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Q8TEA8

- DTD1_HUMAN

UniProt

Q8TEA8 - DTD1_HUMAN

Protein

D-tyrosyl-tRNA(Tyr) deacylase 1

Gene

DTD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (28 Mar 2003)
      Previous versions | rss
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    Functioni

    ATPase involved in DNA replication, may facilitate loading of CDC45 onto pre-replication complexes. May hydrolyze D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr), a possible defense mechanism against a harmful effect of D-tyrosine.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi4 – 41Magnesium; via carbonyl oxygen
    Metal bindingi6 – 61Magnesium
    Metal bindingi28 – 281Magnesium; via carbonyl oxygen
    Active sitei81 – 811NucleophileBy similarity

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. hydrolase activity, acting on ester bonds Source: InterPro
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. D-amino acid catabolic process Source: InterPro
    2. DNA replication Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    DNA-binding, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-tyrosyl-tRNA(Tyr) deacylase 1 (EC:3.1.-.-)
    Alternative name(s):
    DNA-unwinding element-binding protein B
    Short name:
    DUE-B
    Histidyl-tRNA synthase-related
    Gene namesi
    Name:DTD1
    Synonyms:C20orf88, DUEB, HARS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:16219. DTD1.

    Subcellular locationi

    Nucleus 2 Publications. Cytoplasm Curated
    Note: Associated with chromatin at some replication origins containing functional DNA-unwinding elements.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162384107.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 209209D-tyrosyl-tRNA(Tyr) deacylase 1PRO_0000164626Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei197 – 1971Phosphoserine3 Publications
    Modified residuei205 – 2051Phosphoserine2 Publications

    Post-translational modificationi

    Preferentially phosphorylated in cells arrested early in S phase. Phosphorylation in the C-terminus weakens the interaction with CDC45.5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8TEA8.
    PaxDbiQ8TEA8.
    PeptideAtlasiQ8TEA8.
    PRIDEiQ8TEA8.

    PTM databases

    PhosphoSiteiQ8TEA8.

    Expressioni

    Tissue specificityi

    Expressed in many adult and fetal tissues. Highest levels in testis, ovary, spleen and in adult and fetal brain.1 Publication

    Gene expression databases

    BgeeiQ8TEA8.
    CleanExiHS_DTD1.
    HS_HARS2.
    GenevestigatoriQ8TEA8.

    Organism-specific databases

    HPAiHPA040981.
    HPA042653.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with CDC45 and TOPBP1.2 Publications

    Protein-protein interaction databases

    BioGridi124965. 7 interactions.
    IntActiQ8TEA8. 1 interaction.
    STRINGi9606.ENSP00000366672.

    Structurei

    Secondary structure

    1
    209
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 1514
    Beta strandi18 – 3215
    Helixi39 – 5113
    Helixi67 – 704
    Beta strandi73 – 786
    Helixi80 – 823
    Beta strandi87 – 904
    Helixi99 – 11618
    Helixi119 – 1213
    Beta strandi122 – 1243
    Beta strandi131 – 14616

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OKVX-ray2.00A/B/C/D1-209[»]
    ProteinModelPortaliQ8TEA8.
    SMRiQ8TEA8. Positions 1-150.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8TEA8.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DTD family.Curated

    Phylogenomic databases

    eggNOGiCOG1490.
    HOVERGENiHBG039436.
    InParanoidiQ8TEA8.
    KOiK07560.
    OMAiGDENDKM.
    OrthoDBiEOG7SR4P0.
    PhylomeDBiQ8TEA8.
    TreeFamiTF314886.

    Family and domain databases

    Gene3Di3.50.80.10. 1 hit.
    HAMAPiMF_00518. Tyr_Deacylase_Dtd.
    InterProiIPR023509. DTD-like_dom.
    IPR003732. DTyrtRNA_deacyls.
    [Graphical view]
    PANTHERiPTHR10472. PTHR10472. 1 hit.
    PfamiPF02580. Tyr_Deacylase. 1 hit.
    [Graphical view]
    SUPFAMiSSF69500. SSF69500. 1 hit.
    TIGRFAMsiTIGR00256. TIGR00256. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8TEA8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKAVVQRVTR ASVTVGGEQI SAIGRGICVL LGISLEDTQK ELEHMVRKIL    50
    NLRVFEDESG KHWSKSVMDK QYEILCVSQF TLQCVLKGNK PDFHLAMPTE 100
    QAEGFYNSFL EQLRKTYRPE LIKDGKFGAY MQVHIQNDGP VTIELESPAP 150
    GTATSDPKQL SKLEKQQQRK EKTRAKGPSE SSKERNTPRK EDRSASSGAE 200
    GDVSSEREP 209
    Length:209
    Mass (Da):23,424
    Last modified:March 28, 2003 - v2
    Checksum:iF006ED14974ACC92
    GO

    Sequence cautioni

    The sequence BAB85044.1 differs from that shown. Reason: Presence of Alu-repeat DNA.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 941H → N in AAH45167. (PubMed:15489334)Curated
    Sequence conflicti134 – 1341H → R in AAL57046. (PubMed:12392168)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF332356 mRNA. Translation: AAL57046.1.
    AK074304 mRNA. Translation: BAB85044.1. Sequence problems.
    AK291440 mRNA. Translation: BAF84129.1.
    AL121900, AL121780 Genomic DNA. Translation: CAH73147.1.
    AL121780, AL121900 Genomic DNA. Translation: CAI15669.1.
    CH471133 Genomic DNA. Translation: EAX10227.1.
    BC000599 mRNA. No translation available.
    CH471133 Genomic DNA. Translation: EAX10228.1.
    BC045167 mRNA. Translation: AAH45167.1.
    BC100923 mRNA. Translation: AAI00924.1.
    BC100924 mRNA. Translation: AAI00925.1.
    BC100925 mRNA. Translation: AAI00926.1.
    CCDSiCCDS13138.1.
    RefSeqiNP_543010.3. NM_080820.4.
    UniGeneiHs.659442.

    Genome annotation databases

    EnsembliENST00000377452; ENSP00000366672; ENSG00000125821.
    GeneIDi92675.
    KEGGihsa:92675.
    UCSCiuc002wrf.4. human.

    Polymorphism databases

    DMDMi29427856.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF332356 mRNA. Translation: AAL57046.1 .
    AK074304 mRNA. Translation: BAB85044.1 . Sequence problems.
    AK291440 mRNA. Translation: BAF84129.1 .
    AL121900 , AL121780 Genomic DNA. Translation: CAH73147.1 .
    AL121780 , AL121900 Genomic DNA. Translation: CAI15669.1 .
    CH471133 Genomic DNA. Translation: EAX10227.1 .
    BC000599 mRNA. No translation available.
    CH471133 Genomic DNA. Translation: EAX10228.1 .
    BC045167 mRNA. Translation: AAH45167.1 .
    BC100923 mRNA. Translation: AAI00924.1 .
    BC100924 mRNA. Translation: AAI00925.1 .
    BC100925 mRNA. Translation: AAI00926.1 .
    CCDSi CCDS13138.1.
    RefSeqi NP_543010.3. NM_080820.4.
    UniGenei Hs.659442.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2OKV X-ray 2.00 A/B/C/D 1-209 [» ]
    ProteinModelPortali Q8TEA8.
    SMRi Q8TEA8. Positions 1-150.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124965. 7 interactions.
    IntActi Q8TEA8. 1 interaction.
    STRINGi 9606.ENSP00000366672.

    PTM databases

    PhosphoSitei Q8TEA8.

    Polymorphism databases

    DMDMi 29427856.

    Proteomic databases

    MaxQBi Q8TEA8.
    PaxDbi Q8TEA8.
    PeptideAtlasi Q8TEA8.
    PRIDEi Q8TEA8.

    Protocols and materials databases

    DNASUi 92675.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377452 ; ENSP00000366672 ; ENSG00000125821 .
    GeneIDi 92675.
    KEGGi hsa:92675.
    UCSCi uc002wrf.4. human.

    Organism-specific databases

    CTDi 92675.
    GeneCardsi GC20P018568.
    HGNCi HGNC:16219. DTD1.
    HPAi HPA040981.
    HPA042653.
    MIMi 610996. gene.
    neXtProti NX_Q8TEA8.
    PharmGKBi PA162384107.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1490.
    HOVERGENi HBG039436.
    InParanoidi Q8TEA8.
    KOi K07560.
    OMAi GDENDKM.
    OrthoDBi EOG7SR4P0.
    PhylomeDBi Q8TEA8.
    TreeFami TF314886.

    Miscellaneous databases

    ChiTaRSi DTD1. human.
    EvolutionaryTracei Q8TEA8.
    GenomeRNAii 92675.
    NextBioi 77831.
    PROi Q8TEA8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8TEA8.
    CleanExi HS_DTD1.
    HS_HARS2.
    Genevestigatori Q8TEA8.

    Family and domain databases

    Gene3Di 3.50.80.10. 1 hit.
    HAMAPi MF_00518. Tyr_Deacylase_Dtd.
    InterProi IPR023509. DTD-like_dom.
    IPR003732. DTyrtRNA_deacyls.
    [Graphical view ]
    PANTHERi PTHR10472. PTHR10472. 1 hit.
    Pfami PF02580. Tyr_Deacylase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69500. SSF69500. 1 hit.
    TIGRFAMsi TIGR00256. TIGR00256. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and identification of a novel cDNA which may be associated with FKBP25."
      Meng X.X., Chen J.J., Yang Q.Q., Wang S., Chao Y., Ying K., Xie Y., Mao Y.
      Biochem. Genet. 40:303-310(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Fetal brain.
    2. "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: Brain and Hepatoma.
    3. "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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Brain and Skin.
    6. "The c-myc DNA-unwinding element-binding protein modulates the assembly of DNA replication complexes in vitro."
      Casper J.M., Kemp M.G., Ghosh M., Randall G.M., Vaillant A., Leffak M.
      J. Biol. Chem. 280:13071-13083(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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-197 AND SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "The DNA unwinding element binding protein DUE-B interacts with Cdc45 in preinitiation complex formation."
      Chowdhury A., Liu G., Kemp M., Chen X., Katrangi N., Myers S., Ghosh M., Yao J., Gao Y., Bubulya P., Leffak M.
      Mol. Cell. Biol. 30:1495-1507(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH CDC45 AND TOPBP1.
    12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Structure and function of the c-myc DNA-unwinding element-binding protein DUE-B."
      Kemp M., Bae B., Yu J.P., Ghosh M., Leffak M., Nair S.K.
      J. Biol. Chem. 282:10441-10448(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT, MAGNESIUM-BINDING SITES.

    Entry informationi

    Entry nameiDTD1_HUMAN
    AccessioniPrimary (citable) accession number: Q8TEA8
    Secondary accession number(s): A8K5X5
    , D3DW37, Q496D1, Q5W184, Q8WXU8, Q9BW67, Q9H464, Q9H474
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 28, 2003
    Last sequence update: March 28, 2003
    Last modified: October 1, 2014
    This is version 110 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3