Y.1 Publication
Corresponds to variant rs17852990 [ dbSNP | Ensembl ].
VAR_031563

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei117 – 1182FT → WS in isoform 2. VSP_032212
Alternative sequencei119 – 735617Missing in isoform 2. VSP_032213Add
BLAST
Alternative sequencei237 – 24711LCKYTVHDQCA → RPITCVGARRL in isoform 3. VSP_047702Add
BLAST
Alternative sequencei248 – 735488Missing in isoform 3. VSP_047703Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti339 – 3391L → P in AAC34804. 1 Publication
Sequence conflicti379 – 3791V → L in AAC34802. 1 Publication
Sequence conflicti385 – 3851S → W in AAC34802. 1 Publication
Sequence conflicti684 – 6841E → G in AAC34803. 1 Publication
Sequence conflicti699 – 6991G → V in CAA44396. 1 Publication
Sequence conflicti715 – 7151N → K in AAC34803. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X62535 mRNA. Translation: CAA44396.1.
AF064767 mRNA. Translation: AAC34802.1.
AF064768 mRNA. Translation: AAC34803.1.
AF064769 mRNA. Translation: AAC34804.1.
AF064771 mRNA. Translation: AAC34806.1.
AY930112 mRNA. Translation: AAY20994.1.
AC025162 Genomic DNA. No translation available.
BC023523 mRNA. Translation: AAH23523.1.
BC031870 mRNA. Translation: AAH31870.1.
CCDSiCCDS8896.1. [P23743-1]
PIRiS12969.
RefSeqiNP_001336.2. NM_001345.4. [P23743-1]
NP_958852.1. NM_201444.2. [P23743-1]
NP_958853.1. NM_201445.1. [P23743-1]
NP_963848.1. NM_201554.1. [P23743-1]
UniGeneiHs.524488.

Genome annotation databases

EnsembliENST00000331886; ENSP00000328405; ENSG00000065357. [P23743-1]
ENST00000394147; ENSP00000377703; ENSG00000065357. [P23743-1]
ENST00000402956; ENSP00000385792; ENSG00000065357. [P23743-3]
ENST00000548549; ENSP00000448565; ENSG00000065357. [P23743-2]
ENST00000551156; ENSP00000450359; ENSG00000065357. [P23743-1]
ENST00000553084; ENSP00000446605; ENSG00000065357. [P23743-2]
GeneIDi1606.
KEGGihsa:1606.
UCSCiuc001sih.1. human. [P23743-1]

Polymorphism databases

DMDMi281185505.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X62535 mRNA. Translation: CAA44396.1 .
AF064767 mRNA. Translation: AAC34802.1 .
AF064768 mRNA. Translation: AAC34803.1 .
AF064769 mRNA. Translation: AAC34804.1 .
AF064771 mRNA. Translation: AAC34806.1 .
AY930112 mRNA. Translation: AAY20994.1 .
AC025162 Genomic DNA. No translation available.
BC023523 mRNA. Translation: AAH23523.1 .
BC031870 mRNA. Translation: AAH31870.1 .
CCDSi CCDS8896.1. [P23743-1 ]
PIRi S12969.
RefSeqi NP_001336.2. NM_001345.4. [P23743-1 ]
NP_958852.1. NM_201444.2. [P23743-1 ]
NP_958853.1. NM_201445.1. [P23743-1 ]
NP_963848.1. NM_201554.1. [P23743-1 ]
UniGenei Hs.524488.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TUZ NMR - A 1-116 [» ]
ProteinModelPortali P23743.
SMRi P23743. Positions 1-198.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107976. 5 interactions.
IntActi P23743. 3 interactions.
MINTi MINT-8020268.
STRINGi 9606.ENSP00000328405.

Chemistry

DrugBanki DB00163. Vitamin E.

PTM databases

PhosphoSitei P23743.

Polymorphism databases

DMDMi 281185505.

Proteomic databases

MaxQBi P23743.
PaxDbi P23743.
PRIDEi P23743.

Protocols and materials databases

DNASUi 1606.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000331886 ; ENSP00000328405 ; ENSG00000065357 . [P23743-1 ]
ENST00000394147 ; ENSP00000377703 ; ENSG00000065357 . [P23743-1 ]
ENST00000402956 ; ENSP00000385792 ; ENSG00000065357 . [P23743-3 ]
ENST00000548549 ; ENSP00000448565 ; ENSG00000065357 . [P23743-2 ]
ENST00000551156 ; ENSP00000450359 ; ENSG00000065357 . [P23743-1 ]
ENST00000553084 ; ENSP00000446605 ; ENSG00000065357 . [P23743-2 ]
GeneIDi 1606.
KEGGi hsa:1606.
UCSCi uc001sih.1. human. [P23743-1 ]

Organism-specific databases

CTDi 1606.
GeneCardsi GC12P056324.
HGNCi HGNC:2849. DGKA.
HPAi HPA041645.
MIMi 125855. gene.
neXtProti NX_P23743.
PharmGKBi PA27310.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG47311.
HOVERGENi HBG051345.
InParanoidi P23743.
KOi K00901.
OMAi LVGLHCV.
OrthoDBi EOG75XGK8.
PhylomeDBi P23743.
TreeFami TF313104.

Enzyme and pathway databases

Reactomei REACT_2202. Effects of PIP2 hydrolysis.
SABIO-RK P23743.

Miscellaneous databases

ChiTaRSi DGKA. human.
EvolutionaryTracei P23743.
GeneWikii DGKA.
GenomeRNAii 1606.
NextBioi 6590.
PROi P23743.
SOURCEi Search...

Gene expression databases

ArrayExpressi P23743.
Bgeei P23743.
CleanExi HS_DGKA.
Genevestigatori P23743.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
1.10.238.110. 1 hit.
InterProi IPR016064. ATP-NAD_kinase_PpnK-typ.
IPR029477. DAG_kinase_typeI_N.
IPR000756. Diacylglycerol_kin_accessory.
IPR001206. Diacylglycerol_kinase_cat_dom.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
[Graphical view ]
Pfami PF00130. C1_1. 2 hits.
PF14513. DAG_kinase_N. 2 hits.
PF00609. DAGK_acc. 1 hit.
PF00781. DAGK_cat. 1 hit.
PF13405. EF-hand_6. 1 hit.
[Graphical view ]
SMARTi SM00109. C1. 2 hits.
SM00045. DAGKa. 1 hit.
SM00046. DAGKc. 1 hit.
SM00054. EFh. 2 hits.
[Graphical view ]
SUPFAMi SSF111331. SSF111331. 2 hits.
PROSITEi PS50146. DAGK. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Lymphocyte.
  2. "Alternative splicing of diacylglycerol kinase alpha expressed in human neutrophils."
    Champagne C.M.E., Maeda H., Takashiba S., van Dyke T.E.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING.
    Tissue: Uterus.
  3. "Characterization of a novel DGK alpha transcript generated by alternative splicing."
    Batista E.L. Jr., Van Dyke T.E.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 TYR-538.
    Tissue: Brain.
  6. "Assignment of the gene for diacylglycerol kinase (DAGK) to human chromosome 12."
    Hart T.C., Champagne C., Zhou J., van Dyke T.E.
    Mamm. Genome 5:123-124(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL LOCATION.
  7. "Assignment of the human diacylglycerol kinase gene (DAGK) to 12q13.3 using fluorescence in situ hybridization analysis."
    Hart T.C., Zhou J., Champagne C., van Dyke T.E., Rao P.N., Pettenati M.J.
    Genomics 22:246-247(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL LOCATION.
  8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "NMR structure of diacylglycerol kinase alpha, NESGC target HR532."
    Northeast structural genomics consortium (NESG)
    Submitted (JAN-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-118.

Entry informationi

Entry nameiDGKA_HUMAN
AccessioniPrimary (citable) accession number: P23743
Secondary accession number(s): O75481
, O75482, O75483, O95217, Q3ZE25, Q8IZ56, Q8N5Q2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: December 15, 2009
Last modified: September 3, 2014
This is version 155 of the entry and version 3 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 12
    Human chromosome 12: 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

Dasty 3

Similar proteinsi