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Q80YE7 (DAPK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Death-associated protein kinase 1

Short name=DAP kinase 1
EC=2.7.11.1
Gene names
Name:Dapk1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1442 AA.
Sequence statusComplete.
Protein existenceEvidence 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 By similarity. 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.7 Ref.8 Ref.9

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium. Ref.1

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.5 Ref.7

Subunit structure

Interacts with KLHL20. Interacts (via death domain) with MAPK1 and MAPK3. Interacts with MAP1B (via N-terminus). Interacts with PRKD1 in an oxidative stress-regulated manner. Interacts with PIN1, PDCD6, BECN1, TSC2 and STX1A By similarity. Interacts (via death domain) with UNC5B (via death domain). Interacts with GRINB. Ref.5 Ref.8

Tissue specificity

High levels in bladder, uterus, vas deferens, lung, liver and kidney. Ref.1

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 By similarity.

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.5 Ref.7 Ref.8

Disruption phenotype

Mice are protected against cerebral ischemic neuronal death. Ref.8

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 AAH21490.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processApoptosis
Translation regulation
   Coding sequence diversityAlternative splicing
   DomainANK repeat
Repeat
   LigandATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic signaling pathway

Traceable author statement PubMed 7828849. Source: ProtInc

cellular response to interferon-gamma

Inferred from mutant phenotype Ref.9. Source: UniProtKB

extrinsic apoptotic signaling pathway via death domain receptors

Inferred from mutant phenotype PubMed 15010850. Source: MGI

intracellular signal transduction

Inferred from direct assay Ref.1. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.1. Source: UniProtKB

negative regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from direct assay Ref.1. Source: MGI

negative regulation of translation

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of N-methyl-D-aspartate selective glutamate receptor activity

Inferred from mutant phenotype Ref.8. Source: UniProtKB

   Cellular_componentactin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 15010850. Source: MGI

cytosol

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from direct assay Ref.1. Source: UniProtKB

calmodulin binding

Inferred from direct assay Ref.1. Source: UniProtKB

calmodulin-dependent protein kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction Ref.8. Source: IntAct

protein kinase activity

Inferred from direct assay PubMed 20053891. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Grin2bQ010978EBI-2584874,EBI-400125

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q80YE7-1)

Also known as: Beta;

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: Q80YE7-2)

Also known as: Alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     1431-1442: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14421442Death-associated protein kinase 1
PRO_0000085911

Regions

Domain13 – 275263Protein kinase
Repeat378 – 40730ANK 1
Repeat411 – 44030ANK 2
Repeat444 – 47330ANK 3
Repeat477 – 50630ANK 4
Repeat510 – 53930ANK 5
Repeat543 – 57230ANK 6
Repeat576 – 60530ANK 7
Repeat609 – 63830ANK 8
Repeat875 – 90430ANK 9
Repeat1164 – 119633ANK 10
Domain1312 – 139685Death
Nucleotide binding19 – 279ATP By similarity UniProtKB P53355
Region267 – 33468Calmodulin-binding By similarity UniProtKB P53355
Region292 – 30110Autoinhibitory domain By similarity

Sites

Active site1391Proton acceptor By similarity UniProtKB P53355
Binding site421ATP By similarity UniProtKB P53355

Amino acid modifications

Modified residue2891Phosphoserine; by RPS6KA1 and RPS6KA3 By similarity
Modified residue3081Phosphoserine; by autocatalysis Ref.5 Ref.7 Ref.8 UniProtKB P53355
Modified residue3331Phosphoserine Ref.6
Modified residue7341Phosphoserine; by MAPK1 By similarity

Natural variations

Alternative sequence1431 – 144212Missing in isoform 2. Ref.1
VSP_050629

Experimental info

Sequence conflict3541D → N in CAA65762. Ref.2
Sequence conflict4411K → Q in AAH57317. Ref.3
Sequence conflict4411K → Q in AAH60161. Ref.3
Sequence conflict4611V → A in CAA65762. Ref.2
Sequence conflict9601S → P in CAA65762. Ref.2
Sequence conflict10001N → T in CAA65762. Ref.2
Sequence conflict1038 – 10425RWLCT → PMALH in CAA65762. Ref.2
Sequence conflict11051A → V in AAO91934. Ref.1
Sequence conflict11051A → V in AAO91935. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Beta) [UniParc].

Last modified November 28, 2003. Version 3.
Checksum: 243A14D7C6598F63

FASTA1,442161,442
        10         20         30         40         50         60 
MTVFRQENVD DYYDTGEELG SGQFAVVKKC REKSTGLQYA AKFIKKRRTK SSRRGVSRED 

        70         80         90        100        110        120 
IEREVSILKE IRHPNVITLH EVYENKTDVI LILELVAGGE LFDFLAEKES LTEEEATEFL 

       130        140        150        160        170        180 
KQILSGVYYL HSLQIAHFDL KPENIMLLDR NVPKPRIKII DFGLAHKIDF GNEFKNIFGT 

       190        200        210        220        230        240 
PEFVAPEIVN YEPLGLEADM WSIGVITYIL LSGASPFLGD TKQETLANVS AVNYDFEEEF 

       250        260        270        280        290        300 
FRNTSTLAKD FIRRLLVKDP KKRMTIQDSL QHPWIKPKDT QQALSRKASA VNMEKFKKFA 

       310        320        330        340        350        360 
ARKKWKQSVR LISLCQRLSR SFLSRSNMSV ARSDDTLDEE DSFVMKAIIH AINDDNVPGL 

       370        380        390        400        410        420 
QHLLGSLSSY DVNQPNKHGT PPLLIAAGCG NIQMLQLLIK RGSRIDVQDK GGSNAIYWAS 

       430        440        450        460        470        480 
RHGHVDTLKF LNENKCPLDV KDKSGETALH VAARYGHADV VQLLCSFGSN PDFQDKEEET 

       490        500        510        520        530        540 
PLHCAAWHGY YSVAKALCEV GCNVNIKNRE GETPLLTASA RGYHDIVECL AEHGADLNAS 

       550        560        570        580        590        600 
DKDGHIALHL AVRRCQMEVI KTLLGHGSFV DFQDRHGNTP LHVACKDGSA PIVVALCEAS 

       610        620        630        640        650        660 
CNLDISNKYG RTPLHLAANN GILDVVRYLC LMGANVEALT SDGKTAEDLA KAEQHEHVAG 

       670        680        690        700        710        720 
LLARLRKDTH RGLFIQQLRP TQNLQPRIKL KLFGHSGSGK STLVESLKCG LLRSFFRRRR 

       730        740        750        760        770        780 
PRLSSTNSTR FPPSPLAAKP TVSVSINNLY PGCENVSVRS RSMMFEPGLT KGMLEVFVAP 

       790        800        810        820        830        840 
SHHLHCSTDD QSTKAIDIQN AYLNGVGDFS VWEFSGNPVY FCCYDYFAAN DPTSIHIIVF 

       850        860        870        880        890        900 
SLEEPYEIQL NQVIFWLSFL KSLVPVEEPI AFGGKLKNPL RVVLVATHAD IMNIPRPAGG 

       910        920        930        940        950        960 
EFGYDKDTSL LKEIRNRFGN DLHVSNKLFV LDAGASGSKD IKVLRNHLQE IRSQIVSGCS 

       970        980        990       1000       1010       1020 
PMTHLCEKII STLPSWRKLN GPNQLMSLQQ FVYDVQDQLN PLASEDDLRR IAQQLHSTGE 

      1030       1040       1050       1060       1070       1080 
INIMQSETVQ DVLLLDPRWL CTNVLGKLLS VETPRALHHY RGRYTMEDIQ RLVPDSDVEE 

      1090       1100       1110       1120       1130       1140 
LLQILDAMDI CARDLSSGTM VDIPALIKTD SLQRSWADEE DEVMVYGGVR IVPVEHLTPF 

      1150       1160       1170       1180       1190       1200 
PCGIFHKVQV NLCRWIHQQS AEGDADIRLW VSGCRIANRG AELLVLLVNH GQGIEVQVRG 

      1210       1220       1230       1240       1250       1260 
LETEKIKCCL LLDSVCSTIE TVMATTLPGL LTVKHYLSPQ QLREHHEPVM VYQPRDFFRA 

      1270       1280       1290       1300       1310       1320 
QTLKESSLTN TMGGYKESFS SITCFGCHDV YSQASLGMDI HASDLSLLTR RKLSRLLDPP 

      1330       1340       1350       1360       1370       1380 
DPMGKDWCLL AMNLGLPDMV AKHNVNNRAS RDFLPSPVHA LLQEWTSYPE STVGILISKL 

      1390       1400       1410       1420       1430       1440 
RELGRRDAAD FLLKASSVFK INLDGNGQEA YASSCNSGTS YNSISSVVSR RDSHAWTPLY 


DL 

« Hide

Isoform 2 (Alpha) [UniParc].

Checksum: FB5B401603C273D9
Show »

FASTA1,430159,986

References

« Hide 'large scale' references
[1]"Identification of a new form of death-associated protein kinase that promotes cell survival."
Jin Y., Blue E.K., Dixon S., Hou L., Wysolmerski R.B., Gallagher P.J.
J. Biol. Chem. 276:39667-39678(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY.
Tissue: Embryo.
[2]Kimchi A.
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"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 2).
Strain: C57BL/6.
Tissue: Brain and Mammary gland.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1203-1442 (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Embryo.
[5]"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.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"DAP-kinase is a mediator of endoplasmic reticulum stress-induced caspase activation and autophagic cell death."
Gozuacik D., Bialik S., Raveh T., Mitou G., Shohat G., Sabanay H., Mizushima N., Yoshimori T., Kimchi A.
Cell Death Differ. 15:1875-1886(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEPHOSPHORYLATION AT SER-308, ENZYME REGULATION.
[8]"DAPK1 interaction with NMDA receptor NR2B subunits mediates brain damage in stroke."
Tu W., Xu X., Peng L., Zhong X., Zhang W., Soundarapandian M.M., Balel C., Wang M., Jia N., Zhang W., Lew F., Chan S.L., Chen Y., Lu Y.
Cell 140:222-234(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH GRIN2B, AUTOPHOSPHORYLATION AT SER-308, DISRUPTION PHENOTYPE.
[9]"Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages."
Arif A., Chatterjee P., Moodt R.A., Fox P.L.
Mol. Cell. Biol. 32:5046-5055(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY245540 mRNA. Translation: AAO91934.2.
AY245541 mRNA. Translation: AAO91935.1.
X97048 mRNA. Translation: CAA65762.1.
BC021490 mRNA. Translation: AAH21490.1. Different initiation.
BC026671 mRNA. Translation: AAH26671.1.
BC057317 mRNA. Translation: AAH57317.1.
BC060161 mRNA. Translation: AAH60161.1.
AK013153 mRNA. Translation: BAB28681.1.
CCDSCCDS26581.1. [Q80YE7-2]
RefSeqNP_001272846.1. NM_001285917.1. [Q80YE7-1]
NP_083929.2. NM_029653.3. [Q80YE7-2]
NP_598823.1. NM_134062.2. [Q80YE7-2]
XP_006517433.1. XM_006517370.1. [Q80YE7-1]
UniGeneMm.24103.

3D structure databases

ProteinModelPortalQ80YE7.
SMRQ80YE7. Positions 3-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid213581. 3 interactions.
IntActQ80YE7. 3 interactions.

PTM databases

PhosphoSiteQ80YE7.

Proteomic databases

PaxDbQ80YE7.
PRIDEQ80YE7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000044083; ENSMUSP00000040825; ENSMUSG00000021559. [Q80YE7-2]
ENSMUST00000077453; ENSMUSP00000076666; ENSMUSG00000021559. [Q80YE7-2]
GeneID69635.
KEGGmmu:69635.
UCSCuc007qvm.1. mouse. [Q80YE7-1]

Organism-specific databases

CTD1612.
MGIMGI:1916885. Dapk1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000114993.
HOGENOMHOG000082489.
HOVERGENHBG051296.
InParanoidQ80YE7.
KOK08803.
OMACLAEHGA.
OrthoDBEOG7QZGBH.
PhylomeDBQ80YE7.
TreeFamTF314166.

Gene expression databases

BgeeQ80YE7.
CleanExMM_DAPK1.
GenevestigatorQ80YE7.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
1.25.40.20. 3 hits.
InterProIPR002110. 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_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR22964. PTHR22964. 1 hit.
PTHR22964:SF54. PTHR22964:SF54. 1 hit.
PfamPF12796. Ank_2. 3 hits.
PF00531. Death. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 9 hits.
SM00005. DEATH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEPS50297. 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]
ProtoNetSearch...

Other

NextBio329950.
PROQ80YE7.
SOURCESearch...

Entry information

Entry nameDAPK1_MOUSE
AccessionPrimary (citable) accession number: Q80YE7
Secondary accession number(s): Q80YE6 expand/collapse secondary AC list , Q8R341, Q8VDN6, Q9CSD4, Q9JJP7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: November 28, 2003
Last modified: July 9, 2014
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot