Depdc5
entrez
277854
canonical
uniprot
P61460
canonical
ensembl
ENSMUSG00000037426
resolver
ensp
ENSMUSP00000052807
resolver
ensp
ENSMUSP00000085207
resolver
ensp
ENSMUSP00000113862
resolver
ensp
ENSMUSP00000113980
resolver
ensp
ENSMUSP00000179031
resolver
ensp
ENSMUSP00000179032
resolver
ensp
ENSMUSP00000179035
resolver
ensp
ENSMUSP00000179037
resolver
ensp
ENSMUSP00000179039
resolver
ensp
ENSMUSP00000179040
resolver
ensp
ENSMUSP00000179047
resolver
ensp
ENSMUSP00000179048
resolver
ensp
ENSMUSP00000327015
resolver
ensp
ENSMUSP00000327016
resolver
ensp
ENSMUSP00000327020
resolver
ensp
ENSMUSP00000327022
resolver
enst
ENSMUST00000049780
resolver
enst
ENSMUST00000087897
resolver
genesymbol
Depdc5
resolver
genesymbol_syn
Kiaa0645
resolver
uniprot
E9Q5J2
resolver
uniprot
E9Q5Y0
resolver
uniprot
E9QAT3
resolver
uniprot
F7C8L9
resolver
uniprot
Q6GQV2
resolver
uniprot
Q8BVE2
resolver
uniprot_entry
DEPD5_MOUSE
resolver
uniprot_entry
E9QAT3_MOUSE
resolver
uniprot_entry
F7C8L9_MOUSE
resolver
uniprot_entry
Q6GQV2_MOUSE
resolver
uniprot_entry
Q8BVE2_MOUSE
resolver
uniprot_sec
E9Q5J2
resolver
uniprot_sec
E9Q5Y0
resolver
amino_acid_sequence
MRTTKVYKLVIHKKGFGGSDDELVVNPKVFPHIKLGDIVEIAHPNDEYSPLLLQVKSLKEDLQKETISVDQTVTQVFRLRPYQDVYVNVVDPKDVTLDLVELTFKDQYIGRGDMWRLKKSLVSTCAYITQKVEFAGIRAQAGELWVKNEKVMCGYISEETRVVFRSTSAMVYIFIQMSCEMWDFDIYGDLYFEKAVNGFLADLFTKWKEKNCSHEVTVVLFSRTFYDAKSIDEFPEINRASIQEDHKGRFYEDFYKVVVQNERREEWTSLLVTIKKLFIQYPVLVRLEQAGGFPQGDNSTSAQGNYLEAINLSFNVFDKHYINRNFDRTGQMSVVITPGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFKLHNRSVPRDSRLGDDYNIPHWINHSFYTSKSQLFCNSFTPRIKLAGKKSASEKTKNGRDTSLGTPKESENTLPIQVDYDAYDAQVFRLPGPSRAQRLATCRSVREQENHSRKSASSCDVSSSPSLPSRALPTEEVRSQASDDSSLGKSTNILMIPNPHLHQYEVSSSLGYTSTRDVLENMIEPPQRDSSAPGRFHVGSAESMLHVRPGGYTPQRALINPFAPSRMPMKLTSNRRRWMHTFPVGPSGEAIQIHHQTRQNMAELQGSRQRDPTHSSAELLELAYHEAAGRHSTSRQPGDSMSLNFSGTEELSVSLLSNSSTGVNPRTQNKDSLEDSVSTSPDPMPGFCCTVGVDWKSLTTPACLPLTTDYFPDRQGLQNDYTEGCYDLLPEADMDRRDEEGVQMTAQQVFEEFICQRLMQGYQIIVQPKTQKPNTTVPPPLSSSPLYSRGLVSRNRPEEEGQYWLSMGRTFHKVTLKDKMITVTRYLPKYPYESAQIHYTYSLCPSHSDSEFVSCWVDFCHERLEEYKWNYLDQYICSAGSEDFSLIESLKFWRTRFLLLPACVTATKRITEGEVHCDIYGDKPRADEDEWQLLDGFIRFVEGLNRIRRRHRSDRMIRKGTAMKGLQMTGPISAHSLEAAGPPVGKKGTSALSALLEMEASQKSLGEQQTTVHGKSSTQPAENSSVAMTPTYVDSPRKDGAFFMEFVRSPRTASSAFYPQASVDQTAPLVLDSTSLGVSTGQPMDRGNNQTFGNSQNIEQAFPSANSGDYSSQQHVASSLTSSSTLVEILEAMKHPSTGVQLLSEQKGLSPCCFISAEVVHWLMNNVEGVQTQAMGIDIMQKMLEEQLITHASGEAWRTFIYGFYFYKIVMDKEPERVAMQQPSAPWYTAGADDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRPASYASRHSSFSRSFGGRSQAAALLAATVPEQRTVTLDVDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTATVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRAQLFIPLNLSCLLKEGSEHLFDSFEPETYWDRMHLFQEAIAHRFGFVQDKYSVSAFNFPAENKPQYIHVTGTVFLQLPYSKRKFSGQQRRRRNSTSSTNQNMFCEERVGYNWAYNTMLTKTWRSSATGDEKFADRLLKDFTDFCINRDNRLVTFWTNCLEKMHASAP
uniprot
proteins
function
FUNCTION: As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the mTORC1 pathway (PubMed:31548394). In response to amino acid depletion, the GATOR1 complex has GTPase activating protein (GAP) activity and strongly increases GTP hydrolysis by RagA/RRAGA (or RagB/RRAGB) within heterodimeric Rag complexes, thereby turning them into their inactive GDP-bound form, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling (By similarity). In the presence of abundant amino acids, the GATOR1 complex is negatively regulated by GATOR2, the other GATOR subcomplex, in this amino acid-sensing branch of the TORC1 pathway (By similarity). Within the GATOR1 complex, DEPDC5 mediates direct interaction with the nucleotide-binding pocket of small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD) and coordinates their nucleotide loading states by promoting RagA/RRAGA or RagB/RRAGB into their GDP-binding state and RagC/RRAGC or RagD/RRAGD into their GTP-binding state (By similarity). However, it does not execute the GAP activity, which is mediated by NPRL2 (By similarity). {ECO:0000250|UniProtKB:O75140, ECO:0000269|PubMed:31548394}.
uniprot
proteins
mass_dalton
180379
uniprot
proteins
mutagenesis
MUTAGEN 1518; /note="S->E: Mimics phosphorylation; knockin mice show a significant level of resistance to PIM1 inhibitors."; /evidence="ECO:0000269|PubMed:31548394
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-992 and Ser-1518 by AKT1 and PIM1 inhibit the activity of DEPDC5, releasing inhibition of the mTORC1 pathway. {ECO:0000269|PubMed:31548394}.; PTM: Ubiquitinated. Amino acid-induced 'Lys-48'-linked polyubiquitination of DEPDC5 by the BCR(KLHL22) ubiquitin ligase complex leads to DEPDC5 proteasomal degradation and inhibition of the GATOR1 complex. Ubiquitination may occur at multiple lysines. {ECO:0000250|UniProtKB:O75140}.
uniprot
proteins
protein_family
IML1 family
uniprot
proteins
pubmed
14621295
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23542697
uniprot
proteins
pubmed
31548394
uniprot
proteins
sequence_length
1591
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:O75140}. Cytoplasm, cytosol {ECO:0000269|PubMed:23542697}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:23542697}. Note=Localization to lysosomes is mediated by the KICSTOR complex and is amino acid-independent. {ECO:0000250|UniProtKB:O75140}.
uniprot
proteins