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Protein

Death-associated protein kinase 1

Gene

DAPK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. 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.
Isoform 2 cannot induce apoptosis but can induce membrane blebbing.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

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.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei42ATP1
Binding sitei100ATP1
Active sitei139Proton acceptorPROSITE-ProRule annotation1
Binding sitei161ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi19 – 27ATP9
Nucleotide bindingi94 – 96ATP3

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • calmodulin binding Source: UniProtKB
  • calmodulin-dependent protein kinase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • protein kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • syntaxin-1 binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • apoptotic signaling pathway Source: UniProtKB
  • cellular response to interferon-gamma Source: UniProtKB
  • extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  • intracellular signal transduction Source: UniProtKB
  • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  • negative regulation of translation Source: UniProtKB
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of apoptotic process Source: UniProtKB
  • regulation of autophagy Source: UniProtKB
  • regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Translation regulation

Keywords - Ligandi

ATP-binding, Calmodulin-binding, GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS07488-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-418889. Ligand-independent caspase activation via DCC.
SignaLinkiP53355.
SIGNORiP53355.

Names & Taxonomyi

Protein namesi
Recommended name:
Death-associated protein kinase 1 (EC:2.7.11.1)
Short name:
DAP kinase 1
Gene namesi
Name:DAPK1
Synonyms:DAPK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:2674. DAPK1.

Subcellular locationi

Isoform 1 :

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi42K → A: Loss of activity, apoptotic function and of autophosphorylation. 2 Publications1
Mutagenesisi289S → A: Loss of phosphorylation and significant increase in proapoptotic activity. 1
Mutagenesisi289S → E: Reduction in proapoptotic activity. 1
Mutagenesisi308S → A: Elevated Ca(2+)-calmodulin binding and Ca(2+)-calmodulin-independent kinase activity. Increases apoptotic activity. 1 Publication1
Mutagenesisi308S → D: Reduced Ca(2+)-calmodulin binding and Ca(2+)-calmodulin-independent kinase activity. Decreases apoptotic activity. 1 Publication1
Mutagenesisi313S → A: Minimal effect on activity. 1 Publication1

Organism-specific databases

DisGeNETi1612.
OpenTargetsiENSG00000196730.
PharmGKBiPA27142.

Chemistry databases

ChEMBLiCHEMBL2558.
GuidetoPHARMACOLOGYi2002.

Polymorphism and mutation databases

BioMutaiDAPK1.
DMDMi317373595.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000859101 – 1430Death-associated protein kinase 1Add BLAST1430

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei289Phosphoserine; by RPS6KA1 and RPS6KA31 Publication1
Modified residuei308Phosphoserine; by autocatalysis3 Publications1
Modified residuei319PhosphoserineCombined sources1
Modified residuei333PhosphoserineCombined sources1
Modified residuei734Phosphoserine; by MAPK11 Publication1
Modified residuei1115PhosphoserineBy similarity1

Post-translational modificationi

Ubiquitinated by the BCR(KLHL20) E3 ubiquitin ligase complex, leading to its degradation by the proteasome.1 Publication
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.1 Publication
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-308.5 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP53355.
MaxQBiP53355.
PaxDbiP53355.
PeptideAtlasiP53355.
PRIDEiP53355.

PTM databases

iPTMnetiP53355.
PhosphoSitePlusiP53355.

Expressioni

Tissue specificityi

Isoform 2 is expressed in normal intestinal tissue as well as in colorectal carcinomas.1 Publication

Inductioni

Up-regulated following treatment with IFNG/IFN-gamma.1 Publication

Gene expression databases

BgeeiENSG00000196730.
CleanExiHS_DAPK1.
ExpressionAtlasiP53355. baseline and differential.
GenevisibleiP53355. HS.

Organism-specific databases

HPAiCAB037302.
HPA040472.
HPA048436.

Interactioni

Subunit structurei

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).15 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself6EBI-358616,EBI-358616
BECN1Q144574EBI-358616,EBI-949378
CALM3P621586EBI-358616,EBI-397435
KLHL20Q9Y2M511EBI-358616,EBI-714379
LRRK1Q38SD22EBI-358616,EBI-1050422
LRRK2Q5S0072EBI-358616,EBI-5323863
MAPK3P273615EBI-358616,EBI-73995
PDCD6O753403EBI-358616,EBI-352915
PKMP146183EBI-358616,EBI-353408
PKMP14618-12EBI-358616,EBI-4304679

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • syntaxin-1 binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107982. 51 interactors.
IntActiP53355. 33 interactors.
MINTiMINT-1136108.
STRINGi9606.ENSP00000350785.

Chemistry databases

BindingDBiP53355.

Structurei

Secondary structure

11430
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 11Combined sources3
Beta strandi13 – 21Combined sources9
Beta strandi23 – 32Combined sources10
Turni33 – 35Combined sources3
Beta strandi38 – 46Combined sources9
Beta strandi48 – 51Combined sources4
Beta strandi53 – 56Combined sources4
Helixi58 – 70Combined sources13
Beta strandi79 – 84Combined sources6
Beta strandi86 – 94Combined sources9
Helixi101 – 107Combined sources7
Beta strandi108 – 110Combined sources3
Helixi113 – 132Combined sources20
Beta strandi134 – 136Combined sources3
Helixi142 – 144Combined sources3
Beta strandi145 – 148Combined sources4
Beta strandi150 – 154Combined sources5
Beta strandi157 – 159Combined sources3
Helixi162 – 164Combined sources3
Beta strandi169 – 171Combined sources3
Helixi181 – 183Combined sources3
Helixi186 – 189Combined sources4
Helixi197 – 212Combined sources16
Helixi222 – 230Combined sources9
Helixi238 – 241Combined sources4
Beta strandi242 – 244Combined sources3
Helixi246 – 255Combined sources10
Turni260 – 262Combined sources3
Helixi266 – 271Combined sources6
Turni273 – 275Combined sources3
Helixi280 – 288Combined sources9
Helixi293 – 302Combined sources10
Helixi304 – 318Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IG1X-ray1.80A2-285[»]
1JKKX-ray2.40A2-285[»]
1JKLX-ray1.62A2-285[»]
1JKSX-ray1.50A2-285[»]
1JKTX-ray3.50A/B2-285[»]
1P4FX-ray1.90A2-285[»]
1WVWX-ray2.40A1-278[»]
1WVXX-ray2.60A1-278[»]
1WVYX-ray2.80A1-278[»]
1YR5X-ray1.70B302-320[»]
2W4JX-ray1.30A1-277[»]
2W4KX-ray1.90A1-302[»]
2X0GX-ray2.20A1-334[»]
2XUUX-ray1.80A1-334[»]
2XZSX-ray2.00A/B2-312[»]
2Y0AX-ray2.60A2-304[»]
2Y4PX-ray2.65A/B/C/D1-285[»]
2Y4VX-ray1.80B302-320[»]
2YAKX-ray2.20A1-285[»]
3DFCX-ray1.90B1-285[»]
3DGKX-ray1.70A1-285[»]
3EH9X-ray1.70A2-285[»]
3EHAX-ray1.60A2-285[»]
3F5GX-ray1.85A2-285[»]
3F5UX-ray2.00A1-285[»]
3GU4X-ray1.35A1-285[»]
3GU5X-ray1.65A1-285[»]
3GU6X-ray1.49A1-285[»]
3GU7X-ray1.90A1-285[»]
3GU8X-ray1.60A1-285[»]
3GUBX-ray1.71A1-285[»]
3ZXTX-ray2.65A/B/C/D1-285[»]
4B4LX-ray1.75A1-334[»]
4PF4X-ray1.13A1-277[»]
4TL0X-ray2.70A1-334[»]
4TXCX-ray1.95A1-285[»]
4UV0X-ray2.49A1-321[»]
4YO4X-ray1.60A2-285[»]
4YPDX-ray1.40A2-285[»]
5AUTX-ray1.70A1-285[»]
5AUUX-ray1.70A1-285[»]
5AUVX-ray1.50A1-285[»]
5AUWX-ray1.50A1-285[»]
5AUXX-ray1.50A1-285[»]
5AUYX-ray2.00A1-285[»]
5AUZX-ray1.60A1-285[»]
5AV0X-ray1.85A1-285[»]
5AV1X-ray1.50A1-285[»]
5AV2X-ray1.50A1-285[»]
5AV3X-ray1.90A1-285[»]
5AV4X-ray1.40A1-285[»]
ProteinModelPortaliP53355.
SMRiP53355.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53355.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 275Protein kinasePROSITE-ProRule annotationAdd BLAST263
Repeati378 – 407ANK 1Add BLAST30
Repeati411 – 440ANK 2Add BLAST30
Repeati444 – 473ANK 3Add BLAST30
Repeati477 – 506ANK 4Add BLAST30
Repeati510 – 539ANK 5Add BLAST30
Repeati543 – 572ANK 6Add BLAST30
Repeati576 – 605ANK 7Add BLAST30
Repeati609 – 638ANK 8Add BLAST30
Domaini681 – 955RocPROSITE-ProRule annotationAdd BLAST275
Repeati875 – 904ANK 9Add BLAST30
Repeati1162 – 1196ANK 10Add BLAST35
Domaini1312 – 1396DeathPROSITE-ProRule annotationAdd BLAST85

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni267 – 334Calmodulin-bindingAdd BLAST68
Regioni292 – 301Autoinhibitory domainBy similarity10

Domaini

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

Sequence similaritiesi

Contains 10 ANK repeats.PROSITE-ProRule annotation
Contains 1 death domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 Roc domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG0032. Eukaryota.
ENOG410XRMJ. LUCA.
GeneTreeiENSGT00760000118877.
HOGENOMiHOG000082489.
HOVERGENiHBG051296.
InParanoidiP53355.
KOiK08803.
OMAiIDVQDKG.
OrthoDBiEOG091G0J2O.
PhylomeDBiP53355.
TreeFamiTF314166.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR020676. DAPK1.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR011009. Kinase-like_dom.
IPR027417. P-loop_NTPase.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR020859. ROC_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR10489:SF699. PTHR10489:SF699. 1 hit.
PfamiPF12796. Ank_2. 2 hits.
PF00531. Death. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 9 hits.
SM00005. DEATH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50297. 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.
PS51424. ROC. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P53355-1) [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
MTVFRQENVD DYYDTGEELG SGQFAVVKKC REKSTGLQYA AKFIKKRRTK
60 70 80 90 100
SSRRGVSRED IEREVSILKE IQHPNVITLH EVYENKTDVI LILELVAGGE
110 120 130 140 150
LFDFLAEKES LTEEEATEFL KQILNGVYYL HSLQIAHFDL KPENIMLLDR
160 170 180 190 200
NVPKPRIKII DFGLAHKIDF GNEFKNIFGT PEFVAPEIVN YEPLGLEADM
210 220 230 240 250
WSIGVITYIL LSGASPFLGD TKQETLANVS AVNYEFEDEY FSNTSALAKD
260 270 280 290 300
FIRRLLVKDP KKRMTIQDSL QHPWIKPKDT QQALSRKASA VNMEKFKKFA
310 320 330 340 350
ARKKWKQSVR LISLCQRLSR SFLSRSNMSV ARSDDTLDEE DSFVMKAIIH
360 370 380 390 400
AINDDNVPGL QHLLGSLSNY DVNQPNKHGT PPLLIAAGCG NIQILQLLIK
410 420 430 440 450
RGSRIDVQDK GGSNAVYWAA RHGHVDTLKF LSENKCPLDV KDKSGEMALH
460 470 480 490 500
VAARYGHADV AQLLCSFGSN PNIQDKEEET PLHCAAWHGY YSVAKALCEA
510 520 530 540 550
GCNVNIKNRE GETPLLTASA RGYHDIVECL AEHGADLNAC DKDGHIALHL
560 570 580 590 600
AVRRCQMEVI KTLLSQGCFV DYQDRHGNTP LHVACKDGNM PIVVALCEAN
610 620 630 640 650
CNLDISNKYG RTPLHLAANN GILDVVRYLC LMGASVEALT TDGKTAEDLA
660 670 680 690 700
RSEQHEHVAG LLARLRKDTH RGLFIQQLRP TQNLQPRIKL KLFGHSGSGK
710 720 730 740 750
TTLVESLKCG LLRSFFRRRR PRLSSTNSSR FPPSPLASKP TVSVSINNLY
760 770 780 790 800
PGCENVSVRS RSMMFEPGLT KGMLEVFVAP THHPHCSADD QSTKAIDIQN
810 820 830 840 850
AYLNGVGDFS VWEFSGNPVY FCCYDYFAAN DPTSIHVVVF SLEEPYEIQL
860 870 880 890 900
NQVIFWLSFL KSLVPVEEPI AFGGKLKNPL QVVLVATHAD IMNVPRPAGG
910 920 930 940 950
EFGYDKDTSL LKEIRNRFGN DLHISNKLFV LDAGASGSKD MKVLRNHLQE
960 970 980 990 1000
IRSQIVSVCP PMTHLCEKII STLPSWRKLN GPNQLMSLQQ FVYDVQDQLN
1010 1020 1030 1040 1050
PLASEEDLRR IAQQLHSTGE INIMQSETVQ DVLLLDPRWL CTNVLGKLLS
1060 1070 1080 1090 1100
VETPRALHHY RGRYTVEDIQ RLVPDSDVEE LLQILDAMDI CARDLSSGTM
1110 1120 1130 1140 1150
VDVPALIKTD NLHRSWADEE DEVMVYGGVR IVPVEHLTPF PCGIFHKVQV
1160 1170 1180 1190 1200
NLCRWIHQQS TEGDADIRLW VNGCKLANRG AELLVLLVNH GQGIEVQVRG
1210 1220 1230 1240 1250
LETEKIKCCL LLDSVCSTIE NVMATTLPGL LTVKHYLSPQ QLREHHEPVM
1260 1270 1280 1290 1300
IYQPRDFFRA QTLKETSLTN TMGGYKESFS SIMCFGCHDV YSQASLGMDI
1310 1320 1330 1340 1350
HASDLNLLTR RKLSRLLDPP DPLGKDWCLL AMNLGLPDLV AKYNTSNGAP
1360 1370 1380 1390 1400
KDFLPSPLHA LLREWTTYPE STVGTLMSKL RELGRRDAAD FLLKASSVFK
1410 1420 1430
INLDGNGQEA YASSCNSGTS YNSISSVVSR
Length:1,430
Mass (Da):160,046
Last modified:January 11, 2011 - v6
Checksum:iE2C4246E7C78A6D2
GO
Isoform 2 (identifier: P53355-2) [UniParc]FASTAAdd to basket
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.

Show »
Length:337
Mass (Da):36,765
Checksum:i3BA58BA79D87E0C6
GO
Isoform 3 (identifier: P53355-3) [UniParc]FASTAAdd to basket
Also known as: Beta

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

Show »
Length:1,440
Mass (Da):161,237
Checksum:iD43BB6B6A3F0ABF9
GO
Isoform 4 (identifier: P53355-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     805-870: Missing.

Note: No experimental confirmation available.
Show »
Length:1,364
Mass (Da):152,467
Checksum:i60E285E6A32348CB
GO

Sequence cautioni

The sequence AAP35581 differs from that shown. Contaminating sequence. Sequence of unknown origin in the C-terminal part.Curated
The sequence CAA53712 differs from that shown. Reason: Frameshift at positions 462 and 464.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti490Y → H in BAC87163 (PubMed:14702039).Curated1
Sequence conflicti1217S → G in CAH18690 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_033235416V → I.1 PublicationCorresponds to variant rs12343465dbSNPEnsembl.1
Natural variantiVAR_040420461A → S.1 Publication1
Natural variantiVAR_040421519S → A.1 Publication1
Natural variantiVAR_040422540C → Y.1 PublicationCorresponds to variant rs56327474dbSNPEnsembl.1
Natural variantiVAR_060693591P → L.1 PublicationCorresponds to variant rs36214022dbSNPEnsembl.1
Natural variantiVAR_060694622I → M.1 PublicationCorresponds to variant rs36215047dbSNPEnsembl.1
Natural variantiVAR_040423941M → T.1 Publication1
Natural variantiVAR_040424977R → W.1 Publication1
Natural variantiVAR_040425978K → N.1 Publication1
Natural variantiVAR_040426993Y → C.1 Publication1
Natural variantiVAR_040427994D → E.1 Publication1
Natural variantiVAR_0404281005E → Q.1 Publication1
Natural variantiVAR_0404291007D → Y.1 Publication1
Natural variantiVAR_0404301008L → P.1 Publication1
Natural variantiVAR_0404311010R → C.1 PublicationCorresponds to variant rs371784492dbSNPEnsembl.1
Natural variantiVAR_0404321018T → A.1 Publication1
Natural variantiVAR_0404331272M → I.1 PublicationCorresponds to variant rs56169226dbSNPEnsembl.1
Natural variantiVAR_0404341346S → N.5 PublicationsCorresponds to variant rs1056719dbSNPEnsembl.1
Natural variantiVAR_0404351405G → V.2 PublicationsCorresponds to variant rs36220450dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0420531 – 446Missing in isoform 2. 1 PublicationAdd BLAST446
Alternative sequenceiVSP_042054742 – 783VSVSI…APTHH → GRNLHAGPVSPAGVGFRTLS FQGLGGKGVVFGSLGLYWTL WP in isoform 2. 1 PublicationAdd BLAST42
Alternative sequenceiVSP_042055784 – 1430Missing in isoform 2. 1 PublicationAdd BLAST647
Alternative sequenceiVSP_054478805 – 870Missing in isoform 4. 1 PublicationAdd BLAST66
Alternative sequenceiVSP_0420561430R → RRNSHVWNPTV in isoform 3. Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BC143759 mRNA. Translation: AAI43760.1.
BT006935 mRNA. Translation: AAP35581.1. Sequence problems.
CCDSiCCDS43842.1. [P53355-1]
PIRiI37275.
RefSeqiNP_001275658.1. NM_001288729.1. [P53355-1]
NP_001275659.1. NM_001288730.1. [P53355-1]
NP_001275660.1. NM_001288731.1. [P53355-1]
NP_004929.2. NM_004938.3. [P53355-1]
UniGeneiHs.380277.
Hs.693441.

Genome annotation databases

EnsembliENST00000358077; ENSP00000350785; ENSG00000196730. [P53355-1]
ENST00000408954; ENSP00000386135; ENSG00000196730. [P53355-1]
ENST00000469640; ENSP00000418885; ENSG00000196730. [P53355-4]
ENST00000472284; ENSP00000417076; ENSG00000196730. [P53355-1]
ENST00000491893; ENSP00000419026; ENSG00000196730. [P53355-4]
ENST00000622514; ENSP00000484267; ENSG00000196730. [P53355-1]
GeneIDi1612.
KEGGihsa:1612.
UCSCiuc004apc.5. human. [P53355-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BC143759 mRNA. Translation: AAI43760.1.
BT006935 mRNA. Translation: AAP35581.1. Sequence problems.
CCDSiCCDS43842.1. [P53355-1]
PIRiI37275.
RefSeqiNP_001275658.1. NM_001288729.1. [P53355-1]
NP_001275659.1. NM_001288730.1. [P53355-1]
NP_001275660.1. NM_001288731.1. [P53355-1]
NP_004929.2. NM_004938.3. [P53355-1]
UniGeneiHs.380277.
Hs.693441.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IG1X-ray1.80A2-285[»]
1JKKX-ray2.40A2-285[»]
1JKLX-ray1.62A2-285[»]
1JKSX-ray1.50A2-285[»]
1JKTX-ray3.50A/B2-285[»]
1P4FX-ray1.90A2-285[»]
1WVWX-ray2.40A1-278[»]
1WVXX-ray2.60A1-278[»]
1WVYX-ray2.80A1-278[»]
1YR5X-ray1.70B302-320[»]
2W4JX-ray1.30A1-277[»]
2W4KX-ray1.90A1-302[»]
2X0GX-ray2.20A1-334[»]
2XUUX-ray1.80A1-334[»]
2XZSX-ray2.00A/B2-312[»]
2Y0AX-ray2.60A2-304[»]
2Y4PX-ray2.65A/B/C/D1-285[»]
2Y4VX-ray1.80B302-320[»]
2YAKX-ray2.20A1-285[»]
3DFCX-ray1.90B1-285[»]
3DGKX-ray1.70A1-285[»]
3EH9X-ray1.70A2-285[»]
3EHAX-ray1.60A2-285[»]
3F5GX-ray1.85A2-285[»]
3F5UX-ray2.00A1-285[»]
3GU4X-ray1.35A1-285[»]
3GU5X-ray1.65A1-285[»]
3GU6X-ray1.49A1-285[»]
3GU7X-ray1.90A1-285[»]
3GU8X-ray1.60A1-285[»]
3GUBX-ray1.71A1-285[»]
3ZXTX-ray2.65A/B/C/D1-285[»]
4B4LX-ray1.75A1-334[»]
4PF4X-ray1.13A1-277[»]
4TL0X-ray2.70A1-334[»]
4TXCX-ray1.95A1-285[»]
4UV0X-ray2.49A1-321[»]
4YO4X-ray1.60A2-285[»]
4YPDX-ray1.40A2-285[»]
5AUTX-ray1.70A1-285[»]
5AUUX-ray1.70A1-285[»]
5AUVX-ray1.50A1-285[»]
5AUWX-ray1.50A1-285[»]
5AUXX-ray1.50A1-285[»]
5AUYX-ray2.00A1-285[»]
5AUZX-ray1.60A1-285[»]
5AV0X-ray1.85A1-285[»]
5AV1X-ray1.50A1-285[»]
5AV2X-ray1.50A1-285[»]
5AV3X-ray1.90A1-285[»]
5AV4X-ray1.40A1-285[»]
ProteinModelPortaliP53355.
SMRiP53355.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107982. 51 interactors.
IntActiP53355. 33 interactors.
MINTiMINT-1136108.
STRINGi9606.ENSP00000350785.

Chemistry databases

BindingDBiP53355.
ChEMBLiCHEMBL2558.
GuidetoPHARMACOLOGYi2002.

PTM databases

iPTMnetiP53355.
PhosphoSitePlusiP53355.

Polymorphism and mutation databases

BioMutaiDAPK1.
DMDMi317373595.

Proteomic databases

EPDiP53355.
MaxQBiP53355.
PaxDbiP53355.
PeptideAtlasiP53355.
PRIDEiP53355.

Protocols and materials databases

DNASUi1612.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358077; ENSP00000350785; ENSG00000196730. [P53355-1]
ENST00000408954; ENSP00000386135; ENSG00000196730. [P53355-1]
ENST00000469640; ENSP00000418885; ENSG00000196730. [P53355-4]
ENST00000472284; ENSP00000417076; ENSG00000196730. [P53355-1]
ENST00000491893; ENSP00000419026; ENSG00000196730. [P53355-4]
ENST00000622514; ENSP00000484267; ENSG00000196730. [P53355-1]
GeneIDi1612.
KEGGihsa:1612.
UCSCiuc004apc.5. human. [P53355-1]

Organism-specific databases

CTDi1612.
DisGeNETi1612.
GeneCardsiDAPK1.
HGNCiHGNC:2674. DAPK1.
HPAiCAB037302.
HPA040472.
HPA048436.
MIMi600831. gene.
neXtProtiNX_P53355.
OpenTargetsiENSG00000196730.
PharmGKBiPA27142.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0032. Eukaryota.
ENOG410XRMJ. LUCA.
GeneTreeiENSGT00760000118877.
HOGENOMiHOG000082489.
HOVERGENiHBG051296.
InParanoidiP53355.
KOiK08803.
OMAiIDVQDKG.
OrthoDBiEOG091G0J2O.
PhylomeDBiP53355.
TreeFamiTF314166.

Enzyme and pathway databases

BioCyciZFISH:HS07488-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-418889. Ligand-independent caspase activation via DCC.
SignaLinkiP53355.
SIGNORiP53355.

Miscellaneous databases

ChiTaRSiDAPK1. human.
EvolutionaryTraceiP53355.
GeneWikiiDAPK1.
GenomeRNAii1612.
PROiP53355.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000196730.
CleanExiHS_DAPK1.
ExpressionAtlasiP53355. baseline and differential.
GenevisibleiP53355. HS.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR020676. DAPK1.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR011009. Kinase-like_dom.
IPR027417. P-loop_NTPase.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR020859. ROC_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR10489:SF699. PTHR10489:SF699. 1 hit.
PfamiPF12796. Ank_2. 2 hits.
PF00531. Death. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 9 hits.
SM00005. DEATH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50297. 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.
PS51424. ROC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDAPK1_HUMAN
AccessioniPrimary (citable) accession number: P53355
Secondary accession number(s): B7ZLD2
, B7ZLE7, Q14CQ7, Q1W5W0, Q68CP8, Q6ZRZ3, Q9BTL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: November 2, 2016
This is version 186 of the entry and version 6 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 9
    Human chromosome 9: 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.