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O95400

- CD2B2_HUMAN

UniProt

O95400 - CD2B2_HUMAN

Protein

CD2 antigen cytoplasmic tail-binding protein 2

Gene

CD2BP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Involved in pre-mRNA splicing as component of the U5 snRNP complex that is involved in spliceosome assembly.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. ribonucleoprotein complex binding Source: BHF-UCL

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA splicing, via spliceosome Source: Reactome
    3. negative regulation of phosphatase activity Source: UniProtKB
    4. RNA splicing Source: Reactome
    5. spliceosomal tri-snRNP complex assembly Source: BHF-UCL

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Enzyme and pathway databases

    ReactomeiREACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CD2 antigen cytoplasmic tail-binding protein 2
    Short name:
    CD2 cytoplasmic domain-binding protein 2
    Short name:
    CD2 tail-binding protein 2
    Alternative name(s):
    U5 snRNP 52K protein
    Short name:
    U5-52K
    Gene namesi
    Name:CD2BP2
    Synonyms:KIAA1178
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:1656. CD2BP2.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Predominantly nuclear.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleoplasm Source: BHF-UCL
    3. nucleus Source: BHF-UCL
    4. U5 snRNP Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26209.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 341341CD2 antigen cytoplasmic tail-binding protein 2PRO_0000089437Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei44 – 441N6-acetyllysineBy similarity
    Modified residuei49 – 491Phosphoserine6 Publications
    Modified residuei118 – 1181Phosphoserine1 Publication
    Modified residuei194 – 1941Phosphoserine1 Publication
    Modified residuei195 – 1951Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO95400.
    PaxDbiO95400.
    PRIDEiO95400.

    PTM databases

    PhosphoSiteiO95400.

    Expressioni

    Gene expression databases

    ArrayExpressiO95400.
    BgeeiO95400.
    CleanExiHS_CD2BP2.
    GenevestigatoriO95400.

    Organism-specific databases

    HPAiHPA041508.

    Interactioni

    Subunit structurei

    Component of the U5 snRNP complex composed of the U5 snRNA and at least PRPF6, PRPF8, SNRNP200, EFTUD2, SNRNP40, DDX23, TXNL4A and CD2BP2. Interacts directly with TXNL4A and PRPF6. Interacts (via GYF domain) with CD2 (via Pro-rich sequence in the cytoplasmic domain). Interacts with PQBP1.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CD2P067293EBI-768015,EBI-3912464
    PPP1CAP621362EBI-768015,EBI-357253
    PRPF6O949064EBI-768015,EBI-536755
    TXNL4AP838762EBI-768015,EBI-746539

    Protein-protein interaction databases

    BioGridi115690. 52 interactions.
    IntActiO95400. 12 interactions.
    MINTiMINT-99472.
    STRINGi9606.ENSP00000304903.

    Structurei

    Secondary structure

    1
    341
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi282 – 29312
    Beta strandi296 – 3005
    Helixi301 – 3099
    Beta strandi318 – 3247
    Helixi332 – 3343
    Helixi337 – 3404

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GYFNMR-A280-341[»]
    1L2ZNMR-A280-341[»]
    1SYXX-ray2.34B/D/F262-341[»]
    4BWSX-ray2.50C/F280-341[»]
    ProteinModelPortaliO95400.
    SMRiO95400. Positions 280-341.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95400.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini280 – 33859GYFPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 GYF domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG301637.
    HOGENOMiHOG000007061.
    HOVERGENiHBG056920.
    InParanoidiO95400.
    KOiK13099.
    OMAiRDNWLDN.
    OrthoDBiEOG7VMP6C.
    PhylomeDBiO95400.
    TreeFamiTF313042.

    Family and domain databases

    Gene3Di3.30.1490.40. 1 hit.
    InterProiIPR003169. GYF.
    [Graphical view]
    PfamiPF02213. GYF. 1 hit.
    [Graphical view]
    SMARTiSM00444. GYF. 1 hit.
    [Graphical view]
    SUPFAMiSSF55277. SSF55277. 1 hit.
    PROSITEiPS50829. GYF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O95400-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKRKVTFQG VGDEEDEDEI IVPKKKLVDP VAGSGGPGSR FKGKHSLDSD    50
    EEEDDDDGGS SKYDILASED VEGQEAATLP SEGGVRITPF NLQEEMEEGH 100
    FDADGNYFLN RDAQIRDSWL DNIDWVKIRE RPPGQRQASD SEEEDSLGQT 150
    SMSAQALLEG LLELLLPRET VAGALRRLGA RGGGKGRKGP GQPSSPQRLD 200
    RLSGLADQMV ARGNLGVYQE TRERLAMRLK GLGCQTLGPH NPTPPPSLDM 250
    FAEELAEEEL ETPTPTQRGE AESRGDGLVD VMWEYKWENT GDAELYGPFT 300
    SAQMQTWVSE GYFPDGVYCR KLDPPGGQFY NSKRIDFDLY T 341
    Length:341
    Mass (Da):37,646
    Last modified:May 1, 1999 - v1
    Checksum:i8E9A7EE0C40474D5
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti231 – 2311G → D.
    Corresponds to variant rs13330462 [ dbSNP | Ensembl ].
    VAR_050772
    Natural varianti262 – 2621T → I.
    Corresponds to variant rs34391305 [ dbSNP | Ensembl ].
    VAR_050773

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF104222 mRNA. Translation: AAC84141.1.
    AK315708 mRNA. Translation: BAG38069.1.
    CH471192 Genomic DNA. Translation: EAW52260.1.
    BC000495 mRNA. Translation: AAH00495.1.
    BC001947 mRNA. Translation: AAH01947.1.
    AB033004 mRNA. Translation: BAA86492.1.
    CCDSiCCDS10675.1.
    RefSeqiNP_001230575.1. NM_001243646.1.
    NP_006101.1. NM_006110.2.
    UniGeneiHs.202677.

    Genome annotation databases

    EnsembliENST00000305596; ENSP00000304903; ENSG00000169217.
    ENST00000569466; ENSP00000456935; ENSG00000169217.
    GeneIDi10421.
    KEGGihsa:10421.
    UCSCiuc002dxr.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF104222 mRNA. Translation: AAC84141.1 .
    AK315708 mRNA. Translation: BAG38069.1 .
    CH471192 Genomic DNA. Translation: EAW52260.1 .
    BC000495 mRNA. Translation: AAH00495.1 .
    BC001947 mRNA. Translation: AAH01947.1 .
    AB033004 mRNA. Translation: BAA86492.1 .
    CCDSi CCDS10675.1.
    RefSeqi NP_001230575.1. NM_001243646.1.
    NP_006101.1. NM_006110.2.
    UniGenei Hs.202677.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GYF NMR - A 280-341 [» ]
    1L2Z NMR - A 280-341 [» ]
    1SYX X-ray 2.34 B/D/F 262-341 [» ]
    4BWS X-ray 2.50 C/F 280-341 [» ]
    ProteinModelPortali O95400.
    SMRi O95400. Positions 280-341.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115690. 52 interactions.
    IntActi O95400. 12 interactions.
    MINTi MINT-99472.
    STRINGi 9606.ENSP00000304903.

    PTM databases

    PhosphoSitei O95400.

    Proteomic databases

    MaxQBi O95400.
    PaxDbi O95400.
    PRIDEi O95400.

    Protocols and materials databases

    DNASUi 10421.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000305596 ; ENSP00000304903 ; ENSG00000169217 .
    ENST00000569466 ; ENSP00000456935 ; ENSG00000169217 .
    GeneIDi 10421.
    KEGGi hsa:10421.
    UCSCi uc002dxr.3. human.

    Organism-specific databases

    CTDi 10421.
    GeneCardsi GC16M030363.
    HGNCi HGNC:1656. CD2BP2.
    HPAi HPA041508.
    MIMi 604470. gene.
    neXtProti NX_O95400.
    PharmGKBi PA26209.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG301637.
    HOGENOMi HOG000007061.
    HOVERGENi HBG056920.
    InParanoidi O95400.
    KOi K13099.
    OMAi RDNWLDN.
    OrthoDBi EOG7VMP6C.
    PhylomeDBi O95400.
    TreeFami TF313042.

    Enzyme and pathway databases

    Reactomei REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    ChiTaRSi CD2BP2. human.
    EvolutionaryTracei O95400.
    GeneWikii CD2BP2.
    GenomeRNAii 10421.
    NextBioi 39496.
    PROi O95400.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95400.
    Bgeei O95400.
    CleanExi HS_CD2BP2.
    Genevestigatori O95400.

    Family and domain databases

    Gene3Di 3.30.1490.40. 1 hit.
    InterProi IPR003169. GYF.
    [Graphical view ]
    Pfami PF02213. GYF. 1 hit.
    [Graphical view ]
    SMARTi SM00444. GYF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55277. SSF55277. 1 hit.
    PROSITEi PS50829. GYF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation."
      Nishizawa K., Freund C., Li J., Wagner G., Reinherz E.L.
      Proc. Natl. Acad. Sci. U.S.A. 95:14897-14902(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CD2.
    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: Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Lung.
    5. "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
      Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
      DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 218-341.
      Tissue: Brain.
    6. "The human U5 snRNP 52K protein (CD2BP2) interacts with U5-102K (hPrp6), a U4/U6.U5 tri-snRNP bridging protein, but dissociates upon tri-snRNP formation."
      Laggerbauer B., Liu S., Makarov E., Vornlocher H.P., Makarova O., Ingelfinger D., Achsel T., Luhrmann R.
      RNA 11:598-608(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, INTERACTION WITH PRPF6 AND TXNL4A, SUBCELLULAR LOCATION.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP."
      Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.
      RNA 12:1418-1430(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    9. "Investigating the functional role of CD2BP2 in T cells."
      Heinze M., Kofler M., Freund C.
      Int. Immunol. 19:1313-1318(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
      Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
      Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    11. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-118; SER-194 AND SER-195, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences."
      Freund C., Dotsch V., Nishizawa K., Reinherz E.L., Wagner G.
      Nat. Struct. Biol. 6:656-660(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 280-341.
    18. "Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules."
      Freund C., Kuhne R., Yang H., Park S., Reinherz E.L., Wagner G.
      EMBO J. 21:5985-5995(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 280-341, INTERACTION WITH CD2 PEPTIDE, SUBCELLULAR LOCATION.
    19. "Structural basis for the bifunctionality of the U5 snRNP 52K protein (CD2BP2)."
      Nielsen T.K., Liu S., Luhrmann R., Ficner R.
      J. Mol. Biol. 369:902-908(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 256-341 IN COMPLEX WITH TXNL4A, INTERACTION WITH TXNL4A.
    20. "Mutations in the PQBP1 gene prevent its interaction with the spliceosomal protein U5-15 kD."
      Mizuguchi M., Obita T., Serita T., Kojima R., Nabeshima Y., Okazawa H.
      Nat. Commun. 5:3822-3822(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 280-341 IN COMPLEX WITH PQBP1 AND TXNL4A, SUBUNIT.

    Entry informationi

    Entry nameiCD2B2_HUMAN
    AccessioniPrimary (citable) accession number: O95400
    Secondary accession number(s): B2RDX2, Q9ULP2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2003
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 124 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, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3