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P53355

- DAPK1_HUMAN

UniProt

P53355 - DAPK1_HUMAN

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Protein

Death-associated protein kinase 1

Gene

DAPK1

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. 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei42 – 421ATP
Binding sitei100 – 1001ATP
Active sitei139 – 1391Proton acceptorPROSITE-ProRule annotation
Binding sitei161 – 1611ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 279ATP
Nucleotide bindingi94 – 963ATP

GO - Molecular functioni

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

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. apoptotic signaling pathway Source: UniProtKB
  3. cellular response to interferon-gamma Source: UniProtKB
  4. extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  5. intracellular signal transduction Source: UniProtKB
  6. negative regulation of apoptotic process Source: Ensembl
  7. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  8. negative regulation of translation Source: UniProtKB
  9. positive regulation of apoptotic process Source: Reactome
  10. protein autophosphorylation Source: UniProtKB
  11. protein phosphorylation Source: UniProtKB
  12. regulation of apoptotic process Source: UniProtKB
  13. regulation of autophagy Source: UniProtKB
  14. 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, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_22128. Role of DCC in regulating apoptosis.
SignaLinkiP53355.

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
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:2674. DAPK1.

Subcellular locationi

Isoform 1 : Cytoplasm. Cytoplasmcytoskeleton
Note: Colocalizes with MAP1B in the microtubules and cortical actin fibers.

GO - Cellular componenti

  1. actin cytoskeleton Source: UniProtKB
  2. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi42 – 421K → A: Loss of activity, apoptotic function and of autophosphorylation. 2 Publications
Mutagenesisi289 – 2891S → A: Loss of phosphorylation and significant increase in proapoptotic activity.
Mutagenesisi289 – 2891S → E: Reduction in proapoptotic activity.
Mutagenesisi308 – 3081S → A: Elevated Ca(2+)-calmodulin binding and Ca(2+)-calmodulin-independent kinase activity. Increases apoptotic activity. 1 Publication
Mutagenesisi308 – 3081S → D: Reduced Ca(2+)-calmodulin binding and Ca(2+)-calmodulin-independent kinase activity. Decreases apoptotic activity. 1 Publication
Mutagenesisi313 – 3131S → A: Minimal effect on activity. 1 Publication

Organism-specific databases

PharmGKBiPA27142.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14301430Death-associated protein kinase 1PRO_0000085910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei289 – 2891Phosphoserine; by RPS6KA1 and RPS6KA31 Publication
Modified residuei308 – 3081Phosphoserine; by autocatalysis3 Publications
Modified residuei333 – 3331Phosphoserine1 Publication
Modified residuei734 – 7341Phosphoserine; by MAPK11 Publication

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-308.6 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP53355.
PaxDbiP53355.
PRIDEiP53355.

PTM databases

PhosphoSiteiP53355.

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

BgeeiP53355.
CleanExiHS_DAPK1.
ExpressionAtlasiP53355. baseline and differential.
GenevestigatoriP53355.

Organism-specific databases

HPAiCAB037302.

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
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

Protein-protein interaction databases

BioGridi107982. 25 interactions.
IntActiP53355. 18 interactions.
MINTiMINT-1136108.
STRINGi9606.ENSP00000350785.

Structurei

Secondary structure

1
1430
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113Combined sources
Beta strandi13 – 219Combined sources
Beta strandi23 – 3210Combined sources
Turni33 – 353Combined sources
Beta strandi38 – 469Combined sources
Beta strandi48 – 514Combined sources
Beta strandi53 – 564Combined sources
Helixi58 – 7013Combined sources
Beta strandi79 – 846Combined sources
Beta strandi86 – 949Combined sources
Helixi101 – 1077Combined sources
Beta strandi108 – 1103Combined sources
Helixi113 – 13220Combined sources
Beta strandi134 – 1363Combined sources
Helixi142 – 1443Combined sources
Beta strandi145 – 1484Combined sources
Beta strandi150 – 1545Combined sources
Beta strandi157 – 1593Combined sources
Helixi162 – 1643Combined sources
Beta strandi169 – 1713Combined sources
Helixi181 – 1833Combined sources
Helixi186 – 1894Combined sources
Helixi197 – 21216Combined sources
Helixi222 – 2309Combined sources
Helixi238 – 2414Combined sources
Beta strandi242 – 2443Combined sources
Helixi246 – 25510Combined sources
Turni260 – 2623Combined sources
Helixi266 – 2716Combined sources
Turni273 – 2753Combined sources
Helixi280 – 2889Combined sources
Helixi293 – 30210Combined sources
Helixi304 – 31815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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-ray1.90B1-295[»]
3DGKX-ray1.70A1-295[»]
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[»]
4TXCX-ray1.95A1-285[»]
ProteinModelPortaliP53355.
SMRiP53355. Positions 3-320, 345-712.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53355.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 275263Protein kinasePROSITE-ProRule annotationAdd
BLAST
Repeati378 – 40730ANK 1Add
BLAST
Repeati411 – 44030ANK 2Add
BLAST
Repeati444 – 47330ANK 3Add
BLAST
Repeati477 – 50630ANK 4Add
BLAST
Repeati510 – 53930ANK 5Add
BLAST
Repeati543 – 57230ANK 6Add
BLAST
Repeati576 – 60530ANK 7Add
BLAST
Repeati609 – 63830ANK 8Add
BLAST
Repeati875 – 90430ANK 9Add
BLAST
Repeati1162 – 119635ANK 10Add
BLAST
Domaini1312 – 139685DeathPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni267 – 33468Calmodulin-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.

Sequence similaritiesi

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

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00760000118877.
HOVERGENiHBG051296.
InParanoidiP53355.
KOiK08803.
OrthoDBiEOG7QZGBH.
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.
IPR020675. Myosin_light_ch_kinase-rel.
IPR027417. P-loop_NTPase.
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.
PTHR22964:SF54. PTHR22964:SF54. 1 hit.
PfamiPF00023. Ank. 6 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.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

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 AAP35581.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.Curated
The sequence CAA53712.1 differs from that shown. Reason: Frameshift at positions 462 and 464. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti490 – 4901Y → H in BAC87163. (PubMed:14702039)Curated
Sequence conflicti1217 – 12171S → G in CAH18690. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti416 – 4161V → I.1 Publication
Corresponds to variant rs12343465 [ dbSNP | Ensembl ].
VAR_033235
Natural varianti461 – 4611A → S.1 Publication
VAR_040420
Natural varianti519 – 5191S → A.1 Publication
VAR_040421
Natural varianti540 – 5401C → Y.1 Publication
Corresponds to variant rs56327474 [ dbSNP | Ensembl ].
VAR_040422
Natural varianti591 – 5911P → L.1 Publication
VAR_060693
Natural varianti622 – 6221I → M.1 Publication
Corresponds to variant rs36215047 [ dbSNP | Ensembl ].
VAR_060694
Natural varianti941 – 9411M → T.1 Publication
VAR_040423
Natural varianti977 – 9771R → W.1 Publication
VAR_040424
Natural varianti978 – 9781K → N.1 Publication
VAR_040425
Natural varianti993 – 9931Y → C.1 Publication
VAR_040426
Natural varianti994 – 9941D → E.1 Publication
VAR_040427
Natural varianti1005 – 10051E → Q.1 Publication
VAR_040428
Natural varianti1007 – 10071D → Y.1 Publication
VAR_040429
Natural varianti1008 – 10081L → P.1 Publication
VAR_040430
Natural varianti1010 – 10101R → C.1 Publication
VAR_040431
Natural varianti1018 – 10181T → A.1 Publication
VAR_040432
Natural varianti1272 – 12721M → I.1 Publication
Corresponds to variant rs56169226 [ dbSNP | Ensembl ].
VAR_040433
Natural varianti1346 – 13461S → N.5 Publications
Corresponds to variant rs1056719 [ dbSNP | Ensembl ].
VAR_040434
Natural varianti1405 – 14051G → V.2 Publications
Corresponds to variant rs36220450 [ dbSNP | Ensembl ].
VAR_040435

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 446446Missing in isoform 2. 1 PublicationVSP_042053Add
BLAST
Alternative sequencei742 – 78342VSVSI…APTHH → GRNLHAGPVSPAGVGFRTLS FQGLGGKGVVFGSLGLYWTL WP in isoform 2. 1 PublicationVSP_042054Add
BLAST
Alternative sequencei784 – 1430647Missing in isoform 2. 1 PublicationVSP_042055Add
BLAST
Alternative sequencei805 – 87066Missing in isoform 4. 1 PublicationVSP_054478Add
BLAST
Alternative sequencei1430 – 14301R → RRNSHVWNPTV in isoform 3. CuratedVSP_042056

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.3. human. [P53355-1]
uc004apf.1. human. [P53355-2]
uc011ltg.2. human.

Polymorphism databases

DMDMi317373595.

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.
CCDSi CCDS43842.1. [P53355-1 ]
PIRi I37275.
RefSeqi NP_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 ]
UniGenei Hs.380277.
Hs.693441.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 1-295 [» ]
3DGK X-ray 1.70 A 1-295 [» ]
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 [» ]
4B4L X-ray 1.75 A 1-334 [» ]
4PF4 X-ray 1.13 A 1-277 [» ]
4TXC X-ray 1.95 A 1-285 [» ]
ProteinModelPortali P53355.
SMRi P53355. Positions 3-320, 345-712.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107982. 25 interactions.
IntActi P53355. 18 interactions.
MINTi MINT-1136108.
STRINGi 9606.ENSP00000350785.

Chemistry

BindingDBi P53355.
ChEMBLi CHEMBL2558.
GuidetoPHARMACOLOGYi 2002.

PTM databases

PhosphoSitei P53355.

Polymorphism databases

DMDMi 317373595.

Proteomic databases

MaxQBi P53355.
PaxDbi P53355.
PRIDEi P53355.

Protocols and materials databases

DNASUi 1612.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358077 ; 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 ]
GeneIDi 1612.
KEGGi hsa:1612.
UCSCi uc004apc.3. human. [P53355-1 ]
uc004apf.1. human. [P53355-2 ]
uc011ltg.2. human.

Organism-specific databases

CTDi 1612.
GeneCardsi GC09P090112.
HGNCi HGNC:2674. DAPK1.
HPAi CAB037302.
MIMi 600831. gene.
neXtProti NX_P53355.
PharmGKBi PA27142.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00760000118877.
HOVERGENi HBG051296.
InParanoidi P53355.
KOi K08803.
OrthoDBi EOG7QZGBH.
PhylomeDBi P53355.
TreeFami TF314166.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 2681.
Reactomei REACT_22128. Role of DCC in regulating apoptosis.
SignaLinki P53355.

Miscellaneous databases

ChiTaRSi DAPK1. human.
EvolutionaryTracei P53355.
GeneWikii DAPK1.
GenomeRNAii 1612.
NextBioi 35481278.
PROi P53355.
SOURCEi Search...

Gene expression databases

Bgeei P53355.
CleanExi HS_DAPK1.
ExpressionAtlasi P53355. baseline and differential.
Genevestigatori P53355.

Family and domain databases

Gene3Di 1.10.533.10. 1 hit.
1.25.40.20. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR020676. DAPK1.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR011009. Kinase-like_dom.
IPR020675. Myosin_light_ch_kinase-rel.
IPR027417. P-loop_NTPase.
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.
PTHR22964:SF54. PTHR22964:SF54. 1 hit.
Pfami PF00023. Ank. 6 hits.
PF00531. Death. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR01415. ANKYRIN.
SMARTi SM00248. ANK. 9 hits.
SM00005. DEATH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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] (ISOFORMS 1 AND 4).
    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: PHOSPHORYLATION 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), PHOSPHORYLATION 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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.

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 26, 2014
This is version 165 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

External Data

Dasty 3