Q13098 · CSN1_HUMAN
- ProteinCOP9 signalosome complex subunit 1
- GeneGPS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids491 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Suppresses G-protein- and mitogen-activated protein kinase-mediated signal transduction.
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 | COP9 signalosome | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | GTPase inhibitor activity | |
Biological Process | JNK cascade | |
Biological Process | protein deneddylation | |
Biological Process | protein neddylation | |
Biological Process | regulation of protein neddylation |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCOP9 signalosome complex subunit 1
- Short namesSGN1; Signalosome subunit 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ13098
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 506 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 initiator methionine, chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Chain | PRO_0000120959 | 2-491 | UniProt | COP9 signalosome complex subunit 1 | |||
Sequence: PLPVQVFNLQGAVEPMQIDVDPQEDPQNAPDVNYVVENPSLDLEQYAASYSGLMRIERLQFIADHCPTLRVEALKMALSFVQRTFNVDMYEEIHRKLSEATRSSLRELQNAPDAIPESGVEPPALDTAWVEATRKKALLKLEKLDTDLKNYKGNSIKESIRRGHDDLGDHYLDCGDLSNALKCYSRARDYCTSAKHVINMCLNVIKVSVYLQNWSHVLSYVSKAESTPEIAEQRGERDSQTQAILTKLKCAAGLAELAARKYKQAAKCLLLASFDHCDFPELLSPSNVAIYGGLCALATFDRQELQRNVISSSSFKLFLELEPQVRDIIFKFYESKYASCLKMLDEMKDNLLLDMYLAPHVRTLYTQIRNRALIQYFSPYVSADMHRMAAAFNTTVAALEDELTQLILEGLISARVDSHSKILYARDVDQRSTTFEKSLLMGKEFQRRAKAMMLRAAVLRNQIHVKSPPREGSQGELTPANSQSRMSTNM | |||||||
Modified residue (large scale data) | 240 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 468 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 468 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 474 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 474 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 479 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 479 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 483 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 483 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 485 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9 isoform 1 (PubMed:11337588, PubMed:18850735, PubMed:26456823).
In the complex, it probably interacts directly with COPS2, COPS3, COPS4 and COPS5 (PubMed:11114242).
Interacts directly with inositol kinase ITPK1 (PubMed:12324474).
Interacts with CAPN8 (By similarity).
Interacts with USP48 (PubMed:35913642).
In the complex, it probably interacts directly with COPS2, COPS3, COPS4 and COPS5 (PubMed:11114242).
Interacts directly with inositol kinase ITPK1 (PubMed:12324474).
Interacts with CAPN8 (By similarity).
Interacts with USP48 (PubMed:35913642).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q13098 | COPS5 Q92905 | 19 | EBI-725197, EBI-594661 | |
BINARY | Q13098-7 | CNOT2 Q9NZN8 | 3 | EBI-10983983, EBI-743033 | |
BINARY | Q13098-7 | COPS2 P61201 | 5 | EBI-10983983, EBI-1050386 | |
BINARY | Q13098-7 | COPS8 Q99627 | 4 | EBI-10983983, EBI-2510102 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 269-431 | PCI | ||||
Sequence: CLLLASFDHCDFPELLSPSNVAIYGGLCALATFDRQELQRNVISSSSFKLFLELEPQVRDIIFKFYESKYASCLKMLDEMKDNLLLDMYLAPHVRTLYTQIRNRALIQYFSPYVSADMHRMAAAFNTTVAALEDELTQLILEGLISARVDSHSKILYARDVDQ | ||||||
Region | 465-491 | Disordered | ||||
Sequence: HVKSPPREGSQGELTPANSQSRMSTNM | ||||||
Compositional bias | 475-491 | Polar residues | ||||
Sequence: QGELTPANSQSRMSTNM |
Domain
The PCI domain is necessary and sufficient for the interactions with other CSN subunits of the complex. Mediates the interaction with CAPN8 (By similarity).
The N-terminal part (1-216), which is not required for deneddylating activity and CSN complex formation, is nevertheless essential for other aspects of CSN complex function, such as repression of c-fos/FOS expression.
Sequence similarities
Belongs to the CSN1 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q13098-4
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
- Length491
- Mass (Da)55,537
- Last updated2009-02-10 v4
- ChecksumBF925164ED985638
Q13098-5
- Name4
- Differences from canonical
- 103-106: Missing
Q13098-6
- Name3
- Differences from canonical
- 12-109: GAVEPMQIDVDPQEDPQNAPDVNYVVENPSLDLEQYAASYSGLMRIERLQFIADHCPTLRVEALKMALSFVQRTFNVDMYEEIHRKLSEATRSSLREL → PASSVSGSGGAESQDRMRDSSAPSSASSSVTDLYCTPHSSRSDLVLPGMAGDFSLSASLSACTLLYEGAVEPMQIDVDPQEDP
- 471-491: REGSQGELTPANSQSRMSTNM → TSTDLGPPGGSVLPAAQLRGLATGCHPACVPSLGLRRQAAASCGPSWKERPAGLDPVGFCPQGADCAAPRPSGTISQTPPVPASVRCRQVGGVH
Q13098-7
- Name2
Computationally mapped potential isoform sequences
There are 19 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
J3KRJ4 | J3KRJ4_HUMAN | GPS1 | 253 | ||
J3KRE8 | J3KRE8_HUMAN | GPS1 | 186 | ||
J3KRY5 | J3KRY5_HUMAN | GPS1 | 44 | ||
J3KSA5 | J3KSA5_HUMAN | GPS1 | 210 | ||
J3KSY1 | J3KSY1_HUMAN | GPS1 | 93 | ||
J3KTB0 | J3KTB0_HUMAN | GPS1 | 139 | ||
A0A096LP07 | A0A096LP07_HUMAN | GPS1 | 486 | ||
A0A096LPJ3 | A0A096LPJ3_HUMAN | GPS1 | 490 | ||
A8K070 | A8K070_HUMAN | GPS1 | 526 | ||
C9JFE4 | C9JFE4_HUMAN | GPS1 | 471 | ||
A0A9L9PXT0 | A0A9L9PXT0_HUMAN | GPS1 | 559 | ||
A0A9L9PX62 | A0A9L9PX62_HUMAN | GPS1 | 558 | ||
J3QL53 | J3QL53_HUMAN | GPS1 | 168 | ||
J3QLE8 | J3QLE8_HUMAN | GPS1 | 166 | ||
J3QLT0 | J3QLT0_HUMAN | GPS1 | 168 | ||
J3QQX0 | J3QQX0_HUMAN | GPS1 | 79 | ||
J3QQP2 | J3QQP2_HUMAN | GPS1 | 60 | ||
J3QS88 | J3QS88_HUMAN | GPS1 | 134 | ||
J3QS84 | J3QS84_HUMAN | GPS1 | 101 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_036240 | 1-11 | in isoform 2 | |||
Sequence: MPLPVQVFNLQ → MRDSSAPSSASSSVTDLYCTPHSSRSDLVLPGTAGDFSLSASLSACTLLYE | ||||||
Alternative sequence | VSP_036241 | 12-109 | in isoform 3 | |||
Sequence: GAVEPMQIDVDPQEDPQNAPDVNYVVENPSLDLEQYAASYSGLMRIERLQFIADHCPTLRVEALKMALSFVQRTFNVDMYEEIHRKLSEATRSSLREL → PASSVSGSGGAESQDRMRDSSAPSSASSSVTDLYCTPHSSRSDLVLPGMAGDFSLSASLSACTLLYEGAVEPMQIDVDPQEDP | ||||||
Alternative sequence | VSP_036242 | 103-106 | in isoform 2 and isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 259 | in Ref. 2; BAC04120 | ||||
Sequence: A → T | ||||||
Alternative sequence | VSP_011882 | 471-491 | in isoform 3 | |||
Sequence: REGSQGELTPANSQSRMSTNM → TSTDLGPPGGSVLPAAQLRGLATGCHPACVPSLGLRRQAAASCGPSWKERPAGLDPVGFCPQGADCAAPRPSGTISQTPPVPASVRCRQVGGVH | ||||||
Compositional bias | 475-491 | Polar residues | ||||
Sequence: QGELTPANSQSRMSTNM |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U20285 EMBL· GenBank· DDBJ | AAC50906.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK093283 EMBL· GenBank· DDBJ | BAC04120.1 EMBL· GenBank· DDBJ | mRNA | ||
AC135056 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC000155 EMBL· GenBank· DDBJ | AAH00155.3 EMBL· GenBank· DDBJ | mRNA | ||
BC064503 EMBL· GenBank· DDBJ | AAH64503.1 EMBL· GenBank· DDBJ | mRNA | ||
BT009834 EMBL· GenBank· DDBJ | AAP88836.1 EMBL· GenBank· DDBJ | mRNA |