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P36542

- ATPG_HUMAN

UniProt

P36542 - ATPG_HUMAN

Protein

ATP synthase subunit gamma, mitochondrial

Gene

ATP5C1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F1 domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha3beta3. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. proton-transporting ATPase activity, rotational mechanism Source: InterPro
    3. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro
    4. transmembrane transporter activity Source: UniProtKB

    GO - Biological processi

    1. ATP biosynthetic process Source: UniProtKB
    2. ATP catabolic process Source: GOC
    3. cellular metabolic process Source: Reactome
    4. mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
    5. oxidative phosphorylation Source: UniProtKB
    6. respiratory electron transport chain Source: Reactome
    7. small molecule metabolic process Source: Reactome

    Keywords - Biological processi

    ATP synthesis, Hydrogen ion transport, Ion transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_6759. Formation of ATP by chemiosmotic coupling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP synthase subunit gamma, mitochondrial
    Alternative name(s):
    F-ATPase gamma subunit
    Gene namesi
    Name:ATP5C1
    Synonyms:ATP5C, ATP5CL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:833. ATP5C1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. membrane Source: UniProtKB
    3. mitochondrial inner membrane Source: UniProtKB
    4. mitochondrial matrix Source: Reactome
    5. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
    6. mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) Source: UniProtKB
    7. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25125.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2525MitochondrionAdd
    BLAST
    Chaini26 – 298273ATP synthase subunit gamma, mitochondrialPRO_0000002685Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei39 – 391N6-acetyllysineBy similarity
    Modified residuei49 – 491N6-succinyllysineBy similarity
    Modified residuei55 – 551N6-acetyllysine1 Publication
    Modified residuei115 – 1151N6-acetyllysine; alternateBy similarity
    Modified residuei115 – 1151N6-succinyllysine; alternateBy similarity
    Modified residuei154 – 1541N6-acetyllysine; alternate1 Publication
    Modified residuei154 – 1541N6-succinyllysine; alternateBy similarity
    Modified residuei197 – 1971N6-acetyllysine1 Publication
    Modified residuei270 – 2701N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP36542.
    PaxDbiP36542.
    PRIDEiP36542.

    2D gel databases

    UCD-2DPAGEP36542.

    PTM databases

    PhosphoSiteiP36542.

    Expressioni

    Tissue specificityi

    Isoform Heart is expressed specifically in the heart and skeletal muscle, which require rapid energy supply. Isoform Liver is expressed in the brain, liver and kidney. Isoform Heart and Isoform Liver are expressed in the skin, intestine, stomach and aorta.

    Gene expression databases

    ArrayExpressiP36542.
    BgeeiP36542.
    CleanExiHS_ATP5C1.
    GenevestigatoriP36542.

    Organism-specific databases

    HPAiHPA060949.

    Interactioni

    Subunit structurei

    F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi106997. 46 interactions.
    IntActiP36542. 35 interactions.
    MINTiMINT-1378900.
    STRINGi9606.ENSP00000349142.

    Structurei

    3D structure databases

    ProteinModelPortaliP36542.
    SMRiP36542. Positions 26-297.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase gamma chain family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0224.
    HOGENOMiHOG000215911.
    HOVERGENiHBG000933.
    InParanoidiP36542.
    KOiK02136.
    OMAiMATLKDX.
    OrthoDBiEOG7QK0D3.
    PhylomeDBiP36542.
    TreeFamiTF105765.

    Family and domain databases

    InterProiIPR000131. ATPase_F1-cplx_gsu.
    IPR023632. ATPase_F1_gsu_CS.
    IPR023633. ATPase_F1_gsu_dom.
    [Graphical view]
    PANTHERiPTHR11693. PTHR11693. 1 hit.
    PfamiPF00231. ATP-synt. 1 hit.
    [Graphical view]
    PRINTSiPR00126. ATPASEGAMMA.
    SUPFAMiSSF52943. SSF52943. 1 hit.
    TIGRFAMsiTIGR01146. ATPsyn_F1gamma. 1 hit.
    PROSITEiPS00153. ATPASE_GAMMA. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Liver (identifier: P36542-1) [UniParc]FASTAAdd to Basket

    Also known as: L

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MFSRAGVAGL SAWTLQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM    50
    VAAAKYARAE RELKPARIYG LGSLALYEKA DIKGPEDKKK HLLIGVSSDR 100
    GLCGAIHSSI AKQMKSEVAT LTAAGKEVML VGIGDKIRGI LYRTHSDQFL 150
    VAFKEVGRKP PTFGDASVIA LELLNSGYEF DEGSIIFNKF RSVISYKTEE 200
    KPIFSLNTVA SADSMSIYDD IDADVLQNYQ EYNLANIIYY SLKESTTSEQ 250
    SARMTAMDNA SKNASEMIDK LTLTFNRTRQ AVITKELIEI ISGAAALD 298
    Length:298
    Mass (Da):32,996
    Last modified:June 1, 1994 - v1
    Checksum:i021A95168FD53E04
    GO
    Isoform Heart (identifier: P36542-2) [UniParc]FASTAAdd to Basket

    Also known as: H

    The sequence of this isoform differs from the canonical sequence as follows:
         298-298: Missing.

    Show »
    Length:297
    Mass (Da):32,881
    Checksum:iCA95168FD53E0447
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 451T → A in AAH16812. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei298 – 2981Missing in isoform Heart. 2 PublicationsVSP_000439

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16561 Genomic DNA. Translation: BAA03994.1.
    D16561 Genomic DNA. Translation: BAA03995.1.
    D16562 mRNA. Translation: BAA03996.1.
    D16563 mRNA. Translation: BAA03997.1.
    AK292896 mRNA. Translation: BAF85585.1.
    CR457403 mRNA. Translation: CAG33684.1.
    AL353754, AL158044 Genomic DNA. Translation: CAH73453.1.
    AL353754, AL158044 Genomic DNA. Translation: CAH73454.1.
    AL158044, AL353754 Genomic DNA. Translation: CAI12960.1.
    AL158044, AL353754 Genomic DNA. Translation: CAI12961.1.
    CH471072 Genomic DNA. Translation: EAW86372.1.
    CH471072 Genomic DNA. Translation: EAW86373.1.
    BC000470 mRNA. Translation: AAH00470.1.
    BC000931 mRNA. Translation: AAH00931.1.
    BC013394 mRNA. Translation: AAH13394.1.
    BC016812 mRNA. Translation: AAH16812.1.
    BC020824 mRNA. Translation: AAH20824.1.
    CCDSiCCDS31142.1. [P36542-1]
    CCDS7081.1. [P36542-2]
    PIRiA49108.
    RefSeqiNP_001001973.1. NM_001001973.1. [P36542-1]
    NP_005165.1. NM_005174.2. [P36542-2]
    UniGeneiHs.271135.

    Genome annotation databases

    EnsembliENST00000335698; ENSP00000338568; ENSG00000165629. [P36542-2]
    ENST00000356708; ENSP00000349142; ENSG00000165629. [P36542-1]
    GeneIDi509.
    KEGGihsa:509.
    UCSCiuc001iju.3. human. [P36542-1]

    Polymorphism databases

    DMDMi543875.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16561 Genomic DNA. Translation: BAA03994.1 .
    D16561 Genomic DNA. Translation: BAA03995.1 .
    D16562 mRNA. Translation: BAA03996.1 .
    D16563 mRNA. Translation: BAA03997.1 .
    AK292896 mRNA. Translation: BAF85585.1 .
    CR457403 mRNA. Translation: CAG33684.1 .
    AL353754 , AL158044 Genomic DNA. Translation: CAH73453.1 .
    AL353754 , AL158044 Genomic DNA. Translation: CAH73454.1 .
    AL158044 , AL353754 Genomic DNA. Translation: CAI12960.1 .
    AL158044 , AL353754 Genomic DNA. Translation: CAI12961.1 .
    CH471072 Genomic DNA. Translation: EAW86372.1 .
    CH471072 Genomic DNA. Translation: EAW86373.1 .
    BC000470 mRNA. Translation: AAH00470.1 .
    BC000931 mRNA. Translation: AAH00931.1 .
    BC013394 mRNA. Translation: AAH13394.1 .
    BC016812 mRNA. Translation: AAH16812.1 .
    BC020824 mRNA. Translation: AAH20824.1 .
    CCDSi CCDS31142.1. [P36542-1 ]
    CCDS7081.1. [P36542-2 ]
    PIRi A49108.
    RefSeqi NP_001001973.1. NM_001001973.1. [P36542-1 ]
    NP_005165.1. NM_005174.2. [P36542-2 ]
    UniGenei Hs.271135.

    3D structure databases

    ProteinModelPortali P36542.
    SMRi P36542. Positions 26-297.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106997. 46 interactions.
    IntActi P36542. 35 interactions.
    MINTi MINT-1378900.
    STRINGi 9606.ENSP00000349142.

    PTM databases

    PhosphoSitei P36542.

    Polymorphism databases

    DMDMi 543875.

    2D gel databases

    UCD-2DPAGE P36542.

    Proteomic databases

    MaxQBi P36542.
    PaxDbi P36542.
    PRIDEi P36542.

    Protocols and materials databases

    DNASUi 509.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000335698 ; ENSP00000338568 ; ENSG00000165629 . [P36542-2 ]
    ENST00000356708 ; ENSP00000349142 ; ENSG00000165629 . [P36542-1 ]
    GeneIDi 509.
    KEGGi hsa:509.
    UCSCi uc001iju.3. human. [P36542-1 ]

    Organism-specific databases

    CTDi 509.
    GeneCardsi GC10P007830.
    HGNCi HGNC:833. ATP5C1.
    HPAi HPA060949.
    MIMi 108729. gene.
    neXtProti NX_P36542.
    PharmGKBi PA25125.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0224.
    HOGENOMi HOG000215911.
    HOVERGENi HBG000933.
    InParanoidi P36542.
    KOi K02136.
    OMAi MATLKDX.
    OrthoDBi EOG7QK0D3.
    PhylomeDBi P36542.
    TreeFami TF105765.

    Enzyme and pathway databases

    Reactomei REACT_6759. Formation of ATP by chemiosmotic coupling.

    Miscellaneous databases

    ChiTaRSi ATP5C1. human.
    GeneWikii ATP5C1.
    GenomeRNAii 509.
    NextBioi 2117.
    PROi P36542.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P36542.
    Bgeei P36542.
    CleanExi HS_ATP5C1.
    Genevestigatori P36542.

    Family and domain databases

    InterProi IPR000131. ATPase_F1-cplx_gsu.
    IPR023632. ATPase_F1_gsu_CS.
    IPR023633. ATPase_F1_gsu_dom.
    [Graphical view ]
    PANTHERi PTHR11693. PTHR11693. 1 hit.
    Pfami PF00231. ATP-synt. 1 hit.
    [Graphical view ]
    PRINTSi PR00126. ATPASEGAMMA.
    SUPFAMi SSF52943. SSF52943. 1 hit.
    TIGRFAMsi TIGR01146. ATPsyn_F1gamma. 1 hit.
    PROSITEi PS00153. ATPASE_GAMMA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Gene structure of human mitochondrial ATP synthase gamma-subunit. Tissue specificity produced by alternative RNA splicing."
      Matsuda C., Endo H., Ohta S., Kagawa Y.
      J. Biol. Chem. 268:24950-24958(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS HEART AND LIVER).
      Tissue: Heart and Liver.
    2. "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] (ISOFORM HEART).
      Tissue: Trachea.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LIVER).
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM LIVER).
      Tissue: Liver, Muscle, Placenta and Urinary bladder.
    7. Bienvenut W.V., Glen H., Frame M.C.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 68-79; 116-126; 144-154; 263-277 AND 286-298, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Osteosarcoma.
    8. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55; LYS-154 AND LYS-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiATPG_HUMAN
    AccessioniPrimary (citable) accession number: P36542
    Secondary accession number(s): A8KA31
    , Q5VYP3, Q6I9V2, Q96AS8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 148 of the entry and version 1 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3