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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. Required both for the formation and autophagic degradation of polyubiquitin-containing bodies, called ALIS (aggresome-like induced structures) and links ALIS to the autophagic machinery. Involved in midbody ring degradation. 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.By similarity13 Publications

Regions

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

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • 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

  • apoptotic process Source: UniProtKB-KW
  • autophagy Source: UniProtKB
  • cell differentiation Source: UniProtKB-KW
  • endosomal transport Source: UniProtKB
  • immune system process Source: UniProtKB-KW
  • intracellular signal transduction Source: UniProtKB
  • macroautophagy Source: UniProtKB
  • mitophagy Source: ParkinsonsUK-UCL
  • mitophagy in response to mitochondrial depolarization 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 macroautophagy Source: UniProtKB
  • 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
  • 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 stress Source: UniProtKB
  • ubiquitin-dependent protein catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Autophagy, Differentiation, Immunity

Keywords - Ligandi

Metal-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 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

HGNCiHGNC:11280. SQSTM1.

Subcellular locationi

  • Cytoplasm
  • Late endosome
  • Lysosome
  • Cytoplasmic vesicleautophagosome
  • Nucleus
  • Endoplasmic reticulum
  • CytoplasmP-body

  • Note: Sarcomere (By similarity). In cardiac muscles localizes to the sarcomeric band (By similarity). Commonly found in inclusion bodies containing polyubiquitinated protein aggregates. In neurodegenerative diseases, detected in Lewy bodies in Parkinson disease, neurofibrillary tangles in Alzheimer disease, and HTT aggregates in Huntington disease. 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. Enriched in Rosenthal fibers of pilocytic astrocytoma. In the cytoplasm, observed in both membrane-free ubiquitin-containing protein aggregates (sequestosomes) and membrane-surrounded autophagosomes. Colocalizes with TRIM13 in the perinuclear endoplasmic reticulum. Co-localizes with TRIM5 in the cytoplasmic bodies.By similarity

GO - Cellular componenti

  • aggresome Source: GO_Central
  • amphisome Source: ParkinsonsUK-UCL
  • autolysosome Source: ParkinsonsUK-UCL
  • autophagosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoplasmic mRNA processing body Source: UniProtKB
  • cytoplasmic vesicle Source: UniProtKB-KW
  • cytosol Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • inclusion body Source: UniProtKB
  • late endosome Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • PML body Source: UniProtKB
  • pre-autophagosomal structure Source: Ensembl
  • sperm midpiece Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Paget disease of bone 3 (PDB3)7 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 rs776749939dbSNPEnsembl.1
Natural variantiVAR_023593392P → L in PDB3 and FTDALS3; no effect on polyubiquitin-binding. 9 PublicationsCorresponds to variant rs104893941dbSNPEnsembl.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 rs771966860dbSNPEnsembl.1
Natural variantiVAR_023597411G → S in PDB3 and FTDALS3; no effect on polyubiquitin-binding. 2 PublicationsCorresponds to variant rs143511494dbSNPEnsembl.1
Natural variantiVAR_023598425G → R in PDB3 and FTDALS3; loss of polyubiquitin-binding and increased activation of NF-kappa-B. 5 PublicationsCorresponds to variant rs757212984dbSNPEnsembl.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.

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 rs200396166dbSNPEnsembl.1
Natural variantiVAR_07390280D → E in FTDALS3. 1 PublicationCorresponds to variant rs148366738dbSNPEnsembl.1
Natural variantiVAR_07390390V → M in FTDALS3. 1 PublicationCorresponds to variant rs181263868dbSNPEnsembl.1
Natural variantiVAR_073906107R → W in FTDALS3. 1 PublicationCorresponds to variant rs771903158dbSNPEnsembl.1
Natural variantiVAR_073912129D → N in FTDALS3. 1 PublicationCorresponds to variant rs753212399dbSNPEnsembl.1
Natural variantiVAR_073914153V → I in FTDALS3. 2 PublicationsCorresponds to variant rs145056421dbSNPEnsembl.1
Natural variantiVAR_073916212R → C in FTDALS3. 1 PublicationCorresponds to variant rs201263163dbSNPEnsembl.1
Natural variantiVAR_073918219G → V in FTDALS3. 1 Publication1
Natural variantiVAR_073919226S → P in FTDALS3. 1 PublicationCorresponds to variant rs765200636dbSNPEnsembl.1
Natural variantiVAR_073920228P → L in FTDALS3. 2 PublicationsCorresponds to variant rs151191977dbSNPEnsembl.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 rs774986849dbSNPEnsembl.1
Natural variantiVAR_073927318S → P in FTDALS3. 1 Publication1
Natural variantiVAR_073929321R → C in FTDALS3. 2 PublicationsCorresponds to variant rs140226523dbSNPEnsembl.1
Natural variantiVAR_073930329D → G in FTDALS3. 1 PublicationCorresponds to variant rs148294622dbSNPEnsembl.1
Natural variantiVAR_073932348P → L in FTDALS3. 1 PublicationCorresponds to variant rs772889843dbSNPEnsembl.1
Natural variantiVAR_073934370S → P in FTDALS3. 1 PublicationCorresponds to variant rs143956614dbSNPEnsembl.1
Natural variantiVAR_073935381A → V in FTDALS3. 1 PublicationCorresponds to variant rs772122047dbSNPEnsembl.1
Natural variantiVAR_023592387P → L in PDB3 and FTDALS3. 3 PublicationsCorresponds to variant rs776749939dbSNPEnsembl.1
Natural variantiVAR_023593392P → L in PDB3 and FTDALS3; no effect on polyubiquitin-binding. 9 PublicationsCorresponds to variant rs104893941dbSNPEnsembl.1
Natural variantiVAR_023597411G → S in PDB3 and FTDALS3; no effect on polyubiquitin-binding. 2 PublicationsCorresponds to variant rs143511494dbSNPEnsembl.1
Natural variantiVAR_023598425G → R in PDB3 and FTDALS3; loss of polyubiquitin-binding and increased activation of NF-kappa-B. 5 PublicationsCorresponds to variant rs757212984dbSNPEnsembl.1
Natural variantiVAR_073936430T → P in FTDALS3. 1 PublicationCorresponds to variant rs770118706dbSNPEnsembl.1

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.
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
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

Keywords - PTMi

Acetylation, Phosphoprotein

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.

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).By similarityCurated33 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself6EBI-307104,EBI-307104
ATG8P381823EBI-307104,EBI-2684From a different organism.
BAG3O958173EBI-307104,EBI-747185
CDC37Q165435EBI-307104,EBI-295634
FHOD3Q2V2M96EBI-307104,EBI-6395541
FHOD3Q2V2M9-44EBI-307104,EBI-6395505
GABARAPO9516610EBI-307104,EBI-712001
GABARAPL1Q9H0R812EBI-307104,EBI-746969
GABARAPL2P6052015EBI-307104,EBI-720116
IKBKGQ9Y6K92EBI-307104,EBI-81279
KEAP1Q1414513EBI-307104,EBI-751001
Keap1Q9Z2X82EBI-307104,EBI-647110From a different organism.
MALT1Q9UDY82EBI-307104,EBI-1047372
MAP1LC3AQ9H4929EBI-307104,EBI-720768
MAP1LC3BQ9GZQ819EBI-307104,EBI-373144
MAP1LC3CQ9BXW43EBI-307104,EBI-2603996
NBR1Q145966EBI-307104,EBI-742698
OPTNQ96CV97EBI-307104,EBI-748974
PRKCIP417437EBI-307104,EBI-286199
RAD23AP547252EBI-307104,EBI-746453
SESN2P580045EBI-307104,EBI-3939642
SH3KBP1Q96B974EBI-307104,EBI-346595
SMAD3P840223EBI-307104,EBI-347161
TRAF6Q9Y4K32EBI-307104,EBI-359276
UBCP0CG483EBI-307104,EBI-3390054
Ulk1O704052EBI-307104,EBI-8390771From a different organism.
vifP125042EBI-307104,EBI-779991From a different organism.

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • 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. 251 interactors.
DIPiDIP-34443N.
IntActiQ13501. 136 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.
The PB1 domain mediates homooligomerization and interactions with FHOD3, MAP2K5, NBR1, PRKCI and PRKCZ. Both the PB1 and UBA domains are necessary and sufficient for the localization into the ubiquitin-containing inclusion bodies.
The ZZ-type zinc finger mediates the interaction with RIPK1.
The LIR (LC3-interacting region) motif mediates the interaction with ATG8 family proteins.1 Publication

Sequence similaritiesi

Contains 1 PB1 domain.PROSITE-ProRule annotation
Contains 1 UBA domain.PROSITE-ProRule annotation
Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

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.
OMAiDDELMMG.
OrthoDBiEOG091G08ES.
PhylomeDBiQ13501.
TreeFamiTF328470.

Family and domain databases

CDDicd14320. UBA_SQSTM. 1 hit.
InterProiIPR000270. PB1_dom.
IPR033741. SQSTM_UBA.
IPR015940. UBA.
IPR009060. UBA-like.
IPR000433. Znf_ZZ.
[Graphical view]
PfamiPF00564. PB1. 1 hit.
PF16577. UBA_5. 1 hit.
PF00569. ZZ. 1 hit.
[Graphical view]
SMARTiSM00666. PB1. 1 hit.
SM00165. UBA. 1 hit.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
PROSITEiPS51745. PB1. 1 hit.
PS50030. UBA. 1 hit.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]

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.

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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 → V.1 PublicationCorresponds to variant rs141502868dbSNPEnsembl.1
Natural variantiVAR_07390133A → V in FTDALS3. 3 PublicationsCorresponds to variant rs200396166dbSNPEnsembl.1
Natural variantiVAR_07390280D → E in FTDALS3. 1 PublicationCorresponds to variant rs148366738dbSNPEnsembl.1
Natural variantiVAR_07390390V → M in FTDALS3. 1 PublicationCorresponds to variant rs181263868dbSNPEnsembl.1
Natural variantiVAR_073904103K → R.1 PublicationCorresponds to variant rs748170760dbSNPEnsembl.1
Natural variantiVAR_073905107R → Q.1 Publication1
Natural variantiVAR_073906107R → W in FTDALS3. 1 PublicationCorresponds to variant rs771903158dbSNPEnsembl.1
Natural variantiVAR_073907108D → Y.1 Publication1
Natural variantiVAR_073908110R → H.1 Publication1
Natural variantiVAR_023590117A → V.2 PublicationsCorresponds to variant rs147810437dbSNPEnsembl.1
Natural variantiVAR_073909118P → S.1 PublicationCorresponds to variant rs200152247dbSNPEnsembl.1
Natural variantiVAR_073910119R → G.1 PublicationCorresponds to variant rs548787835dbSNPEnsembl.1
Natural variantiVAR_073911125N → S.1 PublicationCorresponds to variant rs769325755dbSNPEnsembl.1
Natural variantiVAR_073912129D → N in FTDALS3. 1 PublicationCorresponds to variant rs753212399dbSNPEnsembl.1
Natural variantiVAR_073913139R → C.1 PublicationCorresponds to variant rs750256905dbSNPEnsembl.1
Natural variantiVAR_073914153V → I in FTDALS3. 2 PublicationsCorresponds to variant rs145056421dbSNPEnsembl.1
Natural variantiVAR_073915180S → L.1 Publication1
Natural variantiVAR_073916212R → C in FTDALS3. 1 PublicationCorresponds to variant rs201263163dbSNPEnsembl.1
Natural variantiVAR_073917217R → H.1 PublicationCorresponds to variant rs761822261dbSNPEnsembl.1
Natural variantiVAR_073918219G → V in FTDALS3. 1 Publication