Dapk1
entrez
69635
canonical
uniprot
Q80YE7
canonical
ensembl
ENSMUSG00000021559
resolver
ensp
ENSMUSP00000040825
resolver
ensp
ENSMUSP00000076666
resolver
ensp
ENSMUSP00000153607
resolver
genesymbol
Dapk1
resolver
uniprot
Q3UKP8
resolver
uniprot
Q80YE6
resolver
uniprot
Q8R341
resolver
uniprot
Q8VDN6
resolver
uniprot
Q9CSD4
resolver
uniprot
Q9JJP7
resolver
uniprot_entry
DAPK1_MOUSE
resolver
uniprot_entry
Q3UKP8_MOUSE
resolver
uniprot_sec
Q80YE6
resolver
uniprot_sec
Q8R341
resolver
uniprot_sec
Q8VDN6
resolver
uniprot_sec
Q9CSD4
resolver
uniprot_sec
Q9JJP7
resolver
activity_regulation
ACTIVITY REGULATION: Activated by Ca(2+)/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. {ECO:0000269|PubMed:15729359, ECO:0000269|PubMed:18806755}.
uniprot
proteins
amino_acid_sequence
MTVFRQENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIRHPNVITLHEVYENKTDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILSGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAHKIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYDFEEEFFRNTSTLAKDFIRRLLVKDPKKRMTIQDSLQHPWIKPKDTQQALSRKASAVNMEKFKKFAARKKWKQSVRLISLCQRLSRSFLSRSNMSVARSDDTLDEEDSFVMKAIIHAINDDNVPGLQHLLGSLSSYDVNQPNKHGTPPLLIAAGCGNIQMLQLLIKRGSRIDVQDKGGSNAIYWASRHGHVDTLKFLNENKCPLDVKDKSGETALHVAARYGHADVVQLLCSFGSNPDFQDKEEETPLHCAAWHGYYSVAKALCEVGCNVNIKNREGETPLLTASARGYHDIVECLAEHGADLNASDKDGHIALHLAVRRCQMEVIKTLLGHGSFVDFQDRHGNTPLHVACKDGSAPIVVALCEASCNLDISNKYGRTPLHLAANNGILDVVRYLCLMGANVEALTSDGKTAEDLAKAEQHEHVAGLLARLRKDTHRGLFIQQLRPTQNLQPRIKLKLFGHSGSGKSTLVESLKCGLLRSFFRRRRPRLSSTNSTRFPPSPLAAKPTVSVSINNLYPGCENVSVRSRSMMFEPGLTKGMLEVFVAPSHHLHCSTDDQSTKAIDIQNAYLNGVGDFSVWEFSGNPVYFCCYDYFAANDPTSIHIIVFSLEEPYEIQLNQVIFWLSFLKSLVPVEEPIAFGGKLKNPLRVVLVATHADIMNIPRPAGGEFGYDKDTSLLKEIRNRFGNDLHVSNKLFVLDAGASGSKDIKVLRNHLQEIRSQIVSGCSPMTHLCEKIISTLPSWRKLNGPNQLMSLQQFVYDVQDQLNPLASEDDLRRIAQQLHSTGEINIMQSETVQDVLLLDPRWLCTNVLGKLLSVETPRALHHYRGRYTMEDIQRLVPDSDVEELLQILDAMDICARDLSSGTMVDIPALIKTDSLQRSWADEEDEVMVYGGVRIVPVEHLTPFPCGIFHKVQVNLCRWIHQQSAEGDADIRLWVSGCRIANRGAELLVLLVNHGQGIEVQVRGLETEKIKCCLLLDSVCSTIETVMATTLPGLLTVKHYLSPQQLREHHEPVMVYQPRDFFRAQTLKESSLTNTMGGYKESFSSITCFGCHDVYSQASLGMDIHASDLSLLTRRKLSRLLDPPDPMGKDWCLLAMNLGLPDMVAKHNVNNRASRDFLPSPVHALLQEWTSYPESTVGILISKLRELGRRDAADFLLKASSVFKINLDGNGQEAYASSCNSGTSYNSISSVVSRRDSHAWTPLYDL
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
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 Ca(2+) 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. {ECO:0000250, ECO:0000269|PubMed:11485996, ECO:0000269|PubMed:18806755, ECO:0000269|PubMed:20141836, ECO:0000269|PubMed:23071094}.
uniprot
proteins
mass_dalton
161442
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by the BCR(KLHL20) E3 ubiquitin ligase complex, leading to its degradation by the proteasome. {ECO:0000250}.; PTM: 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. {ECO:0000269|PubMed:15729359, ECO:0000269|PubMed:20141836}.
uniprot
proteins
protein_family
CAMK Ser/Thr protein kinase family
uniprot
proteins
protein_family
DAP kinase subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
11485996
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15729359
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
18806755
uniprot
proteins
pubmed
20141836
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23071094
uniprot
proteins
sequence_length
1442
uniprot
proteins