P53355 (DAPK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Death-associated protein kinase 1
Short name=DAP kinase 1
EC=2.7.11.1

Gene names

Name:	DAPK1
Synonyms:	DAPK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1430 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Phosphorylates PIN1 resulting in inhibition of its catalytic activity, nuclear localization, and cellular function. Phosphorylates TPM1, enhancing stress fiber formation in endothelial cells. Phosphorylates STX1A and significantly decreases its binding to STXBP1. Phosphorylates PRKD1 and regulates JNK signaling by binding and activating PRKD1 under oxidative stress. Phosphorylates BECN1, reducing its interaction with BCL2 and BCL2L1 and promoting the induction of autophagy. Phosphorylates TSC2, disrupting the TSC1-TSC2 complex and stimulating mTORC1 activity in a growth factor-dependent pathway. Phosphorylates RPS6, MYL9 and DAPK3. Acts as a signaling amplifier of NMDA receptors at extrasynaptic sites for mediating brain damage in stroke. Cerebral ischemia recruits DAPK1 into the NMDA receptor complex and it phosphorylates GRINB at Ser-1303 inducing injurious Ca2+ influx through NMDA receptor channels, resulting in an irreversible neuronal death. Required together with DAPK3 for phosphorylation of RPL13A upon interferon-gamma activation which is causing RPL13A involvement in transcript-selective translation inhibition. Ref.1 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.30 Ref.31 Isoform 2 cannot induce apoptosis but can induce membrane blebbing. Ref.1 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.30 Ref.31
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Activated by Ca2+/calmodulin. Regulated by a locking mechanism, involving autophosphorylation at Ser-308 and calmodulin binding. In the inactive state, Ser-308 is phosphorylated. Activation involves its dephosphorylation and a release-of-autoinhibition mechanism where binding of calmodulin induces a conformational change that relieves the steric block of the active site by the autoinhibitory domain. Activity is modulated by UNC5B and NTN1. UNC5B activates it by inhibiting the phosphorylation at Ser-308, whereas NTN1 inhibits UNC5B-mediated activation of DAPK1. Endoplasmic-stress activates by causing Ser-308 dephosphorylation. Ref.11 Ref.18 Ref.20
Subunit structure	Interacts with KLHL20. Interacts (via death domain) with MAPK1 and MAPK3. Interacts with MAP1B (via N-terminus). Interacts (via death domain) with UNC5B (via death domain). Interacts with PRKD1 in an oxidative stress-regulated manner. Interacts with PIN1, PDCD6, BECN1, GRINB, TSC2 and STX1A. Interacts (via kinase domain) with DAPK3 (via kinase domain). Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.21 Ref.24 Ref.26 Ref.27 Ref.28 Ref.30
Subcellular location	Isoform 1: Cytoplasm. Cytoplasm › cytoskeleton Ref.10 Ref.12 Ref.23 Ref.24. Note: Colocalizes with MAP1B in the microtubules and cortical actin fibers. Ref.10 Ref.12 Ref.23 Ref.24 Isoform 2: Cytoplasm. Cytoplasm › cytoskeleton Ref.10 Ref.12 Ref.23 Ref.24.
Tissue specificity	Isoform 2 is expressed in normal intestinal tissue as well as in colorectal carcinomas. Ref.23
Induction	Up-regulated following treatment with IFNG/IFN-gamma. Ref.1 Ref.11 Ref.18 Ref.20
Domain	The autoinhibitory domain sterically blocks the substrate peptide-binding site by making both hydrophobic and electrostatic contacts with the kinase core.
Post-translational modification	Ubiquitinated by the BCR(KLHL20) E3 ubiquitin ligase complex, leading to its degradation by the proteasome. Ref.28 Removal of the C-terminal tail of isoform 2 (corresponding to amino acids 296-337 of isoform 2) by proteolytic cleavage stimulates maximally its membrane-blebbing function. In response to mitogenic stimulation (PMA or EGF), phosphorylated at Ser-289; phosphorylation suppresses DAPK1 pro-apoptotic function. Autophosphorylation at Ser-308 inhibits its catalytic activity. Phosphorylation at Ser-734 by MAPK1 increases its catalytic activity and promotes cytoplasmic retention of MAPK1. Endoplasmic-stress can cause dephosphorylation at Ser-308. Ref.11 Ref.16 Ref.17 Ref.18 Ref.20
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. DAP kinase subfamily. Contains 10 ANK repeats. Contains 1 death domain. Contains 1 protein kinase domain.
Sequence caution	The sequence AAP35581.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part. The sequence CAA53712.1 differs from that shown. Reason: Frameshift at positions 462 and 464.

Ontologies

Keywords
Biological process	Apoptosis Translation regulation
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Domain	ANK repeat Repeat
Ligand	ATP-binding Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic signaling pathway Inferred from mutant phenotype Ref.1. Source: UniProtKB cellular response to interferon-gamma Inferred from direct assay Ref.25. Source: UniProtKB induction of apoptosis Inferred from mutant phenotype Ref.10. Source: UniProtKB intracellular protein kinase cascade Inferred from direct assay Ref.10. Source: UniProtKB negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of translation Inferred from direct assay Ref.25. Source: UniProtKB protein autophosphorylation Traceable author statement Ref.19. Source: UniProtKB regulation of N-methyl-D-aspartate selective glutamate receptor activity Inferred from sequence or structural similarity. Source: UniProtKB regulation of autophagy Traceable author statement Ref.19. Source: UniProtKB
Cellular_component	actin cytoskeleton Inferred from direct assay Ref.10. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from direct assay Ref.10. Source: UniProtKB calmodulin binding Inferred from direct assay Ref.10. Source: UniProtKB protein serine/threonine kinase activity Traceable author statement Ref.19. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-358616,EBI-358616
LRRK1	Q38SD2	2	EBI-358616,EBI-1050422
LRRK2	Q5S007	2	EBI-358616,EBI-5323863
MAPK3	P27361	4	EBI-358616,EBI-73995
PDCD6	O75340	3	EBI-358616,EBI-352915

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P53355-1)

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.

Isoform 2 (identifier: P53355-2)

Also known as: s-DAPK-1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-446: Missing.
     742-783: VSVSINNLYP...LEVFVAPTHH → GRNLHAGPVS...SLGLYWTLWP
     784-1430: Missing.

Isoform 3 (identifier: P53355-3)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1430-1430: R → RRNSHVWNPTV

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1430

1430

Death-associated protein kinase 1

PRO_0000085910

Regions

Domain

13 – 275

263

Protein kinase

Repeat

378 – 407

30

ANK 1

Repeat

411 – 440

30

ANK 2

Repeat

444 – 473

30

ANK 3

Repeat

477 – 506

30

ANK 4

Repeat

510 – 539

30

ANK 5

Repeat

543 – 572

30

ANK 6

Repeat

576 – 605

30

ANK 7

Repeat

609 – 638

30

ANK 8

Repeat

875 – 904

30

ANK 9

Repeat

1162 – 1196

35

ANK 10

Domain

1312 – 1396

85

Death

Nucleotide binding

19 – 27

9

ATP

Nucleotide binding

94 – 96

3

ATP

Region

267 – 334

68

Calmodulin-binding

Region

292 – 301

10

Autoinhibitory domain By similarity

Sites

Active site

139

1

Proton acceptor By similarity

Binding site

42

1

ATP

Binding site

100

1

ATP

Binding site

161

1

ATP

Amino acid modifications

Modified residue

289

1

Phosphoserine; by RPS6KA1 and RPS6KA3 Ref.16

Modified residue

308

1

Phosphoserine; by autocatalysis Ref.11 Ref.18 Ref.20

Modified residue

333

1

Phosphoserine Ref.32

Modified residue

734

1

Phosphoserine; by MAPK1 Ref.17

Natural variations

Alternative sequence

1 – 446

446

Missing in isoform 2.

VSP_042053

Alternative sequence

742 – 783

42

VSVSI…APTHH → GRNLHAGPVSPAGVGFRTLS FQGLGGKGVVFGSLGLYWTL WP in isoform 2.

VSP_042054

Alternative sequence

784 – 1430

647

Missing in isoform 2.

VSP_042055

Alternative sequence

1430

1

R → RRNSHVWNPTV in isoform 3.

VSP_042056

Natural variant

416

1

V → I. Ref.37
Corresponds to variant rs12343465 [ dbSNP | Ensembl ].

VAR_033235

Natural variant

461

1

A → S. Ref.37

VAR_040420

Natural variant

519

1

S → A. Ref.37

VAR_040421

Natural variant

540

1

C → Y. Ref.37
Corresponds to variant rs56327474 [ dbSNP | Ensembl ].

VAR_040422

Natural variant

591

1

P → L. Ref.5

VAR_060693

Natural variant

622

1

I → M. Ref.5

VAR_060694

Natural variant

941

1

M → T. Ref.37

VAR_040423

Natural variant

977

1

R → W. Ref.37

VAR_040424

Natural variant

978

1

K → N. Ref.37

VAR_040425

Natural variant

993

1

Y → C. Ref.37

VAR_040426

Natural variant

994

1

D → E. Ref.37

VAR_040427

Natural variant

1005

1

E → Q. Ref.37

VAR_040428

Natural variant

1007

1

D → Y. Ref.37

VAR_040429

Natural variant

1008

1

L → P. Ref.37

VAR_040430

Natural variant

1010

1

R → C. Ref.37

VAR_040431

Natural variant

1018

1

T → A. Ref.37

VAR_040432

Natural variant

1272

1

M → I. Ref.37
Corresponds to variant rs56169226 [ dbSNP | Ensembl ].

VAR_040433

Natural variant

1346

1

S → N. Ref.1 Ref.4 Ref.5 Ref.6 Ref.37
Corresponds to variant rs1056719 [ dbSNP | Ensembl ].

VAR_040434

Natural variant

1405

1

G → V. Ref.5 Ref.37
Corresponds to variant rs36220450 [ dbSNP | Ensembl ].

VAR_040435

Experimental info

Mutagenesis

42

1

K → A: Loss of activity, apoptotic function and of autophosphorylation. Ref.1 Ref.11

Mutagenesis

289

1

S → A: Loss of phosphorylation and significant increase in proapoptotic activity.

Mutagenesis

289

1

S → E: Reduction in proapoptotic activity.

Mutagenesis

308

1

S → A: Elevated Ca(2+)-calmodulin binding and Ca(2+)-calmodulin-independent kinase activity. Increases apoptotic activity. Ref.11

Mutagenesis

308

1

S → D: Reduced Ca(2+)-calmodulin binding and Ca(2+)-calmodulin-independent kinase activity. Decreases apoptotic activity. Ref.11

Mutagenesis

313

1

S → A: Minimal effect on activity. Ref.11

Sequence conflict

490

1

Y → H in BAC87163. Ref.3

Sequence conflict

1217

1

S → G in CAH18690. Ref.4

Secondary structure

1

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1430

Helix Strand Turn

Details...

Helix

9 – 11

3

Beta strand

13 – 22

10

Beta strand

25 – 32

8

Turn

33 – 35

3

Beta strand

38 – 46

9

Beta strand

48 – 51

4

Beta strand

54 – 56

3

Helix

58 – 70

13

Beta strand

79 – 84

6

Beta strand

86 – 94

9

Helix

101 – 107

7

Beta strand

108 – 110

3

Helix

113 – 132

20

Beta strand

134 – 136

3

Helix

142 – 144

3

Beta strand

145 – 148

4

Beta strand

150 – 154

5

Beta strand

157 – 159

3

Helix

162 – 164

3

Beta strand

169 – 171

3

Turn

181 – 183

3

Helix

186 – 189

4

Helix

197 – 212

16

Helix

222 – 230

9

Helix

238 – 241

4

Beta strand

242 – 244

3

Helix

246 – 255

10

Helix

260 – 262

3

Helix

266 – 271

6

Turn

273 – 275

3

Helix

280 – 288

9

Helix

293 – 300

8

Helix

304 – 318

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha) [UniParc]. Last modified January 11, 2011. Version 6. Checksum: E2C4246E7C78A6D2	FASTA	1,430	160,046
	10 20 30 40 50 60 MTVFRQENVD DYYDTGEELG SGQFAVVKKC REKSTGLQYA AKFIKKRRTK SSRRGVSRED 70 80 90 100 110 120 IEREVSILKE IQHPNVITLH EVYENKTDVI LILELVAGGE LFDFLAEKES LTEEEATEFL 130 140 150 160 170 180 KQILNGVYYL HSLQIAHFDL KPENIMLLDR NVPKPRIKII DFGLAHKIDF GNEFKNIFGT 190 200 210 220 230 240 PEFVAPEIVN YEPLGLEADM WSIGVITYIL LSGASPFLGD TKQETLANVS AVNYEFEDEY 250 260 270 280 290 300 FSNTSALAKD FIRRLLVKDP KKRMTIQDSL QHPWIKPKDT QQALSRKASA VNMEKFKKFA 310 320 330 340 350 360 ARKKWKQSVR LISLCQRLSR SFLSRSNMSV ARSDDTLDEE DSFVMKAIIH AINDDNVPGL 370 380 390 400 410 420 QHLLGSLSNY DVNQPNKHGT PPLLIAAGCG NIQILQLLIK RGSRIDVQDK GGSNAVYWAA 430 440 450 460 470 480 RHGHVDTLKF LSENKCPLDV KDKSGEMALH VAARYGHADV AQLLCSFGSN PNIQDKEEET 490 500 510 520 530 540 PLHCAAWHGY YSVAKALCEA GCNVNIKNRE GETPLLTASA RGYHDIVECL AEHGADLNAC 550 560 570 580 590 600 DKDGHIALHL AVRRCQMEVI KTLLSQGCFV DYQDRHGNTP LHVACKDGNM PIVVALCEAN 610 620 630 640 650 660 CNLDISNKYG RTPLHLAANN GILDVVRYLC LMGASVEALT TDGKTAEDLA RSEQHEHVAG 670 680 690 700 710 720 LLARLRKDTH RGLFIQQLRP TQNLQPRIKL KLFGHSGSGK TTLVESLKCG LLRSFFRRRR 730 740 750 760 770 780 PRLSSTNSSR FPPSPLASKP TVSVSINNLY PGCENVSVRS RSMMFEPGLT KGMLEVFVAP 790 800 810 820 830 840 THHPHCSADD QSTKAIDIQN AYLNGVGDFS VWEFSGNPVY FCCYDYFAAN DPTSIHVVVF 850 860 870 880 890 900 SLEEPYEIQL NQVIFWLSFL KSLVPVEEPI AFGGKLKNPL QVVLVATHAD IMNVPRPAGG 910 920 930 940 950 960 EFGYDKDTSL LKEIRNRFGN DLHISNKLFV LDAGASGSKD MKVLRNHLQE IRSQIVSVCP 970 980 990 1000 1010 1020 PMTHLCEKII STLPSWRKLN GPNQLMSLQQ FVYDVQDQLN PLASEEDLRR IAQQLHSTGE 1030 1040 1050 1060 1070 1080 INIMQSETVQ DVLLLDPRWL CTNVLGKLLS VETPRALHHY RGRYTVEDIQ RLVPDSDVEE 1090 1100 1110 1120 1130 1140 LLQILDAMDI CARDLSSGTM VDVPALIKTD NLHRSWADEE DEVMVYGGVR IVPVEHLTPF 1150 1160 1170 1180 1190 1200 PCGIFHKVQV NLCRWIHQQS TEGDADIRLW VNGCKLANRG AELLVLLVNH GQGIEVQVRG 1210 1220 1230 1240 1250 1260 LETEKIKCCL LLDSVCSTIE NVMATTLPGL LTVKHYLSPQ QLREHHEPVM IYQPRDFFRA 1270 1280 1290 1300 1310 1320 QTLKETSLTN TMGGYKESFS SIMCFGCHDV YSQASLGMDI HASDLNLLTR RKLSRLLDPP 1330 1340 1350 1360 1370 1380 DPLGKDWCLL AMNLGLPDLV AKYNTSNGAP KDFLPSPLHA LLREWTTYPE STVGTLMSKL 1390 1400 1410 1420 1430 RELGRRDAAD FLLKASSVFK INLDGNGQEA YASSCNSGTS YNSISSVVSR
	Isoform 2 (s-DAPK-1) [UniParc]. Checksum: 3BA58BA79D87E0C6	FASTA	337	36,765
	10 20 30 40 50 60 MALHVAARYG HADVAQLLCS FGSNPNIQDK EEETPLHCAA WHGYYSVAKA LCEAGCNVNI 70 80 90 100 110 120 KNREGETPLL TASARGYHDI VECLAEHGAD LNACDKDGHI ALHLAVRRCQ MEVIKTLLSQ 130 140 150 160 170 180 GCFVDYQDRH GNTPLHVACK DGNMPIVVAL CEANCNLDIS NKYGRTPLHL AANNGILDVV 190 200 210 220 230 240 RYLCLMGASV EALTTDGKTA EDLARSEQHE HVAGLLARLR KDTHRGLFIQ QLRPTQNLQP 250 260 270 280 290 300 RIKLKLFGHS GSGKTTLVES LKCGLLRSFF RRRRPRLSST NSSRFPPSPL ASKPTGRNLH 310 320 330 AGPVSPAGVG FRTLSFQGLG GKGVVFGSLG LYWTLWP
	Isoform 3 (Beta) [UniParc]. Checksum: D43BB6B6A3F0ABF9	FASTA	1,440	161,237
	10 20 30 40 50 60 MTVFRQENVD DYYDTGEELG SGQFAVVKKC REKSTGLQYA AKFIKKRRTK SSRRGVSRED 70 80 90 100 110 120 IEREVSILKE IQHPNVITLH EVYENKTDVI LILELVAGGE LFDFLAEKES LTEEEATEFL 130 140 150 160 170 180 KQILNGVYYL HSLQIAHFDL KPENIMLLDR NVPKPRIKII DFGLAHKIDF GNEFKNIFGT 190 200 210 220 230 240 PEFVAPEIVN YEPLGLEADM WSIGVITYIL LSGASPFLGD TKQETLANVS AVNYEFEDEY 250 260 270 280 290 300 FSNTSALAKD FIRRLLVKDP KKRMTIQDSL QHPWIKPKDT QQALSRKASA VNMEKFKKFA 310 320 330 340 350 360 ARKKWKQSVR LISLCQRLSR SFLSRSNMSV ARSDDTLDEE DSFVMKAIIH AINDDNVPGL 370 380 390 400 410 420 QHLLGSLSNY DVNQPNKHGT PPLLIAAGCG NIQILQLLIK RGSRIDVQDK GGSNAVYWAA 430 440 450 460 470 480 RHGHVDTLKF LSENKCPLDV KDKSGEMALH VAARYGHADV AQLLCSFGSN PNIQDKEEET 490 500 510 520 530 540 PLHCAAWHGY YSVAKALCEA GCNVNIKNRE GETPLLTASA RGYHDIVECL AEHGADLNAC 550 560 570 580 590 600 DKDGHIALHL AVRRCQMEVI KTLLSQGCFV DYQDRHGNTP LHVACKDGNM PIVVALCEAN 610 620 630 640 650 660 CNLDISNKYG RTPLHLAANN GILDVVRYLC LMGASVEALT TDGKTAEDLA RSEQHEHVAG 670 680 690 700 710 720 LLARLRKDTH RGLFIQQLRP TQNLQPRIKL KLFGHSGSGK TTLVESLKCG LLRSFFRRRR 730 740 750 760 770 780 PRLSSTNSSR FPPSPLASKP TVSVSINNLY PGCENVSVRS RSMMFEPGLT KGMLEVFVAP 790 800 810 820 830 840 THHPHCSADD QSTKAIDIQN AYLNGVGDFS VWEFSGNPVY FCCYDYFAAN DPTSIHVVVF 850 860 870 880 890 900 SLEEPYEIQL NQVIFWLSFL KSLVPVEEPI AFGGKLKNPL QVVLVATHAD IMNVPRPAGG 910 920 930 940 950 960 EFGYDKDTSL LKEIRNRFGN DLHISNKLFV LDAGASGSKD MKVLRNHLQE IRSQIVSVCP 970 980 990 1000 1010 1020 PMTHLCEKII STLPSWRKLN GPNQLMSLQQ FVYDVQDQLN PLASEEDLRR IAQQLHSTGE 1030 1040 1050 1060 1070 1080 INIMQSETVQ DVLLLDPRWL CTNVLGKLLS VETPRALHHY RGRYTVEDIQ RLVPDSDVEE 1090 1100 1110 1120 1130 1140 LLQILDAMDI CARDLSSGTM VDVPALIKTD NLHRSWADEE DEVMVYGGVR IVPVEHLTPF 1150 1160 1170 1180 1190 1200 PCGIFHKVQV NLCRWIHQQS TEGDADIRLW VNGCKLANRG AELLVLLVNH GQGIEVQVRG 1210 1220 1230 1240 1250 1260 LETEKIKCCL LLDSVCSTIE NVMATTLPGL LTVKHYLSPQ QLREHHEPVM IYQPRDFFRA 1270 1280 1290 1300 1310 1320 QTLKETSLTN TMGGYKESFS SIMCFGCHDV YSQASLGMDI HASDLNLLTR RKLSRLLDPP 1330 1340 1350 1360 1370 1380 DPLGKDWCLL AMNLGLPDLV AKYNTSNGAP KDFLPSPLHA LLREWTTYPE STVGTLMSKL 1390 1400 1410 1420 1430 1440 RELGRRDAAD FLLKASSVFK INLDGNGQEA YASSCNSGTS YNSISSVVSR RNSHVWNPTV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a novel serine/threonine kinase and a novel 15-kD protein as potential mediators of the gamma interferon-induced cell death." Deiss L.P., Feinstein E., Berissi H., Cohen O., Kimchi A. Genes Dev. 9:15-30(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION, MUTAGENESIS OF LYS-42, VARIANT ASN-1346.
[2]	Feinstein E. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 164-171.
[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] (ISOFORM 2). Tissue: Placenta.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASN-1346. Tissue: Amygdala.
[5]	NIEHS SNPs program Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-591; MET-622; ASN-1346 AND VAL-1405.
[6]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-1346.
[7]	Mural R.J., Istrail S., Sutton G.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. , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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). Tissue: Cerebellum.
[9]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-363.
[10]	"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: FUNCTION, SUBCELLULAR LOCATION.
[11]	"The pro-apoptotic function of death-associated protein kinase is controlled by a unique inhibitory autophosphorylation-based mechanism." Shohat G., Spivak-Kroizman T., Cohen O., Bialik S., Shani G., Berissi H., Eisenstein M., Kimchi A. J. Biol. Chem. 276:47460-47467(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS OF LYS-42; SER-308 AND SER-313, PHOSPHORYLATION AT SER-308.
[12]	"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.
[13]	"Ca2+-dependent phosphorylation of syntaxin-1A by the death-associated protein (DAP) kinase regulates its interaction with Munc18." Tian J.H., Das S., Sheng Z.H. J. Biol. Chem. 278:26265-26274(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF STX1A, INTERACTION WITH STX1A.
[14]	"Death-associated protein kinase phosphorylates ZIP kinase, forming a unique kinase hierarchy to activate its cell death functions." Shani G., Marash L., Gozuacik D., Bialik S., Teitelbaum L., Shohat G., Kimchi A. Mol. Cell. Biol. 24:8611-8626(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF DAPK3, INTERACTION WITH DAPK3.
[15]	"Programmed cell death 6 (PDCD6) protein interacts with death-associated protein kinase 1 (DAPk1): additive effect on apoptosis via caspase-3 dependent pathway." Lee J.H., Rho S.B., Chun T. Biotechnol. Lett. 27:1011-1015(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PDCD6.
[16]	"The tumor suppressor DAP kinase is a target of RSK-mediated survival signaling." Anjum R., Roux P.P., Ballif B.A., Gygi S.P., Blenis J. Curr. Biol. 15:1762-1767(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-289.
[17]	"Bidirectional signals transduced by DAPK-ERK interaction promote the apoptotic effect of DAPK." Chen C.H., Wang W.J., Kuo J.C., Tsai H.C., Lin J.R., Chang Z.F., Chen R.H. EMBO J. 24:294-304(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-734, INTERACTION WITH MAPK1 AND MAPK3.
[18]	"The dependence receptor UNC5H2 mediates apoptosis through DAP-kinase." Llambi F., Lourenco F.C., Gozuacik D., Guix C., Pays L., Del Rio G., Kimchi A., Mehlen P. EMBO J. 24:1192-1201(2005) [PubMed] [Europe PMC] [Abstract] Cited for: AUTOPHOSPHORYLATION AT SER-308, ENZYME REGULATION, INTERACTION WITH UNC5B.
[19]	"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.
[20]	"Control of death-associated protein kinase (DAPK) activity by phosphorylation and proteasomal degradation." Jin Y., Blue E.K., Gallagher P.J. J. Biol. Chem. 281:39033-39040(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORM 3), AUTOPHOSPHORYLATION AT SER-308, DEPHOSPHORYLATION, ENZYME REGULATION.
[21]	"DAP kinase regulates JNK signaling by binding and activating protein kinase D under oxidative stress." Eisenberg-Lerner A., Kimchi A. Cell Death Differ. 14:1908-1915(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PRKD1, INTERACTION WITH PRKD1.
[22]	"DAP kinase mediates the phosphorylation of tropomyosin-1 downstream of the ERK pathway, which regulates the formation of stress fibers in response to oxidative stress." Houle F., Poirier A., Dumaresq J., Huot J. J. Cell Sci. 120:3666-3677(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF TPM1.
[23]	"An alternative transcript from the death-associated protein kinase 1 locus encoding a small protein selectively mediates membrane blebbing." Lin Y., Stevens C., Hrstka R., Harrison B., Fourtouna A., Pathuri S., Vojtesek B., Hupp T. FEBS J. 275:2574-2584(2008) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORM 2), PROTEOLYTIC PROCESSING, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[24]	"DAPK-1 binding to a linear peptide motif in MAP1B stimulates autophagy and membrane blebbing." Harrison B., Kraus M., Burch L., Stevens C., Craig A., Gordon-Weeks P., Hupp T.R. J. Biol. Chem. 283:9999-10014(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAP1B.
[25]	"DAPK-ZIPK-L13a axis constitutes a negative-feedback module regulating inflammatory gene expression." Mukhopadhyay R., Ray P.S., Arif A., Brady A.K., Kinter M., Fox P.L. Mol. Cell 32:371-382(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[26]	"DAP-kinase-mediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy." Zalckvar E., Berissi H., Mizrachy L., Idelchuk Y., Koren I., Eisenstein M., Sabanay H., Pinkas-Kramarski R., Kimchi A. EMBO Rep. 10:285-292(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF BECN1, INTERACTION WITH BECN1.
[27]	"Peptide combinatorial libraries identify TSC2 as a death-associated protein kinase (DAPK) death domain-binding protein and reveal a stimulatory role for DAPK in mTORC1 signaling." Stevens C., Lin Y., Harrison B., Burch L., Ridgway R.A., Sansom O., Hupp T. J. Biol. Chem. 284:334-344(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF TSC2 AND RPS6, INTERACTION WITH TSC2.
[28]	"The Cullin 3 substrate adaptor KLHL20 mediates DAPK ubiquitination to control interferon responses." Lee Y.R., Yuan W.C., Ho H.C., Chen C.H., Shih H.M., Chen R.H. EMBO J. 29:1748-1761(2010) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH KLHL20.
[29]	"Death-associated protein kinase (DAPK) and signal transduction: additional roles beyond cell death." Lin Y., Hupp T.R., Stevens C. FEBS J. 277:48-57(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[30]	"Death-associated protein kinase 1 phosphorylates Pin1 and inhibits its prolyl isomerase activity and cellular function." Lee T.H., Chen C.H., Suizu F., Huang P., Schiene-Fischer C., Daum S., Zhang Y.J., Goate A., Chen R.H., Zhou X.Z., Lu K.P. Mol. Cell 42:147-159(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PIN1, INTERACTION WITH PIN1.
[31]	"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: FUNCTION.
[32]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, MASS SPECTROMETRY.
[33]	"Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression." Tereshko V., Teplova M., Brunzelle J., Watterson D.M., Egli M. Nat. Struct. Biol. 8:899-907(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-285 IN COMPLEX WITH ATP ANALOG AND DIVALENT METAL CATION.
[34]	"An aminopyridazine-based inhibitor of a pro-apoptotic protein kinase attenuates hypoxia-ischemia induced acute brain injury." Velentza A.V., Wainwright M.S., Zasadzki M., Mirzoeva S., Schumacher A.M., Haiech J., Focia P.J., Egli M., Watterson D.M. Bioorg. Med. Chem. Lett. 13:3465-3470(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-285 IN COMPLEX WITH SYNTHETIC INHIBITOR.
[35]	"Complex structure of kinase domain of DAP kinase with staurosporine." Ueda Y., Ogata H., Yamakawa A., Higuchi Y. Submitted (APR-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-278 IN COMPLEX WITH INHIBITORS.
[36]	"Recognition of human death-associated protein kinases by calmodulin." Kursula P., Vahokoski J., Wilmanns M. Submitted (JUL-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 302-320 IN COMPLEX WITH CALMODULIN.
[37]	"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] ILE-416; SER-461; ALA-519; TYR-540; THR-941; TRP-977; ASN-978; CYS-993; GLU-994; GLN-1005; TYR-1007; PRO-1008; CYS-1010; ALA-1018; ILE-1272; ASN-1346 AND VAL-1405.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X76104 mRNA. Translation: CAA53712.1. Frameshift.
AK127855 mRNA. Translation: BAC87163.1.
CR749834 mRNA. Translation: CAH18690.1.
DQ436495 Genomic DNA. Translation: ABD96827.1.
AL160279 Genomic DNA. No translation available.
AL161787 Genomic DNA. No translation available.
AL591852 Genomic DNA. No translation available.
CH471089 Genomic DNA. Translation: EAW62727.1.
BC113660 mRNA. Translation: AAI13661.1.
BC143733 mRNA. Translation: AAI43734.1.
BT006935 mRNA. Translation: AAP35581.1. Sequence problems.

IPI

IPI00745936.
IPI00947196.
IPI01010067.

PIR

I37275.

RefSeq

NP_004929.2. NM_004938.2.

UniGene

Hs.380277.
Hs.693441.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IG1	X-ray	1.80	A	2-285	[»]
1JKK	X-ray	2.40	A	2-285	[»]
1JKL	X-ray	1.62	A	2-285	[»]
1JKS	X-ray	1.50	A	2-285	[»]
1JKT	X-ray	3.50	A/B	2-285	[»]
1P4F	X-ray	1.90	A	2-285	[»]
1WVW	X-ray	2.40	A	1-278	[»]
1WVX	X-ray	2.60	A	1-278	[»]
1WVY	X-ray	2.80	A	1-278	[»]
1YR5	X-ray	1.70	B	302-320	[»]
2W4J	X-ray	1.30	A	1-277	[»]
2W4K	X-ray	1.90	A	1-302	[»]
2X0G	X-ray	2.20	A	1-334	[»]
2XUU	X-ray	1.80	A	1-334	[»]
2XZS	X-ray	2.00	A/B	2-312	[»]
2Y0A	X-ray	2.60	A	2-304	[»]
2Y4P	X-ray	2.65	A/B/C/D	1-285	[»]
2Y4V	X-ray	1.80	B	302-320	[»]
2YAK	X-ray	2.20	A	1-285	[»]
3DFC	X-ray	1.90	B	1-285	[»]
3DGK	X-ray	1.70	A	1-285	[»]
3EH9	X-ray	1.70	A	2-285	[»]
3EHA	X-ray	1.60	A	2-285	[»]
3F5G	X-ray	1.85	A	2-285	[»]
3F5U	X-ray	2.00	A	1-285	[»]
3GU4	X-ray	1.35	A	1-285	[»]
3GU5	X-ray	1.65	A	1-285	[»]
3GU6	X-ray	1.49	A	1-285	[»]
3GU7	X-ray	1.90	A	1-285	[»]
3GU8	X-ray	1.60	A	1-285	[»]
3GUB	X-ray	1.71	A	1-285	[»]
3ZXT	X-ray	2.65	A/B/C/D	1-285	[»]

ProteinModelPortal

P53355.

SMR

P53355. Positions 3-336, 345-749.

ModBase

Search...

Protein-protein interaction databases

IntAct

P53355. 7 interactions.

MINT

MINT-1136108.

STRING

9606.ENSP00000350785.

PTM databases

PhosphoSite

P53355.

Polymorphism databases

DMDM

206729939.

Proteomic databases

PaxDb

P53355.

PRIDE

P53355.

Protocols and materials databases

DNASU

1612.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000358077; ENSP00000350785; ENSG00000196730.
ENST00000408954; ENSP00000386135; ENSG00000196730.
ENST00000472284; ENSP00000417076; ENSG00000196730.

GeneID

1612.

KEGG

hsa:1612.

UCSC

uc004apc.3. human.

Organism-specific databases

CTD

1612.

GeneCards

GC09P090112.

HGNC

HGNC:2674. DAPK1.

HPA

CAB037302.

MIM

600831. gene.

neXtProt

NX_P53355.

PharmGKB

PA27142.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0666.

HOVERGEN

HBG051296.

KO

K08803.

OrthoDB

EOG4KD6K6.

Enzyme and pathway databases

BRENDA

2.7.11.1. 2681.

Pathway_Interaction_DB

ifngpathway. IFN-gamma pathway.

Reactome

REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P53355.

Bgee

P53355.

CleanEx

HS_DAPK1.

Genevestigator

P53355.

GermOnline

ENSG00000196730. Homo sapiens.

Family and domain databases

Gene3D

1.10.533.10. 1 hit.
1.25.40.20. 1 hit.

InterPro

IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR020676. Death-assoc_prot_kinase.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR011009. Kinase-like_dom.
IPR020675. Myosin_light_ch_kinase-rel.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

PANTHER

PTHR22964. PTHR22964. 1 hit.
PTHR22964:SF1. PTHR22964:SF1. 1 hit.

Pfam

PF00023. Ank. 6 hits.
PF00531. Death. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

PRINTS

PR01415. ANKYRIN.

SMART

SM00248. ANK. 9 hits.
SM00005. DEATH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF48403. ANK. 1 hit.
SSF47986. DEATH_like. 1 hit.
SSF56112. Kinase_like. 1 hit.

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 7 hits.
PS50017. DEATH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P53355.

ChEMBL

CHEMBL2558.

ChiTaRS

DAPK1. human.

EvolutionaryTrace

P53355.

GenomeRNAi

1612.

NextBio

6626.

SOURCE

Search...

Entry information

Entry name

DAPK1_HUMAN

Accession

Primary (citable) accession number: P53355
Secondary accession number(s): B7ZLD2 , Q14CQ7, Q1W5W0, Q68CP8, Q6ZRZ3, Q9BTL8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 147 of the entry and version 6 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.