LRRK2
entrez
120892
canonical
uniprot
Q5S007
canonical
ensembl
ENSG00000188906
resolver
ensp
ENSP00000298910
resolver
ensp
ENSP00000725867
resolver
ensp
ENSP00000783393
resolver
enst
ENST00000298910
resolver
genesymbol
LRRK2
resolver
genesymbol_syn
PARK8
resolver
hgnc
HGNC:18618
resolver
uniprot
A6NJU2
resolver
uniprot
Q17RV3
resolver
uniprot
Q6ZS50
resolver
uniprot
Q8NCX9
resolver
uniprot_entry
LRRK2_HUMAN
resolver
uniprot_entry
Q17RV3_HUMAN
resolver
uniprot_sec
A6NJU2
resolver
uniprot_sec
Q6ZS50
resolver
uniprot_sec
Q8NCX9
resolver
activity_regulation
ACTIVITY REGULATION: Kinase activity is regulated by the GTPase activity of the ROC domain (PubMed:18230735, PubMed:29212815). GTP-bound LRRK2 kinase activity is stimulated by RAB29 (PubMed:29212815, PubMed:38127736). Phosphorylation of RAB10 'Thr-73' is stimulated by RAB29 and RAB32 (PubMed:38127736). Inhibited by small molecule inhibitor MLi-2 (PubMed:26824392, PubMed:29127255). {ECO:0000269|PubMed:18230735, ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:29127255, ECO:0000269|PubMed:29212815, ECO:0000269|PubMed:38127736}.
uniprot
proteins
amino_acid_sequence
MASGSCQGCEEDEETLKKLIVRLNNVQEGKQIETLVQILEDLLVFTYSERASKLFQGKNIHVPLLIVLDSYMRVASVQQVGWSLLCKLIEVCPGTMQSLMGPQDVGNDWEVLGVHQLILKMLTVHNASVNLSVIGLKTLDLLLTSGKITLLILDEESDIFMLIFDAMHSFPANDEVQKLGCKALHVLFERVSEEQLTEFVENKDYMILLSALTNFKDEEEIVLHVLHCLHSLAIPCNNVEVLMSGNVRCYNIVVEAMKAFPMSERIQEVSCCLLHRLTLGNFFNILVLNEVHEFVVKAVQQYPENAALQISALSCLALLTETIFLNQDLEEKNENQENDDEGEEDKLFWLEACYKALTWHRKNKHVQEAACWALNNLLMYQNSLHEKIGDEDGHFPAHREVMLSMLMHSSSKEVFQASANALSTLLEQNVNFRKILLSKGIHLNVLELMQKHIHSPEVAESGCKMLNHLFEGSNTSLDIMAAVVPKILTVMKRHETSLPVQLEALRAILHFIVPGMPEESREDTEFHHKLNMVKKQCFKNDIHKLVLAALNRFIGNPGIQKCGLKVISSIVHFPDALEMLSLEGAMDSVLHTLQMYPDDQEIQCLGLSLIGYLITKKNVFIGTGHLLAKILVSSLYRFKDVAEIQTKGFQTILAILKLSASFSKLLVHHSFDLVIFHQMSSNIMEQKDQQFLNLCCKCFAKVAMDDYLKNVMLERACDQNNSIMVECLLLLGADANQAKEGSSLICQVCEKESSPKLVELLLNSGSREQDVRKALTISIGKGDSQIISLLLRRLALDVANNSICLGGFCIGKVEPSWLGPLFPDKTSNLRKQTNIASTLARMVIRYQMKSAVEEGTASGSDGNFSEDVLSKFDEWTFIPDSSMDSVFAQSDDLDSEGSEGSFLVKKKSNSISVGEFYRDAVLQRCSPNLQRHSNSLGPIFDHEDLLKRKRKILSSDDSLRSSKLQSHMRHSDSISSLASEREYITSLDLSANELRDIDALSQKCCISVHLEHLEKLELHQNALTSFPQQLCETLKSLTHLDLHSNKFTSFPSYLLKMSCIANLDVSRNDIGPSVVLDPTVKCPTLKQFNLSYNQLSFVPENLTDVVEKLEQLILEGNKISGICSPLRLKELKILNLSKNHISSLSENFLEACPKVESFSARMNFLAAMPFLPPSMTILKLSQNKFSCIPEAILNLPHLRSLDMSSNDIQYLPGPAHWKSLNLRELLFSHNQISILDLSEKAYLWSRVEKLHLSHNKLKEIPPEIGCLENLTSLDVSYNLELRSFPNEMGKLSKIWDLPLDELHLNFDFKHIGCKAKDIIRFLQQRLKKAVPYNRMKLMIVGNTGSGKTTLLQQLMKTKKSDLGMQSATVGIDVKDWPIQIRDKRKRDLVLNVWDFAGREEFYSTHPHFMTQRALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEKQRKACMSKITKELLNKRGFPAIRDYHFVNATEESDALAKLRKTIINESLNFKIRDQLVVGQLIPDCYVELEKIILSERKNVPIEFPVIDRKRLLQLVRENQLQLDENELPHAVHFLNESGVLLHFQDPALQLSDLYFVEPKWLCKIMAQILTVKVEGCPKHPKGIISRRDVEKFLSKKRKFPKNYMSQYFKLLEKFQIALPIGEEYLLVPSSLSDHRPVIELPHCENSEIIIRLYEMPYFPMGFWSRLINRLLEISPYMLSGRERALRPNRMYWRQGIYLNWSPEAYCLVGSEVLDNHPESFLKITVPSCRKGCILLGQVVDHIDSLMEEWFPGLLEIDICGEGETLLKKWALYSFNDGEEHQKILLDDLMKKAEEGDLLVNPDQPRLTIPISQIAPDLILADLPRNIMLNNDELEFEQAPEFLLGDGSFGSVYRAAYEGEEVAVKIFNKHTSLRLLRQELVVLCHLHHPSLISLLAAGIRPRMLVMELASKGSLDRLLQQDKASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNAAIIAKIADYGIAQYCCRMGIKTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTTGGRIVEGLKFPNEFDELEIQGKLPDPVKEYGCAPWPMVEKLIKQCLKENPQERPTSAQVFDILNSAELVCLTRRILLPKNVIVECMVATHHNSRNASIWLGCGHTDRGQLSFLDLNTEGYTSEEVADSRILCLALVHLPVEKESWIVSGTQSGTLLVINTEDGKKRHTLEKMTDSVTCLYCNSFSKQSKQKNFLLVGTADGKLAIFEDKTVKLKGAAPLKILNIGNVSTPLMCLSESTNSTERNVMWGGCGTKIFSFSNDFTIQKLIETRTSQLFSYAAFSDSNIITVVVDTALYIAKQNSPVVEVWDKKTEKLCGLIDCVHFLREVMVKENKESKHKMSYSGRVKTLCLQKNTALWIGTGGGHILLLDLSTRRLIRVIYNFCNSVRVMMTAQLGSLKNVMLVLGYNRKNTEGTQKQKEIQSCLTVWDINLPHEVQNLEKHIEVRKELAEKMRRTSVE
uniprot
proteins
disease_involvement
DISEASE: Parkinson disease 8 (PARK8) [MIM:607060]: A slowly progressive neurodegenerative disorder characterized by bradykinesia, rigidity, resting tremor, postural instability, neuronal loss in the substantia nigra, and the presence of neurofibrillary MAPT (tau)-positive and Lewy bodies in some patients. {ECO:0000269|PubMed:15541308, ECO:0000269|PubMed:15541309, ECO:0000269|PubMed:15680455, ECO:0000269|PubMed:15680456, ECO:0000269|PubMed:15680457, ECO:0000269|PubMed:15726496, ECO:0000269|PubMed:15732108, ECO:0000269|PubMed:15811454, ECO:0000269|PubMed:15852371, ECO:0000269|PubMed:15880653, ECO:0000269|PubMed:15925109, ECO:0000269|PubMed:15929036, ECO:0000269|PubMed:16102999, ECO:0000269|PubMed:16157901, ECO:0000269|PubMed:16157908, ECO:0000269|PubMed:16157909, ECO:0000269|PubMed:16172858, ECO:0000269|PubMed:16240353, ECO:0000269|PubMed:16247070, ECO:0000269|PubMed:16250030, ECO:0000269|PubMed:16251215, ECO:0000269|PubMed:16269541, ECO:0000269|PubMed:16272164, ECO:0000269|PubMed:16272257, ECO:0000269|PubMed:16298482, ECO:0000269|PubMed:16321986, ECO:0000269|PubMed:16333314, ECO:0000269|PubMed:16533964, ECO:0000269|PubMed:17114044, ECO:0000269|PubMed:18213618, ECO:0000269|PubMed:21641266, ECO:0000269|PubMed:21850687, ECO:0000269|PubMed:22956510, ECO:0000269|PubMed:23395371, ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:28202711, ECO:0000269|PubMed:28720718, ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:29127255, ECO:0000269|PubMed:29212815, ECO:0000269|PubMed:30209220, ECO:0000269|PubMed:30398148, ECO:0000269|PubMed:30635421}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
FUNCTION: Serine/threonine-protein kinase which phosphorylates a broad range of proteins involved in multiple processes such as neuronal plasticity, innate immunity, autophagy, and vesicle trafficking (PubMed:17114044, PubMed:20949042, PubMed:21850687, PubMed:22012985, PubMed:23395371, PubMed:24687852, PubMed:25201882, PubMed:26014385, PubMed:26824392, PubMed:27830463, PubMed:28720718, PubMed:29125462, PubMed:29127255, PubMed:29212815, PubMed:30398148, PubMed:30635421). Is a key regulator of RAB GTPases by regulating the GTP/GDP exchange and interaction partners of RABs through phosphorylation (PubMed:26824392, PubMed:28720718, PubMed:29125462, PubMed:29127255, PubMed:29212815, PubMed:30398148, PubMed:30635421). Phosphorylates RAB3A, RAB3B, RAB3C, RAB3D, RAB5A, RAB5B, RAB5C, RAB8A, RAB8B, RAB10, RAB12, RAB29, RAB35, and RAB43 (PubMed:23395371, PubMed:26824392, PubMed:28720718, PubMed:29125462, PubMed:29127255, PubMed:29212815, PubMed:30398148, PubMed:30635421, PubMed:38127736). Regulates the RAB3IP-catalyzed GDP/GTP exchange for RAB8A through the phosphorylation of 'Thr-72' on RAB8A (PubMed:26824392). Inhibits the interaction between RAB8A and GDI1 and/or GDI2 by phosphorylating 'Thr-72' on RAB8A (PubMed:26824392). Regulates primary ciliogenesis through phosphorylation of RAB8A and RAB10, which promotes SHH signaling in the brain (PubMed:29125462, PubMed:30398148). Together with RAB29, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose-6-phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (PubMed:23395371). Regulates neuronal process morphology in the intact central nervous system (CNS) (PubMed:17114044). Plays a role in synaptic vesicle trafficking (PubMed:24687852). Plays an important role in recruiting SEC16A to endoplasmic reticulum exit sites (ERES) and in regulating ER to Golgi vesicle-mediated transport and ERES organization (PubMed:25201882). Positively regulates autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway (PubMed:22012985). The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes (PubMed:22012985). Phosphorylates PRDX3 (PubMed:21850687). By phosphorylating APP on 'Thr-743', which promotes the production and the nuclear translocation of the APP intracellular domain (AICD), regulates dopaminergic neuron apoptosis (PubMed:28720718). Acts as a positive regulator of innate immunity by mediating phosphorylation of RIPK2 downstream of NOD1 and NOD2, thereby enhancing RIPK2 activation (PubMed:27830463). Independent of its kinase activity, inhibits the proteasomal degradation of MAPT, thus promoting MAPT oligomerization and secretion (PubMed:26014385). In addition, has GTPase activity via its Roc domain which regulates LRRK2 kinase activity (PubMed:18230735, PubMed:26824392, PubMed:28720718, PubMed:29125462, PubMed:29212815). Recruited by RAB29/RAB7L1 to overloaded lysosomes where it phosphorylates and stabilizes RAB8A and RAB10 which promote lysosomal content release and suppress lysosomal enlargement through the EHBP1 and EHBP1L1 effector proteins (PubMed:30209220, PubMed:38227290). {ECO:0000269|PubMed:17114044, ECO:0000269|PubMed:18230735, ECO:0000269|PubMed:20949042, ECO:0000269|PubMed:21850687, ECO:0000269|PubMed:22012985, ECO:0000269|PubMed:23395371, ECO:0000269|PubMed:24687852, ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:26014385, ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:27830463, ECO:0000269|PubMed:28720718, ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:29127255, ECO:0000269|PubMed:29212815, ECO:0000269|PubMed:30209220, ECO:0000269|PubMed:30398148, ECO:0000269|PubMed:30635421, ECO:0000269|PubMed:38127736, ECO:0000269|PubMed:38227290}.
uniprot
proteins
mass_dalton
286103
uniprot
proteins
mutagenesis
MUTAGEN 399; /note="R->E: Reduces membrane localization and abolishes interaction with RAB29/RAB7L1. Impairs RAB29-stimulated kinase activity on RAB10, RAB29 and LRRK2."; /evidence="ECO:0000269|PubMed:38127736"; MUTAGEN 403; /note="L->E: Reduces membrane localization and abolishes interaction with RAB29/RAB7L1. Impairs RAB29-stimulated kinase activity on RAB10, RAB29 and LRRK2."; /evidence="ECO:0000269|PubMed:38127736"; MUTAGEN 727; /note="C->D: Decreased kinase activity. Loss of RAB29-mediated activation and autophosphorylation of S-910, S-935, S-955, S-973 and S-1292. Decreased membrane association; when associated with G-1441, C-1699 and S-2019."; /evidence="ECO:0000269|PubMed:29212815"; MUTAGEN 728; /note="L->D: Decreased kinase activity. Loss of RAB29-mediated activation and autophosphorylation of S-910, S-935, S-955, S-973 and S-1292. Decreased membrane association; when associated with G-1441, C-1699 and S-2019."; /evidence="ECO:0000269|PubMed:29212815"; MUTAGEN 729; /note="L->D: Decreased kinase activity. Loss of RAB29-mediated activation and autophosphorylation of S-910, S-935, S-955, S-973 and S-1292. Decreased membrane association; when associated with G-1441, C-1699 and S-2019."; /evidence="ECO:0000269|PubMed:29212815"; MUTAGEN 760; /note="L->D: Decreased kinase activity and loss of RAB29-mediated activation."; /evidence="ECO:0000269|PubMed:29212815"; MUTAGEN 761; /note="L->D: Decreased kinase activity and loss of RAB29-mediated activation."; /evidence="ECO:0000269|PubMed:29212815"; MUTAGEN 762; /note="L->D: Decreased kinase activity and loss of RAB29-mediated activation."; /evidence="ECO:0000269|PubMed:29212815"; MUTAGEN 789; /note="L->D: No effect on kinase activity and RAB29-mediated activation."; /evidence="ECO:0000269|PubMed:29212815"; MUTAGEN 790; /note="L->D: No effect on kinase activity and RAB29-mediated activation."; /evidence="ECO:0000269|PubMed:29212815"; MUTAGEN 791; /note="L->D: No effect on kinase activity and RAB29-mediated activation."; /evidence="ECO:0000269|PubMed:29212815"; MUTAGEN 1343; /note="T->G: Decreased kinase activity; when associated with Q-1398."; /evidence="ECO:0000269|PubMed:18230735"; MUTAGEN 1347; /note="K->A: GTPase-dead mutant. Loss of interaction with SEC16A and impaired ability to recruit SEC16A to endoplasmic reticulum exit sites."; /evidence="ECO:0000269|PubMed:25201882"; MUTAGEN 1348; /note="T->N: Loss of GTP binding. Inhibits autophosphorylation and RAB10 phosphorylation; when associated with G-1441, C-1699, or S-2019."; /evidence="ECO:0000269|PubMed:29212815"; MUTAGEN 1398; /note="R->Q: Decreased kinase activity; when associated with G-1343."; /evidence="ECO:0000269|PubMed:18230735"; MUTAGEN 1441; /note="R->G: Decreased membrane association when associated with D-727, D-728, or D-729. Inhibits autophosphorylation and RAB10 phosphorylation when associated with N-1348 or A-2017."; /evidence="ECO:0000269|PubMed:29212815"; MUTAGEN 1588; /note="P->A: Impairs RAB29-stimulated kinase activity on RAB10, RAB29 and LRRK2."; /evidence="ECO:0000269|PubMed:38127736"; MUTAGEN 1699; /note="Y->C: Decreased membrane association when associated with D-727, D-728, or D-729. Inhibits autophosphorylation and RAB10 phosphorylation when associated with N-1348 or A-2017."; /evidence="ECO:0000269|PubMed:29212815"; MUTAGEN 1710; /note="N->A: Impairs RAB29-stimulated kinase activity on RAB10, RAB29 and LRRK2."; /evidence="ECO:0000269|PubMed:38127736"; MUTAGEN 1791; /note="W->A: Impairs RAB29-stimulated kinase activity on RAB10, RAB29 and LRRK2."; /evidence="ECO:0000269|PubMed:38127736"; MUTAGEN 1906; /note="K->A: Loss of kinase activity. Decreases proteasomal degradation of MAPT; when associated with N-1994 and A-2017."; /evidence="ECO:0000269|PubMed:26014385"; MUTAGEN 1994; /note="D->A: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:28720718"; MUTAGEN 1994; /note="D->N: Loss of kinase activity. No loss of interaction with SEC16A and no loss of ability to recruit SEC16A to endoplasmic reticulum exit sites. Decreases proteasomal degradation of MAPT; when associated with A-1906 and A-2017."; /evidence="ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:26014385, ECO:0000269|PubMed:26824392"; MUTAGEN 2017; /note="D->A: Loss of kinase activity. Decreases proteasomal degradation of MAPT; when associated with A-1906 and N-1994. Loss of phosphorylation of RAB10; when associated with G-1441, C-1699, or S-2019."; /evidence="ECO:0000269|PubMed:26014385, ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:29212815, ECO:0000269|PubMed:30635421, ECO:0000269|PubMed:38127736"; MUTAGEN 2019; /note="G->S: Decreased membrane association when associated with D-727, D-728, or D-729. Inhibits autophosphorylation and RAB10 phosphorylation when associated with N-1348 or A-2017."; /evidence="ECO:0000269|PubMed:29212815"; MUTAGEN 2343; /note="L->D: Decreases WD domain homodimerization. No effect on kinase activity."; /evidence="ECO:0000269|PubMed:30635421"; MUTAGEN 2344; /note="F->A: Decreases WD domain homodimerization. No effect on kinase activity."; /evidence="ECO:0000269|PubMed:30635421"; MUTAGEN 2345; /note="S->D: Decreases WD domain homodimerization. No effect on kinase activity."; /evidence="ECO:0000269|PubMed:30635421"; MUTAGEN 2346; /note="Y->A: Decreases WD domain homodimerization. No effect on kinase activity."; /evidence="ECO:0000269|PubMed:30635421"; MUTAGEN 2391; /note="H->D: Increases kinase activity."; /evidence="ECO:0000269|PubMed:30635421"; MUTAGEN 2394; /note="R->E: Decreases WD domain homodimerization. Increases kinase activity and autophosphorylation at Ser-1292."; /evidence="ECO:0000269|PubMed:30635421"; MUTAGEN 2395; /note="E->R: Decreases WD domain homodimerization. No effect on kinase activity."; /evidence="ECO:0000269|PubMed:30635421"; MUTAGEN 2408; /note="M->A,E: No effect on WD domain homodimerization. No effect on kinase activity."; /evidence="ECO:0000269|PubMed:30635421"; MUTAGEN 2409; /note="S->A: Decreases WD domain homodimerization."; /evidence="ECO:0000269|PubMed:30635421
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated at Ser-1292; autophosphorylation is stimulated by RAB29 (PubMed:28202711, PubMed:28720718, PubMed:29127255, PubMed:29212815, PubMed:30635421, PubMed:38127736). Phosphorylation of Ser-910 and either Ser-935 or Ser-1444 facilitates interaction with YWHAG (PubMed:28202711). Phosphorylation of Ser-910 and/or Ser-935 facilitates interaction with SFN (PubMed:28202711). {ECO:0000269|PubMed:28202711, ECO:0000269|PubMed:28720718, ECO:0000269|PubMed:29127255, ECO:0000269|PubMed:29212815, ECO:0000269|PubMed:30635421, ECO:0000269|PubMed:38127736}.; PTM: Ubiquitinated by TRIM1; undergoes 'Lys-48'-linked polyubiquitination leading to proteasomal degradation. {ECO:0000269|PubMed:35266954}.
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
TKL Ser/Thr protein kinase family
uniprot
proteins
pubmed
15541308
uniprot
proteins
pubmed
15541309
uniprot
proteins
pubmed
15680455
uniprot
proteins
pubmed
15680456
uniprot
proteins
pubmed
15680457
uniprot
proteins
pubmed
15726496
uniprot
proteins
pubmed
15732108
uniprot
proteins
pubmed
15811454
uniprot
proteins
pubmed
15852371
uniprot
proteins
pubmed
15880653
uniprot
proteins
pubmed
15925109
uniprot
proteins
pubmed
15929036
uniprot
proteins
pubmed
16001413
uniprot
proteins
pubmed
16081470
uniprot
proteins
pubmed
16087219
uniprot
proteins
pubmed
16102999
uniprot
proteins
pubmed
16157901
uniprot
proteins
pubmed
16157908
uniprot
proteins
pubmed
16157909
uniprot
proteins
pubmed
16172858
uniprot
proteins
pubmed
16240353
uniprot
proteins
pubmed
16247070
uniprot
proteins
pubmed
16250030
uniprot
proteins
pubmed
16251215
uniprot
proteins
pubmed
16269541
uniprot
proteins
pubmed
16272164
uniprot
proteins
pubmed
16272257
uniprot
proteins
pubmed
16298482
uniprot
proteins
pubmed
16321986
uniprot
proteins
pubmed
16333314
uniprot
proteins
pubmed
16352719
uniprot
proteins
pubmed
16532471
uniprot
proteins
pubmed
16533964
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
17019612
uniprot
proteins
pubmed
17114044
uniprot
proteins
pubmed
17120249
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18213618
uniprot
proteins
pubmed
18230735
uniprot
proteins
pubmed
20949042
uniprot
proteins
pubmed
21248752
uniprot
proteins
pubmed
21641266
uniprot
proteins
pubmed
21850687
uniprot
proteins
pubmed
22012985
uniprot
proteins
pubmed
22415848
uniprot
proteins
pubmed
22952686
uniprot
proteins
pubmed
22956510
uniprot
proteins
pubmed
23395371
uniprot
proteins
pubmed
23776530
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24687852
uniprot
proteins
pubmed
25201882
uniprot
proteins
pubmed
26014385
uniprot
proteins
pubmed
26824392
uniprot
proteins
pubmed
27830463
uniprot
proteins
pubmed
28202711
uniprot
proteins
pubmed
28720718
uniprot
proteins
pubmed
29125462
uniprot
proteins
pubmed
29127255
uniprot
proteins
pubmed
29212815
uniprot
proteins
pubmed
30209220
uniprot
proteins
pubmed
30398148
uniprot
proteins
pubmed
30635421
uniprot
proteins
pubmed
30647193
uniprot
proteins
pubmed
35266954
uniprot
proteins
pubmed
38127736
uniprot
proteins
pubmed
38227290
uniprot
proteins
sequence_length
2527
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:16321986, ECO:0000269|PubMed:16352719, ECO:0000269|PubMed:26014385}. Perikaryon {ECO:0000269|PubMed:17120249}. Golgi apparatus membrane {ECO:0000269|PubMed:16321986, ECO:0000269|PubMed:23395371, ECO:0000269|PubMed:38127736}; Peripheral membrane protein {ECO:0000269|PubMed:16321986}. Cell projection, axon {ECO:0000269|PubMed:17120249}. Cell projection, dendrite {ECO:0000269|PubMed:17120249, ECO:0000269|PubMed:21850687}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16321986, ECO:0000269|PubMed:25201882}; Peripheral membrane protein {ECO:0000269|PubMed:16321986}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:24687852}. Endosome {ECO:0000250|UniProtKB:Q5S006}. Lysosome {ECO:0000269|PubMed:17120249, ECO:0000269|PubMed:30209220, ECO:0000269|PubMed:38227290}. Mitochondrion outer membrane {ECO:0000269|PubMed:16269541, ECO:0000269|PubMed:16321986, ECO:0000269|PubMed:17120249, ECO:0000269|PubMed:29212815}; Peripheral membrane protein {ECO:0000269|PubMed:16269541, ECO:0000269|PubMed:16321986, ECO:0000269|PubMed:17120249, ECO:0000269|PubMed:29212815}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:35266954}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q5S006}. Note=Colocalized with RAB29 along tubular structures emerging from Golgi apparatus (PubMed:23395371, PubMed:38127736). Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER) (PubMed:25201882). Detected on phagosomes and stressed lysosomes but not detected on autophagosomes induced by starvation (By similarity). Recruitment to stressed lysosomes is dependent on the ATG8 conjugation system composed of ATG5, ATG12 and ATG16L1 and leads to lysosomal stress-induced activation of LRRK2 (By similarity). {ECO:0000250|UniProtKB:Q5S006, ECO:0000269|PubMed:23395371, ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:38127736}.
uniprot
proteins