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Protein

Sequestosome-1

Gene

SQSTM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family (PubMed:16286508, PubMed:20168092, PubMed:24128730, PubMed:28404643). Along with WDFY3, involved in the formation and autophagic degradation of cytoplasmic ubiquitin-containing inclusions (p62 bodies, ALIS/aggresome-like induced structures). Along with SQSTM1, required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:24128730, PubMed:20168092). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1. May play a role in titin/TTN downstream signaling in muscle cells. May regulate signaling cascades through ubiquitination. Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). May be involved in cell differentiation, apoptosis, immune response and regulation of K+ channels. 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).By similarity15 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri122 – 167ZZ-typePROSITE-ProRule annotationAdd BLAST46

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • ionotropic glutamate receptor binding Source: ARUK-UCL
  • K63-linked polyubiquitin modification-dependent protein binding Source: UniProtKB
  • protein homodimerization activity Source: Ensembl
  • protein kinase binding Source: UniProtKB
  • protein kinase C binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • receptor tyrosine kinase binding Source: ProtInc
  • SH2 domain binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • aggrephagy Source: UniProtKB
  • apoptotic process Source: UniProtKB-KW
  • autophagy Source: UniProtKB
  • autophagy of mitochondrion Source: ParkinsonsUK-UCL
  • cell differentiation Source: UniProtKB-KW
  • endosomal transport Source: UniProtKB
  • endosome organization Source: UniProtKB
  • immune system process Source: UniProtKB-KW
  • intracellular signal transduction Source: UniProtKB
  • macroautophagy Source: GO_Central
  • mitophagy Source: ParkinsonsUK-UCL
  • negative regulation of apoptotic process Source: Reactome
  • negative regulation of growth of symbiont in host Source: Ensembl
  • negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • positive regulation of apoptotic process Source: Reactome
  • positive regulation of long-term synaptic potentiation Source: ARUK-UCL
  • positive regulation of protein localization to plasma membrane Source: ARUK-UCL
  • positive regulation of protein phosphorylation Source: Ensembl
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • protein heterooligomerization Source: Ensembl
  • protein localization Source: UniProtKB
  • protein localization to perinuclear region of cytoplasm Source: UniProtKB
  • regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • regulation of mitochondrion organization Source: ParkinsonsUK-UCL
  • regulation of protein complex stability Source: UniProtKB
  • regulation of Ras protein signal transduction Source: UniProtKB
  • response to mitochondrial depolarisation Source: ParkinsonsUK-UCL
  • response to stress Source: UniProtKB
  • ubiquitin-dependent protein catabolic process Source: ProtInc

Keywordsi

Biological processApoptosis, Autophagy, Differentiation, Immunity
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-205043. NRIF signals cell death from the nucleus.
R-HSA-209543. p75NTR recruits signalling complexes.
R-HSA-209560. NF-kB is activated and signals survival.
R-HSA-446652. Interleukin-1 family signaling.
R-HSA-5205685. Pink/Parkin Mediated Mitophagy.
SignaLinkiQ13501.
SIGNORiQ13501.

Names & Taxonomyi

Protein namesi
Recommended name:
Sequestosome-1
Alternative name(s):
EBI3-associated protein of 60 kDa
Short name:
EBIAP
Short name:
p60
Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa
Ubiquitin-binding protein p62
Gene namesi
Name:SQSTM1
Synonyms:ORCA, OSIL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiHostDB:ENSG00000161011.19.
HGNCiHGNC:11280. SQSTM1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Lysosome, Nucleus

Pathology & Biotechi

Involvement in diseasei

Paget disease of bone 3 (PDB3)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:167250
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023592387P → L in PDB3 and FTDALS3. 3 PublicationsCorresponds to variant dbSNP:rs776749939Ensembl.1
Natural variantiVAR_023593392P → L in PDB3 and FTDALS3; no effect on polyubiquitin-binding. 9 PublicationsCorresponds to variant dbSNP:rs104893941Ensembl.1
Natural variantiVAR_023594399S → P in PDB3. 1 Publication1
Natural variantiVAR_023595404M → T in PDB3. 1 Publication1
Natural variantiVAR_023596404M → V in PDB3; loss of polyubiquitin-binding. 2 PublicationsCorresponds to variant dbSNP:rs771966860Ensembl.1
Natural variantiVAR_023597411G → S in PDB3 and FTDALS3; no effect on polyubiquitin-binding. 2 PublicationsCorresponds to variant dbSNP:rs143511494Ensembl.1
Natural variantiVAR_023598425G → R in PDB3 and FTDALS3; loss of polyubiquitin-binding and increased activation of NF-kappa-B. 5 PublicationsCorresponds to variant dbSNP:rs757212984Ensembl.1
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.1 Publication
Frontotemporal dementia and/or amyotrophic lateral sclerosis 3 (FTDALS3)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:616437
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07389916A → V in FTDALS3. 1 Publication1
Natural variantiVAR_07390133A → V in FTDALS3. 3 PublicationsCorresponds to variant dbSNP:rs200396166Ensembl.1
Natural variantiVAR_07390280D → E in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs148366738Ensembl.1
Natural variantiVAR_07390390V → M in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs181263868Ensembl.1
Natural variantiVAR_073906107R → W in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs771903158Ensembl.1
Natural variantiVAR_073912129D → N in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs753212399Ensembl.1
Natural variantiVAR_073914153V → I in FTDALS3. 2 PublicationsCorresponds to variant dbSNP:rs145056421Ensembl.1
Natural variantiVAR_073916212R → C in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs201263163Ensembl.1
Natural variantiVAR_073918219G → V in FTDALS3. 1 Publication1
Natural variantiVAR_073919226S → P in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs765200636Ensembl.1
Natural variantiVAR_073920228P → L in FTDALS3. 2 PublicationsCorresponds to variant dbSNP:rs151191977Ensembl.1
Natural variantiVAR_073921232P → T in FTDALS3. 1 Publication1
Natural variantiVAR_073922238Missing in FTDALS3. 3 Publications1
Natural variantiVAR_073923258D → N in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs774986849Ensembl.1
Natural variantiVAR_073927318S → P in FTDALS3. 1 Publication1
Natural variantiVAR_073929321R → C in FTDALS3. 2 PublicationsCorresponds to variant dbSNP:rs140226523Ensembl.1
Natural variantiVAR_073930329D → G in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs148294622Ensembl.1
Natural variantiVAR_073932348P → L in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs772889843Ensembl.1
Natural variantiVAR_073934370S → P in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs143956614Ensembl.1
Natural variantiVAR_073935381A → V in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs772122047Ensembl.1
Natural variantiVAR_023592387P → L in PDB3 and FTDALS3. 3 PublicationsCorresponds to variant dbSNP:rs776749939Ensembl.1
Natural variantiVAR_023593392P → L in PDB3 and FTDALS3; no effect on polyubiquitin-binding. 9 PublicationsCorresponds to variant dbSNP:rs104893941Ensembl.1
Natural variantiVAR_023597411G → S in PDB3 and FTDALS3; no effect on polyubiquitin-binding. 2 PublicationsCorresponds to variant dbSNP:rs143511494Ensembl.1
Natural variantiVAR_023598425G → R in PDB3 and FTDALS3; loss of polyubiquitin-binding and increased activation of NF-kappa-B. 5 PublicationsCorresponds to variant dbSNP:rs757212984Ensembl.1
Natural variantiVAR_073936430T → P in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs770118706Ensembl.1
Neurodegeneration with ataxia, dystonia, and gaze palsy, childhood-onset (NADGP)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:617145
Myopathy, distal, with rimmed vacuoles (DMRV)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:617158

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi7K → A: Loss of interactions with PRKCZ, PRCKI and NBR1. Loss of dimerization; when associated with A-69. 2 Publications1
Mutagenesisi9Y → F: No effect on interaction with LCK. 1 Publication1
Mutagenesisi13K → A: No effect on interaction with PRKCI. 1 Publication1
Mutagenesisi21 – 22RR → AA: Loss of interaction with PRKCI. Alters dimerization. 1 Publication2
Mutagenesisi67Y → A: No effect on interaction with PRKCZ. 1 Publication1
Mutagenesisi69D → 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. 3 Publications1
Mutagenesisi71D → A: No effect on interaction with PRKCI. 1 Publication1
Mutagenesisi73D → A: No effect on interactions with PRKCZ and PRKCI. 2 Publications1
Mutagenesisi80D → A: No effect on interaction with PRKCI. 1 Publication1
Mutagenesisi82E → A: No effect on interaction with PRKCI. 1 Publication1
Mutagenesisi323 – 324EE → AA: No effect on MAP1LC3B-binding. 1 Publication2
Mutagenesisi332S → A: No effect on MAP1LC3B-binding. 1 Publication1
Mutagenesisi335 – 337DDD → ADA: 75% decrease in MAP1LC3B-binding. 1 Publication3
Mutagenesisi338W → A: Strong decrease in MAP1LC3B-binding, disupts interaction with GABARAP. 2 Publications1
Mutagenesisi342S → A: No effect on MAP1LC3B-binding. 1 Publication1
Mutagenesisi398L → V: No effect on polyubiquitin-binding. 1 Publication1
Mutagenesisi406F → V: Loss of polyubiquitin-binding. 1 Publication1
Mutagenesisi409E → K: Decreased activation of NF-kappa-B. 1 Publication1
Mutagenesisi410G → K: Decreased activation of NF-kappa-B. 1 Publication1
Mutagenesisi413L → V: No effect on polyubiquitin-binding. 1 Publication1
Mutagenesisi417L → V: Loss of polyubiquitin-binding. 1 Publication1
Mutagenesisi431I → V: Partial loss of polyubiquitin-binding. Loss of localization to cytoplasmic inclusion bodies. 2 Publications1

Keywords - Diseasei

Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNETi8878.
MalaCardsiSQSTM1.
MIMi167250. phenotype.
616437. phenotype.
617145. phenotype.
617158. phenotype.
OpenTargetsiENSG00000161011.
Orphaneti803. Amyotrophic lateral sclerosis.
280110. Paget disease of bone.
PharmGKBiPA36109.

Polymorphism and mutation databases

BioMutaiSQSTM1.
DMDMi74735628.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000721762 – 440Sequestosome-1Add BLAST439
Isoform 2 (identifier: Q13501-2)
Initiator methionineiRemovedCombined sources

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei24PhosphoserineCombined sources1
Modified residuei148PhosphotyrosineCombined sources1
Modified residuei170PhosphoserineCombined sources1
Modified residuei176PhosphoserineCombined sources1
Modified residuei207PhosphoserineCombined sources1
Modified residuei233PhosphoserineCombined sources1
Modified residuei249PhosphoserineCombined sources1
Modified residuei266PhosphoserineCombined sources1
Modified residuei269PhosphothreonineCombined sources1
Modified residuei272PhosphoserineCombined sources1
Modified residuei306PhosphoserineCombined sources1
Modified residuei328PhosphoserineCombined sources1
Modified residuei332PhosphoserineCombined sources1
Modified residuei355PhosphoserineCombined sources1
Modified residuei361PhosphoserineCombined sources1
Modified residuei365PhosphoserineBy similarity1
Modified residuei366PhosphoserineCombined sources1
Modified residuei403Phosphoserine; by ULK11 Publication1
Cross-linki435Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Isoform 2 (identifier: Q13501-2)
Modified residuei2N-acetylalanineCombined sources1

Post-translational modificationi

Phosphorylated. May be phosphorylated by PRKCZ (By similarity). Phosphorylated in vitro by TTN. Phosphorylation at Ser-403 by ULK1 is stimulated by SESN2 (PubMed:25040165).By similarity2 Publications
Ubiquitinated by RNF26: 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). Deubiquitination by USP15 releases target vesicles for fast transport into the cell periphery (PubMed:27368102).1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ13501.
MaxQBiQ13501.
PaxDbiQ13501.
PeptideAtlasiQ13501.
PRIDEiQ13501.

PTM databases

iPTMnetiQ13501.
PhosphoSitePlusiQ13501.
SwissPalmiQ13501.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Inductioni

By proteasomal inhibitor PSI and prostaglandin J2 (PGJ2) (at protein level). By phorbol 12-myristate 13-acetate (PMA).3 Publications

Gene expression databases

BgeeiENSG00000161011.
CleanExiHS_SQSTM1.
ExpressionAtlasiQ13501. baseline and differential.
GenevisibleiQ13501. HS.

Organism-specific databases

HPAiCAB004587.
HPA064165.

Interactioni

Subunit structurei

Homooligomer or heterooligomer; may form homotypic arrays. Dimerization interferes with ubiquitin binding. Interacts directly with PRKCI and PRKCZ (Probable). Forms ternary complexes with PRKCZ and KCNAB2 or PRKCZ and GABBR3. Also interacts with KCNAB1, GABRR1, GABRR2 and GABRR3. Forms an NGF-induced complex with IKBKB, PRKCI and TRAF6 (By similarity). Interacts with EBI3, LCK, RASA1, PRKCZ, PRKCI, NR2F2, NTRK1, NTRK2, NTRK3, NBR1, MAP2K5, TRIM13, TRIM55 and MAPKAPK5. Interacts with the proteasome subunits PSMD4 and PSMC2. Interacts with K63-polyubiquitinated MAPT/TAU. Interacts with IKBKB through PRKCZ and PRKCI. Interacts with NGFR through TRAF6 and bridges that complex to NTRK1. Forms a complex with MAP2K5 and PRKCZ or PRKCI. Component of a ternary complex with PAWR and PRKCZ. Upon TNF-alpha stimulation, interacts with RIPK1 probably bridging IKBKB to the TNF-R1 complex composed of TNF-R1/TNFRSF1A, TRADD and RIPK1. Forms a complex with JUB/Ajuba, PRKCZ and TRAF6. Interacts with TRAF6 and CYLD. Identified in a complex with TRAF6 and CYLD (By similarity). Identified in a heterotrimeric complex with ubiquitin and ZFAND5, where ZFAND5 and SQSTM1 both interact with the same ubiquitin molecule. Directly interacts with MAP1LC3A and MAP1LC3B, as well as with other MAP1 LC3 family members, including GABARAP, GABARAPL1 and GABARAPL2; these interactions are necessary for the recruitment MAP1 LC3 family members to inclusion bodies containing polyubiquitinated protein aggregates and for their degradation by autophagy. Interacts with FHOD3. Interacts with TRMI5. Interacts with SESN1 (PubMed:23274085). Interacts with SESN2 (PubMed:23274085, PubMed:25040165). Interacts with ULK1 (PubMed:25040165). Interacts with UBD (PubMed:25422469). Interacts with WDR81; the interaction is direct and regulates the interaction of SQSTM1 with ubiquitinated proteins (PubMed:28404643). Interacts with WDFY3; this interaction is required to recruit WDFY3 to cytoplasmic bodies and to PML bodies (PubMed:20168092).By similarityCurated35 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • ionotropic glutamate receptor binding Source: ARUK-UCL
  • K63-linked polyubiquitin modification-dependent protein binding Source: UniProtKB
  • protein homodimerization activity Source: Ensembl
  • protein kinase binding Source: UniProtKB
  • protein kinase C binding Source: UniProtKB
  • receptor tyrosine kinase binding Source: ProtInc
  • SH2 domain binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114397. 269 interactors.
CORUMiQ13501.
DIPiDIP-34443N.
ELMiQ13501.
IntActiQ13501. 148 interactors.
MINTiMINT-269914.
STRINGi9606.ENSP00000374455.

Structurei

Secondary structure

1440
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 10Combined sources6
Beta strandi19 – 24Combined sources6
Helixi43 – 54Combined sources12
Beta strandi62 – 64Combined sources3
Beta strandi66 – 68Combined sources3
Beta strandi74 – 76Combined sources3
Helixi80 – 88Combined sources9
Beta strandi92 – 101Combined sources10
Beta strandi388 – 390Combined sources3
Helixi392 – 402Combined sources11
Turni403 – 405Combined sources3
Beta strandi409 – 411Combined sources3
Helixi412 – 419Combined sources8
Turni420 – 422Combined sources3
Helixi424 – 431Combined sources8
Beta strandi432 – 434Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q02NMR-A387-436[»]
2JY7NMR-A387-436[»]
2JY8NMR-A387-436[»]
2K0BNMR-X387-436[»]
2KNVNMR-A/B387-436[»]
4MJSX-ray2.50B/D/F/H/J/L/N/P/R/T/V/X3-102[»]
4UF8electron microscopy10.90A/B/C/I3-102[»]
4UF9electron microscopy10.30A/B/D1-122[»]
ProteinModelPortaliQ13501.
SMRiQ13501.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13501.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 102PB1PROSITE-ProRule annotationAdd BLAST100
Domaini389 – 434UBAPROSITE-ProRule annotationAdd BLAST46

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 50Interaction with LCKAdd BLAST49
Regioni43 – 107Interaction with PRKCZ and dimerizationBy similarityAdd BLAST65
Regioni50 – 80Interaction with PAWR1 PublicationAdd BLAST31
Regioni122 – 224Interaction with GABRR3By similarityAdd BLAST103
Regioni170 – 220LIM protein-binding (LB)Add BLAST51
Regioni269 – 440Interaction with NTRK1By similarityAdd BLAST172
Regioni321 – 342MAP1LC3B-bindingAdd BLAST22

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi228 – 233TRAF6-binding6
Motifi336 – 341LIR6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi272 – 294Ser-richAdd BLAST23

Domaini

The UBA domain binds specifically 'Lys-63'-linked polyubiquitin chains of polyubiquitinated substrates. Mediates the interaction with TRIM55. Both the UBA and PB1 domains are necessary and sufficient for the localization into the ubiquitin-containing inclusion bodies.2 Publications
The PB1 domain mediates homooligomerization and interactions with FHOD3, MAP2K5, NBR1, PRKCI, PRKCZ and WDR81. Both the PB1 and UBA domains are necessary and sufficient for the localization into the ubiquitin-containing inclusion bodies.4 Publications
The ZZ-type zinc finger mediates the interaction with RIPK1.1 Publication
The LIR (LC3-interacting region) motif mediates the interaction with ATG8 family proteins.1 Publication

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri122 – 167ZZ-typePROSITE-ProRule annotationAdd BLAST46

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG4582. Eukaryota.
ENOG410XYAV. LUCA.
GeneTreeiENSGT00390000002781.
HOVERGENiHBG052750.
InParanoidiQ13501.
KOiK14381.
OMAiSVCPNYD.
OrthoDBiEOG091G08ES.
PhylomeDBiQ13501.
TreeFamiTF328470.

Family and domain databases

CDDicd06402. PB1_p62. 1 hit.
cd14320. UBA_SQSTM. 1 hit.
InterProiView protein in InterPro
IPR000270. PB1_dom.
IPR034866. PB1_p62.
IPR033741. SQSTM_UBA.
IPR015940. UBA.
IPR009060. UBA-like.
IPR000433. Znf_ZZ.
PfamiView protein in Pfam
PF00564. PB1. 1 hit.
PF16577. UBA_5. 1 hit.
PF00569. ZZ. 1 hit.
SMARTiView protein in SMART
SM00666. PB1. 1 hit.
SM00165. UBA. 1 hit.
SM00291. ZnF_ZZ. 1 hit.
SUPFAMiSSF46934. SSF46934. 1 hit.
PROSITEiView protein in PROSITE
PS51745. PB1. 1 hit.
PS50030. UBA. 1 hit.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13501-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MASLTVKAYL LGKEDAAREI RRFSFCCSPE PEAEAEAAAG PGPCERLLSR
60 70 80 90 100
VAALFPALRP GGFQAHYRDE DGDLVAFSSD EELTMAMSYV KDDIFRIYIK
110 120 130 140 150
EKKECRRDHR PPCAQEAPRN MVHPNVICDG CNGPVVGTRY KCSVCPDYDL
160 170 180 190 200
CSVCEGKGLH RGHTKLAFPS PFGHLSEGFS HSRWLRKVKH GHFGWPGWEM
210 220 230 240 250
GPPGNWSPRP PRAGEARPGP TAESASGPSE DPSVNFLKNV GESVAAALSP
260 270 280 290 300
LGIEVDIDVE HGGKRSRLTP VSPESSSTEE KSSSQPSSCC SDPSKPGGNV
310 320 330 340 350
EGATQSLAEQ MRKIALESEG RPEEQMESDN CSGGDDDWTH LSSKEVDPST
360 370 380 390 400
GELQSLQMPE SEGPSSLDPS QEGPTGLKEA ALYPHLPPEA DPRLIESLSQ
410 420 430 440
MLSMGFSDEG GWLTRLLQTK NYDIGAALDT IQYSKHPPPL
Length:440
Mass (Da):47,687
Last modified:November 1, 1996 - v1
Checksum:i462D94C171F337CD
GO
Isoform 2 (identifier: Q13501-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-84: Missing.

Show »
Length:356
Mass (Da):38,629
Checksum:i56E985FFBF86EC1B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti321R → A in AAA93299 (PubMed:8551575).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07389916A → V in FTDALS3. 1 Publication1
Natural variantiVAR_07390017A → V1 PublicationCorresponds to variant dbSNP:rs141502868Ensembl.1
Natural variantiVAR_07390133A → V in FTDALS3. 3 PublicationsCorresponds to variant dbSNP:rs200396166Ensembl.1
Natural variantiVAR_07390280D → E in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs148366738Ensembl.1
Natural variantiVAR_07390390V → M in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs181263868Ensembl.1
Natural variantiVAR_073904103K → R1 PublicationCorresponds to variant dbSNP:rs748170760Ensembl.1
Natural variantiVAR_073905107R → Q1 Publication1
Natural variantiVAR_073906107R → W in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs771903158Ensembl.1
Natural variantiVAR_073907108D → Y1 Publication1