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Q15653

- IKBB_HUMAN

UniProt

Q15653 - IKBB_HUMAN

Protein

NF-kappa-B inhibitor beta

Gene

NFKBIB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (04 Jan 2005)
      Previous versions | rss
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    Functioni

    Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. However, the unphosphorylated form resynthesized after cell stimulation is able to bind NF-kappa-B allowing its transport to the nucleus and protecting it to further NFKBIA-dependent inactivation. Association with inhibitor kappa B-interacting NKIRAS1 and NKIRAS2 prevent its phosphorylation rendering it more resistant to degradation, explaining its slower degradation.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. signal transducer activity Source: ProtInc
    3. transcription coactivator activity Source: ProtInc

    GO - Biological processi

    1. innate immune response Source: Reactome
    2. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    3. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    4. positive regulation of NF-kappaB transcription factor activity Source: Reactome
    5. positive regulation of type I interferon production Source: Reactome
    6. signal transduction Source: ProtInc
    7. toll-like receptor 10 signaling pathway Source: Reactome
    8. toll-like receptor 2 signaling pathway Source: Reactome
    9. toll-like receptor 3 signaling pathway Source: Reactome
    10. toll-like receptor 4 signaling pathway Source: Reactome
    11. toll-like receptor 5 signaling pathway Source: Reactome
    12. toll-like receptor 9 signaling pathway Source: Reactome
    13. toll-like receptor signaling pathway Source: Reactome
    14. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    15. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    16. transcription, DNA-templated Source: ProtInc
    17. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_24969. TRAF6 mediated NF-kB activation.
    SABIO-RKQ15653.
    SignaLinkiQ15653.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NF-kappa-B inhibitor beta
    Short name:
    NF-kappa-BIB
    Alternative name(s):
    I-kappa-B-beta
    Short name:
    IkB-B
    Short name:
    IkB-beta
    Short name:
    IkappaBbeta
    Thyroid receptor-interacting protein 9
    Short name:
    TR-interacting protein 9
    Short name:
    TRIP-9
    Gene namesi
    Name:NFKBIB
    Synonyms:IKBB, TRIP9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:7798. NFKBIB.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi19 – 191S → A: No degradation; when associated with A-23. 1 Publication
    Mutagenesisi23 – 231S → A: No degradation; when associated with A-19. 1 Publication

    Organism-specific databases

    PharmGKBiPA31602.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 356356NF-kappa-B inhibitor betaPRO_0000067004Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei19 – 191Phosphoserine; by RPS6KA11 Publication
    Modified residuei23 – 231Phosphoserine; by RPS6KA11 Publication
    Modified residuei313 – 3131Phosphoserine; by CK21 Publication
    Modified residuei315 – 3151Phosphoserine; by CK21 Publication

    Post-translational modificationi

    Phosphorylated by RPS6KA1; followed by degradation. Interaction with NKIRAS1 and NKIRAS2 probably prevents phosphorylation.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ15653.
    PaxDbiQ15653.
    PRIDEiQ15653.

    PTM databases

    PhosphoSiteiQ15653.

    Expressioni

    Tissue specificityi

    Expressed in all tissues examined.

    Gene expression databases

    ArrayExpressiQ15653.
    BgeeiQ15653.
    CleanExiHS_NFKBIB.
    GenevestigatoriQ15653.

    Organism-specific databases

    HPAiCAB010447.

    Interactioni

    Subunit structurei

    Interacts with THRB (via ligand-binding domain). Interacts with RELA and REL. Interacts with COMMD1 and inhibitor kappa B-interacting Ras-like NKIRAS1 and NKIRAS2.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FBXW11Q9UKB12EBI-352889,EBI-355189
    RELAQ042066EBI-352889,EBI-73886

    Protein-protein interaction databases

    BioGridi110860. 25 interactions.
    DIPiDIP-27532N.
    IntActiQ15653. 29 interactions.
    MINTiMINT-1131598.
    STRINGi9606.ENSP00000312988.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15653.
    SMRiQ15653. Positions 5-345.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati57 – 8630ANK 1Add
    BLAST
    Repeati93 – 12230ANK 2Add
    BLAST
    Repeati126 – 15530ANK 3Add
    BLAST
    Repeati206 – 23530ANK 4Add
    BLAST
    Repeati240 – 26930ANK 5Add
    BLAST
    Repeati273 – 30230ANK 6Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi186 – 19510Asp/Glu-rich (acidic)

    Sequence similaritiesi

    Belongs to the NF-kappa-B inhibitor family.Curated
    Contains 6 ANK repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiNOG272177.
    HOVERGENiHBG019039.
    KOiK02581.
    OMAiDEWCDSG.
    PhylomeDBiQ15653.
    TreeFamiTF320166.

    Family and domain databases

    Gene3Di1.25.40.20. 2 hits.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    [Graphical view]
    PfamiPF00023. Ank. 3 hits.
    PF12796. Ank_2. 1 hit.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    SMARTiSM00248. ANK. 6 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 4 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15653-1) [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

    MAGVACLGKA ADADEWCDSG LGSLGPDAAA PGGPGLGAEL GPGLSWAPLV    50
    FGYVTEDGDT ALHLAVIHQH EPFLDFLLGF SAGTEYMDLQ NDLGQTALHL 100
    AAILGETSTV EKLYAAGAGL CVAERRGHTA LHLACRVGAH ACARALLQPR 150
    PRRPREAPDT YLAQGPDRTP DTNHTPVALY PDSDLEKEEE ESEEDWKLQL 200
    EAENYEGHTP LHVAVIHKDV EMVRLLRDAG ADLDKPEPTC GRSPLHLAVE 250
    AQAADVLELL LRAGANPAAR MYGGRTPLGS AMLRPNPILA RLLRAHGAPE 300
    PEGEDEKSGP CSSSSDSDSG DEGDEYDDIV VHSSRSQTRL PPTPASKPLP 350
    DDPRPV 356
    Length:356
    Mass (Da):37,771
    Last modified:January 4, 2005 - v2
    Checksum:iE84575971B6F81CC
    GO
    Isoform 2 (identifier: Q15653-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         324-338: DEYDDIVVHSSRSQT → VSQEERQGSPAGGSG
         339-356: Missing.

    Show »
    Length:338
    Mass (Da):35,530
    Checksum:iF024666B851DF976
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 191S → T in AAC41742. (PubMed:7776974)Curated
    Sequence conflicti319 – 3191S → G in AAC41742. (PubMed:7776974)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti339 – 3391R → W.1 Publication
    Corresponds to variant rs17886215 [ dbSNP | Ensembl ].
    VAR_020771

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei324 – 33815DEYDD…SRSQT → VSQEERQGSPAGGSG in isoform 2. 2 PublicationsVSP_012409Add
    BLAST
    Alternative sequencei339 – 35618Missing in isoform 2. 2 PublicationsVSP_012410Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L40407 Genomic DNA. Translation: AAC41742.1.
    BT006743 mRNA. Translation: AAP35389.1.
    AY736284 Genomic DNA. Translation: AAU10088.1.
    AK290569 mRNA. Translation: BAF83258.1.
    CH471126 Genomic DNA. Translation: EAW56843.1.
    BC007197 mRNA. Translation: AAH07197.1.
    BC015528 mRNA. Translation: AAH15528.1.
    CCDSiCCDS12524.1. [Q15653-1]
    RefSeqiNP_001230045.1. NM_001243116.1.
    NP_002494.2. NM_002503.4. [Q15653-1]
    UniGeneiHs.9731.

    Genome annotation databases

    EnsembliENST00000313582; ENSP00000312988; ENSG00000104825. [Q15653-1]
    ENST00000572515; ENSP00000459728; ENSG00000104825. [Q15653-2]
    GeneIDi4793.
    KEGGihsa:4793.
    UCSCiuc002ojw.3. human. [Q15653-1]
    uc002ojy.3. human. [Q15653-2]

    Polymorphism databases

    DMDMi57015399.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L40407 Genomic DNA. Translation: AAC41742.1 .
    BT006743 mRNA. Translation: AAP35389.1 .
    AY736284 Genomic DNA. Translation: AAU10088.1 .
    AK290569 mRNA. Translation: BAF83258.1 .
    CH471126 Genomic DNA. Translation: EAW56843.1 .
    BC007197 mRNA. Translation: AAH07197.1 .
    BC015528 mRNA. Translation: AAH15528.1 .
    CCDSi CCDS12524.1. [Q15653-1 ]
    RefSeqi NP_001230045.1. NM_001243116.1.
    NP_002494.2. NM_002503.4. [Q15653-1 ]
    UniGenei Hs.9731.

    3D structure databases

    ProteinModelPortali Q15653.
    SMRi Q15653. Positions 5-345.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110860. 25 interactions.
    DIPi DIP-27532N.
    IntActi Q15653. 29 interactions.
    MINTi MINT-1131598.
    STRINGi 9606.ENSP00000312988.

    Chemistry

    BindingDBi Q15653.

    PTM databases

    PhosphoSitei Q15653.

    Polymorphism databases

    DMDMi 57015399.

    Proteomic databases

    MaxQBi Q15653.
    PaxDbi Q15653.
    PRIDEi Q15653.

    Protocols and materials databases

    DNASUi 4793.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313582 ; ENSP00000312988 ; ENSG00000104825 . [Q15653-1 ]
    ENST00000572515 ; ENSP00000459728 ; ENSG00000104825 . [Q15653-2 ]
    GeneIDi 4793.
    KEGGi hsa:4793.
    UCSCi uc002ojw.3. human. [Q15653-1 ]
    uc002ojy.3. human. [Q15653-2 ]

    Organism-specific databases

    CTDi 4793.
    GeneCardsi GC19P039390.
    HGNCi HGNC:7798. NFKBIB.
    HPAi CAB010447.
    MIMi 604495. gene.
    neXtProti NX_Q15653.
    PharmGKBi PA31602.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG272177.
    HOVERGENi HBG019039.
    KOi K02581.
    OMAi DEWCDSG.
    PhylomeDBi Q15653.
    TreeFami TF320166.

    Enzyme and pathway databases

    Reactomei REACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_24969. TRAF6 mediated NF-kB activation.
    SABIO-RK Q15653.
    SignaLinki Q15653.

    Miscellaneous databases

    ChiTaRSi NFKBIB. human.
    GeneWikii NFKBIB.
    GenomeRNAii 4793.
    NextBioi 18470.
    PROi Q15653.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15653.
    Bgeei Q15653.
    CleanExi HS_NFKBIB.
    Genevestigatori Q15653.

    Family and domain databases

    Gene3Di 1.25.40.20. 2 hits.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    [Graphical view ]
    Pfami PF00023. Ank. 3 hits.
    PF12796. Ank_2. 1 hit.
    [Graphical view ]
    PRINTSi PR01415. ANKYRIN.
    SMARTi SM00248. ANK. 6 hits.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor."
      Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.
      Mol. Endocrinol. 9:243-254(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2).
      Tissue: Cervix carcinoma.
    2. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. SeattleSNPs variation discovery resource
      Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TRP-339.
    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 2).
      Tissue: Lung.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 100-338 (ISOFORM 2).
      Tissue: Pancreas and Uterus.
    7. "Role of unphosphorylated, newly synthesized IkappaB beta in persistent activation of NF-kappaB."
      Suyang H., Phillips R.J., Douglas I., Ghosh S.
      Mol. Cell. Biol. 16:5444-5449(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    8. "A subclass of Ras proteins that regulate the degradation of IkappaB."
      Fenwick C., Na S.-Y., Voll R.E., Zhong H., Im S.-Y., Lee J.W., Ghosh S.
      Science 287:869-873(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NKIRAS1 AND NKIRAS2.
    9. "Mapping of the inducible IkappaB phosphorylation sites that signal its ubiquitination and degradation."
      DiDonato J.A., Mercurio F., Rosette C., Wu-Li J., Suyang H., Ghosh S., Karin M.
      Mol. Cell. Biol. 16:1295-1304(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-19 AND SER-23, PHOSPHORYLATION AT SER-19 AND SER-23.
    10. "Basal phosphorylation of the PEST domain in the I(kappa)B(beta) regulates its functional interaction with the c-rel proto-oncogene product."
      Chu Z.L., McKinsey T.A., Liu L., Qi X., Ballard D.W.
      Mol. Cell. Biol. 16:5974-5984(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-313 AND SER-315.
    11. "KappaB-Ras binds to the unique insert within the ankyrin repeat domain of IkappaBbeta and regulates cytoplasmic retention of IkappaBbeta.NF-kappaB complexes."
      Chen Y., Wu J., Ghosh G.
      J. Biol. Chem. 278:23101-23106(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NKIRAS1.
    12. "Inhibition of NF-kappaB activity by IkappaBbeta in association with kappaB-Ras."
      Chen Y., Vallee S., Wu J., Vu D., Sondek J., Ghosh G.
      Mol. Cell. Biol. 24:3048-3056(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NKIRAS1.
    13. "Characterization of COMMD protein-protein interactions in NF-kappaB signalling."
      de Bie P., van de Sluis B., Burstein E., Duran K.J., Berger R., Duckett C.S., Wijmenga C., Klomp L.W.
      Biochem. J. 398:63-71(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COMMD1.

    Entry informationi

    Entry nameiIKBB_HUMAN
    AccessioniPrimary (citable) accession number: Q15653
    Secondary accession number(s): A8K3F4, Q96BJ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 147 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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