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O88351

- IKKB_MOUSE

UniProt

O88351 - IKKB_MOUSE

Protein

Inhibitor of nuclear factor kappa-B kinase subunit beta

Gene

Ikbkb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE. IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Also phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation By similarity.By similarity

    Catalytic activityi

    ATP + [I-kappa-B protein] = ADP + [I-kappa-B phosphoprotein].

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei44 – 441ATPPROSITE-ProRule annotation
    Active sitei145 – 1451Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi21 – 299ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. IkappaB kinase activity Source: MGI
    3. protein binding Source: UniProtKB
    4. protein heterodimerization activity Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. protein kinase activity Source: UniProtKB
    7. receptor signaling protein serine/threonine kinase activity Source: MGI
    8. scaffold protein binding Source: MGI

    GO - Biological processi

    1. B cell homeostasis Source: MGI
    2. cellular response to tumor necrosis factor Source: UniProtKB
    3. I-kappaB phosphorylation Source: MGI
    4. positive regulation of cation channel activity Source: MGI
    5. positive regulation of NF-kappaB transcription factor activity Source: MGI
    6. positive regulation of sodium ion transport Source: MGI
    7. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    8. signal transduction by phosphorylation Source: GOC

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.10. 3474.
    ReactomeiREACT_198543. IRAK1 recruits IKK complex.
    REACT_198546. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
    REACT_199121. Activation of NF-kappaB in B cells.
    REACT_202898. TRAF6 mediated NF-kB activation.
    REACT_205561. FCERI mediated NF-kB activation.
    REACT_205717. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_211125. NOD1/2 Signaling Pathway.
    REACT_214670. p75NTR recruits signalling complexes.
    REACT_218887. NF-kB is activated and signals survival.
    REACT_219800. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_222971. RIP-mediated NFkB activation via ZBP1.
    REACT_224208. Interleukin-1 signaling.
    REACT_225145. Downstream TCR signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inhibitor of nuclear factor kappa-B kinase subunit beta (EC:2.7.11.10)
    Short name:
    I-kappa-B-kinase beta
    Short name:
    IKK-B
    Short name:
    IKK-beta
    Short name:
    IkBKB
    Alternative name(s):
    I-kappa-B kinase 2
    Short name:
    IKK2
    Nuclear factor NF-kappa-B inhibitor kinase beta
    Short name:
    NFKBIKB
    Gene namesi
    Name:Ikbkb
    Synonyms:Ikkb
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1338071. Ikbkb.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. Membrane raft By similarity
    Note: Colocalized with DPP4 in membrane rafts.By similarity

    GO - Cellular componenti

    1. CD40 receptor complex Source: BHF-UCL
    2. cytoplasm Source: MGI
    3. cytoplasmic side of plasma membrane Source: BHF-UCL
    4. membrane raft Source: UniProtKB-SubCell
    5. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice present extensive liver damage from apoptosis and die as embryos. They show a marked reduction in TNF-alpha and IL1-alpha-induced NF-kappa-B activity.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 757757Inhibitor of nuclear factor kappa-B kinase subunit betaPRO_0000086014Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei177 – 1771Phosphoserine; by TBK1 and PKC/PRKCZBy similarity
    Modified residuei179 – 1791S-nitrosocysteineBy similarity
    Modified residuei181 – 1811Phosphoserine; by TBK1, PKC/PRKCZ and PDPK1By similarity
    Modified residuei191 – 1911HydroxyprolineBy similarity
    Modified residuei670 – 6701Phosphoserine; by autocatalysisBy similarity
    Modified residuei672 – 6721Phosphoserine; by autocatalysisBy similarity
    Modified residuei675 – 6751Phosphoserine; by autocatalysisBy similarity
    Modified residuei682 – 6821Phosphoserine; by autocatalysisBy similarity
    Modified residuei689 – 6891Phosphoserine; by autocatalysisBy similarity
    Modified residuei692 – 6921Phosphoserine; by autocatalysisBy similarity
    Modified residuei697 – 6971Phosphoserine; by autocatalysisBy similarity
    Modified residuei705 – 7051Phosphoserine; by autocatalysisBy similarity
    Modified residuei733 – 7331Phosphoserine; by autocatalysisBy similarity
    Modified residuei740 – 7401Phosphoserine; by autocatalysisBy similarity

    Post-translational modificationi

    Upon cytokine stimulation, phosphorylated on Ser-177 and Ser-181 by MEKK1 and/or MAP3K14/NIK as well as TBK1 and PRKCZ; which enhances activity. Once activated, autophosphorylates on the C-terminal serine cluster; which decreases activity and prevents prolonged activation of the inflammatory response. Phosphorylated by the IKK-related kinases TBK1 and IKBKE, which is associated with reduced CHUK/IKKA and IKBKB activity and NF-kappa-B-dependent gene transcription. Dephosphorylated at Ser-177 and Ser-181 by PPM1A and PPM1B By similarity.By similarity
    Acetylation of Thr-180 by Yersinia yopJ prevents phosphorylation and activation, thus blocking the I-kappa-B pathway.By similarity
    Ubiquitinated. Monoubiquitination involves TRIM21 that leads to inhibition of Tax-induced NF-kappa-B signaling. 'Ser-163' may not serve as a monoubiquitination site. Ubiquitination on 'Ser-163' may modulate phosphorylation on C-terminal serine residues. Monoubiquitination by TRIM21 is disrupted by Yersinia yopJ By similarity.By similarity
    Hydroxylated by PHD1/EGLN2, loss of hydroxylation under hypoxic conditions results in activation of NF-kappaB.By similarity

    Keywords - PTMi

    Hydroxylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

    Proteomic databases

    MaxQBiO88351.
    PaxDbiO88351.
    PRIDEiO88351.

    PTM databases

    PhosphoSiteiO88351.

    Expressioni

    Tissue specificityi

    Expressed in liver, kidney and spleen.

    Developmental stagei

    While it is expressed ubiquitously throughout the mouse embryo, at E9.5 day its expression begins to be localized to the brain, neural ganglia, neural tube, and in liver at E12.5 day. At E15.5 day, the expression is further restricted to specific tissues of the embryo.1 Publication

    Gene expression databases

    ArrayExpressiO88351.
    BgeeiO88351.
    CleanExiMM_IKBKB.
    GenevestigatoriO88351.

    Interactioni

    Subunit structurei

    Component of the I-kappa-B-kinase (IKK) core complex consisting of CHUK, IKBKB and IKBKG; probably four alpha/CHUK-beta/IKBKB dimers are associated with four gamma/IKBKG subunits. The IKK core complex seems to associate with regulatory or adapter proteins to form a IKK-signalosome holo-complex. The IKK complex associates with TERF2IP/RAP1, leading to promote IKK-mediated phosphorylation of RELA/p65. Part of a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB, IKBKG and CREBBP. Part of a 70-90 kDa complex at least consisting of CHUK/IKKA, IKBKB, NFKBIA, RELA, IKBKAP and MAP3K14. Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB. Interacts with SQSTM1 through PRKCZ or PRKCI. Forms an NGF-induced complex with IKBKB, PRKCI and TRAF6. May interact with MAVS/IPS1. Interacts with NALP2. Interacts with TICAM1. Interacts with FAF1; the interaction disrupts the IKK complex formation. Interacts with ATM. Part of a ternary complex consisting of TANK, IKBKB and IKBKG. Interacts with NIBP; the interaction is direct. Interacts with ARRB1 and ARRB2. Interacts with TRIM21. Interacts with NLRC5; prevents IKBKB phosphorylation and kinase activity. Interacts with PDPK1. Interacts with EIF2AK2/PKR. The phosphorylated form interacts with PPM1A and PPM1B. Interacts with ZNF268; the interaction is further increased in a TNF-alpha-dependent manner. Interacts with IKBKE. Interacts with IKBKE. Interacts with NAA10, leading to NAA10 degradation By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ChukQ606804EBI-447960,EBI-646245
    Gnb2l1P680404EBI-447960,EBI-296749
    IkbkgO885223EBI-447960,EBI-998011
    KEAP1Q141452EBI-447960,EBI-751001From a different organism.

    Protein-protein interaction databases

    BioGridi200601. 20 interactions.
    DIPiDIP-29813N.
    IntActiO88351. 23 interactions.
    MINTiMINT-135217.

    Structurei

    3D structure databases

    ProteinModelPortaliO88351.
    SMRiO88351. Positions 2-663, 703-743.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini15 – 300286Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni458 – 47922Leucine-zipperAdd
    BLAST
    Regioni737 – 7426NEMO-binding

    Domaini

    The kinase domain is located in the N-terminal region. The leucine zipper is important to allow homo- and hetero-dimerization. At the C-terminal region is located the region responsible for the interaction with NEMO/IKBKG By similarity.By similarity

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. I-kappa-B kinase subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00530000063051.
    HOGENOMiHOG000038048.
    HOVERGENiHBG018241.
    InParanoidiO88351.
    KOiK07209.
    PhylomeDBiO88351.

    Family and domain databases

    InterProiIPR022007. IKKbetaNEMObind.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF12179. IKKbetaNEMObind. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O88351-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSWSPSLPTQ TCGAWEMKER LGTGGFGNVI RWHNQATGEQ IAIKQCRQEL    50
    SPKNRNRWCL EIQIMRRLNH PNVVAARDVP EGMQNLAPND LPLLAMEYCQ 100
    GGDLRRYLNQ FENCCGLREG AVLTLLSDIA SALRYLHENR IIHRDLKPEN 150
    IVLQQGEKRL IHKIIDLGYA KELDQGSLCT SFVGTLQYLA PELLEQQKYT 200
    VTVDYWSFGT LAFECITGFR PFLPNWQPVQ WHSKVRQKSE VDIVVSEDLN 250
    GAVKFSSSLP FPNNLNSVLA ERLEKWLQLM LMWHPRQRGT DPQYGPNGCF 300
    RALDDILNLK LVHVLNMVTG TVHTYPVTED ESLQSLKTRI QENTGILETD 350
    QELLQKAGLV LLPDKPATQC ISDSKTNEGL TLDMDLVFLL DNSKINYETQ 400
    ITPRPPPESV SCILQEPKRN LSFFQLRKVW GQVWHSIQTL KEDCNRLQQG 450
    QRAAMMSLLR NNSCLSKMKN AMASTAQQLK AKLDFFKTSI QIDLEKYKEQ 500
    TEFGITSDKL LLAWREMEQA VEQCGRENDV KHLVERMMAL QTDIVDLQRS 550
    PMGRKQGGTL DDLEEQAREL YRKLREKPRD QRTEGDSQEM VRLLLQAIQS 600
    FEKKVRVIYT QLSKTVVCKQ KALELLPKVE EVVSLMNEDE RTVVRLQEKR 650
    QKELWNLLKI ACSKVRGPVS GSPDSMNVSR LSHPGQLMSQ PSSACDSLPE 700
    SDKKSEELVA EAHALCSRLE SALQDTVKEQ DRSFTTLDWS WLQMEDEERC 750
    SLEQACD 757
    Length:757
    Mass (Da):86,690
    Last modified:November 1, 1998 - v1
    Checksum:iFED962F095449C5E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 561N → D in AAD52095. 1 PublicationCurated
    Sequence conflicti343 – 3431N → D in AAD52095. 1 PublicationCurated
    Sequence conflicti356 – 3561K → E in AAD52095. 1 PublicationCurated
    Sequence conflicti390 – 3901L → F in AAD52095. 1 PublicationCurated
    Sequence conflicti406 – 4061P → Q in AAD52095. 1 PublicationCurated
    Sequence conflicti573 – 5731K → R in AAD52095. 1 PublicationCurated
    Sequence conflicti736 – 75722TLDWS…EQACD → VTA1 PublicationCuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF026524 mRNA. Translation: AAC23557.1.
    AF088910 mRNA. Translation: AAD52095.1.
    CCDSiCCDS52522.1.
    RefSeqiNP_034676.1. NM_010546.2.
    UniGeneiMm.277886.

    Genome annotation databases

    EnsembliENSMUST00000063401; ENSMUSP00000064235; ENSMUSG00000031537.
    GeneIDi16150.
    KEGGimmu:16150.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF026524 mRNA. Translation: AAC23557.1 .
    AF088910 mRNA. Translation: AAD52095.1 .
    CCDSi CCDS52522.1.
    RefSeqi NP_034676.1. NM_010546.2.
    UniGenei Mm.277886.

    3D structure databases

    ProteinModelPortali O88351.
    SMRi O88351. Positions 2-663, 703-743.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200601. 20 interactions.
    DIPi DIP-29813N.
    IntActi O88351. 23 interactions.
    MINTi MINT-135217.

    Chemistry

    ChEMBLi CHEMBL6012.

    PTM databases

    PhosphoSitei O88351.

    Proteomic databases

    MaxQBi O88351.
    PaxDbi O88351.
    PRIDEi O88351.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000063401 ; ENSMUSP00000064235 ; ENSMUSG00000031537 .
    GeneIDi 16150.
    KEGGi mmu:16150.

    Organism-specific databases

    CTDi 3551.
    MGIi MGI:1338071. Ikbkb.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00530000063051.
    HOGENOMi HOG000038048.
    HOVERGENi HBG018241.
    InParanoidi O88351.
    KOi K07209.
    PhylomeDBi O88351.

    Enzyme and pathway databases

    BRENDAi 2.7.11.10. 3474.
    Reactomei REACT_198543. IRAK1 recruits IKK complex.
    REACT_198546. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
    REACT_199121. Activation of NF-kappaB in B cells.
    REACT_202898. TRAF6 mediated NF-kB activation.
    REACT_205561. FCERI mediated NF-kB activation.
    REACT_205717. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_211125. NOD1/2 Signaling Pathway.
    REACT_214670. p75NTR recruits signalling complexes.
    REACT_218887. NF-kB is activated and signals survival.
    REACT_219800. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_222971. RIP-mediated NFkB activation via ZBP1.
    REACT_224208. Interleukin-1 signaling.
    REACT_225145. Downstream TCR signaling.

    Miscellaneous databases

    NextBioi 288941.
    PROi O88351.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O88351.
    Bgeei O88351.
    CleanExi MM_IKBKB.
    Genevestigatori O88351.

    Family and domain databases

    InterProi IPR022007. IKKbetaNEMObind.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF12179. IKKbetaNEMObind. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Differential regulation of IkappaB kinase alpha and beta by two upstream kinases, NF-kappaB-inducing kinase and mitogen-activated protein kinase/ERK kinase kinase-1."
      Nakano H., Shindo M., Sakon S., Nishinaka S., Mihara M., Yagita H., Okumura K.
      Proc. Natl. Acad. Sci. U.S.A. 95:3537-3542(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION BY MEKK1.
      Strain: C57BL/6.
      Tissue: Spleen.
    2. "Murine IkB kinase-B, a developmentally regulated protein kinase that constitutively phosphorylates serine residues of IkB."
      Hu M.C.-T., Wang Y.-P., Mikhail A., Qiu W.R.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Embryonic lethality, liver degeneration, and impaired NF-kappa B activation in IKK-beta-deficient mice."
      Tanaka M., Fuentes M.E., Yamaguchi K., Durnin M.H., Dalrymple S.A., Hardy K.L., Goeddel D.V.
      Immunity 10:421-429(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    4. "Hematopoietic progenitor kinase-1 (HPK1) stress response signaling pathway activates IkappaB kinases (IKK-alpha/beta) and IKK-beta is a developmentally regulated protein kinase."
      Hu M.C.-T., Wang Y.-P., Qiu W.R., Mikhail A., Meyer C.F., Tan T.-H.
      Oncogene 18:5514-5524(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    5. "Coordinate regulation of IkappaB kinases by mitogen-activated protein kinase kinase kinase 1 and NF-kappaB-inducing kinase."
      Nemoto S., DiDonato J.A., Lin A.
      Mol. Cell. Biol. 18:7336-7343(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IKK PHOSPHORYLATION.
    6. "Severe liver degeneration in mice lacking the IkappaB kinase 2 gene."
      Li Q., Van Antwerp D., Mercurio F., Lee K.F., Verma I.M.
      Science 284:321-325(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    7. "The I kappa B/NF-kappa B system: a key determinant of mucosal inflammation and protection."
      Jobin C., Sartor R.B.
      Am. J. Physiol. 278:C451-C462(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    8. "PKR stimulates NF-kappaB irrespective of its kinase function by interacting with the IkappaB kinase complex."
      Bonnet M.C., Weil R., Dam E., Hovanessian A.G., Meurs E.F.
      Mol. Cell. Biol. 20:4532-4542(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF2AK2.
    9. Cited for: INTERACTION WITH TERF2IP.

    Entry informationi

    Entry nameiIKKB_MOUSE
    AccessioniPrimary (citable) accession number: O88351
    Secondary accession number(s): Q9R1J6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 136 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3