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Protein

Adenylyltransferase and sulfurtransferase MOCS3

Gene

MOCS3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.UniRule annotation2 Publications

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

Zn2+UniRule annotationNote: 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

    Pathway:i5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis

    This protein is involved in the pathway 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis, which is part of tRNA modification.UniRule annotation
    View all proteins of this organism that are known to be involved in the pathway 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis and in tRNA modification.

    Pathway:imolybdopterin biosynthesis

    This protein is involved in the pathway molybdopterin biosynthesis, which is part of Cofactor biosynthesis.UniRule annotation
    View all proteins of this organism that are known to be involved in the pathway molybdopterin biosynthesis and in Cofactor biosynthesis.

    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 activityUniRule annotation1 Publication

    Regions

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

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • metal ion binding Source: UniProtKB-KW
    • molybdopterin-synthase adenylyltransferase activity Source: UniProtKB-EC
    • molybdopterin-synthase sulfurtransferase activity Source: UniProtKB-EC
    • nucleotidyltransferase activity Source: UniProtKB
    • protein adenylyltransferase activity Source: GO_Central
    • sulfurtransferase activity Source: UniProtKB
    • thiosulfate sulfurtransferase activity Source: UniProtKB
    • URM1 activating enzyme activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    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.
    BRENDAi2.7.7.80. 2681.
    2.8.1.11. 2681.
    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 Componenti: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:15765. MOCS3.

    Subcellular locationi

    • Cytoplasm UniRule annotation1 Publication

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    Complete GO annotation...

    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.
    GenevisibleiO95396. HS.

    Interactioni

    Subunit structurei

    Interacts with NFS1.UniRule annotation1 Publication

    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 – 34710Combined sources
    Beta strandi352 – 3554Combined sources
    Helixi359 – 3646Combined sources
    Beta strandi370 – 3723Combined sources
    Helixi375 – 3795Combined sources
    Helixi383 – 39715Combined sources
    Beta strandi406 – 4116Combined sources
    Beta strandi413 – 4164Combined sources
    Helixi417 – 43014Combined sources
    Beta strandi433 – 4353Combined sources
    Beta strandi437 – 4426Combined sources
    Helixi445 – 4528Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    GeneTreeiENSGT00800000124206.
    HOGENOMiHOG000281219.
    HOVERGENiHBG052491.
    InParanoidiO95396.
    KOiK11996.
    OMAiVRNPNEY.
    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

            10         20         30         40         50
    MASREEVLAL QAEVAQREEE LNSLKQKLAS ALLAEQEPQP ERLVPVSPLP
    60 70 80 90 100
    PKAALSRDEI LRYSRQLVLP ELGVHGQLRL GTACVLIVGC GGLGCPLAQY
    110 120 130 140 150
    LAAAGVGRLG LVDYDVVEMS NLARQVLHGE ALAGQAKAFS AAASLRRLNS
    160 170 180 190 200
    AVECVPYTQA LTPATALDLV RRYDVVADCS DNVPTRYLVN DACVLAGRPL
    210 220 230 240 250
    VSASALRFEG QITVYHYDGG PCYRCIFPQP PPAETVTNCA DGGVLGVVTG
    260 270 280 290 300
    VLGCLQALEV LKIAAGLGPS YSGSLLLFDA LRGHFRSIRL RSRRLDCAAC
    310 320 330 340 350
    GERPTVTDLL DYEAFCGSSA TDKCRSLQLL SPEERVSVTD YKRLLDSGAF
    360 370 380 390 400
    HLLLDVRPQV EVDICRLPHA LHIPLKHLER RDAESLKLLK EAIWEEKQGT
    410 420 430 440 450
    QEGAAVPIYV ICKLGNDSQK AVKILQSLSA AQELDPLTVR DVVGGLMAWA
    460
    AKIDGTFPQY
    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:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

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

    Protein-protein interaction databases

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

    PTM databases

    PhosphoSiteiO95396.

    Proteomic databases

    MaxQBiO95396.
    PaxDbiO95396.
    PeptideAtlasiO95396.
    PRIDEiO95396.

    Protocols and materials databases

    DNASUi27304.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi27304.
    GeneCardsiGC20P049575.
    HGNCiHGNC:15765. MOCS3.
    MIMi609277. gene.
    neXtProtiNX_O95396.
    PharmGKBiPA30904.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0476.
    GeneTreeiENSGT00800000124206.
    HOGENOMiHOG000281219.
    HOVERGENiHBG052491.
    InParanoidiO95396.
    KOiK11996.
    OMAiVRNPNEY.
    OrthoDBiEOG776SQ3.
    PhylomeDBiO95396.
    TreeFamiTF106103.

    Enzyme and pathway databases

    UniPathwayiUPA00344.
    UPA00988.
    BioCyciMetaCyc:HS04742-MONOMER.
    BRENDAi2.7.7.80. 2681.
    2.8.1.11. 2681.
    ReactomeiREACT_25073. Molybdenum cofactor biosynthesis.

    Miscellaneous databases

    EvolutionaryTraceiO95396.
    GeneWikiiMOCS3.
    GenomeRNAii27304.
    NextBioi50301.
    PROiO95396.
    SOURCEiSearch...

    Gene expression databases

    BgeeiO95396.
    CleanExiHS_MOCS3.
    GenevisibleiO95396. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: July 22, 2015
    This is version 139 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.