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Q13574 (DGKZ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Diacylglycerol kinase zeta

Short name=DAG kinase zeta
EC=2.7.1.107
Alternative name(s):
Diglyceride kinase zeta
Short name=DGK-zeta
Gene names
Name:DGKZ
Synonyms:DAGK6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1117 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. Isoform 2 but not isoform 1 regulates RASGRP1 activity. Ref.10

Catalytic activity

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

Subunit structure

Interacts with the PDZ domain of the syntrophin SNTG1 and that of SNX27. Isoform 2 forms a signaling complex with RASGRP1 and HRAS. Ref.9 Ref.10 Ref.11

Subcellular location

Cytoplasm. Nucleus. Cell membrane Ref.8 Ref.10.

Tissue specificity

Highest levels in brain, and substantial levels in skeletal muscle, heart, and pancreas. Isoform 1 is predominantly expressed in muscle.

Post-translational modification

Phosphorylation of the MARCKS homology domain by PKC reduces nuclear accumulation of DGK-zeta.

Sequence similarities

Belongs to the eukaryotic diacylglycerol kinase family.

Contains 2 ANK repeats.

Contains 1 DAGKc domain.

Contains 2 phorbol-ester/DAG-type zinc fingers.

Sequence caution

The sequence AAB60859.1 differs from that shown. Reason: Frameshift at positions 166 and 167.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainANK repeat
Repeat
Zinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

cell migration

Non-traceable author statement PubMed 15157668. Source: UniProtKB

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

lipid phosphorylation

Inferred from direct assay PubMed 16286473. Source: GOC

mitotic G1 DNA damage checkpoint

Inferred from genetic interaction PubMed 16286473. Source: UniProtKB

negative regulation of Ras protein signal transduction

Inferred from electronic annotation. Source: Ensembl

negative regulation of mitotic cell cycle

Inferred from genetic interaction PubMed 16286473. Source: UniProtKB

phosphorylation

Inferred from direct assay PubMed 16286473. Source: GOC

platelet activation

Traceable author statement. Source: Reactome

protein kinase C-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

lamellipodium

Inferred from direct assay PubMed 15157668. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 15157668PubMed 17664281. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Traceable author statement Ref.1. Source: ProtInc

NAD+ kinase activity

Inferred from electronic annotation. Source: InterPro

diacylglycerol kinase activity

Inferred from direct assay PubMed 16286473. Source: UniProtKB

enzyme inhibitor activity

Inferred from electronic annotation. Source: Ensembl

lipid kinase activity

Inferred from direct assay PubMed 16286473. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein C-terminus binding

Inferred from direct assay PubMed 16286473. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13574-1)

Also known as: Long; zeta2;

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.
Note: Minor isoform.
Isoform 2 (identifier: Q13574-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1-243: METFFRRHFR...GPQAWSALLA → MEPRDGSPEA...FPGLRLFGHR
Note: Major isoform.
Isoform 3 (identifier: Q13574-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-71: METFFRRHFR...SCGVRAQGSS → MAEGQGGGGQ...LHLRKQVSYR
     72-243: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q13574-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-243: METFFRRHFR...GPQAWSALLA → MEPRDGSPEA...FPGLRLFGHR
     311-311: L → LQ
Note: No experimental confirmation available.
Isoform 5 (identifier: Q13574-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-243: METFFRRHFR...GPQAWSALLA → MEPRDGSPEA...FPGLRLFGHR
     311-311: L → LQ
     1046-1046: N → NPCSPS
Note: No experimental confirmation available.
Isoform 6 (identifier: Q13574-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-243: METFFRRHFR...GPQAWSALLA → MEPRDGSPEA...FPGLRLFGHR
     311-311: L → LQ
     356-378: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11171117Diacylglycerol kinase zeta
PRO_0000218468

Regions

Domain480 – 614135DAGKc
Repeat1011 – 104131ANK 1
Repeat1046 – 107530ANK 2
Zinc finger287 – 34155Phorbol-ester/DAG-type 1
Zinc finger361 – 41959Phorbol-ester/DAG-type 2
Region448 – 46215MARCKS homology
Region467 – 605139Mediates interaction with RASGRP1
Motif550 – 5589Nuclear export signal By similarity
Compositional bias256 – 2616Poly-Pro
Compositional bias448 – 4514Poly-Lys
Compositional bias560 – 5634Poly-Pro

Natural variations

Alternative sequence1 – 243243METFF…SALLA → MEPRDGSPEARSSDSESASA SSSGSERDAGPEPDKAPRRL NKRRFPGLRLFGHR in isoform 2, isoform 4, isoform 5 and isoform 6.
VSP_001268
Alternative sequence1 – 7171METFF…AQGSS → MAEGQGGGGQRWDWAGGGRA AEEEVVRRRCRRGEEAQVAQ PWPEGSRGTAAGPPVEERFR QLHLRKQVSYR in isoform 3.
VSP_043163
Alternative sequence72 – 243172Missing in isoform 3.
VSP_043164
Alternative sequence3111L → LQ in isoform 4, isoform 5 and isoform 6.
VSP_045628
Alternative sequence356 – 37823Missing in isoform 6.
VSP_046919
Alternative sequence10461N → NPCSPS in isoform 5.
VSP_046920
Natural variant211Q → R. Ref.2
Corresponds to variant rs1317826 [ dbSNP | Ensembl ].
VAR_047371
Natural variant691G → C.
Corresponds to variant rs901998 [ dbSNP | Ensembl ].
VAR_061131
Natural variant7121Q → K. Ref.7
Corresponds to variant rs17854149 [ dbSNP | Ensembl ].
VAR_069059

Experimental info

Mutagenesis1115 – 11162TA → NS: Loss of interaction with SNTG1. Ref.9
Sequence conflict1591L → V in AAB60859. Ref.2
Sequence conflict4941G → W in BAH11915. Ref.3
Sequence conflict7831A → S in BAH11915. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) (zeta2) [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: F3A7C2382ECF549B

FASTA1,117124,128
        10         20         30         40         50         60 
METFFRRHFR GKVPGPGEGQ QRPSSVGLPT GKARRRSPAG QASSSLAQRR RSSAQLQGCL 

        70         80         90        100        110        120 
LSCGVRAQGS SRRRSSTVPP SCNPRFIVDK VLTPQPTTVG AQLLGAPLLL TGLVGMNEEE 

       130        140        150        160        170        180 
GVQEDVVAEA SSAIQPGTKT PGPPPPRGAQ PLLPLPRYLR RASSHLLPAD AVYDHALWGL 

       190        200        210        220        230        240 
HGYYRRLSQR RPSGQHPGPG GRRASGTTAG TMLPTRVRPL SRRRQVALRR KAAGPQAWSA 

       250        260        270        280        290        300 
LLAKAITKSG LQHLAPPPPT PGAPCSESER QIRSTVDWSE SATYGEHIWF ETNVSGDFCY 

       310        320        330        340        350        360 
VGEQYCVARM LKSVSRRKCA ACKIVVHTPC IEQLEKINFR CKPSFRESGS RNVREPTFVR 

       370        380        390        400        410        420 
HHWVHRRRQD GKCRHCGKGF QQKFTFHSKE IVAISCSWCK QAYHSKVSCF MLQQIEEPCS 

       430        440        450        460        470        480 
LGVHAAVVIP PTWILRARRP QNTLKASKKK KRASFKRKSS KKGPEEGRWR PFIIRPTPSP 

       490        500        510        520        530        540 
LMKPLLVFVN PKSGGNQGAK IIQSFLWYLN PRQVFDLSQG GPKEALEMYR KVHNLRILAC 

       550        560        570        580        590        600 
GGDGTVGWIL STLDQLRLKP PPPVAILPLG TGNDLARTLN WGGGYTDEPV SKILSHVEEG 

       610        620        630        640        650        660 
NVVQLDRWDL HAEPNPEAGP EDRDEGATDR LPLDVFNNYF SLGFDAHVTL EFHESREANP 

       670        680        690        700        710        720 
EKFNSRFRNK MFYAGTAFSD FLMGSSKDLA KHIRVVCDGM DLTPKIQDLK PQCVVFLNIP 

       730        740        750        760        770        780 
RYCAGTMPWG HPGEHHDFEP QRHDDGYLEV IGFTMTSLAA LQVGGHGERL TQCREVVLTT 

       790        800        810        820        830        840 
SKAIPVQVDG EPCKLAASRI RIALRNQATM VQKAKRRSAA PLHSDQQPVP EQLRIQVSRV 

       850        860        870        880        890        900 
SMHDYEALHY DKEQLKEASV PLGTVVVPGD SDLELCRAHI ERLQQEPDGA GAKSPTCQKL 

       910        920        930        940        950        960 
SPKWCFLDAT TASRFYRIDR AQEHLNYVTE IAQDEIYILD PELLGASARP DLPTPTSPLP 

       970        980        990       1000       1010       1020 
TSPCSPTPRS LQGDAAPPQG EELIEAAKRN DFCKLQELHR AGGDLMHRDE QSRTLLHHAV 

      1030       1040       1050       1060       1070       1080 
STGSKDVVRY LLDHAPPEIL DAVEENGETC LHQAAALGQR TICHYIVEAG ASLMKTDQQG 

      1090       1100       1110 
DTPRQRAEKA QDTELAAYLE NRQHYQMIQR EDQETAV 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: 7936A979CB3D35AA
Show »

FASTA928103,981
Isoform 3 [UniParc].

Checksum: 6EF612B9FE91F7E7
Show »

FASTA945106,030
Isoform 4 [UniParc].

Checksum: 362346DD9046B323
Show »

FASTA929104,109
Isoform 5 [UniParc].

Checksum: 3B9CEB5C58B865F7
Show »

FASTA934104,581
Isoform 6 [UniParc].

Checksum: 99789AD08DCCB5BD
Show »

FASTA906101,230

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of a novel human diacylglycerol kinase zeta."
Bunting M., Tang W., Zimmerman G.A., McIntyre T.M., Prescott S.M.
J. Biol. Chem. 271:10230-10236(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Endothelial cell.
[2]"Alternative splicing of the human diacylglycerol kinase zeta gene in muscle."
Ding L., Bunting M., Topham M.K., McIntyre T.M., Zimmerman G.A., Prescott S.M.
Proc. Natl. Acad. Sci. U.S.A. 94:5519-5524(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-21.
Tissue: Skeletal muscle.
[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 3 AND 6).
Tissue: Brain and Cerebellum.
[4]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Brain.
[5]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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 4), VARIANT LYS-712.
Tissue: Brain.
[8]"Protein kinase C regulates the nuclear localization of diacylglycerol kinase-zeta."
Topham M.K., Bunting M., Zimmerman G.A., McIntyre T.M., Blackshear P.J., Prescott S.M.
Nature 394:697-700(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
[9]"Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta. Regulation of nuclear localization by PDZ interactions."
Hogan A., Shepherd L., Chabot J., Quenneville S., Prescott S.M., Topham M.K., Gee S.H.
J. Biol. Chem. 276:26526-26533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNTG1, MUTAGENESIS OF 1115-THR-ALA-1116.
[10]"Diacylglycerol kinase zeta regulates Ras activation by a novel mechanism."
Topham M.K., Prescott S.M.
J. Cell Biol. 152:1135-1143(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A RASGRP1 REGULATOR, IDENTIFICATION IN A COMPLEX WITH RASGRP1 AND HRAS, SUBCELLULAR LOCATION.
[11]"Proteomics identification of sorting nexin 27 as a diacylglycerol kinase zeta-associated protein: new diacylglycerol kinase roles in endocytic recycling."
Rincon E., Santos T., Avila-Flores A., Albar J.P., Lalioti V., Lei C., Hong W., Merida I.
Mol. Cell. Proteomics 6:1073-1087(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNX27.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U51477 mRNA. Translation: AAC50478.1.
U94905 mRNA. Translation: AAB60859.1. Frameshift.
AK124594 mRNA. Translation: BAC85894.1.
AK294888 mRNA. Translation: BAH11915.1.
AK225774 mRNA. No translation available.
AC116021 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68008.1.
BC041770 mRNA. Translation: AAH41770.1.
RefSeqNP_001099010.1. NM_001105540.1.
NP_001186195.1. NM_001199266.1.
NP_001186196.1. NM_001199267.1.
NP_001186197.1. NM_001199268.1.
NP_003637.2. NM_003646.3.
NP_963290.1. NM_201532.2.
NP_963291.2. NM_201533.3.
UniGeneHs.502461.

3D structure databases

ProteinModelPortalQ13574.
SMRQ13574. Positions 980-1099.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114095. 19 interactions.
IntActQ13574. 11 interactions.
MINTMINT-198176.
STRING9606.ENSP00000320340.

PTM databases

PhosphoSiteQ13574.

Polymorphism databases

DMDM215274170.

Proteomic databases

PaxDbQ13574.
PRIDEQ13574.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318201; ENSP00000320340; ENSG00000149091. [Q13574-6]
ENST00000343674; ENSP00000343065; ENSG00000149091. [Q13574-3]
ENST00000421244; ENSP00000391021; ENSG00000149091. [Q13574-4]
ENST00000454345; ENSP00000412178; ENSG00000149091. [Q13574-1]
ENST00000456247; ENSP00000395684; ENSG00000149091. [Q13574-2]
ENST00000527911; ENSP00000436291; ENSG00000149091. [Q13574-5]
GeneID8525.
KEGGhsa:8525.
UCSCuc001nch.2. human. [Q13574-3]
uc001nck.2. human. [Q13574-1]
uc001ncl.2. human.
uc001ncm.2. human. [Q13574-2]

Organism-specific databases

CTD8525.
GeneCardsGC11P046311.
H-InvDBHIX0009600.
HIX0037561.
HGNCHGNC:2857. DGKZ.
HPAHPA051336.
MIM601441. gene.
neXtProtNX_Q13574.
PharmGKBPA27318.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47311.
HOGENOMHOG000231472.
HOVERGENHBG067303.
InParanoidQ13574.
KOK00901.
OMAQQEPDGA.
OrthoDBEOG76HQ0Q.
PhylomeDBQ13574.
TreeFamTF312817.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ13574.
BgeeQ13574.
CleanExHS_DGKZ.
GenevestigatorQ13574.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR016064. ATP-NAD_kinase_PpnK-typ.
IPR000756. Diacylglycerol_kin_accessory.
IPR001206. Diacylglycerol_kinase_cat_dom.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
[Graphical view]
PfamPF00023. Ank. 2 hits.
PF00130. C1_1. 1 hit.
PF00609. DAGK_acc. 1 hit.
PF00781. DAGK_cat. 1 hit.
[Graphical view]
SMARTSM00248. ANK. 2 hits.
SM00109. C1. 2 hits.
SM00045. DAGKa. 1 hit.
SM00046. DAGKc. 1 hit.
[Graphical view]
SUPFAMSSF111331. SSF111331. 1 hit.
SSF48403. SSF48403. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50146. DAGK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDGKZ. human.
GeneWikiDGKZ.
GenomeRNAi8525.
NextBio31916.
PROQ13574.
SOURCESearch...

Entry information

Entry nameDGKZ_HUMAN
AccessionPrimary (citable) accession number: Q13574
Secondary accession number(s): B7Z2M9 expand/collapse secondary AC list , E9PPW4, G3V0F6, J3KNJ6, O00542, Q6ZVG7, Q8IVW9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 144 of the entry and version 3 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

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 11

Human chromosome 11: entries, gene names and cross-references to MIM