Q80YE7 (DAPK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

Dapk1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1442 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Regulates both type I apoptotic and type II autophagic cell deaths signal, depending on the cellular setting. The former is caspase-dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Phosphorylates PIN1 resulting in inhibition of its catalytic activity, nuclear localization, and cellular function. Phosphorylates TPM1, enhancing stress fiber formation in endothelial cells. Phosphorylates STX1A and significantly decreases its binding to STXBP1. Phosphorylates PRKD1 and regulates JNK signaling by binding and activating PRKD1 under oxidative stress. Phosphorylates BECN1, reducing its interaction with BCL2 and BCL2L1 and promoting the induction of autophagy. Phosphorylates TSC2, disrupting the TSC1-TSC2 complex and stimulating mTORC1 activity in a growth factor-dependent pathway. Phosphorylates RPS6, MYL9 and DAPK3 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.6 Ref.7 Ref.8
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.6
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.7
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.6 Ref.7
Disruption phenotype	Mice are protected against cerebral ischemic neuronal death. Ref.7
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 process	Apoptosis Translation regulation
Coding sequence diversity	Alternative splicing
Domain	ANK repeat Repeat
Ligand	ATP-binding Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic signaling pathway Traceable author statement PubMed 7828849. Source: ProtInc cellular response to interferon-gamma Inferred from mutant phenotype Ref.8. Source: UniProtKB induction of apoptosis Inferred from electronic annotation. Source: Compara intracellular protein kinase cascade Inferred from direct assay Ref.1. Source: UniProtKB negative regulation of apoptotic process Inferred from mutant phenotype Ref.1. Source: UniProtKB positive regulation of apoptotic process Inferred from mutant phenotype PubMed 15010850. Source: MGI regulation of N-methyl-D-aspartate selective glutamate receptor activity Inferred from mutant phenotype Ref.7. Source: UniProtKB regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	actin cytoskeleton Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from direct assay Ref.1. Source: UniProtKB calmodulin binding Inferred from direct assay Ref.1. Source: UniProtKB protein kinase activity Inferred from direct assay PubMed 20053891. Source: MGI protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Grin2b	Q01097	8	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1442	1442	Death-associated protein kinase 1		PRO_0000085911
Regions
	Domain	13 – 275	263	Protein kinase
	Repeat	378 – 407	30	ANK 1
	Repeat	411 – 440	30	ANK 2
	Repeat	444 – 473	30	ANK 3
	Repeat	477 – 506	30	ANK 4
	Repeat	510 – 539	30	ANK 5
	Repeat	543 – 572	30	ANK 6
	Repeat	576 – 605	30	ANK 7
	Repeat	609 – 638	30	ANK 8
	Repeat	875 – 904	30	ANK 9
	Repeat	1164 – 1196	33	ANK 10
	Domain	1312 – 1396	85	Death
	Nucleotide binding	19 – 27	9	ATP By similarity UniProtKB P53355
	Region	267 – 334	68	Calmodulin-binding By similarity UniProtKB P53355
	Region	292 – 301	10	Autoinhibitory domain By similarity
Sites
	Active site	139	1	Proton acceptor By similarity UniProtKB P53355
	Binding site	42	1	ATP By similarity UniProtKB P53355
Amino acid modifications
	Modified residue	289	1	Phosphoserine; by RPS6KA1 and RPS6KA3 By similarity
	Modified residue	308	1	Phosphoserine; by autocatalysis Ref.5 Ref.6 Ref.7 UniProtKB P53355
	Modified residue	333	1	Phosphoserine By similarity
	Modified residue	734	1	Phosphoserine; by MAPK1 By similarity
Natural variations
	Alternative sequence	1431 – 1442	12	Missing in isoform 2. Ref.1		VSP_050629
Experimental info
	Sequence conflict	354	1	D → N in CAA65762. Ref.2
	Sequence conflict	441	1	K → Q in AAH57317. Ref.3
	Sequence conflict	441	1	K → Q in AAH60161. Ref.3
	Sequence conflict	461	1	V → A in CAA65762. Ref.2
	Sequence conflict	960	1	S → P in CAA65762. Ref.2
	Sequence conflict	1000	1	N → T in CAA65762. Ref.2
	Sequence conflict	1038 – 1042	5	RWLCT → PMALH in CAA65762. Ref.2
	Sequence conflict	1105	1	A → V in AAO91934. Ref.1
	Sequence conflict	1105	1	A → V in AAO91935. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Beta) [UniParc]. Last modified November 28, 2003. Version 3. Checksum: 243A14D7C6598F63	FASTA	1,442	161,442
	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
	Isoform 2 (Alpha) [UniParc]. Checksum: FB5B401603C273D9	FASTA	1,430	159,986
	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 RELGRRDAAD FLLKASSVFK INLDGNGQEA YASSCNSGTS YNSISSVVSR

References

	« Hide 'large scale' referencesShow '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. , 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: AUTOPHOSPHORYLATION AT SER-308, ENZYME REGULATION, INTERACTION WITH UNC5B.
[6]	"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.
[7]	"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.
[8]	"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.
IPI	IPI00395143. IPI00395144.
RefSeq	NP_083929.2. NM_029653.2.
UniGene	Mm.24103.
3D structure databases
ProteinModelPortal	Q80YE7.
SMR	Q80YE7. Positions 3-741.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q80YE7. 3 interactions.
PTM databases
PhosphoSite	Q80YE7.
Proteomic databases
PaxDb	Q80YE7.
PRIDE	Q80YE7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000044083; ENSMUSP00000040825; ENSMUSG00000021559. ENSMUST00000077453; ENSMUSP00000076666; ENSMUSG00000021559.
GeneID	69635.
KEGG	mmu:69635.
UCSC	uc007qvm.1. mouse.
Organism-specific databases
CTD	1612.
MGI	MGI:1916885. Dapk1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00680000099521.
HOGENOM	HOG000082489.
HOVERGEN	HBG051296.
InParanoid	Q80YE7.
KO	K08803.
OMA	CLAEHGA.
OrthoDB	EOG4KD6K6.
Enzyme and pathway databases
Reactome	REACT_100962. Apoptosis.
Gene expression databases
Bgee	Q80YE7.
CleanEx	MM_DAPK1.
Genevestigator	Q80YE7.
GermOnline	ENSMUSG00000021559. Mus musculus.
Family and domain databases
Gene3D	1.10.533.10. 1 hit. 1.25.40.20. 3 hits.
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR020676. Death-assoc_prot_kinase. IPR011029. DEATH-like_dom. IPR000488. Death_domain. IPR011009. Kinase-like_dom. IPR020675. Myosin_light_ch_kinase-rel. IPR027417. P-loop_NTPase. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
PANTHER	PTHR22964. PTHR22964. 1 hit. PTHR22964:SF1. PTHR22964:SF1. 1 hit.
Pfam	PF00023. Ank. 1 hit. PF12796. Ank_2. 2 hits. PF00531. Death. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
PRINTS	PR01415. ANKYRIN.
SMART	SM00248. ANK. 9 hits. SM00005. DEATH. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit. SSF47986. DEATH_like. 1 hit. SSF56112. Kinase_like. 1 hit. SSF52540. SSF52540. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 7 hits. PS50017. DEATH_DOMAIN. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	329950.
SOURCE	Search...

Entry information

Entry name

DAPK1_MOUSE

Accession

Primary (citable) accession number: Q80YE7
Secondary accession number(s): Q80YE6 , Q8R341, Q8VDN6, Q9CSD4, Q9JJP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	November 28, 2003
Last modified:	May 29, 2013
This is version 107 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program