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Q10588

- BST1_HUMAN

UniProt

Q10588 - BST1_HUMAN

Protein

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2

Gene

BST1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger that elicits calcium release from intracellular stores. May be involved in pre-B-cell growth.1 Publication

    Catalytic activityi

    NAD+ + H2O = ADP-D-ribose + nicotinamide.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei109 – 1091Crucial for NAD binding and catalysis
    Sitei172 – 1721Crucial for NAD binding and catalysis
    Sitei210 – 2101Crucial for NAD binding and catalysis

    GO - Molecular functioni

    1. NAD(P)+ nucleosidase activity Source: UniProtKB-EC
    2. NAD+ nucleosidase activity Source: InterPro
    3. transferase activity Source: UniProtKB-KW

    GO - Biological processi

    1. humoral immune response Source: ProtInc
    2. multicellular organismal development Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Transferase

    Keywords - Ligandi

    NAD, NADP

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2 (EC:3.2.2.6)
    Alternative name(s):
    ADP-ribosyl cyclase 2
    Bone marrow stromal antigen 1
    Short name:
    BST-1
    Cyclic ADP-ribose hydrolase 2
    Short name:
    cADPr hydrolase 2
    CD_antigen: CD157
    Gene namesi
    Name:BST1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:1118. BST1.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. extracellular vesicular exosome Source: UniProt
    3. extrinsic component of membrane Source: ProtInc
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25435.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 293265ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2PRO_0000004032Add
    BLAST
    Propeptidei294 – 31825Removed in mature formSequence AnalysisPRO_0000004033Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi51 ↔ 67
    Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi83 ↔ 163
    Glycosylationi95 – 951N-linked (GlcNAc...)1 Publication
    Disulfide bondi144 ↔ 157
    Glycosylationi148 – 1481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi192 – 1921N-linked (GlcNAc...)1 Publication
    Disulfide bondi238 ↔ 259
    Disulfide bondi271 ↔ 280
    Lipidationi293 – 2931GPI-anchor amidated alanineSequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    MaxQBiQ10588.
    PaxDbiQ10588.
    PRIDEiQ10588.

    PTM databases

    PhosphoSiteiQ10588.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Gene expression databases

    ArrayExpressiQ10588.
    BgeeiQ10588.
    CleanExiHS_BST1.
    GenevestigatoriQ10588.

    Organism-specific databases

    HPAiHPA050121.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi107148. 2 interactions.
    IntActiQ10588. 1 interaction.
    STRINGi9606.ENSP00000265016.

    Structurei

    Secondary structure

    1
    318
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi43 – 5715
    Helixi60 – 623
    Helixi67 – 748
    Helixi75 – 784
    Helixi87 – 904
    Helixi91 – 977
    Beta strandi106 – 1116
    Helixi113 – 1208
    Turni121 – 1244
    Helixi129 – 1313
    Helixi133 – 1364
    Turni137 – 1404
    Beta strandi147 – 1526
    Beta strandi154 – 1574
    Turni160 – 1623
    Helixi167 – 18115
    Beta strandi185 – 1928
    Beta strandi202 – 2043
    Helixi205 – 2095
    Helixi211 – 2133
    Helixi216 – 2183
    Beta strandi219 – 2279
    Helixi242 – 25211
    Beta strandi257 – 2615
    Helixi264 – 2718
    Helixi278 – 2803

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ISFX-ray2.50A/B33-297[»]
    1ISGX-ray2.60A/B33-297[»]
    1ISHX-ray2.40A/B33-297[»]
    1ISIX-ray2.10A/B33-297[»]
    1ISJX-ray2.30A/B33-297[»]
    1ISMX-ray3.00A/B33-297[»]
    ProteinModelPortaliQ10588.
    SMRiQ10588. Positions 34-283.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ10588.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ADP-ribosyl cyclase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG42584.
    HOGENOMiHOG000293141.
    HOVERGENiHBG097049.
    KOiK18152.
    OrthoDBiEOG7RBZ9B.
    PhylomeDBiQ10588.
    TreeFamiTF332530.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR003193. ADP-ribosyl_cyclase.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR10912. PTHR10912. 1 hit.
    PfamiPF02267. Rib_hydrolayse. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q10588-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAQGCAASR LLQLLLQLLL LLLLLAAGGA RARWRGEGTS AHLRDIFLGR    50
    CAEYRALLSP EQRNKNCTAI WEAFKVALDK DPCSVLPSDY DLFINLSRHS 100
    IPRDKSLFWE NSHLLVNSFA DNTRRFMPLS DVLYGRVADF LSWCRQKNDS 150
    GLDYQSCPTS EDCENNPVDS FWKRASIQYS KDSSGVIHVM LNGSEPTGAY 200
    PIKGFFADYE IPNLQKEKIT RIEIWVMHEI GGPNVESCGE GSMKVLEKRL 250
    KDMGFQYSCI NDYRPVKLLQ CVDHSTHPDC ALKSAAAATQ RKAPSLYTEQ 300
    RAGLIIPLFL VLASRTQL 318
    Length:318
    Mass (Da):35,724
    Last modified:October 17, 2006 - v2
    Checksum:iE0DD04C89A8F4215
    GO
    Isoform 2 (identifier: Q10588-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         6-63: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:260
    Mass (Da):29,326
    Checksum:i143EE2A4949B11AB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti36 – 361G → A in BAA04885. (PubMed:8202488)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti77 – 771A → V.
    Corresponds to variant rs2302466 [ dbSNP | Ensembl ].
    VAR_028438
    Natural varianti101 – 1011I → V.
    Corresponds to variant rs6840615 [ dbSNP | Ensembl ].
    VAR_028439
    Natural varianti125 – 1251R → H.
    Corresponds to variant rs2302465 [ dbSNP | Ensembl ].
    VAR_021964
    Natural varianti145 – 1451R → Q.
    Corresponds to variant rs2302464 [ dbSNP | Ensembl ].
    VAR_021965

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei6 – 6358Missing in isoform 2. 1 PublicationVSP_055507Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D21878 mRNA. Translation: BAA04885.1.
    AB175627 mRNA. Translation: BAE92566.1.
    BT019502 mRNA. Translation: AAV38309.1.
    AK312497 mRNA. Translation: BAG35399.1.
    AC114744 Genomic DNA. Translation: AAY40930.1.
    CH471069 Genomic DNA. Translation: EAW92744.1.
    BC012095 mRNA. Translation: AAH12095.1.
    CCDSiCCDS3416.1.
    PIRiI59301.
    RefSeqiNP_004325.2. NM_004334.2.
    UniGeneiHs.720344.

    Genome annotation databases

    EnsembliENST00000265016; ENSP00000265016; ENSG00000109743. [Q10588-1]
    GeneIDi683.
    KEGGihsa:683.
    UCSCiuc003goh.4. human.

    Polymorphism databases

    DMDMi116241273.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D21878 mRNA. Translation: BAA04885.1 .
    AB175627 mRNA. Translation: BAE92566.1 .
    BT019502 mRNA. Translation: AAV38309.1 .
    AK312497 mRNA. Translation: BAG35399.1 .
    AC114744 Genomic DNA. Translation: AAY40930.1 .
    CH471069 Genomic DNA. Translation: EAW92744.1 .
    BC012095 mRNA. Translation: AAH12095.1 .
    CCDSi CCDS3416.1.
    PIRi I59301.
    RefSeqi NP_004325.2. NM_004334.2.
    UniGenei Hs.720344.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ISF X-ray 2.50 A/B 33-297 [» ]
    1ISG X-ray 2.60 A/B 33-297 [» ]
    1ISH X-ray 2.40 A/B 33-297 [» ]
    1ISI X-ray 2.10 A/B 33-297 [» ]
    1ISJ X-ray 2.30 A/B 33-297 [» ]
    1ISM X-ray 3.00 A/B 33-297 [» ]
    ProteinModelPortali Q10588.
    SMRi Q10588. Positions 34-283.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107148. 2 interactions.
    IntActi Q10588. 1 interaction.
    STRINGi 9606.ENSP00000265016.

    PTM databases

    PhosphoSitei Q10588.

    Polymorphism databases

    DMDMi 116241273.

    Proteomic databases

    MaxQBi Q10588.
    PaxDbi Q10588.
    PRIDEi Q10588.

    Protocols and materials databases

    DNASUi 683.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265016 ; ENSP00000265016 ; ENSG00000109743 . [Q10588-1 ]
    GeneIDi 683.
    KEGGi hsa:683.
    UCSCi uc003goh.4. human.

    Organism-specific databases

    CTDi 683.
    GeneCardsi GC04P015704.
    HGNCi HGNC:1118. BST1.
    HPAi HPA050121.
    MIMi 600387. gene.
    neXtProti NX_Q10588.
    PharmGKBi PA25435.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG42584.
    HOGENOMi HOG000293141.
    HOVERGENi HBG097049.
    KOi K18152.
    OrthoDBi EOG7RBZ9B.
    PhylomeDBi Q10588.
    TreeFami TF332530.

    Miscellaneous databases

    ChiTaRSi BST1. human.
    EvolutionaryTracei Q10588.
    GeneWikii BST1.
    GenomeRNAii 683.
    NextBioi 2812.
    PROi Q10588.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q10588.
    Bgeei Q10588.
    CleanExi HS_BST1.
    Genevestigatori Q10588.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR003193. ADP-ribosyl_cyclase.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR10912. PTHR10912. 1 hit.
    Pfami PF02267. Rib_hydrolayse. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "BST-1, a surface molecule of bone marrow stromal cell lines that facilitates pre-B-cell growth."
      Kaisho T., Ishikawa J., Oritani K., Inazawa J., Tomizawa H., Muraoka O., Ochi T., Hirano T.
      Proc. Natl. Acad. Sci. U.S.A. 91:5325-5329(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "BST1 mRNA, nirs splice variant 1."
      Tabata Y., Hayashi A., Mitsuyama M., Kanai S., Furuya T., Saito T.
      Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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] (ISOFORM 1).
      Tissue: Thalamus.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [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] (ISOFORM 1).
      Tissue: Lung.
    8. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-192.
      Tissue: Plasma.
    9. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-95.
      Tissue: Liver.
    10. "Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities."
      Yamamoto-Katayama S., Ariyoshi M., Ishihara K., Hirano T., Jingami H., Morikawa K.
      J. Mol. Biol. 316:711-723(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 33-297, FUNCTION.

    Entry informationi

    Entry nameiBST1_HUMAN
    AccessioniPrimary (citable) accession number: Q10588
    Secondary accession number(s): B2R6A2
    , Q1XII0, Q5U0K0, Q96EN3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 143 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 cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    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