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Protein

Death-associated protein kinase 3

Gene

DAPK3

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

Functioni

Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Involved in the regulation of smooth muscle contraction. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involved in regulation of starvation-induced autophagy. Regulates myosin phosphorylation in both smooth muscle and non-muscle cells. In smooth muscle, regulates myosin either directly by phosphorylating MYL12B and MYL9 or through inhibition of smooth muscle myosin phosphatase (SMPP1M) via phosphorylation of PPP1R12A; the inhibition of SMPP1M functions to enhance muscle responsiveness to Ca2+ and promote a contractile state. Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton. Isoform 2 can phosphorylate myosin, PPP1R12A and MYL12B. Overexpression leads to condensation of actin stress fibers into thick bundles. Involved in actin filament focal adhesion dynamics. The function in both reorganization of actin cytoskeleton and focal adhesion dissolution is modulated by RhoD. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2. Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, RPL13A association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Involved in regulation of cell cycle progression and cell proliferation. May be a tumor suppressor.16 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.6 Publications

Cofactori

Mg2+1 Publication

Enzyme regulationi

A sequential activation is proposed: autophosphorylation at consensus sites is leading to dimerization of the catalytic domain stabilized by phosphorylation at Ser-50 and activation segment exchange (producing an active confirmation of both kinase modules in trans) followed by phosphorylation at Thr-180 in the activation segment and at other regulatory sites (Probable). Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity. Oligomerization is required for full enzymatic activity. Inhibited by pyridone 6 (K00225), a potent, ATP-competitive inhibitor.1 Publication3 Publications

Kineticsi

  1. KM=12 µM for myosin (isoform 2)1 Publication
  2. KM=6.2 µM for myosin (isoform 1)1 Publication
  3. KM=73 µM for MYL12B (isoform 2)1 Publication
  4. KM=10.4 µM for MYL12B (isoform 1)1 Publication
  1. Vmax=248 nmol/min/mg enzyme toward myosin (isoform 2)1 Publication
  2. Vmax=120 nmol/min/mg enzyme toward myosin (isoform 1)1 Publication
  3. Vmax=1.3 µmol/min/mg enzyme toward MYL12B (isoform 2)1 Publication
  4. Vmax=271 nmol/min/mg enzyme toward MYL12B (isoform 1)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei42ATPCurated1
Binding sitei94Inhibitor1 Publication1
Binding sitei96Inhibitor1 Publication1
Active sitei139Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi19 – 27ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • cAMP response element binding protein binding Source: ParkinsonsUK-UCL
  • leucine zipper domain binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • Rho GTPase binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • apoptotic signaling pathway Source: Ensembl
  • cellular response to interferon-gamma Source: UniProtKB
  • chromatin modification Source: UniProtKB-KW
  • cytokinesis Source: UniProtKB
  • intracellular signal transduction Source: UniProtKB
  • negative regulation of translation Source: UniProtKB
  • neuron differentiation Source: Ensembl
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  • positive regulation of cell migration Source: Ensembl
  • positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of actin cytoskeleton reorganization Source: UniProtKB
  • regulation of apoptotic process Source: UniProtKB
  • regulation of autophagy Source: UniProtKB
  • regulation of cell motility Source: UniProtKB
  • regulation of cell shape Source: Ensembl
  • regulation of focal adhesion assembly Source: UniProtKB
  • regulation of mitotic cell cycle Source: UniProtKB
  • regulation of mitotic nuclear division Source: UniProtKB
  • regulation of myosin II filament organization Source: Ensembl
  • regulation of smooth muscle contraction Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation, Translation regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS09602-MONOMER.
ReactomeiR-HSA-418889. Ligand-independent caspase activation via DCC.
SignaLinkiO43293.
SIGNORiO43293.

Names & Taxonomyi

Protein namesi
Recommended name:
Death-associated protein kinase 3 (EC:2.7.11.16 Publications)
Short name:
DAP kinase 3
Alternative name(s):
DAP-like kinase
Short name:
Dlk
MYPT1 kinase
Zipper-interacting protein kinase
Short name:
ZIP-kinase
Gene namesi
Name:DAPK3
Synonyms:ZIPK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:2676. DAPK3.

Subcellular locationi

Isoform 1 :
  • Nucleus 1 Publication
  • Cytoplasm 1 Publication
Isoform 2 :
  • Nucleus 1 Publication
  • Cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi42K → A: Loss of kinase activity at low concentrations of ATP. 1 Publication1
Mutagenesisi161D → A: Loss of kinase activity. 1 Publication1
Mutagenesisi180T → A: Greatly reduced kinase activity. 1 Publication1
Mutagenesisi225T → A: Loss of kinase activity. 1 Publication1
Mutagenesisi265T → A: Loss of phosphorylation by ROCK1, catalytically inactive. 1 Publication1
Mutagenesisi294 – 295RR → AA: Cytoplasmic loalization. 1 Publication2
Mutagenesisi299 – 300TT → AA: Predominantly nuclear localization. 1 Publication2
Mutagenesisi299T → A: Loss of phosphorylation by ROCK1. 1 Publication1
Mutagenesisi299T → D: Predominantly cytoplasmic localization; phosphomimetic. 1 Publication1
Mutagenesisi427V → A: Predominantly nuclear localization; when associated with A-434 and A-441. 1 Publication1
Mutagenesisi434V → A: Predominantly nuclear localization; when associated with A-427 and A-441. 1 Publication1
Mutagenesisi441L → A: Predominantly nuclear localization; when associated with A-427 and A-434. 1 Publication1

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNETi1613.
OpenTargetsiENSG00000167657.
PharmGKBiPA27144.

Chemistry databases

ChEMBLiCHEMBL2468.
GuidetoPHARMACOLOGYi2004.

Polymorphism and mutation databases

BioMutaiDAPK3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000859141 – 454Death-associated protein kinase 3Add BLAST454

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei50Phosphoserine; by autocatalysis1 Publication1
Modified residuei180Phosphothreonine2 Publications1
Modified residuei225Phosphothreonine1 Publication1
Modified residuei265Phosphothreonine; by autocatalysis and ROCK13 Publications1
Modified residuei299Phosphothreonine; by autocatalysis, DAPK1 and ROCK14 Publications1
Modified residuei306Phosphothreonine; by autocatalysis1 Publication1
Modified residuei309Phosphoserine; by DAPK11 Publication1
Modified residuei311Phosphoserine; by autocatalysis and DAPK12 Publications1
Modified residuei312Phosphoserine; by DAPK1Combined sources1 Publication1
Modified residuei318Phosphoserine; by DAPK11 Publication1
Modified residuei326Phosphoserine; by DAPK11 Publication1

Post-translational modificationi

The phosphorylation status is critical for kinase activity, oligomerization and intracellular localization. Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity. The phosphorylated form is localized in the cytoplasm promoted by phosphorylation at Thr-299; nuclear translocation or retention is maximal when it is not phosphorylated. Phosphorylation increases the trimeric form, and its dephosphorylation favors a kinase-inactive monomeric form. Both isoform 1 and isoform 2 can undergo autophosphorylation.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO43293.
MaxQBiO43293.
PaxDbiO43293.
PeptideAtlasiO43293.
PRIDEiO43293.

PTM databases

iPTMnetiO43293.
PhosphoSitePlusiO43293.

Expressioni

Tissue specificityi

Widely expressed. Isoform 1 and isoform 2 are expressed in the bladder smooth muscle.2 Publications

Gene expression databases

BgeeiENSG00000167657.
CleanExiHS_DAPK3.
ExpressionAtlasiO43293. baseline and differential.
GenevisibleiO43293. HS.

Organism-specific databases

HPAiHPA028569.
HPA064809.

Interactioni

Subunit structurei

Homooligomer in its kinase-active form (homotrimers and homodimers are reported); monomeric in its kinase-inactive form. Homodimerization is required for activation segment autophosphorylation (Probable). Isoform 1 and isoform 2 interact with myosin and PPP1R12A; interaction of isoform 1 with PPP1R12A is inhibited by RhoA dominant negative form. Interacts with NLK, DAXX, STAT3, RHOD (GTP-bound form) and TCP10L. Interacts with PAWR; the interaction is reported conflictingly: according to PubMed:17953487 does not interact with PAWR. Interacts with ULK1; may be a substrate of ULK1.1 Publication10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-77293,EBI-77293
PPP1R12AO149745EBI-77293,EBI-351726
Ppp1r12aQ107282EBI-9691390,EBI-918263From a different organism.
TCP10LQ8TDR45EBI-77293,EBI-3923210

GO - Molecular functioni

  • cAMP response element binding protein binding Source: ParkinsonsUK-UCL
  • leucine zipper domain binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • Rho GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107983. 55 interactors.
IntActiO43293. 45 interactors.
MINTiMINT-6505325.
STRINGi9606.ENSP00000301264.

Chemistry databases

BindingDBiO43293.

Structurei

Secondary structure

1454
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 12Combined sources4
Beta strandi13 – 21Combined sources9
Beta strandi23 – 32Combined sources10
Turni33 – 35Combined sources3
Beta strandi38 – 46Combined sources9
Helixi49 – 51Combined sources3
Beta strandi53 – 56Combined sources4
Helixi58 – 70Combined sources13
Beta strandi79 – 84Combined sources6
Beta strandi86 – 94Combined sources9
Helixi101 – 108Combined sources8
Helixi113 – 132Combined sources20
Helixi142 – 144Combined sources3
Beta strandi145 – 148Combined sources4
Beta strandi150 – 154Combined sources5
Beta strandi157 – 159Combined sources3
Helixi171 – 175Combined sources5
Helixi176 – 178Combined sources3
Helixi181 – 183Combined sources3
Helixi186 – 189Combined sources4
Helixi197 – 212Combined sources16
Helixi222 – 230Combined sources9
Helixi238 – 241Combined sources4
Helixi246 – 253Combined sources8
Helixi260 – 262Combined sources3
Helixi266 – 271Combined sources6
Helixi273 – 280Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YRPX-ray3.10A/B1-277[»]
2J90X-ray2.00A/B9-289[»]
3BHYX-ray1.24A9-289[»]
3BQRX-ray1.75A9-289[»]
5A6NX-ray1.70A/B9-289[»]
5A6OX-ray1.60A/B9-289[»]
ProteinModelPortaliO43293.
SMRiO43293.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43293.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 275Protein kinasePROSITE-ProRule annotationAdd BLAST263

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni161 – 204Activation segmentBy similarityAdd BLAST44
Regioni427 – 441Leucine-zipper1 PublicationAdd BLAST15

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0032. Eukaryota.
ENOG410XRMJ. LUCA.
GeneTreeiENSGT00760000118877.
HOGENOMiHOG000233016.
HOVERGENiHBG101549.
InParanoidiO43293.
KOiK08803.
OMAiSLEHPWI.
OrthoDBiEOG091G0J2O.
PhylomeDBiO43293.
TreeFamiTF314166.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 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. AlignAdd to basket

Isoform 1 (identifier: O43293-1) [UniParc]FASTAAdd to basket
Also known as: ZIPK-L

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
MSTFRQEDVE DHYEMGEELG SGQFAIVRKC RQKGTGKEYA AKFIKKRRLS
60 70 80 90 100
SSRRGVSREE IEREVNILRE IRHPNIITLH DIFENKTDVV LILELVSGGE
110 120 130 140 150
LFDFLAEKES LTEDEATQFL KQILDGVHYL HSKRIAHFDL KPENIMLLDK
160 170 180 190 200
NVPNPRIKLI DFGIAHKIEA GNEFKNIFGT PEFVAPEIVN YEPLGLEADM
210 220 230 240 250
WSIGVITYIL LSGASPFLGE TKQETLTNIS AVNYDFDEEY FSNTSELAKD
260 270 280 290 300
FIRRLLVKDP KRRMTIAQSL EHSWIKAIRR RNVRGEDSGR KPERRRLKTT
310 320 330 340 350
RLKEYTIKSH SSLPPNNSYA DFERFSKVLE EAAAAEEGLR ELQRSRRLCH
360 370 380 390 400
EDVEALAAIY EEKEAWYREE SDSLGQDLRR LRQELLKTEA LKRQAQEEAK
410 420 430 440 450
GALLGTSGLK RRFSRLENRY EALAKQVASE MRFVQDLVRA LEQEKLQGVE

CGLR
Length:454
Mass (Da):52,536
Last modified:June 1, 1998 - v1
Checksum:i56773008A6A61CF0
GO
Isoform 2 (identifier: O43293-2) [UniParc]FASTAAdd to basket
Also known as: ZIPK-S

The sequence of this isoform differs from the canonical sequence as follows:
     313-322: LPPNNSYADF → ASPIVAPVDA
     323-454: Missing.

Note: The internal splice site between exon 8 and the 3' UTR, which yields this truncated isoform, is non-canonical.
Show »
Length:322
Mass (Da):37,048
Checksum:i616983FE83F8DDA6
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_040438112T → M in a colorectal adenocarcinoma sample; somatic mutation; greatly reduces kinase acivity, increases cell proliferation and cell survival. 2 Publications1
Natural variantiVAR_040439161D → N in an ovarian mucinous carcinoma sample; somatic mutation; greatly reduces kinase acivity, increases cell proliferation and cell survival. 2 Publications1
Natural variantiVAR_040440216P → S in a lung neuroendocrine carcinoma sample; somatic mutation; greatly reduces kinase acivity, increases cell proliferation, cell adhesion and cell survival. 2 Publications1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_042059313 – 322LPPNNSYADF → ASPIVAPVDA in isoform 2. 1 Publication10
Alternative sequenceiVSP_042060323 – 454Missing in isoform 2. 1 PublicationAdd BLAST132

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007144 mRNA. Translation: BAA24955.1.
AB022341 mRNA. Translation: BAA81746.1.
AK074799 mRNA. Translation: BAG52004.1.
BC126430 mRNA. Translation: AAI26431.1.
BC126432 mRNA. Translation: AAI26433.1.
AB265224 mRNA. Translation: BAF34614.1.
CCDSiCCDS12116.1. [O43293-1]
RefSeqiNP_001339.1. NM_001348.2. [O43293-1]
XP_005259565.1. XM_005259508.1. [O43293-1]
UniGeneiHs.631844.

Genome annotation databases

EnsembliENST00000301264; ENSP00000301264; ENSG00000167657. [O43293-1]
ENST00000545797; ENSP00000442973; ENSG00000167657. [O43293-1]
GeneIDi1613.
KEGGihsa:1613.
UCSCiuc002lzc.2. human. [O43293-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007144 mRNA. Translation: BAA24955.1.
AB022341 mRNA. Translation: BAA81746.1.
AK074799 mRNA. Translation: BAG52004.1.
BC126430 mRNA. Translation: AAI26431.1.
BC126432 mRNA. Translation: AAI26433.1.
AB265224 mRNA. Translation: BAF34614.1.
CCDSiCCDS12116.1. [O43293-1]
RefSeqiNP_001339.1. NM_001348.2. [O43293-1]
XP_005259565.1. XM_005259508.1. [O43293-1]
UniGeneiHs.631844.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YRPX-ray3.10A/B1-277[»]
2J90X-ray2.00A/B9-289[»]
3BHYX-ray1.24A9-289[»]
3BQRX-ray1.75A9-289[»]
5A6NX-ray1.70A/B9-289[»]
5A6OX-ray1.60A/B9-289[»]
ProteinModelPortaliO43293.
SMRiO43293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107983. 55 interactors.
IntActiO43293. 45 interactors.
MINTiMINT-6505325.
STRINGi9606.ENSP00000301264.

Chemistry databases

BindingDBiO43293.
ChEMBLiCHEMBL2468.
GuidetoPHARMACOLOGYi2004.

PTM databases

iPTMnetiO43293.
PhosphoSitePlusiO43293.

Polymorphism and mutation databases

BioMutaiDAPK3.

Proteomic databases

EPDiO43293.
MaxQBiO43293.
PaxDbiO43293.
PeptideAtlasiO43293.
PRIDEiO43293.

Protocols and materials databases

DNASUi1613.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301264; ENSP00000301264; ENSG00000167657. [O43293-1]
ENST00000545797; ENSP00000442973; ENSG00000167657. [O43293-1]
GeneIDi1613.
KEGGihsa:1613.
UCSCiuc002lzc.2. human. [O43293-1]

Organism-specific databases

CTDi1613.
DisGeNETi1613.
GeneCardsiDAPK3.
HGNCiHGNC:2676. DAPK3.
HPAiHPA028569.
HPA064809.
MIMi603289. gene.
neXtProtiNX_O43293.
OpenTargetsiENSG00000167657.
PharmGKBiPA27144.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0032. Eukaryota.
ENOG410XRMJ. LUCA.
GeneTreeiENSGT00760000118877.
HOGENOMiHOG000233016.
HOVERGENiHBG101549.
InParanoidiO43293.
KOiK08803.
OMAiSLEHPWI.
OrthoDBiEOG091G0J2O.
PhylomeDBiO43293.
TreeFamiTF314166.

Enzyme and pathway databases

BioCyciZFISH:HS09602-MONOMER.
ReactomeiR-HSA-418889. Ligand-independent caspase activation via DCC.
SignaLinkiO43293.
SIGNORiO43293.

Miscellaneous databases

ChiTaRSiDAPK3. human.
EvolutionaryTraceiO43293.
GeneWikiiDAPK3.
GenomeRNAii1613.
PROiO43293.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000167657.
CleanExiHS_DAPK3.
ExpressionAtlasiO43293. baseline and differential.
GenevisibleiO43293. HS.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiDAPK3_HUMAN
AccessioniPrimary (citable) accession number: O43293
Secondary accession number(s): A0AVN4, B3KQE2, Q05JY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: June 1, 1998
Last modified: November 2, 2016
This is version 159 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 19
    Human chromosome 19: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.