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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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri122 – 16746ZZ-typePROSITE-ProRule annotationAdd
BLAST

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 signaling pathway Source: Reactome
  • 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
  • macromitophagy Source: Reactome
  • 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
  • neurotrophin TRK receptor signaling pathway Source: Reactome
  • 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
  • protein phosphorylation Source: GOC
  • 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.

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti387 – 3871P → L in PDB3 and FTDALS3. 3 Publications
VAR_023592
Natural varianti392 – 3921P → L in PDB3 and FTDALS3; no effect on polyubiquitin-binding. 9 Publications
Corresponds to variant rs104893941 [ dbSNP | Ensembl ].
VAR_023593
Natural varianti399 – 3991S → P in PDB3. 1 Publication
VAR_023594
Natural varianti404 – 4041M → T in PDB3. 1 Publication
VAR_023595
Natural varianti404 – 4041M → V in PDB3; loss of polyubiquitin-binding. 2 Publications
VAR_023596
Natural varianti411 – 4111G → S in PDB3 and FTDALS3; no effect on polyubiquitin-binding. 2 Publications
VAR_023597
Natural varianti425 – 4251G → R in PDB3 and FTDALS3; loss of polyubiquitin-binding and increased activation of NF-kappa-B. 5 Publications
VAR_023598

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161A → V in FTDALS3. 1 Publication
VAR_073899
Natural varianti33 – 331A → V in FTDALS3. 3 Publications
VAR_073901
Natural varianti80 – 801D → E in FTDALS3. 1 Publication
VAR_073902
Natural varianti90 – 901V → M in FTDALS3. 1 Publication
VAR_073903
Natural varianti107 – 1071R → W in FTDALS3. 1 Publication
VAR_073906
Natural varianti129 – 1291D → N in FTDALS3. 1 Publication
VAR_073912
Natural varianti153 – 1531V → I in FTDALS3. 2 Publications
VAR_073914
Natural varianti212 – 2121R → C in FTDALS3. 1 Publication
VAR_073916
Natural varianti219 – 2191G → V in FTDALS3. 1 Publication
VAR_073918
Natural varianti226 – 2261S → P in FTDALS3. 1 Publication
VAR_073919
Natural varianti228 – 2281P → L in FTDALS3. 2 Publications
VAR_073920
Natural varianti232 – 2321P → T in FTDALS3. 1 Publication
VAR_073921
Natural varianti238 – 2381Missing in FTDALS3. 3 Publications
VAR_073922
Natural varianti258 – 2581D → N in FTDALS3. 1 Publication
VAR_073923
Natural varianti318 – 3181S → P in FTDALS3. 1 Publication
VAR_073927
Natural varianti321 – 3211R → C in FTDALS3. 2 Publications
VAR_073929
Natural varianti329 – 3291D → G in FTDALS3. 1 Publication
VAR_073930
Natural varianti348 – 3481P → L in FTDALS3. 1 Publication
VAR_073932
Natural varianti370 – 3701S → P in FTDALS3. 1 Publication
VAR_073934
Natural varianti381 – 3811A → V in FTDALS3. 1 Publication
VAR_073935
Natural varianti387 – 3871P → L in PDB3 and FTDALS3. 3 Publications
VAR_023592
Natural varianti392 – 3921P → L in PDB3 and FTDALS3; no effect on polyubiquitin-binding. 9 Publications
Corresponds to variant rs104893941 [ dbSNP | Ensembl ].
VAR_023593
Natural varianti411 – 4111G → S in PDB3 and FTDALS3; no effect on polyubiquitin-binding. 2 Publications
VAR_023597
Natural varianti425 – 4251G → R in PDB3 and FTDALS3; loss of polyubiquitin-binding and increased activation of NF-kappa-B. 5 Publications
VAR_023598
Natural varianti430 – 4301T → P in FTDALS3. 1 Publication
VAR_073936

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71K → A: Loss of interactions with PRKCZ, PRCKI and NBR1. Loss of dimerization; when associated with A-69. 2 Publications
Mutagenesisi9 – 91Y → F: No effect on interaction with LCK. 1 Publication
Mutagenesisi13 – 131K → A: No effect on interaction with PRKCI. 1 Publication
Mutagenesisi21 – 222RR → AA: Loss of interaction with PRKCI. Alters dimerization. 1 Publication
Mutagenesisi67 – 671Y → A: No effect on interaction with PRKCZ. 1 Publication
Mutagenesisi69 – 691D → 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 Publications
Mutagenesisi71 – 711D → A: No effect on interaction with PRKCI. 1 Publication
Mutagenesisi73 – 731D → A: No effect on interactions with PRKCZ and PRKCI. 2 Publications
Mutagenesisi80 – 801D → A: No effect on interaction with PRKCI. 1 Publication
Mutagenesisi82 – 821E → A: No effect on interaction with PRKCI. 1 Publication
Mutagenesisi323 – 3242EE → AA: No effect on MAP1LC3B-binding. 1 Publication
Mutagenesisi332 – 3321S → A: No effect on MAP1LC3B-binding. 1 Publication
Mutagenesisi335 – 3373DDD → ADA: 75% decrease in MAP1LC3B-binding. 1 Publication
Mutagenesisi338 – 3381W → A: Strong decrease in MAP1LC3B-binding, disupts interaction with GABARAP. 2 Publications
Mutagenesisi342 – 3421S → A: No effect on MAP1LC3B-binding. 1 Publication
Mutagenesisi398 – 3981L → V: No effect on polyubiquitin-binding. 1 Publication
Mutagenesisi406 – 4061F → V: Loss of polyubiquitin-binding. 1 Publication
Mutagenesisi409 – 4091E → K: Decreased activation of NF-kappa-B. 1 Publication
Mutagenesisi410 – 4101G → K: Decreased activation of NF-kappa-B. 1 Publication
Mutagenesisi413 – 4131L → V: No effect on polyubiquitin-binding. 1 Publication
Mutagenesisi417 – 4171L → V: Loss of polyubiquitin-binding. 1 Publication
Mutagenesisi431 – 4311I → V: Partial loss of polyubiquitin-binding. Loss of localization to cytoplasmic inclusion bodies. 2 Publications

Keywords - Diseasei

Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

Organism-specific databases

MalaCardsiSQSTM1.
MIMi167250. phenotype.
616437. phenotype.
Orphaneti803. Amyotrophic lateral sclerosis.
280110. Paget disease of bone.
PharmGKBiPA36109.

Polymorphism and mutation databases

BioMutaiSQSTM1.
DMDMi74735628.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 440439Sequestosome-1PRO_0000072176Add
BLAST
Isoform 2 (identifier: Q13501-2)
Initiator methionineiRemovedCombined sources

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei24 – 241PhosphoserineCombined sources
Modified residuei148 – 1481PhosphotyrosineCombined sources
Modified residuei170 – 1701PhosphoserineCombined sources
Modified residuei176 – 1761PhosphoserineCombined sources
Modified residuei207 – 2071PhosphoserineCombined sources
Modified residuei233 – 2331PhosphoserineCombined sources
Modified residuei249 – 2491PhosphoserineCombined sources
Modified residuei266 – 2661PhosphoserineCombined sources
Modified residuei269 – 2691PhosphothreonineCombined sources
Modified residuei272 – 2721PhosphoserineCombined sources
Modified residuei306 – 3061PhosphoserineCombined sources
Modified residuei328 – 3281PhosphoserineCombined sources
Modified residuei332 – 3321PhosphoserineCombined sources
Modified residuei355 – 3551PhosphoserineCombined sources
Modified residuei361 – 3611PhosphoserineCombined sources
Modified residuei365 – 3651PhosphoserineBy similarity
Modified residuei366 – 3661PhosphoserineCombined sources
Isoform 2 (identifier: Q13501-2)
Modified residuei2 – 21N-acetylalanineCombined sources

Post-translational modificationi

Phosphorylated. May be phosphorylated by PRKCZ (By similarity). Phosphorylated in vitro by TTN.By similarity1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13501.
MaxQBiQ13501.
PaxDbiQ13501.
PRIDEiQ13501.

PTM databases

iPTMnetiQ13501.
PhosphoSiteiQ13501.

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

BgeeiQ13501.
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 problably 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.By similarityCurated31 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-307104,EBI-307104
ATG8P381823EBI-307104,EBI-2684From a different organism.
BAG3O958173EBI-307104,EBI-747185
CDC37Q165433EBI-307104,EBI-295634
FHOD3Q2V2M96EBI-307104,EBI-6395541
FHOD3Q2V2M9-44EBI-307104,EBI-6395505
GABARAPO9516610EBI-307104,EBI-712001
GABARAPL1Q9H0R810EBI-307104,EBI-746969
GABARAPL2P6052015EBI-307104,EBI-720116
IKBKGQ9Y6K92EBI-307104,EBI-81279
KEAP1Q1414511EBI-307104,EBI-751001
Keap1Q9Z2X82EBI-307104,EBI-647110From a different organism.
MALT1Q9UDY82EBI-307104,EBI-1047372
MAP1LC3AQ9H4927EBI-307104,EBI-720768
MAP1LC3BQ9GZQ817EBI-307104,EBI-373144
MAP1LC3CQ9BXW43EBI-307104,EBI-2603996
NBR1Q145966EBI-307104,EBI-742698
OPTNQ96CV97EBI-307104,EBI-748974
PRKCIP417435EBI-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. 226 interactions.
DIPiDIP-34443N.
IntActiQ13501. 133 interactions.
MINTiMINT-269914.
STRINGi9606.ENSP00000374455.

Structurei

Secondary structure

1
440
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Beta strandi19 – 246Combined sources
Helixi43 – 5412Combined sources
Beta strandi62 – 643Combined sources
Beta strandi66 – 683Combined sources
Beta strandi74 – 763Combined sources
Helixi80 – 889Combined sources
Beta strandi92 – 10110Combined sources
Beta strandi388 – 3903Combined sources
Helixi392 – 40211Combined sources
Turni403 – 4053Combined sources
Beta strandi409 – 4113Combined sources
Helixi412 – 4198Combined sources
Turni420 – 4223Combined sources
Helixi424 – 4318Combined sources
Beta strandi432 – 4343Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 3-102, 117-171, 387-436.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13501.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 102100PB1PROSITE-ProRule annotationAdd
BLAST
Domaini389 – 43446UBAPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 5049Interaction with LCKAdd
BLAST
Regioni43 – 10765Interaction with PRKCZ and dimerizationBy similarityAdd
BLAST
Regioni50 – 8031Interaction with PAWRAdd
BLAST
Regioni122 – 224103Interaction with GABRR3By similarityAdd
BLAST
Regioni170 – 22051LIM protein-binding (LB)Add
BLAST
Regioni269 – 440172Interaction with NTRK1By similarityAdd
BLAST
Regioni321 – 34222MAP1LC3B-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi228 – 2336TRAF6-binding
Motifi336 – 3416LIR

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi272 – 29423Ser-richAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri122 – 16746ZZ-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG4582. Eukaryota.
ENOG410XYAV. LUCA.
GeneTreeiENSGT00390000002781.
HOVERGENiHBG052750.
InParanoidiQ13501.
KOiK14381.
OMAiDDELMMG.
PhylomeDBiQ13501.
TreeFamiTF328470.

Family and domain databases

InterProiIPR000270. PB1_dom.
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.

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti321 – 3211R → A in AAA93299 (PubMed:8551575).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161A → V in FTDALS3. 1 Publication
VAR_073899
Natural varianti17 – 171A → V.1 Publication
VAR_073900
Natural varianti33 – 331A → V in FTDALS3. 3 Publications
VAR_073901
Natural varianti80 – 801D → E in FTDALS3. 1 Publication
VAR_073902
Natural varianti90 – 901V → M in FTDALS3. 1 Publication
VAR_073903
Natural varianti103 – 1031K → R.1 Publication
VAR_073904
Natural varianti107 – 1071R → Q.1 Publication
VAR_073905
Natural varianti107 – 1071R → W in FTDALS3. 1 Publication
VAR_073906
Natural varianti108 – 1081D → Y.1 Publication
VAR_073907
Natural varianti110 – 1101R → H.1 Publication
VAR_073908
Natural varianti117 – 1171A → V.2 Publications
Corresponds to variant rs147810437 [ dbSNP | Ensembl ].
VAR_023590
Natural varianti118 – 1181P → S.1 Publication
VAR_073909
Natural varianti119 – 1191R → G.1 Publication
VAR_073910
Natural varianti125 – 1251N → S.1 Publication
VAR_073911
Natural varianti129 – 1291D → N in FTDALS3. 1 Publication
VAR_073912
Natural varianti139 – 1391R → C.1 Publication
VAR_073913
Natural varianti153 – 1531V → I in FTDALS3. 2 Publications
VAR_073914
Natural varianti180 – 1801S → L.1 Publication
VAR_073915
Natural varianti212 – 2121R → C in FTDALS3. 1 Publication
VAR_073916
Natural varianti217 – 2171R → H.1 Publication
VAR_073917
Natural varianti219 – 2191G → V in FTDALS3. 1 Publication
VAR_073918
Natural varianti226 – 2261S → P in FTDALS3. 1 Publication
VAR_073919
Natural varianti228 – 2281P → L in FTDALS3. 2 Publications
VAR_073920
Natural varianti232 – 2321P → T in FTDALS3. 1 Publication
VAR_073921
Natural varianti238 – 2381K → E Polymorphism; confirmed at protein level. 2 Publications
Corresponds to variant rs11548633 [ dbSNP | Ensembl ].