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Protein

Cytochrome c

Gene

CYCS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei15 – 151Heme (covalent)
Binding sitei18 – 181Heme (covalent)
Metal bindingi19 – 191Iron (heme axial ligand)
Metal bindingi81 – 811Iron (heme axial ligand)

GO - Molecular functioni

  1. electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity Source: UniProtKB
  2. heme binding Source: UniProtKB
  3. iron ion binding Source: InterPro

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c Source: UniProtKB
  2. apoptotic DNA fragmentation Source: UniProtKB
  3. apoptotic process Source: Reactome
  4. cellular metabolic process Source: Reactome
  5. cellular respiration Source: UniProtKB
  6. dephosphorylation Source: GOC
  7. intrinsic apoptotic signaling pathway Source: Reactome
  8. mitochondrial electron transport, cytochrome c to oxygen Source: GO_Central
  9. mitochondrial electron transport, ubiquinol to cytochrome c Source: GO_Central
  10. respiratory electron transport chain Source: Reactome
  11. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Electron transport, Respiratory chain, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_1322. Release of apoptotic factors from the mitochondria.
REACT_172715. Detoxification of Reactive Oxygen Species.
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_22393. Respiratory electron transport.
REACT_267716. Orphan transporters.
REACT_607. Activation of caspases through apoptosome-mediated cleavage.
REACT_89. Formation of apoptosome.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c
Gene namesi
Name:CYCS
Synonyms:CYC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:19986. CYCS.

Subcellular locationi

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

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. mitochondrial inner membrane Source: Reactome
  3. mitochondrial intermembrane space Source: UniProtKB
  4. mitochondrion Source: UniProtKB
  5. nucleus Source: UniProtKB
  6. protein phosphatase type 2A complex Source: UniProtKB
  7. respiratory chain Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Thrombocytopenia 41 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionThrombocytopenia is defined by a decrease in the number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting.

See also OMIM:612004
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti42 – 421G → S in THC4; increases the pro-apoptotic function by triggering caspase activation more efficiently than wild-type; does not affect the redox function. 1 Publication
VAR_044450

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi612004. phenotype.
Orphaneti168629. Autosomal thrombocytopenia with normal platelets.
PharmGKBiPA134981636.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 105104Cytochrome cPRO_0000108218Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycine1 Publication
Modified residuei49 – 491PhosphotyrosineBy similarity
Modified residuei98 – 981PhosphotyrosineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP99999.
PaxDbiP99999.
PeptideAtlasiP99999.
PRIDEiP99999.

PTM databases

PhosphoSiteiP99999.

Expressioni

Gene expression databases

BgeeiP99999.
CleanExiHS_CYCS.
ExpressionAtlasiP99999. baseline and differential.
GenevestigatoriP99999.

Organism-specific databases

HPAiCAB004222.
CAB005126.
CAB018597.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
APAF1O147276EBI-446479,EBI-446492
BCL2L1Q078172EBI-446479,EBI-78035

Protein-protein interaction databases

BioGridi119922. 21 interactions.
DIPiDIP-29683N.
IntActiP99999. 10 interactions.
MINTiMINT-3023956.
STRINGi9606.ENSP00000307786.

Structurei

Secondary structure

1
105
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1411Combined sources
Turni15 – 184Combined sources
Beta strandi23 – 253Combined sources
Beta strandi28 – 303Combined sources
Turni36 – 383Combined sources
Helixi51 – 555Combined sources
Helixi62 – 709Combined sources
Helixi72 – 754Combined sources
Helixi89 – 10214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J3SNMR-A2-105[»]
3NWVX-ray1.90A/B/C/D2-105[»]
3ZCFX-ray1.65A/B/C/D2-105[»]
3ZOOX-ray1.35A/B/C/D2-105[»]
ProteinModelPortaliP99999.
SMRiP99999. Positions 2-105.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP99999.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome c family.Curated

Phylogenomic databases

eggNOGiCOG3474.
GeneTreeiENSGT00390000009405.
HOGENOMiHOG000009762.
HOVERGENiHBG003023.
InParanoidiP99999.
KOiK08738.
OMAiLMIYLEN.
OrthoDBiEOG761BWX.
PhylomeDBiP99999.
TreeFamiTF300226.

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR002327. Cyt_c_1A/1B.
[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.

P99999-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT
60 70 80 90 100
AANKNKGIIW GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK

KATNE
Length:105
Mass (Da):11,749
Last modified:January 23, 2007 - v2
Checksum:i8EE9689E0102506B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181C → Y in AAH15130. (PubMed:15489334)Curated
Sequence conflicti41 – 411T → I in AAH68464. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti42 – 421G → S in THC4; increases the pro-apoptotic function by triggering caspase activation more efficiently than wild-type; does not affect the redox function. 1 Publication
VAR_044450
Natural varianti56 – 561K → R.
Corresponds to variant rs11548795 [ dbSNP | Ensembl ].
VAR_048850
Natural varianti66 – 661M → L in 10% of the molecules.
VAR_002204

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22877 Genomic DNA. Translation: AAA35732.1.
BT006946 mRNA. Translation: AAP35592.1.
AK311836 mRNA. Translation: BAG34778.1.
AL713681 mRNA. Translation: CAD28485.1.
AC007487 Genomic DNA. Translation: AAQ96844.1.
CH236948 Genomic DNA. Translation: EAL24239.1.
CH471073 Genomic DNA. Translation: EAW93822.1.
BC005299 mRNA. Translation: AAH05299.1.
BC008475 mRNA. Translation: AAH08475.1.
BC008477 mRNA. Translation: AAH08477.1.
BC009578 mRNA. Translation: AAH09578.1.
BC009579 mRNA. Translation: AAH09579.1.
BC009582 mRNA. Translation: AAH09582.1.
BC009587 mRNA. Translation: AAH09587.1.
BC009602 mRNA. Translation: AAH09602.1.
BC009607 mRNA. Translation: AAH09607.1.
BC014359 mRNA. Translation: AAH14359.1.
BC014361 mRNA. Translation: AAH14361.1.
BC015130 mRNA. Translation: AAH15130.1.
BC016006 mRNA. Translation: AAH16006.1.
BC021994 mRNA. Translation: AAH21994.1.
BC022330 mRNA. Translation: AAH22330.1.
BC067222 mRNA. Translation: AAH67222.1.
BC068464 mRNA. Translation: AAH68464.1.
BC070156 mRNA. Translation: AAH70156.1.
BC070346 mRNA. Translation: AAH70346.1.
BC071761 mRNA. Translation: AAH71761.1.
CCDSiCCDS5393.1.
PIRiA31764. CCHU.
RefSeqiNP_061820.1. NM_018947.5.
UniGeneiHs.437060.
Hs.617193.

Genome annotation databases

EnsembliENST00000305786; ENSP00000307786; ENSG00000172115.
ENST00000409409; ENSP00000386270; ENSG00000172115.
ENST00000409764; ENSP00000387279; ENSG00000172115.
GeneIDi54205.
KEGGihsa:54205.
UCSCiuc003sxl.3. human.

Polymorphism databases

DMDMi42560196.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Protein Spotlight

Life shuttle - Issue 76 of November 2006

Protein Spotlight

An unexpected place - Issue 88 of November 2007

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22877 Genomic DNA. Translation: AAA35732.1.
BT006946 mRNA. Translation: AAP35592.1.
AK311836 mRNA. Translation: BAG34778.1.
AL713681 mRNA. Translation: CAD28485.1.
AC007487 Genomic DNA. Translation: AAQ96844.1.
CH236948 Genomic DNA. Translation: EAL24239.1.
CH471073 Genomic DNA. Translation: EAW93822.1.
BC005299 mRNA. Translation: AAH05299.1.
BC008475 mRNA. Translation: AAH08475.1.
BC008477 mRNA. Translation: AAH08477.1.
BC009578 mRNA. Translation: AAH09578.1.
BC009579 mRNA. Translation: AAH09579.1.
BC009582 mRNA. Translation: AAH09582.1.
BC009587 mRNA. Translation: AAH09587.1.
BC009602 mRNA. Translation: AAH09602.1.
BC009607 mRNA. Translation: AAH09607.1.
BC014359 mRNA. Translation: AAH14359.1.
BC014361 mRNA. Translation: AAH14361.1.
BC015130 mRNA. Translation: AAH15130.1.
BC016006 mRNA. Translation: AAH16006.1.
BC021994 mRNA. Translation: AAH21994.1.
BC022330 mRNA. Translation: AAH22330.1.
BC067222 mRNA. Translation: AAH67222.1.
BC068464 mRNA. Translation: AAH68464.1.
BC070156 mRNA. Translation: AAH70156.1.
BC070346 mRNA. Translation: AAH70346.1.
BC071761 mRNA. Translation: AAH71761.1.
CCDSiCCDS5393.1.
PIRiA31764. CCHU.
RefSeqiNP_061820.1. NM_018947.5.
UniGeneiHs.437060.
Hs.617193.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J3SNMR-A2-105[»]
3NWVX-ray1.90A/B/C/D2-105[»]
3ZCFX-ray1.65A/B/C/D2-105[»]
3ZOOX-ray1.35A/B/C/D2-105[»]
ProteinModelPortaliP99999.
SMRiP99999. Positions 2-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119922. 21 interactions.
DIPiDIP-29683N.
IntActiP99999. 10 interactions.
MINTiMINT-3023956.
STRINGi9606.ENSP00000307786.

Chemistry

DrugBankiDB01017. Minocycline.

PTM databases

PhosphoSiteiP99999.

Polymorphism databases

DMDMi42560196.

Proteomic databases

MaxQBiP99999.
PaxDbiP99999.
PeptideAtlasiP99999.
PRIDEiP99999.

Protocols and materials databases

DNASUi54205.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000305786; ENSP00000307786; ENSG00000172115.
ENST00000409409; ENSP00000386270; ENSG00000172115.
ENST00000409764; ENSP00000387279; ENSG00000172115.
GeneIDi54205.
KEGGihsa:54205.
UCSCiuc003sxl.3. human.

Organism-specific databases

CTDi54205.
GeneCardsiGC07M025158.
HGNCiHGNC:19986. CYCS.
HPAiCAB004222.
CAB005126.
CAB018597.
MIMi123970. gene.
612004. phenotype.
neXtProtiNX_P99999.
Orphaneti168629. Autosomal thrombocytopenia with normal platelets.
PharmGKBiPA134981636.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3474.
GeneTreeiENSGT00390000009405.
HOGENOMiHOG000009762.
HOVERGENiHBG003023.
InParanoidiP99999.
KOiK08738.
OMAiLMIYLEN.
OrthoDBiEOG761BWX.
PhylomeDBiP99999.
TreeFamiTF300226.

Enzyme and pathway databases

ReactomeiREACT_1322. Release of apoptotic factors from the mitochondria.
REACT_172715. Detoxification of Reactive Oxygen Species.
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_22393. Respiratory electron transport.
REACT_267716. Orphan transporters.
REACT_607. Activation of caspases through apoptosome-mediated cleavage.
REACT_89. Formation of apoptosome.

Miscellaneous databases

ChiTaRSiCYCS. human.
EvolutionaryTraceiP99999.
GeneWikiiCytochrome_c.
GenomeRNAii54205.
NextBioi56526.
PROiP99999.
SOURCEiSearch...

Gene expression databases

BgeeiP99999.
CleanExiHS_CYCS.
ExpressionAtlasiP99999. baseline and differential.
GenevestigatoriP99999.

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR002327. Cyt_c_1A/1B.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The human somatic cytochrome c gene: two classes of processed pseudogenes demarcate a period of rapid molecular evolution."
    Evans M.J., Scarpulla R.C.
    Proc. Natl. Acad. Sci. U.S.A. 85:9625-9629(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Amygdala.
  5. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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].
    Tissue: Bone marrow, Brain, Kidney, Lung, Skeletal muscle, Skin, Testis and Urinary bladder.
  9. "The amino acid sequence of human heart cytochrome c."
    Matsubara H., Smith E.L.
    J. Biol. Chem. 237:3575-3576(1962) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2.
    Tissue: Heart.
  10. "Human heart cytochrome c. Chymotryptic peptides, tryptic peptides, and the complete amino acid sequence."
    Matsubara H., Smith E.L.
    J. Biol. Chem. 238:2732-2753(1963) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-105.
    Tissue: Heart.
  11. "Cytochrome c in the apoptotic and antioxidant cascades."
    Skulachev V.P.
    FEBS Lett. 423:275-280(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ROLE IN APOPTOSIS.
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Solution structure of reduced recombinant human cytochrome c."
    Jeng W.-Y., Shiu J.-H., Tsai Y.-H., Chuang W.-J.
    Submitted (FEB-2003) to the PDB data bank
    Cited for: STRUCTURE BY NMR.
  15. Cited for: VARIANT THC4 SER-42, IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF VARIANT THC4 SER-42, X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF VARIANT THC4 SER-42 AND WILD TYPE.

Entry informationi

Entry nameiCYC_HUMAN
AccessioniPrimary (citable) accession number: P99999
Secondary accession number(s): A4D166
, B2R4I1, P00001, Q6NUR2, Q6NX69, Q96BV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.