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P99999

- CYC_HUMAN

UniProt

P99999 - CYC_HUMAN

Protein

Cytochrome c

Gene

CYCS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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
    4. protein binding Source: UniProtKB

    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. respiratory electron transport chain Source: Reactome
    9. small molecule metabolic process Source: Reactome

    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_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: UniProt
    5. nucleus Source: LIFEdb
    6. protein phosphatase type 2A complex Source: UniProtKB
    7. respiratory chain Source: UniProtKB-KW

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Thrombocytopenia 4 (THC4) [MIM:612004]: Thrombocytopenia 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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

    ArrayExpressiP99999.
    BgeeiP99999.
    CleanExiHS_CYCS.
    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 – 1411
    Turni15 – 184
    Beta strandi23 – 253
    Beta strandi28 – 303
    Turni36 – 383
    Helixi51 – 555
    Helixi62 – 709
    Helixi72 – 754
    Helixi89 – 10214

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000009762.
    HOVERGENiHBG003023.
    InParanoidiP99999.
    KOiK08738.
    OMAiCHNLKEG.
    OrthoDBiEOG761BWX.
    PhylomeDBiP99999.
    TreeFamiTF300226.

    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.

    P99999-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT    50
    AANKNKGIIW GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK 100
    KATNE 105
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS5393.1.
    PIRi A31764. CCHU.
    RefSeqi NP_061820.1. NM_018947.5.
    UniGenei Hs.437060.
    Hs.617193.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1J3S NMR - A 2-105 [» ]
    3NWV X-ray 1.90 A/B/C/D 2-105 [» ]
    3ZCF X-ray 1.65 A/B/C/D 2-105 [» ]
    3ZOO X-ray 1.35 A/B/C/D 2-105 [» ]
    ProteinModelPortali P99999.
    SMRi P99999. Positions 2-105.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119922. 21 interactions.
    DIPi DIP-29683N.
    IntActi P99999. 10 interactions.
    MINTi MINT-3023956.
    STRINGi 9606.ENSP00000307786.

    Chemistry

    DrugBanki DB01065. Melatonin.
    DB01017. Minocycline.

    PTM databases

    PhosphoSitei P99999.

    Polymorphism databases

    DMDMi 42560196.

    Proteomic databases

    MaxQBi P99999.
    PaxDbi P99999.
    PeptideAtlasi P99999.
    PRIDEi P99999.

    Protocols and materials databases

    DNASUi 54205.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000305786 ; ENSP00000307786 ; ENSG00000172115 .
    ENST00000409409 ; ENSP00000386270 ; ENSG00000172115 .
    ENST00000409764 ; ENSP00000387279 ; ENSG00000172115 .
    GeneIDi 54205.
    KEGGi hsa:54205.
    UCSCi uc003sxl.3. human.

    Organism-specific databases

    CTDi 54205.
    GeneCardsi GC07M025158.
    HGNCi HGNC:19986. CYCS.
    HPAi CAB004222.
    CAB005126.
    CAB018597.
    MIMi 123970. gene.
    612004. phenotype.
    neXtProti NX_P99999.
    Orphaneti 168629. Autosomal thrombocytopenia with normal platelets.
    PharmGKBi PA134981636.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3474.
    HOGENOMi HOG000009762.
    HOVERGENi HBG003023.
    InParanoidi P99999.
    KOi K08738.
    OMAi CHNLKEG.
    OrthoDBi EOG761BWX.
    PhylomeDBi P99999.
    TreeFami TF300226.

    Enzyme and pathway databases

    Reactomei REACT_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_607. Activation of caspases through apoptosome-mediated cleavage.
    REACT_89. Formation of apoptosome.

    Miscellaneous databases

    ChiTaRSi CYCS. human.
    EvolutionaryTracei P99999.
    GeneWikii Cytochrome_c.
    GenomeRNAii 54205.
    NextBioi 56526.
    PROi P99999.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P99999.
    Bgeei P99999.
    CleanExi HS_CYCS.
    Genevestigatori P99999.

    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

    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: October 1, 2014
    This is version 128 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