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P00044

- CYC1_YEAST

UniProt

P00044 - CYC1_YEAST

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Protein

Cytochrome c iso-1

Gene

CYC1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei20 – 201Heme (covalent)
Binding sitei23 – 231Heme (covalent)
Metal bindingi24 – 241Iron (heme axial ligand)
Metal bindingi86 – 861Iron (heme axial ligand)

GO - Molecular functioni

  1. electron carrier activity Source: SGD
  2. heme binding Source: InterPro
  3. iron ion binding Source: InterPro

GO - Biological processi

  1. mitochondrial electron transport, cytochrome c to oxygen Source: SGD
  2. mitochondrial electron transport, ubiquinol to cytochrome c Source: SGD
Complete GO annotation...

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31683-MONOMER.
ReactomeiREACT_188673. Release of apoptotic factors from the mitochondria.
REACT_191152. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c iso-1
Gene namesi
Name:CYC1
Ordered Locus Names:YJR048W
ORF Names:J1653
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome X

Organism-specific databases

SGDiS000003809. CYC1.

Subcellular locationi

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

GO - Cellular componenti

  1. mitochondrial intermembrane space Source: SGD
  2. respiratory chain Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi78 – 781K → R: Loss of methylation by CTM1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 109108Cytochrome c iso-1PRO_0000108337Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei78 – 781N6,N6,N6-trimethyllysine; by CTM11 Publication
Modified residuei79 – 791N6,N6,N6-trimethyllysine2 Publications

Post-translational modificationi

Binds 1 heme group per subunit.
Methylation may enhance its transport into mitochondria. Methylation occurs in fungi, plants, and some protozoa, but not in animals. The precise role of methylation at Lys-79 is unknown, but it seems to preclude pro-apoptotic activity, possibly by lowering affinity for APAF1.4 Publications

Keywords - PTMi

Methylation

Proteomic databases

MaxQBiP00044.
PaxDbiP00044.
PeptideAtlasiP00044.

Expressioni

Developmental stagei

Iso-1 is the predominant cytochrome c in aerobically grown cells.

Inductioni

By oxygen.

Gene expression databases

GenevestigatoriP00044.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CCP1P004313EBI-5393,EBI-4389

Protein-protein interaction databases

BioGridi33801. 75 interactions.
DIPiDIP-4265N.
IntActiP00044. 5 interactions.
MINTiMINT-8285287.
STRINGi4932.YJR048W.

Structurei

Secondary structure

1
109
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1911
Turni20 – 234
Beta strandi27 – 293
Beta strandi33 – 353
Turni39 – 435
Beta strandi45 – 473
Beta strandi50 – 523
Helixi56 – 616
Helixi67 – 759
Helixi77 – 804
Beta strandi81 – 833
Helixi94 – 10714

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CHHX-ray1.97A2-107[»]
1CHIX-ray2.00A2-107[»]
1CHJX-ray1.90A2-107[»]
1CIEX-ray1.80A2-107[»]
1CIFX-ray1.90A2-107[»]
1CIGX-ray1.80A2-107[»]
1CIHX-ray1.80A2-107[»]
1CRGX-ray2.00A2-107[»]
1CRHX-ray1.90A2-109[»]
1CRIX-ray2.00A2-107[»]
1CRJX-ray2.05A2-107[»]
1CSUX-ray1.81A2-107[»]
1CSVX-ray1.90A2-107[»]
1CSWX-ray1.90A2-107[»]
1CSXX-ray1.90A2-107[»]
1CTYX-ray2.20A2-107[»]
1CTZX-ray1.90A2-107[»]
1FHBNMR-A2-107[»]
1IRVX-ray1.90A2-107[»]
1IRWX-ray2.00A2-107[»]
1KYOX-ray2.97W2-109[»]
1LMSNMR-A2-107[»]
1NMINMR-A2-107[»]
1RAPX-ray2.25A2-109[»]
1RAQX-ray1.90A2-109[»]
1S6VX-ray1.88B/D2-107[»]
1U74X-ray2.40B/D2-107[»]
1YCCX-ray1.23A2-109[»]
1YFCNMR-A2-107[»]
1YICNMR-A2-107[»]
2B0ZX-ray2.70B2-109[»]
2B10X-ray2.80B/D2-109[»]
2B11X-ray2.30B/D2-109[»]
2B12X-ray3.02B2-109[»]
2BCNX-ray1.70B2-107[»]
2GB8NMR-B2-109[»]
2HV4NMR-A2-107[»]
2JQRNMR-A2-107[»]
2JTINMR-B2-109[»]
2LIRNMR-A2-107[»]
2LITNMR-A2-107[»]
2ORLNMR-A2-107[»]
2PCCX-ray2.30B/D2-109[»]
2YCCX-ray1.90A2-107[»]
3CX5X-ray1.90W2-109[»]
3TYIX-ray1.40A/B2-107[»]
4MU8X-ray1.45A/B2-107[»]
4N0KX-ray1.05A/B2-107[»]
ProteinModelPortaliP00044.
SMRiP00044. Positions 2-109.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00044.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome c family.Curated

Phylogenomic databases

eggNOGiCOG3474.
GeneTreeiENSGT00390000009405.
HOGENOMiHOG000009762.
InParanoidiP00044.
KOiK08738.
OMAiCHNLKEG.
OrthoDBiEOG71RXXT.

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR002327. Cyt_c_1A/1B.
IPR003088. Cyt_c_dom.
[Graphical view]
PANTHERiPTHR11961. PTHR11961. 1 hit.
PfamiPF00034. Cytochrom_C. 1 hit.
[Graphical view]
PRINTSiPR00604. CYTCHRMECIAB.
SUPFAMiSSF46626. SSF46626. 1 hit.
PROSITEiPS51007. CYTC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00044-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTEFKAGSAK KGATLFKTRC LQCHTVEKGG PHKVGPNLHG IFGRHSGQAE
60 70 80 90 100
GYSYTDANIK KNVLWDENNM SEYLTNPKKY IPGTKMAFGG LKKEKDRNDL

ITYLKKACE
Length:109
Mass (Da):12,182
Last modified:January 23, 2007 - v2
Checksum:i1F8B6CB3B60C0BE8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M37696 Genomic DNA. Translation: AAB59344.1.
V01298 Genomic DNA. Translation: CAA24605.1.
L26347 Genomic DNA. Translation: AAA62856.1.
L36344 Genomic DNA. Translation: AAA88751.1.
Z49548 Genomic DNA. Translation: CAA89576.1.
X03472 Genomic DNA. Translation: CAA27189.1.
BK006943 Genomic DNA. Translation: DAA08835.1.
PIRiA00037. CCBY.
RefSeqiNP_012582.1. NM_001181706.1.

Genome annotation databases

EnsemblFungiiYJR048W; YJR048W; YJR048W.
GeneIDi853507.
KEGGisce:YJR048W.

Cross-referencesi

Web resourcesi

Protein Spotlight

Life shuttle - Issue 76 of November 2006

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M37696 Genomic DNA. Translation: AAB59344.1 .
V01298 Genomic DNA. Translation: CAA24605.1 .
L26347 Genomic DNA. Translation: AAA62856.1 .
L36344 Genomic DNA. Translation: AAA88751.1 .
Z49548 Genomic DNA. Translation: CAA89576.1 .
X03472 Genomic DNA. Translation: CAA27189.1 .
BK006943 Genomic DNA. Translation: DAA08835.1 .
PIRi A00037. CCBY.
RefSeqi NP_012582.1. NM_001181706.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CHH X-ray 1.97 A 2-107 [» ]
1CHI X-ray 2.00 A 2-107 [» ]
1CHJ X-ray 1.90 A 2-107 [» ]
1CIE X-ray 1.80 A 2-107 [» ]
1CIF X-ray 1.90 A 2-107 [» ]
1CIG X-ray 1.80 A 2-107 [» ]
1CIH X-ray 1.80 A 2-107 [» ]
1CRG X-ray 2.00 A 2-107 [» ]
1CRH X-ray 1.90 A 2-109 [» ]
1CRI X-ray 2.00 A 2-107 [» ]
1CRJ X-ray 2.05 A 2-107 [» ]
1CSU X-ray 1.81 A 2-107 [» ]
1CSV X-ray 1.90 A 2-107 [» ]
1CSW X-ray 1.90 A 2-107 [» ]
1CSX X-ray 1.90 A 2-107 [» ]
1CTY X-ray 2.20 A 2-107 [» ]
1CTZ X-ray 1.90 A 2-107 [» ]
1FHB NMR - A 2-107 [» ]
1IRV X-ray 1.90 A 2-107 [» ]
1IRW X-ray 2.00 A 2-107 [» ]
1KYO X-ray 2.97 W 2-109 [» ]
1LMS NMR - A 2-107 [» ]
1NMI NMR - A 2-107 [» ]
1RAP X-ray 2.25 A 2-109 [» ]
1RAQ X-ray 1.90 A 2-109 [» ]
1S6V X-ray 1.88 B/D 2-107 [» ]
1U74 X-ray 2.40 B/D 2-107 [» ]
1YCC X-ray 1.23 A 2-109 [» ]
1YFC NMR - A 2-107 [» ]
1YIC NMR - A 2-107 [» ]
2B0Z X-ray 2.70 B 2-109 [» ]
2B10 X-ray 2.80 B/D 2-109 [» ]
2B11 X-ray 2.30 B/D 2-109 [» ]
2B12 X-ray 3.02 B 2-109 [» ]
2BCN X-ray 1.70 B 2-107 [» ]
2GB8 NMR - B 2-109 [» ]
2HV4 NMR - A 2-107 [» ]
2JQR NMR - A 2-107 [» ]
2JTI NMR - B 2-109 [» ]
2LIR NMR - A 2-107 [» ]
2LIT NMR - A 2-107 [» ]
2ORL NMR - A 2-107 [» ]
2PCC X-ray 2.30 B/D 2-109 [» ]
2YCC X-ray 1.90 A 2-107 [» ]
3CX5 X-ray 1.90 W 2-109 [» ]
3TYI X-ray 1.40 A/B 2-107 [» ]
4MU8 X-ray 1.45 A/B 2-107 [» ]
4N0K X-ray 1.05 A/B 2-107 [» ]
ProteinModelPortali P00044.
SMRi P00044. Positions 2-109.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33801. 75 interactions.
DIPi DIP-4265N.
IntActi P00044. 5 interactions.
MINTi MINT-8285287.
STRINGi 4932.YJR048W.

Proteomic databases

MaxQBi P00044.
PaxDbi P00044.
PeptideAtlasi P00044.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YJR048W ; YJR048W ; YJR048W .
GeneIDi 853507.
KEGGi sce:YJR048W.

Organism-specific databases

SGDi S000003809. CYC1.

Phylogenomic databases

eggNOGi COG3474.
GeneTreei ENSGT00390000009405.
HOGENOMi HOG000009762.
InParanoidi P00044.
KOi K08738.
OMAi CHNLKEG.
OrthoDBi EOG71RXXT.

Enzyme and pathway databases

BioCyci YEAST:G3O-31683-MONOMER.
Reactomei REACT_188673. Release of apoptotic factors from the mitochondria.
REACT_191152. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

EvolutionaryTracei P00044.
NextBioi 974162.

Gene expression databases

Genevestigatori P00044.

Family and domain databases

Gene3Di 1.10.760.10. 1 hit.
InterProi IPR009056. Cyt_c-like_dom.
IPR002327. Cyt_c_1A/1B.
IPR003088. Cyt_c_dom.
[Graphical view ]
PANTHERi PTHR11961. PTHR11961. 1 hit.
Pfami PF00034. Cytochrom_C. 1 hit.
[Graphical view ]
PRINTSi PR00604. CYTCHRMECIAB.
SUPFAMi SSF46626. SSF46626. 1 hit.
PROSITEi PS51007. CYTC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the gene for iso-1-cytochrome c in Saccharomyces cerevisiae."
    Smith M., Leung D.W., Gillam S., Astell C.R., Montgomery D.L., Hall B.D.
    Cell 16:753-761(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequence of the yeast iso-1-cytochrome c mRNA."
    Boss J.M., Gillam S., Ziotmer R.S., Smith M.
    J. Biol. Chem. 256:12958-12961(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Nucleotide sequence of the COR region: a cluster of six genes in the yeast Saccharomyces cerevisiae."
    Melnick L., Sherman F.
    Gene 87:157-166(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Revised nucleotide sequence of the COR region of yeast Saccharomyces cerevisiae chromosome X."
    Huang M.-E., Manus V., Chuat J.-C., Galibert F.
    Yeast 10:811-818(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. "The complete amino acid sequence in baker's yeast cytochrome c."
    Narita K., Titani K.
    J. Biochem. 65:259-267(1969) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-109.
    Strain: Oviformis.
  8. "Transcription initiation of the Saccharomyces cerevisiae iso-1-cytochrome c gene. Multiple, independent T-A-T-A sequences."
    McNeil J.B., Smith M.
    J. Mol. Biol. 187:363-378(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
  9. "Studies on cytochrome c. 8. Synthesis of the protected hexadecapeptide (sequence 93-108) of Baker's yeast iso-1-cytochrome c."
    Moroder L., Marchiori F., Borin G., Scoffone E.
    Biopolymers 12:729-750(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: SYNTHESIS.
  10. "Enzymatic methylation of in vitro synthesized apocytochrome c enhances its transport into mitochondria."
    Park K.S., Frost B., Tuck M., Ho L.L., Kim S., Paik W.K.
    J. Biol. Chem. 262:14702-14708(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION.
  11. "Determinants of cytochrome c pro-apoptotic activity. The role of lysine 72 trimethylation."
    Kluck R.M., Ellerby L.M., Ellerby H.M., Naiem S., Yaffe M.P., Margoliash E., Bredesen D., Mauk A.G., Sherman F., Newmeyer D.D.
    J. Biol. Chem. 275:16127-16133(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-79.
  12. Cited for: METHYLATION AT LYS-78, MUTAGENESIS OF LYS-78.
  13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Yeast iso-1-cytochrome c. A 2.8-A resolution three-dimensional structure determination."
    Louie G.V., Hutcheon W.L., Brayer G.D.
    J. Mol. Biol. 199:295-314(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  16. "High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c."
    Louie G.V., Brayer G.D.
    J. Mol. Biol. 214:527-555(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.23 ANGSTROMS).
  17. "Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c."
    Lange C., Hunte C.
    Proc. Natl. Acad. Sci. U.S.A. 99:2800-2805(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS).
  18. "Three-dimensional solution structure of Saccharomyces cerevisiae reduced iso-1-cytochrome c."
    Baistrocchi P., Banci L., Bertini I., Turano P., Bren K.L., Gray H.B.
    Biochemistry 35:13788-13796(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  19. "Solution structure of oxidized Saccharomyces cerevisiae iso-1-cytochrome c."
    Banci L., Bertini I., Bren K.L., Gray H.B., Sompornpisut P., Turano P.
    Biochemistry 36:8992-9001(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  20. "Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer."
    Solmaz S.R., Hunte C.
    J. Biol. Chem. 283:17542-17549(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-109 IN THE BC1 COMPLEX, METHYLATION AT LYS-79.

Entry informationi

Entry nameiCYC1_YEAST
AccessioniPrimary (citable) accession number: P00044
Secondary accession number(s): D6VWL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 169 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7330 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

External Data

Dasty 3