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P62897 (CYC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome c, somatic
Gene names
Name:Cycs
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length105 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Ref.7

Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases. Ref.7

Subcellular location

Mitochondrion intermembrane space. Note: Loosely associated with the inner membrane.

Tissue specificity

Found in embryos and in adult liver and heart.

Post-translational modification

Binds 1 heme group per subunit.

Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration By similarity.

Sequence similarities

Belongs to the cytochrome c family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 105104Cytochrome c, somatic
PRO_0000108225

Sites

Metal binding191Iron (heme axial ligand)
Metal binding811Iron (heme axial ligand)
Binding site151Heme (covalent)
Binding site181Heme (covalent)

Amino acid modifications

Modified residue21N-acetylglycine Ref.4
Modified residue491Phosphotyrosine By similarity
Modified residue981Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
P62897 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B5BCA779BCE40492

FASTA10511,605
        10         20         30         40         50         60 
MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAAGFSYT DANKNKGITW 

        70         80         90        100 
GEDTLMEYLE NPKKYIPGTK MIFAGIKKKG ERADLIAYLK KATNE 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a mouse somatic cytochrome c gene and three cytochrome c pseudogenes."
Limbach K.J., Wu R.
Nucleic Acids Res. 13:617-630(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
[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. expand/collapse author list , 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: NOD.
Tissue: Thymus.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
[4]"Primary structure of mouse, rat, and guinea pig cytochrome c."
Carlson S.S., Mross G.A., Wilson A.C., Mead R.T., Wolin L.D., Bowers S.F., Foley N.T., Muijsers A.O., Margoliash E.
Biochemistry 16:1437-1442(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2.
Strain: BALB/c.
[5]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 29-54; 57-74; 81-88 AND 93-100, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[6]"Change of cytochrome c structure during development of the mouse."
Hennig B.
Eur. J. Biochem. 55:167-183(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: AMINO-ACID COMPOSITION OF TRYPTIC PEPTIDES.
Strain: BALB/c.
[7]"Nuclear Apaf-1 and cytochrome c redistribution following stress-induced apoptosis."
Ruiz-Vela A., Gonzalez de Buitrago G., Martinez-A C.
FEBS Lett. 517:133-138(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN APOPTOSIS.

Web resources

Protein Spotlight

Life shuttle - Issue 76 of November 2006

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01756 Genomic DNA. Translation: CAA25899.1.
AK088098 mRNA. Translation: BAC40143.1.
BC034363 mRNA. Translation: AAH34363.1.
PIRCCMS. A23057.
RefSeqNP_031834.1. NM_007808.4.
UniGeneMm.35389.

3D structure databases

ProteinModelPortalP62897.
SMRP62897. Positions 2-105.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198992. 3 interactions.
583899. 1 interaction.
IntActP62897. 6 interactions.
MINTMINT-1860070.
STRING10090.ENSMUSP00000076944.

PTM databases

PhosphoSiteP62897.

Proteomic databases

PaxDbP62897.
PRIDEP62897.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000073080; ENSMUSP00000072829; ENSMUSG00000058927.
ENSMUST00000161401; ENSMUSP00000124523; ENSMUSG00000063694.
GeneID13063.
KEGGmmu:13063.
UCSCuc009bxc.1. mouse.

Organism-specific databases

CTD54205.
MGIMGI:88578. Cycs.

Phylogenomic databases

eggNOGCOG3474.
HOGENOMHOG000009762.
HOVERGENHBG003023.
InParanoidP62897.
KOK08738.
OMARDYLHNP.
OrthoDBEOG761BWX.
PhylomeDBP62897.
TreeFamTF300226.

Gene expression databases

ArrayExpressP62897.
BgeeP62897.
CleanExMM_CYCS.
GenevestigatorP62897.

Family and domain databases

Gene3D1.10.760.10. 1 hit.
InterProIPR009056. Cyt_c-like_dom.
IPR002327. Cyt_c_1A/1B.
IPR003088. Cyt_c_dom.
[Graphical view]
PANTHERPTHR11961. PTHR11961. 1 hit.
PfamPF00034. Cytochrom_C. 1 hit.
[Graphical view]
PRINTSPR00604. CYTCHRMECIAB.
SUPFAMSSF46626. SSF46626. 1 hit.
PROSITEPS51007. CYTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio282990.
PROP62897.
SOURCESearch...

Entry information

Entry nameCYC_MOUSE
AccessionPrimary (citable) accession number: P62897
Secondary accession number(s): P00009, Q8C2S2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

MGD cross-references

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