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O96007

- MOC2B_HUMAN

UniProt

O96007 - MOC2B_HUMAN

Protein

Molybdopterin synthase catalytic subunit

Gene

MOCS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group.2 PublicationsUniRule annotation

    Catalytic activityi

    Cyclic pyranopterin phosphate + 2 [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH(2)-C(O)SH + H2O = molybdopterin + 2 [molybdopterin-synthase sulfur-carrier protein].2 PublicationsUniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei159 – 1591SubstrateUniRule annotation

    GO - Molecular functioni

    1. molybdopterin synthase activity Source: UniProtKB

    GO - Biological processi

    1. molybdopterin cofactor biosynthetic process Source: Reactome
    2. Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB
    3. small molecule metabolic process Source: Reactome
    4. vitamin metabolic process Source: Reactome
    5. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Molybdenum cofactor biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09033-MONOMER.
    ReactomeiREACT_25073. Molybdenum cofactor biosynthesis.
    UniPathwayiUPA00344.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Molybdopterin synthase catalytic subunitUniRule annotation (EC:2.8.1.12UniRule annotation)
    Alternative name(s):
    MOCO1-B
    Molybdenum cofactor synthesis protein 2 large subunitUniRule annotation
    Molybdenum cofactor synthesis protein 2BUniRule annotation
    Short name:
    MOCS2BUniRule annotation
    Molybdopterin-synthase large subunit
    Short name:
    MPT synthase large subunit
    Gene namesi
    Name:MOCS2UniRule annotation
    Synonyms:MCBPE, MOCO1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:7193. MOCS2.

    Subcellular locationi

    Cytoplasmcytosol 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProtKB
    3. molybdopterin synthase complex Source: UniProtKB
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Molybdenum cofactor deficiency, complementation group B (MOCODB) [MIM:252160]: An autosomal recessive metabolic disorder characterized by neonatal onset of intractable seizures, opisthotonus, and facial dysmorphism associated with hypouricemia and elevated urinary sulfite levels. Affected individuals show severe neurologic damage and often die in early childhood.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti168 – 1681E → K in MOCODB. 1 Publication
    VAR_012765

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi252160. phenotype.
    PharmGKBiPA30903.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 188188Molybdopterin synthase catalytic subunitPRO_0000163111Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei20 – 201Phosphoserine5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO96007.
    PRIDEiO96007.

    PTM databases

    PhosphoSiteiO96007.

    Expressioni

    Tissue specificityi

    Highest levels are found in heart and skeletal muscle. Lower levels are present in brain, kidney and pancreas. Very low levels are found in lung and peripheral blood leukocytes.1 Publication

    Gene expression databases

    ArrayExpressiO96007.
    BgeeiO96007.
    CleanExiHS_MOCS2.
    GenevestigatoriO96007.

    Organism-specific databases

    HPAiHPA037680.

    Interactioni

    Subunit structurei

    Heterotetramer; composed of 2 small (MOCS2A) and 2 large (MOCS2B) subunits.UniRule annotation

    Protein-protein interaction databases

    BioGridi110481. 3 interactions.
    IntActiO96007. 3 interactions.
    STRINGi9606.ENSP00000339580.

    Structurei

    Secondary structure

    1
    188
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi45 – 528
    Helixi56 – 627
    Beta strandi69 – 779
    Beta strandi80 – 823
    Beta strandi85 – 9612
    Helixi98 – 11316
    Beta strandi116 – 1249
    Beta strandi126 – 1294
    Beta strandi132 – 14312
    Helixi144 – 16118
    Beta strandi164 – 1707

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AP8X-ray2.78A/B/C/D38-172[»]
    ProteinModelPortaliO96007.
    SMRiO96007. Positions 38-171.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni143 – 1442Substrate bindingUniRule annotation
    Regioni166 – 1683Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the MoaE family. MOCS2B subfamily.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000280991.
    InParanoidiO96007.
    KOiK03635.
    OMAiGNKECFW.
    PhylomeDBiO96007.
    TreeFamiTF314334.

    Family and domain databases

    Gene3Di3.90.1170.40. 1 hit.
    HAMAPiMF_03052. MOC2B.
    InterProiIPR028888. MOCS2B_euk.
    IPR003448. Mopterin_biosynth_MoaE.
    [Graphical view]
    PANTHERiPTHR23404:SF2. PTHR23404:SF2. 1 hit.
    PfamiPF02391. MoaE. 1 hit.
    [Graphical view]
    SUPFAMiSSF54690. SSF54690. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O96007-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSLEISSSC FSLETKLPLS PPLVEDSAFE PSRKDMDEVE EKSKDVINFT    50
    AEKLSVDEVS QLVISPLCGA ISLFVGTTRN NFEGKKVISL EYEAYLPMAE 100
    NEVRKICSDI RQKWPVKHIA VFHRLGLVPV SEASIIIAVS SAHRAASLEA 150
    VSYAIDTLKA KVPIWKKEIY EESSTWKGNK ECFWASNS 188
    Length:188
    Mass (Da):20,944
    Last modified:May 1, 1999 - v1
    Checksum:iF405256D85621146
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti50 – 501T → A.
    Corresponds to variant rs2233213 [ dbSNP | Ensembl ].
    VAR_050091
    Natural varianti77 – 771T → A.
    Corresponds to variant rs2233215 [ dbSNP | Ensembl ].
    VAR_050092
    Natural varianti123 – 1231H → Y.
    Corresponds to variant rs2233218 [ dbSNP | Ensembl ].
    VAR_050093
    Natural varianti168 – 1681E → K in MOCODB. 1 Publication
    VAR_012765
    Natural varianti187 – 1871N → S.
    Corresponds to variant rs2233221 [ dbSNP | Ensembl ].
    VAR_050094

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF091871 mRNA. Translation: AAD14599.1.
    AF117815 mRNA. Translation: AAD13297.1.
    AF155659 mRNA. Translation: AAF67478.1.
    AK312887 mRNA. Translation: BAG35735.1.
    CR457172 mRNA. Translation: CAG33453.1.
    CH471123 Genomic DNA. Translation: EAW54874.1.
    BC046097 mRNA. Translation: AAH46097.1.
    CCDSiCCDS3958.1.
    PIRiB59370.
    RefSeqiNP_004522.1. NM_004531.4.
    UniGeneiHs.163645.
    Hs.594335.

    Genome annotation databases

    EnsembliENST00000396954; ENSP00000380157; ENSG00000164172.
    GeneIDi4338.
    KEGGihsa:4338.
    UCSCiuc003joz.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF091871 mRNA. Translation: AAD14599.1 .
    AF117815 mRNA. Translation: AAD13297.1 .
    AF155659 mRNA. Translation: AAF67478.1 .
    AK312887 mRNA. Translation: BAG35735.1 .
    CR457172 mRNA. Translation: CAG33453.1 .
    CH471123 Genomic DNA. Translation: EAW54874.1 .
    BC046097 mRNA. Translation: AAH46097.1 .
    CCDSi CCDS3958.1.
    PIRi B59370.
    RefSeqi NP_004522.1. NM_004531.4.
    UniGenei Hs.163645.
    Hs.594335.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4AP8 X-ray 2.78 A/B/C/D 38-172 [» ]
    ProteinModelPortali O96007.
    SMRi O96007. Positions 38-171.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110481. 3 interactions.
    IntActi O96007. 3 interactions.
    STRINGi 9606.ENSP00000339580.

    PTM databases

    PhosphoSitei O96007.

    Proteomic databases

    MaxQBi O96007.
    PRIDEi O96007.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000396954 ; ENSP00000380157 ; ENSG00000164172 .
    GeneIDi 4338.
    KEGGi hsa:4338.
    UCSCi uc003joz.3. human.

    Organism-specific databases

    CTDi 4338.
    GeneCardsi GC05M052429.
    HGNCi HGNC:7193. MOCS2.
    HPAi HPA037680.
    MIMi 252160. phenotype.
    603708. gene.
    neXtProti NX_O96007.
    PharmGKBi PA30903.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000280991.
    InParanoidi O96007.
    KOi K03635.
    OMAi GNKECFW.
    PhylomeDBi O96007.
    TreeFami TF314334.

    Enzyme and pathway databases

    UniPathwayi UPA00344 .
    BioCyci MetaCyc:HS09033-MONOMER.
    Reactomei REACT_25073. Molybdenum cofactor biosynthesis.

    Miscellaneous databases

    GeneWikii MOCS2.
    GenomeRNAii 4338.
    NextBioi 17072.
    PROi O96007.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O96007.
    Bgeei O96007.
    CleanExi HS_MOCS2.
    Genevestigatori O96007.

    Family and domain databases

    Gene3Di 3.90.1170.40. 1 hit.
    HAMAPi MF_03052. MOC2B.
    InterProi IPR028888. MOCS2B_euk.
    IPR003448. Mopterin_biosynth_MoaE.
    [Graphical view ]
    PANTHERi PTHR23404:SF2. PTHR23404:SF2. 1 hit.
    Pfami PF02391. MoaE. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54690. SSF54690. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Human molybdopterin synthase gene: identification of a bicistronic transcript with overlapping reading frames."
      Stallmeyer B., Drugeon G., Reiss J., Haenni A.L., Mendel R.R.
      Am. J. Hum. Genet. 64:698-705(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION OF BICISTRONIC GENE, TISSUE SPECIFICITY.
      Tissue: Liver.
    2. "The two subunits of human molybdopterin synthase: evidence for a bicistronic messenger RNA with overlapping reading frames."
      Sloan J., Kinghorn J.R., Unkles S.E.
      Nucleic Acids Res. 27:854-858(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Huang C., Huang Q., Wu T., Peng Y., Gu Y., Zhang L., Jiang C., Li Y., Han Z., Wang Y., Chen Z., Fu G.
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Adrenal gland.
    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].
      Tissue: Uterus.
    5. "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].
    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].
      Tissue: Duodenum.
    8. "Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency."
      Leimkuehler S., Freuer A., Araujo J.A., Rajagopalan K.V., Mendel R.R.
      J. Biol. Chem. 278:26127-26134(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, FUNCTION, SUBUNIT.
    9. "Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans."
      Matthies A., Rajagopalan K.V., Mendel R.R., Leimkuehler S.
      Proc. Natl. Acad. Sci. U.S.A. 101:5946-5951(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
    10. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Human molybdopterin synthase gene: genomic structure and mutations in molybdenum cofactor deficiency type B."
      Reiss J., Dorche C., Stallmeyer B., Mendel R.R., Cohen N., Zabot M.-T.
      Am. J. Hum. Genet. 64:706-711(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MOCODB LYS-168.
    17. "Ten novel mutations in the molybdenum cofactor genes MOCS1 and MOCS2 and in vitro characterization of a MOCS2 mutation that abolishes the binding ability of molybdopterin synthase."
      Leimkuehler S., Charcosset M., Latour P., Dorche C., Kleppe S., Scaglia F., Szymczak I., Schupp P., Hahnewald R., Reiss J.
      Hum. Genet. 117:565-570(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MOCODB.
    18. "A novel MOCS2 mutation reveals coordinated expression of the small and large subunit of molybdopterin synthase."
      Hahnewald R., Leimkuehler S., Vilaseca A., Acquaviva-Bourdain C., Lenz U., Reiss J.
      Mol. Genet. Metab. 89:210-213(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MOCODB.

    Entry informationi

    Entry nameiMOC2B_HUMAN
    AccessioniPrimary (citable) accession number: O96007
    Secondary accession number(s): Q6IAI3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 11, 2002
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 121 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

    Miscellaneous

    This protein is produced by a bicistronic gene which also produces the small subunit (MOCS2A) from an overlapping reading frame. Expression of these 2 proteins are related since a mutation that removes the start codon of the small subunit (MOCS2A) also impairs expression of the large subunit (MOCS2B).

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3