Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NYJ8

- TAB2_HUMAN

UniProt

Q9NYJ8 - TAB2_HUMAN

Protein

TGF-beta-activated kinase 1 and MAP3K7-binding protein 2

Gene

TAB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Adapter linking MAP3K7/TAK1 and TRAF6. Promotes MAP3K7 activation in the IL1 signaling pathway. The binding of 'Lys-63'-linked polyubiquitin chains to TAB2 promotes autophosphorylation of MAP3K7 at 'Thr-187'. Involved in heart development.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri663 – 69331RanBP2-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. K63-linked polyubiquitin binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. activation of MAPK activity Source: Reactome
    2. Fc-epsilon receptor signaling pathway Source: Reactome
    3. heart development Source: UniProtKB
    4. I-kappaB kinase/NF-kappaB signaling Source: Reactome
    5. innate immune response Source: Reactome
    6. JNK cascade Source: Reactome
    7. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    8. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    9. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
    10. nucleotide-binding oligomerization domain containing signaling pathway Source: Reactome
    11. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    12. positive regulation of NF-kappaB transcription factor activity Source: Reactome
    13. positive regulation of protein kinase activity Source: UniProtKB
    14. stress-activated MAPK cascade Source: Reactome
    15. T cell receptor signaling pathway Source: Reactome
    16. toll-like receptor 10 signaling pathway Source: Reactome
    17. toll-like receptor 2 signaling pathway Source: Reactome
    18. toll-like receptor 3 signaling pathway Source: Reactome
    19. toll-like receptor 4 signaling pathway Source: Reactome
    20. toll-like receptor 5 signaling pathway Source: Reactome
    21. toll-like receptor 9 signaling pathway Source: Reactome
    22. toll-like receptor signaling pathway Source: Reactome
    23. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    24. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    25. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_116022. Nuclear signaling by ERBB4.
    REACT_12555. Downstream TCR signaling.
    REACT_163994. FCERI mediated NF-kB activation.
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    REACT_21399. activated TAK1 mediates p38 MAPK activation.
    REACT_22442. Interleukin-1 signaling.
    REACT_25018. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
    REACT_25351. TRAF6 mediated induction of TAK1 complex.
    REACT_25380. IRAK2 mediated activation of TAK1 complex.
    REACT_75776. NOD1/2 Signaling Pathway.
    SignaLinkiQ9NYJ8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TGF-beta-activated kinase 1 and MAP3K7-binding protein 2
    Alternative name(s):
    Mitogen-activated protein kinase kinase kinase 7-interacting protein 2
    TAK1-binding protein 2
    Short name:
    TAB-2
    TGF-beta-activated kinase 1-binding protein 2
    Gene namesi
    Name:TAB2
    Synonyms:KIAA0733, MAP3K7IP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:17075. TAB2.

    Subcellular locationi

    Membrane 1 Publication; Peripheral membrane protein 1 Publication. Cytoplasmcytosol 1 Publication
    Note: Following IL1 stimulation, translocation occurs from the membrane to cytosol.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. endosome membrane Source: Reactome
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Congenital heart defects, multiple types, 2 (CHTD2) [MIM:614980]: A disease characterized by congenital developmental abnormalities involving structures of the heart. CHTD2 patients have left ventricular outflow tract obstruction, subaortic stenosis, residual aortic regurgitation, atrial fibrillation, bicuspid aortic valve and aortic dilation.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving TAB2 has been found in a family with congenital heart disease. Translocation t(2;6)(q21;q25).
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti208 – 2081P → S in CHTD2. 1 Publication
    Corresponds to variant rs267607101 [ dbSNP | Ensembl ].
    VAR_063774
    Natural varianti230 – 2301Q → K in CHTD2. 1 Publication
    Corresponds to variant rs267607100 [ dbSNP | Ensembl ].
    VAR_063775

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi675 – 6751F → A: Abolishes ubiquitin binding. 1 Publication
    Mutagenesisi678 – 6781H → A: Abolishes ubiquitin binding. 1 Publication
    Mutagenesisi681 – 6811L → A: Abolishes ubiquitin binding. 1 Publication
    Mutagenesisi685 – 6851E → A: Abolishes ubiquitin binding. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi614980. phenotype.
    PharmGKBiPA30605.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 693693TGF-beta-activated kinase 1 and MAP3K7-binding protein 2PRO_0000225695Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei372 – 3721Phosphoserine2 Publications
    Modified residuei450 – 4501Phosphoserine2 Publications
    Modified residuei524 – 5241Phosphoserine2 Publications

    Post-translational modificationi

    Ubiquitinated; following IL1 stimulation or TRAF6 overexpression. Ubiquitination involves RBCK1 leading to proteasomal degradation.2 Publications
    Phosphorylated.3 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9NYJ8.
    PaxDbiQ9NYJ8.
    PRIDEiQ9NYJ8.

    PTM databases

    PhosphoSiteiQ9NYJ8.

    Expressioni

    Tissue specificityi

    Widely expressed. In the embryo, expressed in the ventricular trabeculae, endothelial cells of the conotruncal cushions of the outflow tract and in the endothelial cells lining the developing aortic valves.2 Publications

    Gene expression databases

    ArrayExpressiQ9NYJ8.
    BgeeiQ9NYJ8.
    CleanExiHS_MAP3K7IP2.
    GenevestigatoriQ9NYJ8.

    Interactioni

    Subunit structurei

    Interacts with MAP3K7 and TRAF6. Identified in the TRIKA2 complex composed of MAP3K7, TAB1 and TAB2. Binds 'Lys-63'-linked polyubiquitin chains. Interacts with NCOR1 and HDAC3 to form a ternary complex. Interacts (via C-terminal) with NUMBL (via PTB domain). Interacts (via the C-terminus) with WDR34 (via WD domains). Interacts with RBCK1. Interacts with TRIM5.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BECN1Q1445711EBI-358708,EBI-949378
    MAP3K7O433185EBI-358708,EBI-358684
    MAP3K7O43318-22EBI-358708,EBI-358700
    TAB1Q157504EBI-358708,EBI-358643
    ZBTB16Q055163EBI-358708,EBI-711925

    Protein-protein interaction databases

    BioGridi116740. 72 interactions.
    DIPiDIP-27525N.
    IntActiQ9NYJ8. 30 interactions.
    MINTiMINT-1132340.

    Structurei

    Secondary structure

    1
    693
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 1910
    Beta strandi20 – 234
    Helixi25 – 328
    Turni33 – 364
    Helixi40 – 5314
    Turni54 – 563
    Turni671 – 6733
    Turni685 – 6873

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DAENMR-A7-68[»]
    2WWZX-ray1.40C662-693[»]
    2WX0X-ray2.40C/G663-693[»]
    2WX1X-ray3.00C663-693[»]
    ProteinModelPortaliQ9NYJ8.
    SMRiQ9NYJ8. Positions 5-70, 662-693.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NYJ8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 5144CUEPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni675 – 68511Interaction with polyubiquitinAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili532 – 61988Sequence AnalysisAdd
    BLAST

    Domaini

    The RanBP2-type zinc finger (NZF) mediates binding to two consecutive 'Lys-63'-linked ubiquitins.By similarity

    Sequence similaritiesi

    Contains 1 CUE domain.PROSITE-ProRule annotation
    Contains 1 RanBP2-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri663 – 69331RanBP2-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG47991.
    HOVERGENiHBG056952.
    InParanoidiQ9NYJ8.
    KOiK04404.
    OMAiVYHHGRE.
    OrthoDBiEOG776SPP.
    PhylomeDBiQ9NYJ8.
    TreeFamiTF332021.

    Family and domain databases

    InterProiIPR003892. CUE.
    IPR001876. Znf_RanBP2.
    [Graphical view]
    PfamiPF02845. CUE. 1 hit.
    PF00641. zf-RanBP. 1 hit.
    [Graphical view]
    SMARTiSM00546. CUE. 1 hit.
    SM00547. ZnF_RBZ. 1 hit.
    [Graphical view]
    PROSITEiPS51140. CUE. 1 hit.
    PS01358. ZF_RANBP2_1. 1 hit.
    PS50199. ZF_RANBP2_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NYJ8-1) [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

    MAQGSHQIDF QVLHDLRQKF PEVPEVVVSR CMLQNNNNLD ACCAVLSQES    50
    TRYLYGEGDL NFSDDSGISG LRNHMTSLNL DLQSQNIYHH GREGSRMNGS 100
    RTLTHSISDG QLQGGQSNSE LFQQEPQTAP AQVPQGFNVF GMSSSSGASN 150
    SAPHLGFHLG SKGTSSLSQQ TPRFNPIMVT LAPNIQTGRN TPTSLHIHGV 200
    PPPVLNSPQG NSIYIRPYIT TPGGTTRQTQ QHSGWVSQFN PMNPQQVYQP 250
    SQPGPWTTCP ASNPLSHTSS QQPNQQGHQT SHVYMPISSP TTSQPPTIHS 300
    SGSSQSSAHS QYNIQNISTG PRKNQIEIKL EPPQRNNSSK LRSSGPRTSS 350
    TSSSVNSQTL NRNQPTVYIA ASPPNTDELM SRSQPKVYIS ANAATGDEQV 400
    MRNQPTLFIS TNSGASAASR NMSGQVSMGP AFIHHHPPKS RAIGNNSATS 450
    PRVVVTQPNT KYTFKITVSP NKPPAVSPGV VSPTFELTNL LNHPDHYVET 500
    ENIQHLTDPT LAHVDRISET RKLSMGSDDA AYTQALLVHQ KARMERLQRE 550
    LEIQKKKLDK LKSEVNEMEN NLTRRRLKRS NSISQIPSLE EMQQLRSCNR 600
    QLQIDIDCLT KEIDLFQARG PHFNPSAIHN FYDNIGFVGP VPPKPKDQRS 650
    IIKTPKTQDT EDDEGAQWNC TACTFLNHPA LIRCEQCEMP RHF 693
    Length:693
    Mass (Da):76,494
    Last modified:October 1, 2000 - v1
    Checksum:i47BB8709320084D7
    GO
    Isoform 2 (identifier: Q9NYJ8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         535-536: AL → DI
         537-693: Missing.

    Show »
    Length:536
    Mass (Da):58,131
    Checksum:iD74074A216D23425
    GO

    Sequence cautioni

    The sequence BAA34453.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti196 – 1961H → R in CAG33668. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti208 – 2081P → S in CHTD2. 1 Publication
    Corresponds to variant rs267607101 [ dbSNP | Ensembl ].
    VAR_063774
    Natural varianti230 – 2301Q → K in CHTD2. 1 Publication
    Corresponds to variant rs267607100 [ dbSNP | Ensembl ].
    VAR_063775

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei535 – 5362AL → DI in isoform 2. 3 PublicationsVSP_017419
    Alternative sequencei537 – 693157Missing in isoform 2. 3 PublicationsVSP_017420Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF241230 mRNA. Translation: AAF67176.1.
    AB018276 mRNA. Translation: BAA34453.2. Different initiation.
    AK315038 mRNA. Translation: BAG37521.1.
    CR457387 mRNA. Translation: CAG33668.1.
    DQ314877 Genomic DNA. Translation: ABC40736.1.
    AL117407 mRNA. Translation: CAB55907.1.
    AL031133, AL138727, AL139103 Genomic DNA. Translation: CAI20026.1.
    AL139103, AL031133, AL138727 Genomic DNA. Translation: CAI20971.1.
    AL138727, AL031133, AL139103 Genomic DNA. Translation: CAI19581.1.
    CH471051 Genomic DNA. Translation: EAW47805.1.
    CH471051 Genomic DNA. Translation: EAW47806.1.
    CH471051 Genomic DNA. Translation: EAW47807.1.
    BC035910 mRNA. Translation: AAH35910.1.
    CCDSiCCDS5214.1. [Q9NYJ8-1]
    PIRiT17217.
    RefSeqiNP_055908.1. NM_015093.5. [Q9NYJ8-1]
    XP_006715466.1. XM_006715403.1. [Q9NYJ8-1]
    UniGeneiHs.269775.

    Genome annotation databases

    EnsembliENST00000367456; ENSP00000356426; ENSG00000055208. [Q9NYJ8-1]
    ENST00000470466; ENSP00000432709; ENSG00000055208. [Q9NYJ8-2]
    ENST00000538427; ENSP00000445752; ENSG00000055208. [Q9NYJ8-1]
    GeneIDi23118.
    KEGGihsa:23118.
    UCSCiuc003qmj.3. human. [Q9NYJ8-1]

    Polymorphism databases

    DMDMi74753070.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF241230 mRNA. Translation: AAF67176.1 .
    AB018276 mRNA. Translation: BAA34453.2 . Different initiation.
    AK315038 mRNA. Translation: BAG37521.1 .
    CR457387 mRNA. Translation: CAG33668.1 .
    DQ314877 Genomic DNA. Translation: ABC40736.1 .
    AL117407 mRNA. Translation: CAB55907.1 .
    AL031133 , AL138727 , AL139103 Genomic DNA. Translation: CAI20026.1 .
    AL139103 , AL031133 , AL138727 Genomic DNA. Translation: CAI20971.1 .
    AL138727 , AL031133 , AL139103 Genomic DNA. Translation: CAI19581.1 .
    CH471051 Genomic DNA. Translation: EAW47805.1 .
    CH471051 Genomic DNA. Translation: EAW47806.1 .
    CH471051 Genomic DNA. Translation: EAW47807.1 .
    BC035910 mRNA. Translation: AAH35910.1 .
    CCDSi CCDS5214.1. [Q9NYJ8-1 ]
    PIRi T17217.
    RefSeqi NP_055908.1. NM_015093.5. [Q9NYJ8-1 ]
    XP_006715466.1. XM_006715403.1. [Q9NYJ8-1 ]
    UniGenei Hs.269775.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DAE NMR - A 7-68 [» ]
    2WWZ X-ray 1.40 C 662-693 [» ]
    2WX0 X-ray 2.40 C/G 663-693 [» ]
    2WX1 X-ray 3.00 C 663-693 [» ]
    ProteinModelPortali Q9NYJ8.
    SMRi Q9NYJ8. Positions 5-70, 662-693.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116740. 72 interactions.
    DIPi DIP-27525N.
    IntActi Q9NYJ8. 30 interactions.
    MINTi MINT-1132340.

    PTM databases

    PhosphoSitei Q9NYJ8.

    Polymorphism databases

    DMDMi 74753070.

    Proteomic databases

    MaxQBi Q9NYJ8.
    PaxDbi Q9NYJ8.
    PRIDEi Q9NYJ8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367456 ; ENSP00000356426 ; ENSG00000055208 . [Q9NYJ8-1 ]
    ENST00000470466 ; ENSP00000432709 ; ENSG00000055208 . [Q9NYJ8-2 ]
    ENST00000538427 ; ENSP00000445752 ; ENSG00000055208 . [Q9NYJ8-1 ]
    GeneIDi 23118.
    KEGGi hsa:23118.
    UCSCi uc003qmj.3. human. [Q9NYJ8-1 ]

    Organism-specific databases

    CTDi 23118.
    GeneCardsi GC06P149543.
    HGNCi HGNC:17075. TAB2.
    MIMi 605101. gene.
    614980. phenotype.
    neXtProti NX_Q9NYJ8.
    PharmGKBi PA30605.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47991.
    HOVERGENi HBG056952.
    InParanoidi Q9NYJ8.
    KOi K04404.
    OMAi VYHHGRE.
    OrthoDBi EOG776SPP.
    PhylomeDBi Q9NYJ8.
    TreeFami TF332021.

    Enzyme and pathway databases

    Reactomei REACT_116022. Nuclear signaling by ERBB4.
    REACT_12555. Downstream TCR signaling.
    REACT_163994. FCERI mediated NF-kB activation.
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    REACT_21399. activated TAK1 mediates p38 MAPK activation.
    REACT_22442. Interleukin-1 signaling.
    REACT_25018. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
    REACT_25351. TRAF6 mediated induction of TAK1 complex.
    REACT_25380. IRAK2 mediated activation of TAK1 complex.
    REACT_75776. NOD1/2 Signaling Pathway.
    SignaLinki Q9NYJ8.

    Miscellaneous databases

    ChiTaRSi TAB2. human.
    EvolutionaryTracei Q9NYJ8.
    GeneWikii MAP3K7IP2.
    GenomeRNAii 23118.
    NextBioi 44335.
    PROi Q9NYJ8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NYJ8.
    Bgeei Q9NYJ8.
    CleanExi HS_MAP3K7IP2.
    Genevestigatori Q9NYJ8.

    Family and domain databases

    InterProi IPR003892. CUE.
    IPR001876. Znf_RanBP2.
    [Graphical view ]
    Pfami PF02845. CUE. 1 hit.
    PF00641. zf-RanBP. 1 hit.
    [Graphical view ]
    SMARTi SM00546. CUE. 1 hit.
    SM00547. ZnF_RBZ. 1 hit.
    [Graphical view ]
    PROSITEi PS51140. CUE. 1 hit.
    PS01358. ZF_RANBP2_1. 1 hit.
    PS50199. ZF_RANBP2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway."
      Takaesu G., Kishida S., Hiyama A., Yamaguchi K., Shibuya H., Irie K., Ninomiya-Tsuji J., Matsumoto K.
      Mol. Cell 5:649-658(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH TAK1 AND TRAF6.
      Tissue: Kidney.
    2. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    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: Testis.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    7. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    8. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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: Eye.
    11. "TAK1 is a ubiquitin-dependent kinase of MKK and IKK."
      Wang C., Deng L., Hong M., Akkaraju G.R., Inoue J., Chen Z.J.
      Nature 412:346-351(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, IDENTIFICATION IN THE TRIKA2 COMPLEX.
    12. "Role of the TAB2-related protein TAB3 in IL-1 and TNF signaling."
      Ishitani T., Takaesu G., Ninomiya-Tsuji J., Shibuya H., Gaynor R.B., Matsumoto K.
      EMBO J. 22:6277-6288(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
      Tissue: Kidney.
    13. "RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-triggered NF-kappaB activation by targeting TAB2/3 for degradation."
      Tian Y., Zhang Y., Zhong B., Wang Y.Y., Diao F.C., Wang R.P., Zhang M., Chen D.Y., Zhai Z.H., Shu H.B.
      J. Biol. Chem. 282:16776-16782(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH RBCK1.
    14. "NUMBL interacts with TAB2 and inhibits TNFalpha and IL-1beta-induced NF-kappaB activation."
      Ma Q., Zhou L., Shi H., Huo K.
      Cell. Signal. 20:1044-1051(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NUMBL.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "WDR34 is a novel TAK1-associated suppressor of the IL-1R/TLR3/TLR4-induced NF-kappaB activation pathway."
      Gao D., Wang R., Li B., Yang Y., Zhai Z., Chen D.Y.
      Cell. Mol. Life Sci. 66:2573-2584(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WDR34.
    17. "Direct activation of protein kinases by unanchored polyubiquitin chains."
      Xia Z.-P., Sun L., Chen X., Pineda G., Jiang X., Adhikari A., Zeng W., Chen Z.J.
      Nature 461:114-119(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH POLYUBIQUITIN.
    18. Cited for: FUNCTION IN HEART DEVELOPMENT, TISSUE SPECIFICITY, VARIANTS CHTD2 SER-208 AND LYS-230, CHROMOSOMAL TRANSLOCATION.
    19. "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-450 AND SER-524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: INTERACTION WITH TRIM5.
    22. "Solution structure of the N-terminal CUE domain in the human mitogen-activated protein kinase kinase kinase 7-interacting protein 2 (MAP3K7IP2)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (FEB-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 5-70.
    23. "Two-sided ubiquitin binding explains specificity of the TAB2 NZF domain."
      Kulathu Y., Akutsu M., Bremm A., Hofmann K., Komander D.
      Nat. Struct. Mol. Biol. 16:1328-1330(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 662-693 IN COMPLEX WITH POLYUBIQUITIN CHAINS, MUTAGENESIS OF PHE-675; HIS-678; LEU-681 AND GLU-685, SUBUNIT.

    Entry informationi

    Entry nameiTAB2_HUMAN
    AccessioniPrimary (citable) accession number: Q9NYJ8
    Secondary accession number(s): B2RCC4
    , E1P5A0, O94838, Q6I9W8, Q76N06, Q9UFP7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 7, 2006
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 130 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 6
      Human chromosome 6: 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