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Protein

COP9 signalosome complex subunit 4

Gene

Cops4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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. Also involved in the deneddylation of non-cullin subunits such as STON2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1, IRF8/ICSBP and SNAPIN, 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 (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-5696394. DNA Damage Recognition in GG-NER.
R-MMU-6781823. Formation of TC-NER Pre-Incision Complex.

Names & Taxonomyi

Protein namesi
Recommended name:
COP9 signalosome complex subunit 4
Short name:
SGN4
Short name:
Signalosome subunit 4
Alternative name(s):
JAB1-containing signalosome subunit 4
Gene namesi
Name:Cops4
Synonyms:Csn4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1349414. Cops4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Nucleus, Signalosome, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 406405COP9 signalosome complex subunit 4PRO_0000120988Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei25 – 251N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiO88544.
PaxDbiO88544.
PeptideAtlasiO88544.
PRIDEiO88544.

2D gel databases

REPRODUCTION-2DPAGEO88544.

PTM databases

iPTMnetiO88544.
PhosphoSiteiO88544.
SwissPalmiO88544.

Expressioni

Gene expression databases

BgeeiO88544.
ExpressionAtlasiO88544. baseline and differential.
GenevisibleiO88544. MM.

Interactioni

Subunit structurei

Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B) and COPS8. In the complex, it probably interacts directly with COPS1, COPS2, COPS3, COPS5, COPS6, COPS7 (COPS7A or COPS7B) and COPS8. Interacts with TOR1A; the interaction is direct and associates TOR1A and SNAPIN with the CSN complex. Interacts with STON2; controls STON2 neddylation levels (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Stat2Q9QXJ26EBI-646659,EBI-646643

Protein-protein interaction databases

BioGridi205043. 6 interactions.
IntActiO88544. 3 interactions.
MINTiMINT-1869855.
STRINGi10090.ENSMUSP00000048416.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi302 – 31413Combined sources
Beta strandi317 – 3204Combined sources
Helixi321 – 3277Combined sources
Helixi332 – 34413Combined sources
Beta strandi350 – 3534Combined sources
Turni354 – 3574Combined sources
Beta strandi358 – 3614Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UFMNMR-A296-366[»]
ProteinModelPortaliO88544.
SMRiO88544. Positions 1-406.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO88544.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini201 – 363163PCIAdd
BLAST

Sequence similaritiesi

Belongs to the CSN4 family.Curated
Contains 1 PCI domain.Curated

Phylogenomic databases

eggNOGiKOG1497. Eukaryota.
ENOG410XPDE. LUCA.
HOGENOMiHOG000158382.
HOVERGENiHBG051136.
InParanoidiO88544.
KOiK12178.
OMAiKRFLDHM.
OrthoDBiEOG7P02HX.
PhylomeDBiO88544.
TreeFamiTF101147.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O88544-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAVRQDLA QLMNSSGSHK DLAGKYRQIL EKAIQLSGTE QLEALKAFVE
60 70 80 90 100
AMVNENVSLV ISRQLLTDFC THLPNLPDST AKEVYHFTLE KIQPRVISFE
110 120 130 140 150
EQVASIRQHL ASIYEKEEDW RNAAQVLVGI PLETGQKQYN VDYKLETYLK
160 170 180 190 200
IARLYLEDDD PVQAEAYINR ASLLQNESTN EQLQIHYKVC YARVLDYRRK
210 220 230 240 250
FIEAAQRYNE LSYKTIVHES ERLEALKHAL HCTILASAGQ QRSRMLATLF
260 270 280 290 300
KDERCQQLAA YGILEKMYLD RIIRGNQLQE FAAMLMPHQK ATTADGSSIL
310 320 330 340 350
DRAVIEHNLL SASKLYNNIT FEELGALLEI PAAKAEKIAS QMITEGRMNG
360 370 380 390 400
FIDQIDGIVH FETREALPTW DKQIQSLCFQ VNNLLEKISQ TAPEWTAQAM

EAQMAQ
Length:406
Mass (Da):46,285
Last modified:November 1, 1998 - v1
Checksum:i9584559823F99EB4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071314 mRNA. Translation: AAC33901.1.
AK009955 mRNA. Translation: BAB26607.1.
CCDSiCCDS19463.1.
RefSeqiNP_036131.1. NM_012001.2.
UniGeneiMm.957.

Genome annotation databases

EnsembliENSMUST00000045993; ENSMUSP00000048416; ENSMUSG00000035297.
GeneIDi26891.
KEGGimmu:26891.
UCSCiuc008yhs.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071314 mRNA. Translation: AAC33901.1.
AK009955 mRNA. Translation: BAB26607.1.
CCDSiCCDS19463.1.
RefSeqiNP_036131.1. NM_012001.2.
UniGeneiMm.957.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UFMNMR-A296-366[»]
ProteinModelPortaliO88544.
SMRiO88544. Positions 1-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205043. 6 interactions.
IntActiO88544. 3 interactions.
MINTiMINT-1869855.
STRINGi10090.ENSMUSP00000048416.

PTM databases

iPTMnetiO88544.
PhosphoSiteiO88544.
SwissPalmiO88544.

2D gel databases

REPRODUCTION-2DPAGEO88544.

Proteomic databases

EPDiO88544.
PaxDbiO88544.
PeptideAtlasiO88544.
PRIDEiO88544.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045993; ENSMUSP00000048416; ENSMUSG00000035297.
GeneIDi26891.
KEGGimmu:26891.
UCSCiuc008yhs.2. mouse.

Organism-specific databases

CTDi51138.
MGIiMGI:1349414. Cops4.

Phylogenomic databases

eggNOGiKOG1497. Eukaryota.
ENOG410XPDE. LUCA.
HOGENOMiHOG000158382.
HOVERGENiHBG051136.
InParanoidiO88544.
KOiK12178.
OMAiKRFLDHM.
OrthoDBiEOG7P02HX.
PhylomeDBiO88544.
TreeFamiTF101147.

Enzyme and pathway databases

ReactomeiR-MMU-5696394. DNA Damage Recognition in GG-NER.
R-MMU-6781823. Formation of TC-NER Pre-Incision Complex.

Miscellaneous databases

EvolutionaryTraceiO88544.
PROiO88544.
SOURCEiSearch...

Gene expression databases

BgeeiO88544.
ExpressionAtlasiO88544. baseline and differential.
GenevisibleiO88544. MM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex."
    Wei N., Tsuge T., Serino G., Dohmae N., Takio K., Matsui M., Deng X.-W.
    Curr. Biol. 8:919-922(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE CSN COMPLEX.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Tongue.
  3. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 96-107; 154-170 AND 228-242, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "Solution structure of the PCI domain."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 296-366.

Entry informationi

Entry nameiCSN4_MOUSE
AccessioniPrimary (citable) accession number: O88544
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.