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O95396

- MOCS3_HUMAN

UniProt

O95396 - MOCS3_HUMAN

Protein

Adenylyltransferase and sulfurtransferase MOCS3

Gene

MOCS3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Plays a central role in 2-thiolation of mcm5S2U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions.2 PublicationsUniRule annotation

    Catalytic activityi

    ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly = diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP.UniRule annotation
    [Molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-cysteine = AMP + [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH(2)-C(O)SH + cysteine desulfurase.UniRule annotation

    Cofactori

    Binds 1 zinc ion per subunit.UniRule annotation

    Kineticsi

    1. KM=0.25 mM for thiosulfate1 Publication
    2. KM=0.28 mM for cyanide1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei92 – 921ATP; via amide nitrogenUniRule annotation
    Binding sitei113 – 1131ATPUniRule annotation
    Binding sitei137 – 1371ATPUniRule annotation
    Metal bindingi222 – 2221ZincUniRule annotation
    Metal bindingi225 – 2251ZincUniRule annotation
    Active sitei239 – 2391Glycyl thioester intermediate; for adenylyltransferase activityUniRule annotation
    Metal bindingi297 – 2971ZincUniRule annotation
    Metal bindingi300 – 3001ZincUniRule annotation
    Active sitei412 – 4121Cysteine persulfide intermediate; for sulfurtransferase activity1 PublicationUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi120 – 1245ATPUniRule annotation
    Nucleotide bindingi181 – 1822ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. molybdopterin-synthase adenylyltransferase activity Source: UniProtKB-EC
    4. molybdopterin-synthase sulfurtransferase activity Source: UniProtKB-EC
    5. nucleotidyltransferase activity Source: UniProtKB
    6. protein adenylyltransferase activity Source: RefGenome
    7. protein binding Source: UniProtKB
    8. sulfurtransferase activity Source: UniProtKB
    9. thiosulfate sulfurtransferase activity Source: UniProtKB
    10. URM1 activating enzyme activity Source: UniProtKB

    GO - Biological processi

    1. enzyme active site formation via L-cysteine persulfide Source: UniProtKB
    2. molybdopterin cofactor biosynthetic process Source: Reactome
    3. Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB
    4. protein adenylylation Source: GOC
    5. protein urmylation Source: RefGenome
    6. small molecule metabolic process Source: Reactome
    7. tRNA thio-modification Source: UniProtKB
    8. tRNA wobble position uridine thiolation Source: RefGenome
    9. tRNA wobble uridine modification Source: UniProtKB
    10. vitamin metabolic process Source: Reactome
    11. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Molybdenum cofactor biosynthesis, tRNA processing

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04742-MONOMER.
    ReactomeiREACT_25073. Molybdenum cofactor biosynthesis.
    UniPathwayiUPA00344.
    UPA00988.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylyltransferase and sulfurtransferase MOCS3UniRule annotation
    Alternative name(s):
    Molybdenum cofactor synthesis protein 3UniRule annotation
    Molybdopterin synthase sulfurylase
    Short name:
    MPT synthase sulfurylase
    Including the following 2 domains:
    Molybdopterin-synthase adenylyltransferaseUniRule annotation (EC:2.7.7.80UniRule annotation)
    Alternative name(s):
    Adenylyltransferase MOCS3UniRule annotation
    Sulfur carrier protein MOCS2A adenylyltransferaseUniRule annotation
    Molybdopterin-synthase sulfurtransferaseUniRule annotation (EC:2.8.1.11UniRule annotation)
    Alternative name(s):
    Sulfur carrier protein MOCS2A sulfurtransferaseUniRule annotation
    Sulfurtransferase MOCS3UniRule annotation
    Gene namesi
    Name:MOCS3UniRule annotation
    Synonyms:UBA4UniRule annotation
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:15765. MOCS3.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi239 – 2391C → A: Impairs sulfurtransferase activity. 1 Publication
    Mutagenesisi316 – 3161C → A: Does not affect sulfurtransferase activity. 1 Publication
    Mutagenesisi324 – 3241C → A: Does not affect sulfurtransferase activity. 1 Publication
    Mutagenesisi365 – 3651C → A: Does not affect sulfurtransferase activity. 1 Publication
    Mutagenesisi412 – 4121C → A: Abolishes sulfurtransferase activity. 1 Publication
    Mutagenesisi413 – 4131K → R: Does not affect sulfurtransferase specificity and activity. 1 Publication
    Mutagenesisi414 – 4141L → K: Does not affect sulfurtransferase specificity and activity. 1 Publication
    Mutagenesisi415 – 4151G → A: Does not affect sulfurtransferase specificity and activity. 1 Publication
    Mutagenesisi416 – 4161N → V: Does not affect sulfurtransferase specificity and activity. 1 Publication
    Mutagenesisi417 – 4171D → R: Results in 470-fold increased activity. 1 Publication
    Mutagenesisi417 – 4171D → T: Results in 90-fold increased activity. 1 Publication
    Mutagenesisi458 – 4581P → G: Does not affect sulfurtransferase specificity and activity. 1 Publication
    Mutagenesisi460 – 4601Y → A: Does not affect sulfurtransferase specificity and activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA30904.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 460460Adenylyltransferase and sulfurtransferase MOCS3PRO_0000120583Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi316 ↔ 3241 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiO95396.
    PaxDbiO95396.
    PeptideAtlasiO95396.
    PRIDEiO95396.

    PTM databases

    PhosphoSiteiO95396.

    Expressioni

    Gene expression databases

    BgeeiO95396.
    CleanExiHS_MOCS3.
    GenevestigatoriO95396.

    Organism-specific databases

    HPAiHPA027556.

    Interactioni

    Subunit structurei

    Interacts with NFS1.1 PublicationUniRule annotation

    Protein-protein interaction databases

    BioGridi118127. 4 interactions.
    DIPiDIP-31168N.
    IntActiO95396. 1 interaction.
    MINTiMINT-5003967.
    STRINGi9606.ENSP00000244051.

    Structurei

    Secondary structure

    1
    460
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi338 – 34710
    Beta strandi352 – 3554
    Helixi359 – 3646
    Beta strandi370 – 3723
    Helixi375 – 3795
    Helixi383 – 39715
    Beta strandi406 – 4116
    Beta strandi413 – 4164
    Helixi417 – 43014
    Beta strandi433 – 4353
    Beta strandi437 – 4426
    Helixi445 – 4528

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3I2VX-ray1.25A335-460[»]
    ProteinModelPortaliO95396.
    SMRiO95396. Positions 5-301, 335-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95396.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini347 – 458112RhodaneseUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily.UniRule annotation
    Contains 1 rhodanese domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0476.
    HOGENOMiHOG000281219.
    HOVERGENiHBG052491.
    InParanoidiO95396.
    KOiK11996.
    OMAiTDYVFFC.
    OrthoDBiEOG776SQ3.
    PhylomeDBiO95396.
    TreeFamiTF106103.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    3.40.50.720. 1 hit.
    HAMAPiMF_03049. MOCS3_Uba4.
    InterProiIPR028885. MOCS3/Uba4.
    IPR007901. MoeZ_MoeB.
    IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR001763. Rhodanese-like_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    [Graphical view]
    PfamiPF05237. MoeZ_MoeB. 1 hit.
    PF00581. Rhodanese. 1 hit.
    PF00899. ThiF. 1 hit.
    [Graphical view]
    SMARTiSM00450. RHOD. 1 hit.
    [Graphical view]
    SUPFAMiSSF69572. SSF69572. 1 hit.
    PROSITEiPS50206. RHODANESE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O95396-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASREEVLAL QAEVAQREEE LNSLKQKLAS ALLAEQEPQP ERLVPVSPLP    50
    PKAALSRDEI LRYSRQLVLP ELGVHGQLRL GTACVLIVGC GGLGCPLAQY 100
    LAAAGVGRLG LVDYDVVEMS NLARQVLHGE ALAGQAKAFS AAASLRRLNS 150
    AVECVPYTQA LTPATALDLV RRYDVVADCS DNVPTRYLVN DACVLAGRPL 200
    VSASALRFEG QITVYHYDGG PCYRCIFPQP PPAETVTNCA DGGVLGVVTG 250
    VLGCLQALEV LKIAAGLGPS YSGSLLLFDA LRGHFRSIRL RSRRLDCAAC 300
    GERPTVTDLL DYEAFCGSSA TDKCRSLQLL SPEERVSVTD YKRLLDSGAF 350
    HLLLDVRPQV EVDICRLPHA LHIPLKHLER RDAESLKLLK EAIWEEKQGT 400
    QEGAAVPIYV ICKLGNDSQK AVKILQSLSA AQELDPLTVR DVVGGLMAWA 450
    AKIDGTFPQY 460
    Length:460
    Mass (Da):49,669
    Last modified:May 1, 1999 - v1
    Checksum:i299A4E755173E324
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti429 – 4291S → A.
    Corresponds to variant rs7269297 [ dbSNP | Ensembl ].
    VAR_049349

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF102544 mRNA. Translation: AAC72412.1.
    AL034553 Genomic DNA. Translation: CAB53750.1.
    BC015939 mRNA. Translation: AAH15939.1.
    CCDSiCCDS13435.1.
    RefSeqiNP_055299.1. NM_014484.4.
    UniGeneiHs.159410.
    Hs.736268.

    Genome annotation databases

    EnsembliENST00000244051; ENSP00000244051; ENSG00000124217.
    GeneIDi27304.
    KEGGihsa:27304.
    UCSCiuc002xvy.2. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF102544 mRNA. Translation: AAC72412.1 .
    AL034553 Genomic DNA. Translation: CAB53750.1 .
    BC015939 mRNA. Translation: AAH15939.1 .
    CCDSi CCDS13435.1.
    RefSeqi NP_055299.1. NM_014484.4.
    UniGenei Hs.159410.
    Hs.736268.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3I2V X-ray 1.25 A 335-460 [» ]
    ProteinModelPortali O95396.
    SMRi O95396. Positions 5-301, 335-460.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118127. 4 interactions.
    DIPi DIP-31168N.
    IntActi O95396. 1 interaction.
    MINTi MINT-5003967.
    STRINGi 9606.ENSP00000244051.

    PTM databases

    PhosphoSitei O95396.

    Proteomic databases

    MaxQBi O95396.
    PaxDbi O95396.
    PeptideAtlasi O95396.
    PRIDEi O95396.

    Protocols and materials databases

    DNASUi 27304.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000244051 ; ENSP00000244051 ; ENSG00000124217 .
    GeneIDi 27304.
    KEGGi hsa:27304.
    UCSCi uc002xvy.2. human.

    Organism-specific databases

    CTDi 27304.
    GeneCardsi GC20P049575.
    HGNCi HGNC:15765. MOCS3.
    HPAi HPA027556.
    MIMi 609277. gene.
    neXtProti NX_O95396.
    PharmGKBi PA30904.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0476.
    HOGENOMi HOG000281219.
    HOVERGENi HBG052491.
    InParanoidi O95396.
    KOi K11996.
    OMAi TDYVFFC.
    OrthoDBi EOG776SQ3.
    PhylomeDBi O95396.
    TreeFami TF106103.

    Enzyme and pathway databases

    UniPathwayi UPA00344 .
    UPA00988 .
    BioCyci MetaCyc:HS04742-MONOMER.
    Reactomei REACT_25073. Molybdenum cofactor biosynthesis.

    Miscellaneous databases

    EvolutionaryTracei O95396.
    GeneWikii MOCS3.
    GenomeRNAii 27304.
    NextBioi 50301.
    PROi O95396.
    SOURCEi Search...

    Gene expression databases

    Bgeei O95396.
    CleanExi HS_MOCS3.
    Genevestigatori O95396.

    Family and domain databases

    Gene3Di 3.40.250.10. 1 hit.
    3.40.50.720. 1 hit.
    HAMAPi MF_03049. MOCS3_Uba4.
    InterProi IPR028885. MOCS3/Uba4.
    IPR007901. MoeZ_MoeB.
    IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR001763. Rhodanese-like_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    [Graphical view ]
    Pfami PF05237. MoeZ_MoeB. 1 hit.
    PF00581. Rhodanese. 1 hit.
    PF00899. ThiF. 1 hit.
    [Graphical view ]
    SMARTi SM00450. RHOD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69572. SSF69572. 1 hit.
    PROSITEi PS50206. RHODANESE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: FUNCTION IN BIOSYNTHESIS OF THE MOLYBDENUM COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-239; CYS-316; CYS-324; CYS-365 AND CYS-412.
    2. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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: Uterus.
    4. "Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry."
      Matthies A., Nimtz M., Leimkuehler S.
      Biochemistry 44:7912-7920(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE, DISULFIDE BOND.
    5. "Site-directed mutagenesis of the active site loop of the rhodanese-like domain of the human molybdopterin synthase sulfurase MOCS3. Major differences in substrate specificity between eukaryotic and bacterial homologs."
      Krepinsky K., Leimkuehler S.
      FEBS J. 274:2778-2787(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, MUTAGENESIS OF LYS-413; LEU-414; GLY-415; ASN-416; ASP-417; PRO-458 AND TYR-460.
    6. "A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis."
      Marelja Z., Stoecklein W., Nimtz M., Leimkuehler S.
      J. Biol. Chem. 283:25178-25185(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, INTERACTION WITH NFS1.
    7. "A functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathway."
      Schlieker C.D., Van der Veen A.G., Damon J.R., Spooner E., Ploegh H.L.
      Proc. Natl. Acad. Sci. U.S.A. 105:18255-18260(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN 2-THIOLATION OF TRNA.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Crystal structure of the human MOCS3 rhodanese-like domain."
      Structural genomics consortium (SGC)
      Submitted (JUL-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 335-460.

    Entry informationi

    Entry nameiMOCS3_HUMAN
    AccessioniPrimary (citable) accession number: O95396
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 26, 2002
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 129 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

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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