Q9H1I8 · ASCC2_HUMAN
- ProteinActivating signal cointegrator 1 complex subunit 2
- GeneASCC2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids757 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Ubiquitin-binding protein involved in DNA repair and rescue of stalled ribosomes (PubMed:29144457, PubMed:32099016, PubMed:32579943, PubMed:36302773).
Plays a role in DNA damage repair as component of the ASCC complex (PubMed:29144457).
Recruits ASCC3 and ALKBH3 to sites of DNA damage by binding to polyubiquitinated proteins that have 'Lys-63'-linked polyubiquitin chains (PubMed:29144457).
Part of the ASC-1 complex that enhances NF-kappa-B, SRF and AP1 transactivation (PubMed:12077347).
Involved in activation of the ribosome quality control (RQC) pathway, a pathway that degrades nascent peptide chains during problematic translation (PubMed:32099016, PubMed:32579943, PubMed:36302773).
Specifically recognizes and binds RPS20/uS10 ubiquitinated by ZNF598, promoting recruitment of the RQT (ribosome quality control trigger) complex on stalled ribosomes, followed by disassembly of stalled ribosomes (PubMed:36302773).
Plays a role in DNA damage repair as component of the ASCC complex (PubMed:29144457).
Recruits ASCC3 and ALKBH3 to sites of DNA damage by binding to polyubiquitinated proteins that have 'Lys-63'-linked polyubiquitin chains (PubMed:29144457).
Part of the ASC-1 complex that enhances NF-kappa-B, SRF and AP1 transactivation (PubMed:12077347).
Involved in activation of the ribosome quality control (RQC) pathway, a pathway that degrades nascent peptide chains during problematic translation (PubMed:32099016, PubMed:32579943, PubMed:36302773).
Specifically recognizes and binds RPS20/uS10 ubiquitinated by ZNF598, promoting recruitment of the RQT (ribosome quality control trigger) complex on stalled ribosomes, followed by disassembly of stalled ribosomes (PubMed:36302773).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | activating signal cointegrator 1 complex | |
Cellular Component | cytosolic ribosome | |
Cellular Component | DNA repair complex | |
Cellular Component | nuclear speck | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | K63-linked polyubiquitin modification-dependent protein binding | |
Molecular Function | ubiquitin binding | |
Biological Process | DNA alkylation repair | |
Biological Process | DNA duplex unwinding | |
Biological Process | regulation of DNA-templated transcription | |
Biological Process | rescue of stalled ribosome | |
Biological Process | ribosome disassembly | |
Biological Process | ribosome-associated ubiquitin-dependent protein catabolic process |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameActivating signal cointegrator 1 complex subunit 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H1I8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with the spliceosomal components PRPF8 and SNRNP200/BRR2 in nuclear foci when cells have been exposed to alkylating agents that cause DNA damage. Colocalizes with RNF113A and 'Lys-63'-linked polyubiquitinated proteins, ALKBH3 and ASCC3 in nuclear foci when cells have been exposed to alkylating agents that cause DNA damage.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_050675 | 96 | in dbSNP:rs1894473 | |||
Sequence: R → C | ||||||
Natural variant | VAR_050676 | 123 | in dbSNP:rs11549795 | |||
Sequence: V → I | ||||||
Natural variant | VAR_025512 | 407 | in dbSNP:rs28265 | |||
Sequence: D → H | ||||||
Natural variant | VAR_025513 | 423 | in dbSNP:rs36571 | |||
Sequence: P → S | ||||||
Mutagenesis | 478-479 | Loss of ubiquitin binding. | ||||
Sequence: LL → AA | ||||||
Mutagenesis | 479-491 | Decreases ubiquitin binding. | ||||
Sequence: LPDLGEGFILACL → AADLGEGFALACA | ||||||
Mutagenesis | 506 | Loss of ubiquitin binding. | ||||
Sequence: L → A | ||||||
Natural variant | VAR_019464 | 509 | in dbSNP:rs4823054 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_050677 | 546 | in dbSNP:rs34833047 | |||
Sequence: D → G | ||||||
Natural variant | VAR_050678 | 588 | in dbSNP:rs34062345 | |||
Sequence: E → K | ||||||
Natural variant | VAR_025514 | 639 | in dbSNP:rs6006259 | |||
Sequence: R → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 874 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000064689 | 1-757 | UniProt | Activating signal cointegrator 1 complex subunit 2 | |||
Sequence: MPALPLDQLQITHKDPKTGKLRTSPALHPEQKADRYFVLYKPPPKDNIPALVEEYLERATFVANDLDWLLALPHDKFWCQVIFDETLQKCLDSYLRYVPRKFDEGVASAPEVVDMQKRLHRSVFLTFLRMSTHKESKDHFISPSAFGEILYNNFLFDIPKILDLCVLFGKGNSPLLQKMIGNIFTQQPSYYSDLDETLPTILQVFSNILQHCGLQGDGANTTPQKLEERGRLTPSDMPLLELKDIVLYLCDTCTTLWAFLDIFPLACQTFQKHDFCYRLASFYEAAIPEMESAIKKRRLEDSKLLGDLWQRLSHSRKKLMEIFHIILNQICLLPILESSCDNIQGFIEEFLQIFSSLLQEKRFLRDYDALFPVAEDISLLQQASSVLDETRTAYILQAVESAWEGVDRRKATDAKDPSVIEEPNGEPNGVTVTAEAVSQASSHPENSEEEECMGAAAAVGPAMCGVELDSLISQVKDLLPDLGEGFILACLEYYHYDPEQVINNILEERLAPTLSQLDRNLDREMKPDPTPLLTSRHNVFQNDEFDVFSRDSVDLSRVHKGKSTRKEENTRSLLNDKRAVAAQRQRYEQYSVVVEEVPLQPGESLPYHSVYYEDEYDDTYDGNQVGANDADSDDELISRRPFTIPQVLRTKVPREGQEEDDDDEEDDADEEAPKPDHFVQDPAVLREKAEARRMAFLAKKGYRHDSSTAVAGSPRGHGQSRETTQERRKKEANKATRANHNRRTMADRKRSKGMIPS | |||||||
Modified residue | 233 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 233 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 447 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 632 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 632 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 706 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 713 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 713 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Identified in the ASCC complex that contains ASCC1, ASCC2 and ASCC3 (PubMed:29144457, PubMed:29997253).
Interacts directly with ASCC3 (PubMed:29997253, PubMed:32099016).
The ASCC complex interacts with ALKBH3 (PubMed:22055184, PubMed:29144457).
Interacts (via CUE domain) with 'Lys-63'-linked polyubiquitin chains, but not with 'Lys-48'-linked polyubiquitin chains (PubMed:29144457).
Part of the ASC-1 complex, that contains TRIP4, ASCC1, ASCC2 and ASCC3 (PubMed:12077347).
Component of the RQT (ribosome quality control trigger) complex, that contains ASCC2, ASCC3 and TRIP4 (PubMed:32099016, PubMed:32579943, PubMed:36302773).
Interacts with CSRP1 (PubMed:26924529).
Interacts with PRPF8, a component of the spliceosome (PubMed:29144457).
Interacts with ZCCHC4 (PubMed:31799605).
Interacts directly with ASCC3 (PubMed:29997253, PubMed:32099016).
The ASCC complex interacts with ALKBH3 (PubMed:22055184, PubMed:29144457).
Interacts (via CUE domain) with 'Lys-63'-linked polyubiquitin chains, but not with 'Lys-48'-linked polyubiquitin chains (PubMed:29144457).
Part of the ASC-1 complex, that contains TRIP4, ASCC1, ASCC2 and ASCC3 (PubMed:12077347).
Component of the RQT (ribosome quality control trigger) complex, that contains ASCC2, ASCC3 and TRIP4 (PubMed:32099016, PubMed:32579943, PubMed:36302773).
Interacts with CSRP1 (PubMed:26924529).
Interacts with PRPF8, a component of the spliceosome (PubMed:29144457).
Interacts with ZCCHC4 (PubMed:31799605).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9H1I8 | ASCC3 Q8N3C0 | 9 | EBI-711197, EBI-1210710 | |
BINARY | Q9H1I8 | KATNAL1 Q9BW62 | 3 | EBI-711197, EBI-743591 | |
BINARY | Q9H1I8 | PRPF18 Q99633 | 3 | EBI-711197, EBI-2798416 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 467-510 | CUE | ||||
Sequence: ELDSLISQVKDLLPDLGEGFILACLEYYHYDPEQVINNILEERL | ||||||
Region | 617-687 | Disordered | ||||
Sequence: DDTYDGNQVGANDADSDDELISRRPFTIPQVLRTKVPREGQEEDDDDEEDDADEEAPKPDHFVQDPAVLRE | ||||||
Compositional bias | 657-671 | Acidic residues | ||||
Sequence: QEEDDDDEEDDADEE | ||||||
Compositional bias | 672-687 | Basic and acidic residues | ||||
Sequence: APKPDHFVQDPAVLRE | ||||||
Region | 699-757 | Disordered | ||||
Sequence: KKGYRHDSSTAVAGSPRGHGQSRETTQERRKKEANKATRANHNRRTMADRKRSKGMIPS | ||||||
Compositional bias | 720-742 | Basic and acidic residues | ||||
Sequence: SRETTQERRKKEANKATRANHNR |
Domain
The CUE domain specifically binds RPS20/uS10 ubiquitinated via 'Lys-63'-linked ubiquitin chains by ZNF598.
Sequence similarities
Belongs to the ASCC2 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9H1I8-1
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.
- Name1
- Length757
- Mass (Da)86,360
- Last updated2006-03-07 v3
- ChecksumBB1DCE21E3068E64
Q9H1I8-2
- Name2
Q9H1I8-3
- Name3
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_011009 | 1-114 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_045878 | 28-80 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_045879 | 137-159 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 344 | in Ref. 2; BAB15089 | ||||
Sequence: Q → H | ||||||
Alternative sequence | VSP_011010 | 483-484 | in isoform 2 | |||
Sequence: GE → EK | ||||||
Alternative sequence | VSP_011011 | 485-757 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 526 | in Ref. 2; BAB15089 | ||||
Sequence: K → N | ||||||
Sequence conflict | 586 | in Ref. 2; BAB15089 | ||||
Sequence: R → C | ||||||
Sequence conflict | 639 | in Ref. 2; BAH13926 | ||||
Sequence: R → G | ||||||
Sequence conflict | 645 | in Ref. 1; AAG45475 | ||||
Sequence: P → L | ||||||
Sequence conflict | 653 | in Ref. 1; AAG45475 | ||||
Sequence: P → L | ||||||
Compositional bias | 657-671 | Acidic residues | ||||
Sequence: QEEDDDDEEDDADEE | ||||||
Sequence conflict | 661 | in Ref. 2; BAH13926 | ||||
Sequence: D → G | ||||||
Compositional bias | 672-687 | Basic and acidic residues | ||||
Sequence: APKPDHFVQDPAVLRE | ||||||
Compositional bias | 720-742 | Basic and acidic residues | ||||
Sequence: SRETTQERRKKEANKATRANHNR | ||||||
Sequence conflict | 744 | in Ref. 2; BAH13926 | ||||
Sequence: T → I |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY013289 EMBL· GenBank· DDBJ | AAG45475.1 EMBL· GenBank· DDBJ | mRNA | ||
AK022886 EMBL· GenBank· DDBJ | BAB14293.1 EMBL· GenBank· DDBJ | mRNA | ||
AK025241 EMBL· GenBank· DDBJ | BAB15089.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK303257 EMBL· GenBank· DDBJ | BAH13926.1 EMBL· GenBank· DDBJ | mRNA | ||
AC004882 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
Z82171 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC025368 EMBL· GenBank· DDBJ | AAH25368.1 EMBL· GenBank· DDBJ | mRNA |