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Q9UIK4

- DAPK2_HUMAN

UniProt

Q9UIK4 - DAPK2_HUMAN

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Protein

Death-associated protein kinase 2

Gene

DAPK2

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

Functioni

Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Regulates both type I apoptotic and type II autophagic cell deaths signal, depending on the cellular setting. The former is caspase-dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Acts as a mediator of anoikis and a suppressor of beta-catenin-dependent anchorage-independent growth of malignant epithelial cells. May play a role in granulocytic maturation.
Isoform 2 is not regulated by calmodulin. It can phosphorylate MYL9. It can induce membrane blebbing and autophagic cell death.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+3 Publications

Enzyme regulationi

Activated by Ca2+/calmodulin. Regulated by a double locking mechanism, involving autophosphorylation at Ser-318, calmodulin binding, and dimerization. In the inactive state, Ser-318 is phosphorylated, and the kinase is dimeric. Activation involves: dephosphorylation at Ser-318, release-of-autoinhibition mechanism where calmodulin binding induces a conformational change that relieves the steric block of the active site by the autoinhibitory domain, and generation of the monomeric active form of the kinase.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521ATP2 PublicationsPROSITE-ProRule annotation
Active sitei149 – 1491Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 379ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. calmodulin binding Source: UniProtKB
  3. calmodulin-dependent protein kinase activity Source: RefGenome
  4. identical protein binding Source: IntAct
  5. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. anoikis Source: UniProtKB
  2. apoptotic process Source: UniProtKB
  3. intracellular signal transduction Source: UniProtKB
  4. protein autophosphorylation Source: UniProtKB
  5. protein phosphorylation Source: UniProtKB
  6. regulation of apoptotic process Source: UniProtKB
  7. regulation of autophagy Source: UniProtKB
  8. regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_22128. Role of DCC in regulating apoptosis.
SignaLinkiQ9UIK4.

Names & Taxonomyi

Protein namesi
Recommended name:
Death-associated protein kinase 2 (EC:2.7.11.1)
Short name:
DAP kinase 2
Alternative name(s):
DAP-kinase-related protein 1
Short name:
DRP-1
Gene namesi
Name:DAPK2
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:2675. DAPK2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic vesicle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521K → A: Loss of activity, apoptotic function and of autophosphorylation. 3 Publications
Mutagenesisi299 – 33032Missing: Loss of ca(2+)-calmodulin binding, increase in activity, loss of autophosphorylation. Add
BLAST
Mutagenesisi299 – 2991S → A: No effect on Ca(2+)-calmodulin independent phosphorylation or apoptotic activity. 1 Publication
Mutagenesisi318 – 3181S → A: Loss of Ca(2+)-calmodulin independent phosphorylation, increase in apoptotic activity. 1 Publication
Mutagenesisi318 – 3181S → D: Abolishes apoptotic activity. 1 Publication
Mutagenesisi320 – 3201S → A: No effect on Ca(2+)-calmodulin independent phosphorylation or apoptotic activity. 1 Publication
Mutagenesisi323 – 3231S → A: No effect on Ca(2+)-calmodulin independent phosphorylation or apoptotic activity. 1 Publication
Mutagenesisi329 – 3291T → A: No effect on Ca(2+)-calmodulin independent phosphorylation or apoptotic activity. 1 Publication

Organism-specific databases

PharmGKBiPA27143.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 370370Death-associated protein kinase 2PRO_0000085912Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei299 – 2991PhosphoserineBy similarity
Modified residuei318 – 3181Phosphoserine; by autocatalysis1 Publication
Modified residuei349 – 3491Phosphoserine1 Publication

Post-translational modificationi

Autophosphorylation at Ser-318 inhibits its catalytic activity. Dephosphorylated at Ser-318 in response to activated Fas and TNF-alpha receptors.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UIK4.
PaxDbiQ9UIK4.
PRIDEiQ9UIK4.

PTM databases

PhosphoSiteiQ9UIK4.

Expressioni

Tissue specificityi

Isoform 2 is expressed in embryonic stem cells (at protein level). Isoform 1 is ubiquitously expressed in all tissue types examined with high levels in heart, lung and skeletal muscle. It is expressed abundantly in cells differentiated toward granulocytes and low in undifferentiated, normal and leukemic hematopoietic cells and monocytes/macrophages.3 Publications

Inductioni

Up-regulated during granulocytic maturation.1 Publication

Gene expression databases

BgeeiQ9UIK4.
CleanExiHS_DAPK2.
ExpressionAtlasiQ9UIK4. baseline and differential.
GenevestigatoriQ9UIK4.

Interactioni

Subunit structurei

Homodimer in its autoinhibited state. Active as monomer (By similarity). Isoform 2 but not isoform 1 can interact with ATF4.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-77154,EBI-77154
ATF4P188482EBI-9693115,EBI-492498

Protein-protein interaction databases

BioGridi117137. 2 interactions.
IntActiQ9UIK4. 1 interaction.
STRINGi9606.ENSP00000261891.

Structurei

Secondary structure

1
370
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 224Combined sources
Beta strandi23 – 319Combined sources
Beta strandi33 – 4210Combined sources
Turni43 – 453Combined sources
Beta strandi48 – 569Combined sources
Beta strandi58 – 614Combined sources
Beta strandi63 – 664Combined sources
Helixi68 – 8013Combined sources
Beta strandi89 – 946Combined sources
Beta strandi96 – 1038Combined sources
Helixi111 – 1166Combined sources
Helixi123 – 14220Combined sources
Beta strandi144 – 1463Combined sources
Helixi152 – 1543Combined sources
Beta strandi155 – 1584Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi167 – 1693Combined sources
Helixi191 – 1933Combined sources
Helixi196 – 1994Combined sources
Helixi207 – 22216Combined sources
Helixi232 – 2409Combined sources
Helixi248 – 2514Combined sources
Helixi256 – 2638Combined sources
Turni270 – 2723Combined sources
Helixi276 – 2816Combined sources
Turni283 – 2853Combined sources
Helixi290 – 2989Combined sources
Helixi303 – 31210Combined sources
Helixi314 – 32815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WMKX-ray3.60A/B/C/D/E/F/G/H11-330[»]
1WRZX-ray2.00B312-330[»]
1Z9XX-ray3.93A/B/C11-330[»]
1ZUZX-ray1.91B312-330[»]
1ZWSX-ray2.90A/B/C/D/E/F/G/H11-297[»]
2A27X-ray3.00A/B/C/D/E/F/G/H11-330[»]
2A2AX-ray1.47A/B/C/D11-330[»]
2CKEX-ray2.80A/B/C/D11-330[»]
ProteinModelPortaliQ9UIK4.
SMRiQ9UIK4. Positions 12-315.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UIK4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 285263Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni277 – 34468Calmodulin-bindingAdd
BLAST
Regioni292 – 30110Autoinhibitory domainBy similarity

Domaini

The autoinhibitory domain sterically blocks the substrate peptide-binding site by making both hydrophobic and electrostatic contacts with the kinase core.By similarity

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118877.
HOGENOMiHOG000233016.
HOVERGENiHBG100551.
InParanoidiQ9UIK4.
KOiK08803.
OMAiCNHLSRS.
PhylomeDBiQ9UIK4.
TreeFamiTF314166.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR020675. Myosin_light_ch_kinase-rel.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR22964. PTHR22964. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UIK4-1) [UniParc]FASTAAdd to Basket

Also known as: Alpha

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
MFQASMRSPN MEPFKQQKVE DFYDIGEELG SGQFAIVKKC REKSTGLEYA
60 70 80 90 100
AKFIKKRQSR ASRRGVSREE IEREVSILRQ VLHHNVITLH DVYENRTDVV
110 120 130 140 150
LILELVSGGE LFDFLAQKES LSEEEATSFI KQILDGVNYL HTKKIAHFDL
160 170 180 190 200
KPENIMLLDK NIPIPHIKLI DFGLAHEIED GVEFKNIFGT PEFVAPEIVN
210 220 230 240 250
YEPLGLEADM WSIGVITYIL LSGASPFLGD TKQETLANIT AVSYDFDEEF
260 270 280 290 300
FSQTSELAKD FIRKLLVKET RKRLTIQEAL RHPWITPVDN QQAMVRRESV
310 320 330 340 350
VNLENFRKQY VRRRWKLSFS IVSLCNHLTR SLMKKVHLRP DEDLRNCESD
360 370
TEEDIARRKA LHPRRRSSTS
Length:370
Mass (Da):42,898
Last modified:May 1, 2000 - v1
Checksum:i035E914BBCD881A2
GO
Isoform 2 (identifier: Q9UIK4-2) [UniParc]FASTAAdd to Basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     287-370: PVDNQQAMVR...LHPRRRSSTS → SKGEGRAPEQ...TEEFLAGWKL

Note: Contains a leucine zipper at positions 434-451.

Show »
Length:488
Mass (Da):55,931
Checksum:i34F716A709C569B8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti241 – 2411A → S in AAC35001. (PubMed:10629061)Curated
Sequence conflicti253 – 2531Q → H in AAC35001. (PubMed:10629061)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601R → W.1 Publication
Corresponds to variant rs56047843 [ dbSNP | Ensembl ].
VAR_040436
Natural varianti271 – 2711R → W.1 Publication
Corresponds to variant rs34270163 [ dbSNP | Ensembl ].
VAR_040437

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei287 – 37084PVDNQ…RSSTS → SKGEGRAPEQRKTEPTQLKT KHLREYTLKCHSSMPPNNSY VNFERFACVVEDVARVDLGC RALVEAHDTIQDDVEALVSI FNEKEAWYREENESARHDLS QLRYEFRKVESLKKLLREDI QATGCSLGSMARKLDHLQAQ FEILRQELSADLQWIQELVG SFQLESGSSEGLGSTFYQDT SESLSELLSRSCTEEFLAGW KL in isoform 2. 1 PublicationVSP_042057Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018001 mRNA. Translation: BAA88063.1.
AF052941 mRNA. Translation: AAC35001.1.
GU056176 mRNA. Translation: ADD83109.1.
AC015914 Genomic DNA. No translation available.
AC021541 Genomic DNA. No translation available.
BC114506 mRNA. Translation: AAI14507.1.
CCDSiCCDS10188.1. [Q9UIK4-1]
RefSeqiNP_055141.2. NM_014326.3. [Q9UIK4-1]
XP_005254323.1. XM_005254266.2. [Q9UIK4-2]
UniGeneiHs.237886.

Genome annotation databases

GeneIDi23604.
KEGGihsa:23604.
UCSCiuc002amr.3. human. [Q9UIK4-1]

Polymorphism databases

DMDMi38605084.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018001 mRNA. Translation: BAA88063.1 .
AF052941 mRNA. Translation: AAC35001.1 .
GU056176 mRNA. Translation: ADD83109.1 .
AC015914 Genomic DNA. No translation available.
AC021541 Genomic DNA. No translation available.
BC114506 mRNA. Translation: AAI14507.1 .
CCDSi CCDS10188.1. [Q9UIK4-1 ]
RefSeqi NP_055141.2. NM_014326.3. [Q9UIK4-1 ]
XP_005254323.1. XM_005254266.2. [Q9UIK4-2 ]
UniGenei Hs.237886.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WMK X-ray 3.60 A/B/C/D/E/F/G/H 11-330 [» ]
1WRZ X-ray 2.00 B 312-330 [» ]
1Z9X X-ray 3.93 A/B/C 11-330 [» ]
1ZUZ X-ray 1.91 B 312-330 [» ]
1ZWS X-ray 2.90 A/B/C/D/E/F/G/H 11-297 [» ]
2A27 X-ray 3.00 A/B/C/D/E/F/G/H 11-330 [» ]
2A2A X-ray 1.47 A/B/C/D 11-330 [» ]
2CKE X-ray 2.80 A/B/C/D 11-330 [» ]
ProteinModelPortali Q9UIK4.
SMRi Q9UIK4. Positions 12-315.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117137. 2 interactions.
IntActi Q9UIK4. 1 interaction.
STRINGi 9606.ENSP00000261891.

Chemistry

BindingDBi Q9UIK4.
ChEMBLi CHEMBL3123.
GuidetoPHARMACOLOGYi 2003.

PTM databases

PhosphoSitei Q9UIK4.

Polymorphism databases

DMDMi 38605084.

Proteomic databases

MaxQBi Q9UIK4.
PaxDbi Q9UIK4.
PRIDEi Q9UIK4.

Protocols and materials databases

DNASUi 23604.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 23604.
KEGGi hsa:23604.
UCSCi uc002amr.3. human. [Q9UIK4-1 ]

Organism-specific databases

CTDi 23604.
GeneCardsi GC15M064199.
HGNCi HGNC:2675. DAPK2.
neXtProti NX_Q9UIK4.
PharmGKBi PA27143.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118877.
HOGENOMi HOG000233016.
HOVERGENi HBG100551.
InParanoidi Q9UIK4.
KOi K08803.
OMAi CNHLSRS.
PhylomeDBi Q9UIK4.
TreeFami TF314166.

Enzyme and pathway databases

Reactomei REACT_22128. Role of DCC in regulating apoptosis.
SignaLinki Q9UIK4.

Miscellaneous databases

ChiTaRSi DAPK2. human.
EvolutionaryTracei Q9UIK4.
GeneWikii DAPK2.
GenomeRNAii 23604.
NextBioi 35500973.
PROi Q9UIK4.

Gene expression databases

Bgeei Q9UIK4.
CleanExi HS_DAPK2.
ExpressionAtlasi Q9UIK4. baseline and differential.
Genevestigatori Q9UIK4.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR020675. Myosin_light_ch_kinase-rel.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
PANTHERi PTHR22964. PTHR22964. 1 hit.
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Death-associated protein kinase 2 is a new calcium/calmodulin-dependent protein kinase that signals apoptosis through its catalytic activity."
    Kawai T., Nomura F., Hoshino K., Copeland N.G., Gilbert D.J., Jenkins N.A., Akira S.
    Oncogene 18:3471-3480(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-52.
    Tissue: Skeletal muscle1 Publication.
  2. "Death-associated protein kinase-related protein 1, a novel serine/threonine kinase involved in apoptosis."
    Inbal B., Shani G., Cohen O., Kissil J.L., Kimchi A.
    Mol. Cell. Biol. 20:1044-1054(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, HOMODIMERIZATION, MUTAGENESIS OF LYS-52.
    Tissue: KidneyImported.
  3. "New modularity of DAP-kinases: alternative splicing of the DRP-1 gene produces a ZIPk-like isoform."
    Shoval Y., Berissi H., Kimchi A., Pietrokovski S.
    PLoS ONE 6:E17344-E17344(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), TISSUE SPECIFICITY, INTERACTION WITH ATF4 (ISOFORM 2).
  4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(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].
  6. "Autophosphorylation restrains the apoptotic activity of DRP-1 kinase by controlling dimerization and calmodulin binding."
    Shani G., Henis-Korenblit S., Jona G., Gileadi O., Eisenstein M., Ziv T., Admon A., Kimchi A.
    EMBO J. 20:1099-1113(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HOMODIMERIZATION, MUTAGENESIS OF LYS-52; SER-299; SER-318; SER-320; SER-323 AND THR-329, PHOSPHORYLATION AT SER-318.
  7. "The DAP-kinase family of proteins: study of a novel group of calcium-regulated death-promoting kinases."
    Shohat G., Shani G., Eisenstein M., Kimchi A.
    Biochim. Biophys. Acta 1600:45-50(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  8. "DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death."
    Inbal B., Bialik S., Sabanay I., Shani G., Kimchi A.
    J. Cell Biol. 157:455-468(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "The death-associated protein kinases: structure, function, and beyond."
    Bialik S., Kimchi A.
    Annu. Rev. Biochem. 75:189-210(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  10. "The death-associated protein kinase 2 is up-regulated during normal myeloid differentiation and enhances neutrophil maturation in myeloid leukemic cells."
    Rizzi M., Tschan M.P., Britschgi C., Britschgi A., Huegli B., Grob T.J., Leupin N., Mueller B.U., Simon H.U., Ziemiecki A., Torbett B.E., Fey M.F., Tobler A.
    J. Leukoc. Biol. 81:1599-1608(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Down-regulation of death-associated protein kinase-2 is required for beta-catenin-induced anoikis resistance of malignant epithelial cells."
    Li H., Ray G., Yoo B.H., Erdogan M., Rosen K.V.
    J. Biol. Chem. 284:2012-2022(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] TRP-60 AND TRP-271.

Entry informationi

Entry nameiDAPK2_HUMAN
AccessioniPrimary (citable) accession number: Q9UIK4
Secondary accession number(s): E9JGM7, O75892, Q24JS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: May 1, 2000
Last modified: November 26, 2014
This is version 138 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 15
    Human chromosome 15: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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