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Q16762

- THTR_HUMAN

UniProt

Q16762 - THTR_HUMAN

Protein

Thiosulfate sulfurtransferase

Gene

TST

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Formation of iron-sulfur complexes, cyanide detoxification or modification of sulfur-containing enzymes. Other thiol compounds, besides cyanide, can act as sulfur ion acceptors. Also has weak mercaptopyruvate sulfurtransferase (MST) activity By similarity. Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA.By similarity2 Publications

    Catalytic activityi

    Thiosulfate + cyanide = sulfite + thiocyanate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei187 – 1871SubstrateBy similarity
    Active sitei248 – 2481Cysteine persulfide intermediatePROSITE-ProRule annotation
    Binding sitei250 – 2501SubstrateBy similarity

    GO - Molecular functioni

    1. 5S rRNA binding Source: UniProtKB
    2. thiosulfate sulfurtransferase activity Source: ProtInc

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. cyanate catabolic process Source: ProtInc
    3. epithelial cell differentiation Source: UniProt
    4. rRNA import into mitochondrion Source: UniProtKB
    5. rRNA transport Source: UniProtKB
    6. small molecule metabolic process Source: Reactome
    7. sulfide oxidation, using sulfide:quinone oxidoreductase Source: Reactome
    8. sulfur amino acid catabolic process Source: Reactome
    9. sulfur amino acid metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_116010. Sulfide oxidation to sulfate.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thiosulfate sulfurtransferase (EC:2.8.1.1)
    Alternative name(s):
    Rhodanese
    Gene namesi
    Name:TST
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:12388. TST.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProt
    2. extracellular vesicular exosome Source: UniProt
    3. mitochondrial inner membrane Source: Ensembl
    4. mitochondrial matrix Source: Reactome
    5. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37055.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 297296Thiosulfate sulfurtransferasePRO_0000139395Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141N6-acetyllysine; alternate1 Publication
    Modified residuei14 – 141N6-succinyllysine; alternateBy similarity
    Glycosylationi35 – 351O-linked (GlcNAc)By similarity
    Modified residuei136 – 1361N6-acetyllysine; alternateBy similarity
    Modified residuei136 – 1361N6-succinyllysine; alternateBy similarity
    Modified residuei163 – 1631N6-acetyllysineBy similarity
    Modified residuei175 – 1751N6-acetyllysine; alternateBy similarity
    Modified residuei175 – 1751N6-succinyllysine; alternateBy similarity
    Modified residuei224 – 2241N6-acetyllysine; alternateBy similarity
    Modified residuei224 – 2241N6-succinyllysine; alternateBy similarity
    Modified residuei236 – 2361N6-acetyllysineBy similarity
    Modified residuei237 – 2371N6-acetyllysine; alternateBy similarity
    Modified residuei237 – 2371N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation, Glycoprotein

    Proteomic databases

    MaxQBiQ16762.
    PaxDbiQ16762.
    PeptideAtlasiQ16762.
    PRIDEiQ16762.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00216293.

    PTM databases

    PhosphoSiteiQ16762.

    Expressioni

    Gene expression databases

    ArrayExpressiQ16762.
    BgeeiQ16762.
    CleanExiHS_TST.
    GenevestigatoriQ16762.

    Organism-specific databases

    HPAiCAB009546.
    HPA003044.
    HPA003643.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi113114. 13 interactions.
    IntActiQ16762. 2 interactions.
    STRINGi9606.ENSP00000249042.

    Structurei

    3D structure databases

    ProteinModelPortaliQ16762.
    SMRiQ16762. Positions 2-293.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 143119Rhodanese 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini173 – 288116Rhodanese 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni144 – 15916HingeAdd
    BLAST

    Domaini

    Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (By similarity).By similarity

    Sequence similaritiesi

    Contains 2 rhodanese domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG2897.
    HOGENOMiHOG000157237.
    HOVERGENiHBG002345.
    InParanoidiQ16762.
    KOiK01011.
    OMAiAPPEYPN.
    OrthoDBiEOG72ZCGB.
    PhylomeDBiQ16762.
    TreeFamiTF315133.

    Family and domain databases

    Gene3Di3.40.250.10. 2 hits.
    InterProiIPR001763. Rhodanese-like_dom.
    IPR001307. Thiosulphate_STrfase_CS.
    [Graphical view]
    PfamiPF00581. Rhodanese. 2 hits.
    [Graphical view]
    SMARTiSM00450. RHOD. 2 hits.
    [Graphical view]
    SUPFAMiSSF52821. SSF52821. 2 hits.
    PROSITEiPS00380. RHODANESE_1. 1 hit.
    PS00683. RHODANESE_2. 1 hit.
    PS50206. RHODANESE_3. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q16762-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVHQVLYRAL VSTKWLAESI RTGKLGPGLR VLDASWYSPG TREARKEYLE    50
    RHVPGASFFD IEECRDTASP YEMMLPSEAG FAEYVGRLGI SNHTHVVVYD 100
    GEHLGSFYAP RVWWMFRVFG HRTVSVLNGG FRNWLKEGHP VTSEPSRPEP 150
    AVFKATLDRS LLKTYEQVLE NLESKRFQLV DSRSQGRFLG TEPEPDAVGL 200
    DSGHIRGAVN MPFMDFLTED GFEKGPEELR ALFQTKKVDL SQPLIATCRK 250
    GVTACHVALA AYLCGKPDVA VYDGSWSEWF RRAPPESRVS QGKSEKA 297
    Length:297
    Mass (Da):33,429
    Last modified:January 23, 2007 - v4
    Checksum:iBDAE6EE4E47A5650
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti102 – 1021E → D.1 Publication
    Corresponds to variant rs35156365 [ dbSNP | Ensembl ].
    VAR_051799
    Natural varianti228 – 2281E → G.
    Corresponds to variant rs1049270 [ dbSNP | Ensembl ].
    VAR_051800

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D87292 mRNA. Translation: BAA13327.1.
    CR456598 mRNA. Translation: CAG30484.1.
    CR456998 mRNA. Translation: CAG33279.1.
    AK091874 mRNA. Translation: BAG52433.1.
    Z73420 Genomic DNA. Translation: CAA97762.1.
    CH471095 Genomic DNA. Translation: EAW60132.1.
    BC010148 mRNA. Translation: AAH10148.1.
    CCDSiCCDS13938.1.
    PIRiJC5286.
    RefSeqiNP_001257412.1. NM_001270483.1.
    NP_003303.2. NM_003312.5.
    UniGeneiHs.474783.

    Genome annotation databases

    EnsembliENST00000249042; ENSP00000249042; ENSG00000128311.
    ENST00000403892; ENSP00000385828; ENSG00000128311.
    GeneIDi7263.
    KEGGihsa:7263.
    UCSCiuc003aqg.4. human.

    Polymorphism databases

    DMDMi3122965.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D87292 mRNA. Translation: BAA13327.1 .
    CR456598 mRNA. Translation: CAG30484.1 .
    CR456998 mRNA. Translation: CAG33279.1 .
    AK091874 mRNA. Translation: BAG52433.1 .
    Z73420 Genomic DNA. Translation: CAA97762.1 .
    CH471095 Genomic DNA. Translation: EAW60132.1 .
    BC010148 mRNA. Translation: AAH10148.1 .
    CCDSi CCDS13938.1.
    PIRi JC5286.
    RefSeqi NP_001257412.1. NM_001270483.1.
    NP_003303.2. NM_003312.5.
    UniGenei Hs.474783.

    3D structure databases

    ProteinModelPortali Q16762.
    SMRi Q16762. Positions 2-293.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113114. 13 interactions.
    IntActi Q16762. 2 interactions.
    STRINGi 9606.ENSP00000249042.

    PTM databases

    PhosphoSitei Q16762.

    Polymorphism databases

    DMDMi 3122965.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00216293.

    Proteomic databases

    MaxQBi Q16762.
    PaxDbi Q16762.
    PeptideAtlasi Q16762.
    PRIDEi Q16762.

    Protocols and materials databases

    DNASUi 7263.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000249042 ; ENSP00000249042 ; ENSG00000128311 .
    ENST00000403892 ; ENSP00000385828 ; ENSG00000128311 .
    GeneIDi 7263.
    KEGGi hsa:7263.
    UCSCi uc003aqg.4. human.

    Organism-specific databases

    CTDi 7263.
    GeneCardsi GC22M037408.
    HGNCi HGNC:12388. TST.
    HPAi CAB009546.
    HPA003044.
    HPA003643.
    MIMi 180370. gene.
    neXtProti NX_Q16762.
    PharmGKBi PA37055.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2897.
    HOGENOMi HOG000157237.
    HOVERGENi HBG002345.
    InParanoidi Q16762.
    KOi K01011.
    OMAi APPEYPN.
    OrthoDBi EOG72ZCGB.
    PhylomeDBi Q16762.
    TreeFami TF315133.

    Enzyme and pathway databases

    Reactomei REACT_116010. Sulfide oxidation to sulfate.

    Miscellaneous databases

    GeneWikii TST_(gene).
    GenomeRNAii 7263.
    NextBioi 28395.
    PROi Q16762.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16762.
    Bgeei Q16762.
    CleanExi HS_TST.
    Genevestigatori Q16762.

    Family and domain databases

    Gene3Di 3.40.250.10. 2 hits.
    InterProi IPR001763. Rhodanese-like_dom.
    IPR001307. Thiosulphate_STrfase_CS.
    [Graphical view ]
    Pfami PF00581. Rhodanese. 2 hits.
    [Graphical view ]
    SMARTi SM00450. RHOD. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52821. SSF52821. 2 hits.
    PROSITEi PS00380. RHODANESE_1. 1 hit.
    PS00683. RHODANESE_2. 1 hit.
    PS50206. RHODANESE_3. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal liver.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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], VARIANT ASP-102.
    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: Kidney.
    5. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [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].
      Tissue: Uterus.
    8. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-8.
      Tissue: Platelet.
    9. "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-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Mitochondrial enzyme rhodanese is essential for 5 S ribosomal RNA import into human mitochondria."
      Smirnov A., Comte C., Mager-Heckel A.M., Addis V., Krasheninnikov I.A., Martin R.P., Entelis N., Tarassov I.
      J. Biol. Chem. 285:30792-30803(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Biological significance of 5S rRNA import into human mitochondria: role of ribosomal protein MRP-L18."
      Smirnov A., Entelis N., Martin R.P., Tarassov I.
      Genes Dev. 25:1289-1305(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING.

    Entry informationi

    Entry nameiTHTR_HUMAN
    AccessioniPrimary (citable) accession number: Q16762
    Secondary accession number(s): B3KRM1, Q6IB06
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 130 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 22
      Human chromosome 22: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3