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P36957

- ODO2_HUMAN

UniProt

P36957 - ODO2_HUMAN

Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial

Gene

DLST

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 4 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).

    Catalytic activityi

    Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.

    Cofactori

    Binds 1 lipoyl cofactor covalently.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei424 – 4241Sequence Analysis
    Active sitei428 – 4281Sequence Analysis

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular metabolic process Source: Reactome
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. generation of precursor metabolites and energy Source: ProtInc
    4. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
    5. lysine catabolic process Source: Reactome
    6. small molecule metabolic process Source: Reactome
    7. tricarboxylic acid cycle Source: Reactome

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04324-MONOMER.
    ReactomeiREACT_1298. Lysine catabolism.
    REACT_1785. Citric acid cycle (TCA cycle).
    UniPathwayiUPA00868; UER00840.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (EC:2.3.1.61)
    Alternative name(s):
    2-oxoglutarate dehydrogenase complex component E2
    Short name:
    OGDC-E2
    Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
    E2K
    Gene namesi
    Name:DLST
    Synonyms:DLTS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:2911. DLST.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. membrane Source: UniProtKB
    3. mitochondrial matrix Source: Reactome
    4. nucleus Source: UniProt
    5. oxoglutarate dehydrogenase complex Source: InterPro

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27367.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 6767Mitochondrion1 PublicationAdd
    BLAST
    Chaini68 – 453386Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialPRO_0000020472Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei110 – 1101N6-lipoyllysineSequence Analysis
    Modified residuei154 – 1541N6-acetyllysineBy similarity
    Modified residuei267 – 2671N6-acetyllysineBy similarity
    Modified residuei272 – 2721N6-acetyllysineBy similarity
    Modified residuei273 – 2731N6-acetyllysineBy similarity
    Modified residuei277 – 2771N6-acetyllysineBy similarity
    Modified residuei307 – 3071N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP36957.
    PaxDbiP36957.
    PRIDEiP36957.

    2D gel databases

    OGPiP36957.
    UCD-2DPAGEP36957.

    PTM databases

    PhosphoSiteiP36957.

    Expressioni

    Gene expression databases

    ArrayExpressiP36957.
    BgeeiP36957.
    CleanExiHS_DLST.
    GenevestigatoriP36957.

    Organism-specific databases

    HPAiHPA003010.

    Interactioni

    Subunit structurei

    Forms a 24-polypeptide structural core with octahedral symmetry.

    Protein-protein interaction databases

    BioGridi108087. 26 interactions.
    IntActiP36957. 19 interactions.
    MINTiMINT-3014449.
    STRINGi9606.ENSP00000335304.

    Structurei

    3D structure databases

    ProteinModelPortaliP36957.
    SMRiP36957. Positions 73-140, 220-453.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini71 – 14373Lipoyl-bindingAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 1 lipoyl-binding domain.Curated

    Keywords - Domaini

    Lipoyl, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0508.
    HOGENOMiHOG000281563.
    HOVERGENiHBG000268.
    InParanoidiP36957.
    KOiK00658.
    OMAiQIFRNIF.
    PhylomeDBiP36957.
    TreeFamiTF314164.

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR011053. Single_hybrid_motif.
    IPR006255. SucB.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    [Graphical view]
    SUPFAMiSSF51230. SSF51230. 1 hit.
    TIGRFAMsiTIGR01347. sucB. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 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 1 (identifier: P36957-1) [UniParc]FASTAAdd to Basket

    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

    MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCQGP GYPNSRKVVI    50
    NNSVFSVRFF RTTAVCKDDL VTVKTPAFAE SVTEGDVRWE KAVGDTVAED 100
    EVVCEIETDK TSVQVPSPAN GVIEALLVPD GGKVEGGTPL FTLRKTGAAP 150
    AKAKPAEAPA AAAPKAEPTA AAVPPPAAPI PTQMPPVPSP SQPPSGKPVS 200
    AVKPTVAPPL AEPGAGKGLR SEHREKMNRM RQRIAQRLKE AQNTCAMLTT 250
    FNEIDMSNIQ EMRARHKEAF LKKHNLKLGF MSAFVKASAF ALQEQPVVNA 300
    VIDDTTKEVV YRDYIDISVA VATPRGLVVP VIRNVEAMNF ADIERTITEL 350
    GEKARKNELA IEDMDGGTFT ISNGGVFGSL FGTPIINPPQ SAILGMHGIF 400
    DRPVAIGGKV EVRPMMYVAL TYDHRLIDGR EAVTFLRKIK AAVEDPRVLL 450
    LDL 453
    Length:453
    Mass (Da):48,755
    Last modified:January 11, 2011 - v4
    Checksum:iA30E8CC959106B8F
    GO
    Isoform 2 (identifier: P36957-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-23: MLSRSRCVSRAFSRSLSAFQKGN → MTWLQSKPQRLQNLSQREMSGGR
         24-109: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:367
    Mass (Da):39,553
    Checksum:i3EEF7F48175530EC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 152RS → AP in BAA03871. (PubMed:8268217)Curated
    Sequence conflicti14 – 152RS → AP in BAA05536. (PubMed:8076640)Curated
    Sequence conflicti14 – 152RS → AP in AAB59629. 1 PublicationCurated
    Sequence conflicti132 – 1321G → T in BAA03871. (PubMed:8268217)Curated
    Sequence conflicti212 – 2121E → D in BAA03871. (PubMed:8268217)Curated
    Sequence conflicti212 – 2121E → D in BAA05536. (PubMed:8076640)Curated
    Sequence conflicti312 – 3121R → T in BAA05536. (PubMed:8076640)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti213 – 2131P → A.2 Publications
    Corresponds to variant rs2853769 [ dbSNP | Ensembl ].
    VAR_004976
    Natural varianti384 – 3841P → T.
    VAR_004977

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2323MLSRS…FQKGN → MTWLQSKPQRLQNLSQREMS GGR in isoform 2. 1 PublicationVSP_056439Add
    BLAST
    Alternative sequencei24 – 10986Missing in isoform 2. 1 PublicationVSP_056440Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16373 mRNA. Translation: BAA03871.1.
    D26535 Genomic DNA. Translation: BAA05536.1.
    L37418 mRNA. Translation: AAB59629.1.
    AK289414 mRNA. Translation: BAF82103.1.
    AK299505 mRNA. Translation: BAH13054.1.
    AC006530 Genomic DNA. Translation: AAD30181.1.
    CH471061 Genomic DNA. Translation: EAW81199.1.
    BC000302 mRNA. Translation: AAH00302.1.
    BC001922 mRNA. Translation: AAH01922.1.
    CCDSiCCDS9833.1.
    PIRiS39786. PN0673.
    RefSeqiNP_001924.2. NM_001933.4.
    UniGeneiHs.525459.

    Genome annotation databases

    EnsembliENST00000334212; ENSP00000335465; ENSG00000119689.
    ENST00000334220; ENSP00000335304; ENSG00000119689.
    GeneIDi1743.
    KEGGihsa:1743.
    UCSCiuc001xqs.3. human.

    Polymorphism databases

    DMDMi317373578.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16373 mRNA. Translation: BAA03871.1 .
    D26535 Genomic DNA. Translation: BAA05536.1 .
    L37418 mRNA. Translation: AAB59629.1 .
    AK289414 mRNA. Translation: BAF82103.1 .
    AK299505 mRNA. Translation: BAH13054.1 .
    AC006530 Genomic DNA. Translation: AAD30181.1 .
    CH471061 Genomic DNA. Translation: EAW81199.1 .
    BC000302 mRNA. Translation: AAH00302.1 .
    BC001922 mRNA. Translation: AAH01922.1 .
    CCDSi CCDS9833.1.
    PIRi S39786. PN0673.
    RefSeqi NP_001924.2. NM_001933.4.
    UniGenei Hs.525459.

    3D structure databases

    ProteinModelPortali P36957.
    SMRi P36957. Positions 73-140, 220-453.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108087. 26 interactions.
    IntActi P36957. 19 interactions.
    MINTi MINT-3014449.
    STRINGi 9606.ENSP00000335304.

    PTM databases

    PhosphoSitei P36957.

    Polymorphism databases

    DMDMi 317373578.

    2D gel databases

    OGPi P36957.
    UCD-2DPAGE P36957.

    Proteomic databases

    MaxQBi P36957.
    PaxDbi P36957.
    PRIDEi P36957.

    Protocols and materials databases

    DNASUi 1743.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334212 ; ENSP00000335465 ; ENSG00000119689 .
    ENST00000334220 ; ENSP00000335304 ; ENSG00000119689 .
    GeneIDi 1743.
    KEGGi hsa:1743.
    UCSCi uc001xqs.3. human.

    Organism-specific databases

    CTDi 1743.
    GeneCardsi GC14P075348.
    H-InvDB HIX0131240.
    HGNCi HGNC:2911. DLST.
    HPAi HPA003010.
    MIMi 126063. gene.
    neXtProti NX_P36957.
    PharmGKBi PA27367.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281563.
    HOVERGENi HBG000268.
    InParanoidi P36957.
    KOi K00658.
    OMAi QIFRNIF.
    PhylomeDBi P36957.
    TreeFami TF314164.

    Enzyme and pathway databases

    UniPathwayi UPA00868 ; UER00840 .
    BioCyci MetaCyc:HS04324-MONOMER.
    Reactomei REACT_1298. Lysine catabolism.
    REACT_1785. Citric acid cycle (TCA cycle).

    Miscellaneous databases

    ChiTaRSi DLST. human.
    GeneWikii DLST.
    GenomeRNAii 1743.
    NextBioi 7071.
    PROi P36957.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P36957.
    Bgeei P36957.
    CleanExi HS_DLST.
    Genevestigatori P36957.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR011053. Single_hybrid_motif.
    IPR006255. SucB.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51230. SSF51230. 1 hit.
    TIGRFAMsi TIGR01347. sucB. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human dihydrolipoamide succinyltransferase: cDNA cloning and localization on chromosome 14q24.2-q24.3."
      Nakano K., Matsuda S., Sakamoto T., Takase C., Nakagawa S., Ohta S., Ariyama T., Inazawa J., Abe T., Miyata T.
      Biochim. Biophys. Acta 1216:360-368(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-213.
    2. "Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex."
      Nakano K., Takase C., Sakamoto T., Nakagawa S., Inazawa J., Ohta S., Matuda S.
      Eur. J. Biochem. 224:179-189(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-213.
      Tissue: Peripheral blood.
    3. "Physical mapping and nucleotide sequence analysis of the human dihydrolipoamide succinyltransferase gene."
      Keryanov S., Liang Y., Rogaev E.I., Sherrington R., Tsuda T., Rogaeva E., Chi H., Crapper-Mclachlan D., Chumakov Y., Rommens J.M., St George-Hyslop P.H.
      Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    4. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    5. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 1).
      Tissue: Lung.
    8. "Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
      Xu G., Shin S.B., Jaffrey S.R.
      Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 68-89.
      Tissue: Leukemic T-cell.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiODO2_HUMAN
    AccessioniPrimary (citable) accession number: P36957
    Secondary accession number(s): B7Z5W8
    , E7ESY5, Q7LDY7, Q9BQ32
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 161 of the entry and version 4 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 14
      Human chromosome 14: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3