SQSTM1
entrez
8878
canonical
uniprot
Q13501
canonical
ensembl
ENSG00000161011
resolver
ensembl
ENSG00000284099
resolver
ensp
ENSP00000353944
resolver
ensp
ENSP00000374455
resolver
genesymbol
SQSTM1
resolver
genesymbol_syn
ORCA
resolver
genesymbol_syn
OSIL
resolver
hgnc
HGNC:11280
resolver
uniprot
A6NFN7
resolver
uniprot
B2R661
resolver
uniprot
B3KUW5
resolver
uniprot
Q13446
resolver
uniprot
Q9BUV7
resolver
uniprot
Q9BVS6
resolver
uniprot
Q9UEU1
resolver
uniprot_entry
SQSTM_HUMAN
resolver
uniprot_sec
A6NFN7
resolver
uniprot_sec
B2R661
resolver
uniprot_sec
B3KUW5
resolver
uniprot_sec
Q13446
resolver
uniprot_sec
Q9BUV7
resolver
uniprot_sec
Q9BVS6
resolver
uniprot_sec
Q9UEU1
resolver
amino_acid_sequence
MASLTVKAYLLGKEDAAREIRRFSFCCSPEPEAEAEAAAGPGPCERLLSRVAALFPALRPGGFQAHYRDEDGDLVAFSSDEELTMAMSYVKDDIFRIYIKEKKECRRDHRPPCAQEAPRNMVHPNVICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKGLHRGHTKLAFPSPFGHLSEGFSHSRWLRKVKHGHFGWPGWEMGPPGNWSPRPPRAGEARPGPTAESASGPSEDPSVNFLKNVGESVAAALSPLGIEVDIDVEHGGKRSRLTPVSPESSSTEEKSSSQPSSCCSDPSKPGGNVEGATQSLAEQMRKIALESEGRPEEQMESDNCSGGDDDWTHLSSKEVDPSTGELQSLQMPESEGPSSLDPSQEGPTGLKEAALYPHLPPEADPRLIESLSQMLSMGFSDEGGWLTRLLQTKNYDIGAALDTIQYSKHPPPL
uniprot
proteins
disease_involvement
DISEASE: Paget disease of bone 3 (PDB3) [MIM:167250]: A disorder of bone remodeling characterized by increased bone turnover affecting one or more sites throughout the skeleton, primarily the axial skeleton. Osteoclastic overactivity followed by compensatory osteoblastic activity leads to a structurally disorganized mosaic of bone (woven bone), which is mechanically weaker, larger, less compact, more vascular, and more susceptible to fracture than normal adult lamellar bone. {ECO:0000269|PubMed:11992264, ECO:0000269|PubMed:12374763, ECO:0000269|PubMed:14584883, ECO:0000269|PubMed:15125799, ECO:0000269|PubMed:15146436, ECO:0000269|PubMed:15176995, ECO:0000269|PubMed:15207768, ECO:0000269|PubMed:19931284, ECO:0000269|PubMed:29507397}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=In a cell model for Huntington disease (HD), appears to form a shell surrounding aggregates of mutant HTT that may protect cells from apoptosis, possibly by recruiting autophagosomal components to the polyubiquitinated protein aggregates. {ECO:0000269|PubMed:16286508}.; DISEASE: Frontotemporal dementia and/or amyotrophic lateral sclerosis 3 (FTDALS3) [MIM:616437]: A neurodegenerative disorder characterized by frontotemporal dementia and/or amyotrophic lateral sclerosis in affected individuals. There is high intrafamilial variation. Frontotemporal dementia is characterized by frontal and temporal lobe atrophy associated with neuronal loss, gliosis, and dementia. Patients exhibit progressive changes in social, behavioral, and/or language function. Amyotrophic lateral sclerosis is characterized by the death of motor neurons in the brain, brainstem, and spinal cord, resulting in fatal paralysis. Some FTDALS3 patients may also develop Paget disease of bone. {ECO:0000269|PubMed:22084127, ECO:0000269|PubMed:24042580, ECO:0000269|PubMed:24899140, ECO:0000269|PubMed:25114083}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Neurodegeneration with ataxia, dystonia, and gaze palsy, childhood-onset (NADGP) [MIM:617145]: A neurodegenerative disorder characterized by gait abnormalities, ataxia, dysarthria, dystonia, vertical gaze palsy, and cognitive decline. Disease onset is in childhood or adolescence. NADGP transmission pattern is consistent with autosomal recessive inheritance. {ECO:0000269|PubMed:27545679}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Myopathy, distal, with rimmed vacuoles (DMRV) [MIM:617158]: An autosomal dominant myopathy with adult onset, characterized by muscle weakness of the distal upper and lower limbs, walking difficulties, and proximal weakness of the shoulder girdle muscles. Muscle biopsy shows rimmed vacuoles. {ECO:0000269|PubMed:26208961}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving SQSTM1 is found in a form of acute lymphoblastic leukemia. Translocation t(5;9)(q35;q34) with NUP214. {ECO:0000269|PubMed:20851865}.
uniprot
proteins
function
FUNCTION: Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a bridge between polyubiquitinated proteins and autophagosomes (PubMed:15340068, PubMed:15953362, PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22017874, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:33509017, PubMed:34471133, PubMed:34893540, PubMed:35831301, PubMed:37306101, PubMed:37802024, PubMed:40542578). Promotes the recruitment of ubiquitinated cargo proteins to autophagosomes via multiple domains that bridge proteins and organelles in different steps (PubMed:16286508, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:34893540, PubMed:37802024). SQSTM1 first mediates the assembly and removal of ubiquitinated proteins by undergoing liquid-liquid phase separation upon binding to ubiquitinated proteins via its UBA domain, leading to the formation of insoluble cytoplasmic inclusions, known as p62 bodies (PubMed:15911346, PubMed:20168092, PubMed:22017874, PubMed:24128730, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:37802024). SQSTM1 then interacts with ATG8 family proteins on autophagosomes via its LIR motif, leading to p62 body recruitment to autophagosomes, followed by autophagic clearance of ubiquitinated proteins (PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:37802024). SQSTM1 is itself degraded along with its ubiquitinated cargos (PubMed:16286508, PubMed:17580304, PubMed:37802024). Also required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (PubMed:26344566). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex by sequestering the complex in inclusion bodies, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357, PubMed:33393215, PubMed:37306101). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). May regulate the activation of NFKB1 by TNF, nerve growth factor (NGF) and interleukin-1 (PubMed:10356400, PubMed:10747026, PubMed:11244088, PubMed:12471037, PubMed:16079148, PubMed:19931284). May play a role in titin/TTN downstream signaling in muscle cells (PubMed:15802564). Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). {ECO:0000250|UniProtKB:Q64337, ECO:0000269|PubMed:10356400, ECO:0000269|PubMed:10747026, ECO:0000269|PubMed:11244088, ECO:0000269|PubMed:12471037, ECO:0000269|PubMed:15340068, ECO:0000269|PubMed:15802564, ECO:0000269|PubMed:15911346, ECO:0000269|PubMed:15953362, ECO:0000269|PubMed:16079148, ECO:0000269|PubMed:16286508, ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:19931284, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20452972, ECO:0000269|PubMed:22017874, ECO:0000269|PubMed:22622177, ECO:0000269|PubMed:24128730, ECO:0000269|PubMed:25101860, ECO:0000269|PubMed:26344566, ECO:0000269|PubMed:27368102, ECO:0000269|PubMed:28380357, ECO:0000269|PubMed:28404643, ECO:0000269|PubMed:29343546, ECO:0000269|PubMed:29496741, ECO:0000269|PubMed:29507397, ECO:0000269|PubMed:31857589, ECO:0000269|PubMed:33393215, ECO:0000269|PubMed:33472082, ECO:0000269|PubMed:33509017, ECO:0000269|PubMed:34471133, ECO:0000269|PubMed:34893540, ECO:0000269|PubMed:35831301, ECO:0000269|PubMed:37306101, ECO:0000269|PubMed:37802024, ECO:0000269|PubMed:40542578}.
uniprot
proteins
mass_dalton
47687
uniprot
proteins
mutagenesis
MUTAGEN 7; /note="K->A: Loss of interactions with PRKCZ, PRCKI and NBR1. Loss of dimerization; when associated with A-69."; /evidence="ECO:0000269|PubMed:12813044, ECO:0000269|PubMed:12887891"; MUTAGEN 7; /note="K->R: Almost complete loss of TRIM25-mediated ubiquitination; when associated with R-189."; /evidence="ECO:0000269|PubMed:40542578"; MUTAGEN 9; /note="Y->F: No effect on interaction with LCK."; /evidence="ECO:0000269|PubMed:8650207"; MUTAGEN 13; /note="K->A: No effect on interaction with PRKCI."; /evidence="ECO:0000269|PubMed:12813044"; MUTAGEN 21..22; /note="RR->AA: Loss of interaction with PRKCI. Alters dimerization."; /evidence="ECO:0000269|PubMed:12813044"; MUTAGEN 67; /note="Y->A: No effect on interaction with PRKCZ."; /evidence="ECO:0000269|PubMed:12813044"; MUTAGEN 69; /note="D->A: No effect on interactions with PRKCZ, PRKCI and NBR1. Loss of localization in cytoplasmic inclusion bodies. Loss of dimerization; when associated with A-7."; /evidence="ECO:0000269|PubMed:12813044, ECO:0000269|PubMed:12887891, ECO:0000269|PubMed:16286508"; MUTAGEN 71; /note="D->A: No effect on interaction with PRKCI."; /evidence="ECO:0000269|PubMed:12813044"; MUTAGEN 73; /note="D->A: No effect on interactions with PRKCZ and PRKCI."; /evidence="ECO:0000269|PubMed:12813044, ECO:0000269|PubMed:12887891"; MUTAGEN 80; /note="D->A: No effect on interaction with PRKCI."; /evidence="ECO:0000269|PubMed:12813044"; MUTAGEN 82; /note="E->A: No effect on interaction with PRKCI."; /evidence="ECO:0000269|PubMed:12813044"; MUTAGEN 189; /note="K->R: Almost complete loss of TRIM25-mediated ubiquitination; when associated with R-7."; /evidence="ECO:0000269|PubMed:40542578"; MUTAGEN 289..290; /note="CC->SS: Abolished palmitoylation."; /evidence="ECO:0000269|PubMed:37802024"; MUTAGEN 323..324; /note="EE->AA: No effect on MAP1LC3B-binding."; /evidence="ECO:0000269|PubMed:17580304"; MUTAGEN 332; /note="S->A: No effect on MAP1LC3B-binding."; /evidence="ECO:0000269|PubMed:17580304"; MUTAGEN 335..337; /note="DDD->ADA: 75% decrease in MAP1LC3B-binding."; /evidence="ECO:0000269|PubMed:17580304"; MUTAGEN 338; /note="W->A: Strong decrease in MAP1LC3B-binding, disrupts interaction with GABARAP."; /evidence="ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:24668264"; MUTAGEN 342; /note="S->A: No effect on MAP1LC3B-binding."; /evidence="ECO:0000269|PubMed:17580304"; MUTAGEN 347; /note="D->A: Strongly decreased interaction with KEAP1."; /evidence="ECO:0000269|PubMed:20452972"; MUTAGEN 349; /note="S->A: Impaired phosphorylation by ULK1, leading to decreased p62 body formation."; /evidence="ECO:0000269|PubMed:37306101"; MUTAGEN 350; /note="T->A: Strongly decreased interaction with KEAP1."; /evidence="ECO:0000269|PubMed:20452972, ECO:0000269|PubMed:37306101"; MUTAGEN 351; /note="G->A: Strongly decreased interaction with KEAP1."; /evidence="ECO:0000269|PubMed:20452972"; MUTAGEN 352; /note="E->A: Strongly decreased interaction with KEAP1."; /evidence="ECO:0000269|PubMed:20452972"; MUTAGEN 398; /note="L->V: No effect on polyubiquitin-binding."; /evidence="ECO:0000269|PubMed:15340068"; MUTAGEN 403..407; /note="SMGFS->EMGFE: Mimics phosphorylation; increased phosphorylation at S-349."; /evidence="ECO:0000269|PubMed:37306101"; MUTAGEN 403; /note="S->A: Abolished phosphorylation by CK2, leading to decreased affinity for ubiquitinated proteins. Abolished ability to promote relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes."; /evidence="ECO:0000269|PubMed:22017874, ECO:0000269|PubMed:29496741"; MUTAGEN 403; /note="S->E: Mimmics phosphorylation; increased affinity for ubiquitinated proteins, leading to increased p62 body formation and autophagic degradation."; /evidence="ECO:0000269|PubMed:22017874, ECO:0000269|PubMed:29507397"; MUTAGEN 406; /note="F->V: Loss of polyubiquitin-binding."; /evidence="ECO:0000269|PubMed:15340068"; MUTAGEN 409; /note="E->K: Decreased activation of NF-kappa-B."; /evidence="ECO:0000269|PubMed:19931284"; MUTAGEN 410; /note="G->K: Decreased activation of NF-kappa-B."; /evidence="ECO:0000269|PubMed:19931284"; MUTAGEN 413; /note="L->V: No effect on polyubiquitin-binding."; /evidence="ECO:0000269|PubMed:15340068"; MUTAGEN 417; /note="L->V: Loss of polyubiquitin-binding."; /evidence="ECO:0000269|PubMed:15340068"; MUTAGEN 420; /note="K->Q: Mimics acetylation; leading to increased ability to bind ubiquitinated proteins; when associated with Q-435."; /evidence="ECO:0000269|PubMed:31857589"; MUTAGEN 420; /note="K->R: Decreased ubiquitination by the BCR(KEAP1) complex, leading to decreased sequestering activity. Strongly reduced acetylation; when associated with R-435."; /evidence="ECO:0000269|PubMed:28380357, ECO:0000269|PubMed:31857589"; MUTAGEN 431; /note="I->V: Partial loss of polyubiquitin-binding. Loss of localization to cytoplasmic inclusion bodies."; /evidence="ECO:0000269|PubMed:15340068, ECO:0000269|PubMed:16286508"; MUTAGEN 435; /note="K->Q: Mimics acetylation; leading to increased ability to bind ubiquitinated proteins; when associated with Q-420."; /evidence="ECO:0000269|PubMed:31857589"; MUTAGEN 435; /note="K->R: Strongly reduced acetylation; when associated with R-420."; /evidence="ECO:0000269|PubMed:31857589
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-407 by ULK1 destabilizes the UBA dimer interface and increases binding affinity to ubiquitinated proteins (By similarity). Phosphorylation at Ser-407 also primes for subsequent phosphorylation at Ser-403 (By similarity). Phosphorylation at Ser-403 by CK2 or ULK1 promotes binding to ubiquitinated proteins by increasing the affinity between the UBA domain and polyubiquitin chains (PubMed:22017874, PubMed:25040165). Phosphorylation at Ser-403 by ULK1 is stimulated by SESN2 (PubMed:25040165). Phosphorylated at Ser-403 by TBK1, leading to promote relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Phosphorylation at Ser-349 by ULK1 promotes interaction with KEAP1 and inactivation of the BCR(KEAP1) complex, promoting NFE2L2/NRF2 nuclear accumulation and expression of phase II detoxifying enzymes (PubMed:37306101). Phosphorylated in vitro by TTN (PubMed:15802564). {ECO:0000250|UniProtKB:Q64337, ECO:0000269|PubMed:15802564, ECO:0000269|PubMed:22017874, ECO:0000269|PubMed:25040165, ECO:0000269|PubMed:29496741, ECO:0000269|PubMed:37306101}.; PTM: Ubiquitinated by UBE2J1 and RNF26 at Lys-435: ubiquitinated SQSTM1 attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Ubiquitination by UBE2D2 and UBE2D3 increases its ability to bind polyubiquitin chains by destabilizing the UBA dimer interface (PubMed:28322253). Deubiquitination by USP15 releases target vesicles for fast transport into the cell periphery (PubMed:27368102). Ubiquitinated by the BCR(KEAP1) complex at Lys-420, increasing SQSTM1 sequestering activity and promoting its degradation (PubMed:28380357). Ubiquitinated via 'Lys-29' and 'Lys-33'-linked polyubiquitination leading to xenophagic targeting of bacteria and inhibition of their replication (PubMed:27880896). Ubiquitinated by TRIM25, targeting SQSTM1 for lysosomal degradation, thereby inhibiting autophagy activation (PubMed:40542578). {ECO:0000269|PubMed:27368102, ECO:0000269|PubMed:27880896, ECO:0000269|PubMed:28322253, ECO:0000269|PubMed:28380357, ECO:0000269|PubMed:33472082, ECO:0000269|PubMed:40542578}.; PTM: Acetylated at Lys-420 and Lys-435 by KAT5/TIP60, promotes activity by destabilizing the UBA dimer interface and increases binding affinity to ubiquitinated proteins (PubMed:31857589). Deacetylated by HDAC6 (PubMed:31857589). {ECO:0000269|PubMed:31857589}.; PTM: Palmitoylation at Cys-289 and Cys-290 by ZDHHC19 is required for efficient autophagic degradation of SQSTM1-cargo complexes by promoting affinity for ATG8 proteins and recruitment of p62 bodies to autophagosomes (PubMed:37802024). Dealmitoylated at Cys-289 and Cys-290 by LYPLA1 (PubMed:37802024). {ECO:0000269|PubMed:37802024}.; PTM: (Microbial infection) Cleaved by S.pyogenes SpeB protease; leading to its degradation (PubMed:24331465). Degradation by SpeB prevents autophagy, promoting to S.pyogenes intracellular replication (PubMed:24331465). {ECO:0000269|PubMed:24331465}.; PTM: (Microbial infection) Deubiquitinated by Epstein-Barr virus BPLF1; leading to inhibition of the recruitment of MAP1LC3A/LC3 to SQSTM1-positive structures. {ECO:0000269|PubMed:33509017}.
uniprot
proteins
pubmed
10356400
uniprot
proteins
pubmed
10362795
uniprot
proteins
pubmed
10708586
uniprot
proteins
pubmed
10747026
uniprot
proteins
pubmed
11244088
uniprot
proteins
pubmed
11755531
uniprot
proteins
pubmed
11786419
uniprot
proteins
pubmed
11981755
uniprot
proteins
pubmed
11992264
uniprot
proteins
pubmed
12374763
uniprot
proteins
pubmed
12471037
uniprot
proteins
pubmed
12700667
uniprot
proteins
pubmed
12813044
uniprot
proteins
pubmed
12857745
uniprot
proteins
pubmed
12887891
uniprot
proteins
pubmed
14584883
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15125799
uniprot
proteins
pubmed
15146436
uniprot
proteins
pubmed
15158159
uniprot
proteins
pubmed
15176995
uniprot
proteins
pubmed
15207768
uniprot
proteins
pubmed
15340068
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
15802564
uniprot
proteins
pubmed
15870274
uniprot
proteins
pubmed
15911346
uniprot
proteins
pubmed
15953362
uniprot
proteins
pubmed
16079148
uniprot
proteins
pubmed
16286508
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17488105
uniprot
proteins
pubmed
17580304
uniprot
proteins
pubmed
17932931
uniprot
proteins
pubmed
18083707
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19931284
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20168092
uniprot
proteins
pubmed
20357094
uniprot
proteins
pubmed
20452972
uniprot
proteins
pubmed
20495340
uniprot
proteins
pubmed
20851865
uniprot
proteins
pubmed
21149568
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21923101
uniprot
proteins
pubmed
22017874
uniprot
proteins
pubmed
22084127
uniprot
proteins
pubmed
22178386
uniprot
proteins
pubmed
22421968
uniprot
proteins
pubmed
22622177
uniprot
proteins
pubmed
22792322
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23274085
uniprot
proteins
pubmed
23908376
uniprot
proteins
pubmed
24042580
uniprot
proteins
pubmed
24089205
uniprot
proteins
pubmed
24128730
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24331465
uniprot
proteins
pubmed
24668264
uniprot
proteins
pubmed
24899140
uniprot
proteins
pubmed
25040165
uniprot
proteins
pubmed
25101860
uniprot
proteins
pubmed
25114083
uniprot
proteins
pubmed
25127057
uniprot
proteins
pubmed
25422469
uniprot
proteins
pubmed
26208961
uniprot
proteins
pubmed
26344566
uniprot
proteins
pubmed
27368102
uniprot
proteins
pubmed
27498865
uniprot
proteins
pubmed
27545679
uniprot
proteins
pubmed
27880896
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28322253
uniprot
proteins
pubmed
28380357
uniprot
proteins
pubmed
28404643
uniprot
proteins
pubmed
28871090
uniprot
proteins
pubmed
29288164
uniprot
proteins
pubmed
29343546
uniprot
proteins
pubmed
29496741
uniprot
proteins
pubmed
29507397
uniprot
proteins
pubmed
30143514
uniprot
proteins
pubmed
30266909
uniprot
proteins
pubmed
31281713
uniprot
proteins
pubmed
31857589
uniprot
proteins
pubmed
32185393
uniprot
proteins
pubmed
33393215
uniprot
proteins
pubmed
33472082
uniprot
proteins
pubmed
33509017
uniprot
proteins
pubmed
34164402
uniprot
proteins
pubmed
34471133
uniprot
proteins
pubmed
34893540
uniprot
proteins
pubmed
35831301
uniprot
proteins
pubmed
37306101
uniprot
proteins
pubmed
37802024
uniprot
proteins
pubmed
38103557
uniprot
proteins
pubmed
40542578
uniprot
proteins
pubmed
8551575
uniprot
proteins
pubmed
8618896
uniprot
proteins
pubmed
8650207
uniprot
proteins
pubmed
8702753
uniprot
proteins
pubmed
8910285
uniprot
proteins
pubmed
9566925
uniprot
proteins
pubmed
9762895
uniprot
proteins
sequence_length
440
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:15953362, ECO:0000269|PubMed:16286508, ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:37802024}. Preautophagosomal structure {ECO:0000269|PubMed:34471133}. Cytoplasm, cytosol {ECO:0000269|PubMed:11786419, ECO:0000269|PubMed:11981755, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20357094, ECO:0000269|PubMed:21923101, ECO:0000269|PubMed:22017874, ECO:0000269|PubMed:22792322, ECO:0000269|PubMed:29343546, ECO:0000269|PubMed:29507397, ECO:0000269|PubMed:31857589, ECO:0000269|PubMed:37306101, ECO:0000269|PubMed:37802024}. Nucleus, PML body {ECO:0000269|PubMed:20168092}. Late endosome {ECO:0000269|PubMed:12471037, ECO:0000269|PubMed:9566925}. Lysosome {ECO:0000269|PubMed:9566925}. Nucleus {ECO:0000269|PubMed:10708586}. Endoplasmic reticulum {ECO:0000269|PubMed:22178386}. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:O08623}. Note=In cardiac muscle, localizes to the sarcomeric band (By similarity). Localizes to cytoplasmic membraneless inclusion bodies, known as p62 bodies, containing polyubiquitinated protein aggregates (PubMed:11786419, PubMed:20357094, PubMed:22017874, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:37306101, PubMed:37802024). In neurodegenerative diseases, detected in Lewy bodies in Parkinson disease, neurofibrillary tangles in Alzheimer disease, and HTT aggregates in Huntington disease (PubMed:15158159). In protein aggregate diseases of the liver, found in large amounts in Mallory bodies of alcoholic and nonalcoholic steatohepatitis, hyaline bodies in hepatocellular carcinoma, and in SERPINA1 aggregates (PubMed:11981755). Enriched in Rosenthal fibers of pilocytic astrocytoma (PubMed:11786419). In the cytoplasm, observed in both membrane-free ubiquitin-containing protein aggregates (sequestosomes) and membrane-surrounded autophagosomes (PubMed:15953362, PubMed:17580304). Colocalizes with TRIM13 in the perinuclear endoplasmic reticulum (PubMed:22178386). Co-localizes with TRIM5 in cytoplasmic bodies (PubMed:20357094). When nuclear export is blocked by treatment with leptomycin B, accumulates in PML bodies (PubMed:20168092). {ECO:0000250|UniProtKB:O08623, ECO:0000269|PubMed:11786419, ECO:0000269|PubMed:11981755, ECO:0000269|PubMed:15158159, ECO:0000269|PubMed:15953362, ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20357094, ECO:0000269|PubMed:22017874, ECO:0000269|PubMed:22178386, ECO:0000269|PubMed:29343546, ECO:0000269|PubMed:29507397, ECO:0000269|PubMed:31857589, ECO:0000269|PubMed:37306101, ECO:0000269|PubMed:37802024}.
uniprot
proteins