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Protein

Copper chaperone for superoxide dismutase

Gene

Ccs

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

Functioni

Delivers copper to copper zinc superoxide dismutase (SOD1).

Cofactori

Protein has several cofactor binding sites:
  • Cu2+By similarityNote: Binds 2 copper ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi22Copper 1PROSITE-ProRule annotation1
Metal bindingi25Copper 1PROSITE-ProRule annotation1
Metal bindingi147ZincPROSITE-ProRule annotation1
Metal bindingi155ZincPROSITE-ProRule annotation1
Metal bindingi164ZincPROSITE-ProRule annotation1
Metal bindingi167ZincPROSITE-ProRule annotation1
Metal bindingi244Copper 2PROSITE-ProRule annotation1
Metal bindingi246Copper 2PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

  • metal ion transport Source: InterPro
  • positive regulation of oxidoreductase activity Source: MGI
  • removal of superoxide radicals Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-3299685. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Copper chaperone for superoxide dismutase
Alternative name(s):
Superoxide dismutase copper chaperone
Gene namesi
Name:Ccs
Synonyms:Ccsd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1333783. Ccs.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002135441 – 274Copper chaperone for superoxide dismutaseAdd BLAST274

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki76Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Disulfide bondi141 ↔ 227By similarity
Cross-linki189Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki216Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki241Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei267PhosphoserineCombined sources1

Post-translational modificationi

Ubiquitinion by XIAP/BIRC4 leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. XIAP/BIRC4 preferentially ubiquitinates at Lys-241 (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9WU84.
MaxQBiQ9WU84.
PaxDbiQ9WU84.
PRIDEiQ9WU84.

PTM databases

iPTMnetiQ9WU84.
PhosphoSitePlusiQ9WU84.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSMUSG00000034108.
CleanExiMM_CCS.
ExpressionAtlasiQ9WU84. baseline and differential.
GenevisibleiQ9WU84. MM.

Interactioni

Subunit structurei

Homodimer, and heterodimer with SOD1. Interacts with COMMD1 (By similarity). Interacts with XIAP/BIRC4 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198563. 1 interactor.
DIPiDIP-48692N.
IntActiQ9WU84. 1 interactor.
STRINGi10090.ENSMUSP00000035486.

Structurei

3D structure databases

ProteinModelPortaliQ9WU84.
SMRiQ9WU84.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 75HMAPROSITE-ProRule annotationAdd BLAST64

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni88 – 234Superoxide dismutase-likeAdd BLAST147

Sequence similaritiesi

In the C-terminal section; belongs to the Cu-Zn superoxide dismutase family.Curated
Contains 1 HMA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IPMW. Eukaryota.
COG2032. LUCA.
GeneTreeiENSGT00530000063226.
HOGENOMiHOG000263450.
HOVERGENiHBG018933.
InParanoidiQ9WU84.
KOiK04569.
OMAiDNDKMVC.
OrthoDBiEOG091G0FQ1.
PhylomeDBiQ9WU84.
TreeFamiTF105184.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
cd00371. HMA. 1 hit.
Gene3Di2.60.40.200. 1 hit.
InterProiIPR024142. Ccs1.
IPR006121. HMA_dom.
IPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PTHR10003:SF27. PTHR10003:SF27. 1 hit.
PfamiPF00403. HMA. 1 hit.
PF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
SSF55008. SSF55008. 1 hit.
PROSITEiPS50846. HMA_2. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9WU84-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASKSGDGGT VCALEFAVQM SCQSCVDAVH KTLKGVAGVQ NVDVQLENQM
60 70 80 90 100
VLVQTTLPSQ EVQALLESTG RQAVLKGMGS SQLQNLGAAV AILEGCGSIQ
110 120 130 140 150
GVVRFLQLSS ELCLIEGTID GLEPGLHGLH VHQYGDLTRD CNSCGDHFNP
160 170 180 190 200
DGASHGGPQD TDRHRGDLGN VRAEAGGRAT FRIEDKQLKV WDVIGRSLVI
210 220 230 240 250
DEGEDDLGRG GHPLSKITGN SGKRLACGII ARSAGLFQNP KQICSCDGLT
260 270
IWEERGRPIA GQGRKDSAQP PAHL
Length:274
Mass (Da):28,912
Last modified:November 1, 1999 - v1
Checksum:i19DCE48376C9D5A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121906 mRNA. Translation: AAD23832.1.
AF173379 mRNA. Translation: AAF70242.1.
AK010264 mRNA. Translation: BAB26806.1.
BC026938 mRNA. Translation: AAH26938.1.
CCDSiCCDS29438.1.
RefSeqiNP_058588.1. NM_016892.3.
UniGeneiMm.434411.

Genome annotation databases

EnsembliENSMUST00000037246; ENSMUSP00000035486; ENSMUSG00000034108.
GeneIDi12460.
KEGGimmu:12460.
UCSCiuc008gba.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121906 mRNA. Translation: AAD23832.1.
AF173379 mRNA. Translation: AAF70242.1.
AK010264 mRNA. Translation: BAB26806.1.
BC026938 mRNA. Translation: AAH26938.1.
CCDSiCCDS29438.1.
RefSeqiNP_058588.1. NM_016892.3.
UniGeneiMm.434411.

3D structure databases

ProteinModelPortaliQ9WU84.
SMRiQ9WU84.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198563. 1 interactor.
DIPiDIP-48692N.
IntActiQ9WU84. 1 interactor.
STRINGi10090.ENSMUSP00000035486.

PTM databases

iPTMnetiQ9WU84.
PhosphoSitePlusiQ9WU84.

Proteomic databases

EPDiQ9WU84.
MaxQBiQ9WU84.
PaxDbiQ9WU84.
PRIDEiQ9WU84.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000037246; ENSMUSP00000035486; ENSMUSG00000034108.
GeneIDi12460.
KEGGimmu:12460.
UCSCiuc008gba.1. mouse.

Organism-specific databases

CTDi9973.
MGIiMGI:1333783. Ccs.

Phylogenomic databases

eggNOGiENOG410IPMW. Eukaryota.
COG2032. LUCA.
GeneTreeiENSGT00530000063226.
HOGENOMiHOG000263450.
HOVERGENiHBG018933.
InParanoidiQ9WU84.
KOiK04569.
OMAiDNDKMVC.
OrthoDBiEOG091G0FQ1.
PhylomeDBiQ9WU84.
TreeFamiTF105184.

Enzyme and pathway databases

ReactomeiR-MMU-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

PROiQ9WU84.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000034108.
CleanExiMM_CCS.
ExpressionAtlasiQ9WU84. baseline and differential.
GenevisibleiQ9WU84. MM.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
cd00371. HMA. 1 hit.
Gene3Di2.60.40.200. 1 hit.
InterProiIPR024142. Ccs1.
IPR006121. HMA_dom.
IPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PTHR10003:SF27. PTHR10003:SF27. 1 hit.
PfamiPF00403. HMA. 1 hit.
PF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
SSF55008. SSF55008. 1 hit.
PROSITEiPS50846. HMA_2. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCCS_MOUSE
AccessioniPrimary (citable) accession number: Q9WU84
Secondary accession number(s): Q9CRJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 139 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.