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Q92844

- TANK_HUMAN

UniProt

Q92844 - TANK_HUMAN

Protein

TRAF family member-associated NF-kappa-B activator

Gene

TANK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (03 Apr 2007)
      Previous versions | rss
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    Functioni

    Adapter protein involved in I-kappa-B-kinase (IKK) regulation which constitutively binds TBK1 and IKBKE playing a role in antiviral innate immunity. Acts as a regulator of TRAF function by maintaining them in a latent state. Blocks TRAF2 binding to LMP1 and inhibits LMP1-mediated NF-kappa-B activation. May control negatively TRAF2-mediated NF-kappa-B activation signaled by CD40, TNFR1 and TNFR2.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri394 – 42027C2H2-typeAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    2. innate immune response Source: Reactome
    3. signal transduction Source: ProtInc

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_24938. TRAF6 mediated IRF7 activation.
    SignaLinkiQ92844.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TRAF family member-associated NF-kappa-B activator
    Alternative name(s):
    TRAF-interacting protein
    Short name:
    I-TRAF
    Gene namesi
    Name:TANK
    Synonyms:ITRAF, TRAF2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:11562. TANK.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi182 – 1821Q → A: Abolishes interaction with TRAF2 and TRAF3. 1 Publication
    Mutagenesisi184 – 1841T → A: Abolishes interaction with TRAF2 and TRAF3. 1 Publication
    Mutagenesisi185 – 1851D → A: Abolishes interaction with TRAF2; greatly diminishes interaction with TRAF3. 1 Publication
    Mutagenesisi188 – 1881D → A: Diminishes interaction with TRAF2 and TRAF3. 1 Publication
    Mutagenesisi194 – 1941F → A: Diminishes interaction with TRAF2 and TRAF3. 1 Publication

    Organism-specific databases

    PharmGKBiPA36330.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 425425TRAF family member-associated NF-kappa-B activatorPRO_0000072427Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei126 – 1261Phosphoserine2 Publications
    Modified residuei129 – 1291Phosphoserine4 Publications
    Modified residuei341 – 3411Phosphoserine2 Publications
    Modified residuei354 – 3541Phosphoserine2 Publications
    Modified residuei357 – 3571Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated by IKBKE.4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ92844.
    PaxDbiQ92844.
    PeptideAtlasiQ92844.
    PRIDEiQ92844.

    PTM databases

    PhosphoSiteiQ92844.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ92844.
    BgeeiQ92844.
    CleanExiHS_TANK.
    HS_TRAF2.
    GenevestigatoriQ92844.

    Organism-specific databases

    HPAiCAB010345.
    HPA037676.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with TBK1 and IKBKE. Interacts also with TRAF1, TRAF2, and TRAF3 by binding to their TRAF-C domains; the interaction with TRAF2 is disrupted by the phosphorylation of TANK by IKBKE. Interacts more strongly with TRAF1 and TRAF2 than TRAF3. Interacts with IKBKG; the interaction is enhanced by IKBKE and TBK1. Part of a ternary complex consisting of TANK, IKBKB and IKBKG.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APBA3O960182EBI-356349,EBI-6115839
    HTTP428583EBI-356349,EBI-466029
    IKBKEQ141642EBI-356349,EBI-307369
    NSP034952EBI-356349,EBI-2548993From a different organism.
    PLK1P533503EBI-356349,EBI-476768
    SUMO1P631658EBI-356349,EBI-80140
    SUMO2P619563EBI-356349,EBI-473220
    TBK1Q9UHD26EBI-356349,EBI-356402
    TRAF2Q129334EBI-356349,EBI-355744
    TRAF3Q131144EBI-356349,EBI-357631

    Protein-protein interaction databases

    BioGridi115328. 39 interactions.
    DIPiDIP-27516N.
    IntActiQ92844. 31 interactions.
    MINTiMINT-111947.
    STRINGi9606.ENSP00000259075.

    Structurei

    Secondary structure

    1
    425
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi191 – 1933

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KZZX-ray3.50B177-187[»]
    1L0AX-ray2.90B178-195[»]
    ProteinModelPortaliQ92844.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92844.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni133 – 17240Interaction with TBK1 and IKBKEBy similarityAdd
    BLAST
    Regioni172 – 19120TRAF family member interactionAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili22 – 6241Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 C2H2-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri394 – 42027C2H2-typeAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG44252.
    HOGENOMiHOG000231816.
    HOVERGENiHBG019299.
    InParanoidiQ92844.
    KOiK12650.
    OMAiLHSTPER.
    OrthoDBiEOG7ZKSBN.
    PhylomeDBiQ92844.
    TreeFamiTF336453.

    Family and domain databases

    InterProiIPR024581. TBD.
    [Graphical view]
    PfamiPF12845. TBD. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q92844-1) [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

    MDKNIGEQLN KAYEAFRQAC MDRDSAVKEL QQKTENYEQR IREQQEQLSL    50
    QQTIIDKLKS QLLLVNSTQD NNYGCVPLLE DSETRKNNLT LDQPQDKVIS 100
    GIAREKLPKV RRQEVSSPRK ETSARSLGSP LLHERGNIEK TFWDLKEEFH 150
    KICMLAKAQK DHLSKLNIPD TATETQCSVP IQCTDKTDKQ EALFKPQAKD 200
    DINRGAPSIT SVTPRGLCRD EEDTSFESLS KFNVKFPPMD NDSTFLHSTP 250
    ERPGILSPAT SEAVCQEKFN MEFRDNPGNF VKTEETLFEI QGIDPIASAI 300
    QNLKTTDKTK PSNLVNTCIR TTLDRAACLP PGDHNALYVN SFPLLDPSDA 350
    PFPSLDSPGK AIRGPQQPIW KPFPNQDSDS VVLSGTDSEL HIPRVCEFCQ 400
    AVFPPSITSR GDFLRHLNSH FNGET 425
    Length:425
    Mass (Da):47,816
    Last modified:April 3, 2007 - v2
    Checksum:i718D30CF03EB27FF
    GO
    Isoform Short (identifier: Q92844-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         111-117: RRQEVSS → DIASAES
         118-425: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:117
    Mass (Da):13,426
    Checksum:i22A8BEC63333011C
    GO
    Isoform 3 (identifier: Q92844-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         111-119: RRQEVSSPR → DIASAESSI
         120-425: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:119
    Mass (Da):13,626
    Checksum:i61E5B2A8BEC63333
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti83 – 831E → D in AAC50681. (PubMed:8710854)Curated
    Sequence conflicti88 – 881N → T in AAC50681. (PubMed:8710854)Curated
    Sequence conflicti92 – 921D → A in AAC50681. (PubMed:8710854)Curated
    Sequence conflicti142 – 1421F → S in AAC50681. (PubMed:8710854)Curated
    Sequence conflicti195 – 1951K → T in AAC50681. (PubMed:8710854)Curated
    Sequence conflicti226 – 2261F → L in AAC50681. (PubMed:8710854)Curated
    Sequence conflicti303 – 3031L → P in AAC50770. (PubMed:8855313)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti292 – 2921G → R.
    Corresponds to variant rs10183668 [ dbSNP | Ensembl ].
    VAR_051409
    Natural varianti358 – 3581P → L.
    Corresponds to variant rs2229759 [ dbSNP | Ensembl ].
    VAR_051410
    Natural varianti394 – 3941R → Q.
    Corresponds to variant rs3769969 [ dbSNP | Ensembl ].
    VAR_051411

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei111 – 1199RRQEVSSPR → DIASAESSI in isoform 3. 1 PublicationVSP_043702
    Alternative sequencei111 – 1177RRQEVSS → DIASAES in isoform Short. 1 PublicationVSP_004442
    Alternative sequencei118 – 425308Missing in isoform Short. 1 PublicationVSP_004443Add
    BLAST
    Alternative sequencei120 – 425306Missing in isoform 3. 1 PublicationVSP_043703Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59863 mRNA. Translation: AAC50681.1.
    U63830 mRNA. Translation: AAC50770.1.
    BT009855 mRNA. Translation: AAP88857.1.
    AC009299 Genomic DNA. No translation available.
    AC009313 Genomic DNA. No translation available.
    CH471058 Genomic DNA. Translation: EAX11374.1.
    CH471058 Genomic DNA. Translation: EAX11375.1.
    CH471058 Genomic DNA. Translation: EAX11377.1.
    BC003388 mRNA. Translation: AAH03388.1.
    CCDSiCCDS2215.1. [Q92844-1]
    CCDS46436.1. [Q92844-3]
    RefSeqiNP_001186064.1. NM_001199135.1. [Q92844-1]
    NP_004171.2. NM_004180.2. [Q92844-1]
    NP_597841.1. NM_133484.1. [Q92844-3]
    UniGeneiHs.132257.

    Genome annotation databases

    EnsembliENST00000259075; ENSP00000259075; ENSG00000136560. [Q92844-1]
    ENST00000392749; ENSP00000376505; ENSG00000136560. [Q92844-1]
    ENST00000403609; ENSP00000385983; ENSG00000136560. [Q92844-3]
    GeneIDi10010.
    KEGGihsa:10010.
    UCSCiuc002ubq.1. human. [Q92844-3]
    uc002ubr.2. human. [Q92844-1]

    Polymorphism databases

    DMDMi143811466.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59863 mRNA. Translation: AAC50681.1 .
    U63830 mRNA. Translation: AAC50770.1 .
    BT009855 mRNA. Translation: AAP88857.1 .
    AC009299 Genomic DNA. No translation available.
    AC009313 Genomic DNA. No translation available.
    CH471058 Genomic DNA. Translation: EAX11374.1 .
    CH471058 Genomic DNA. Translation: EAX11375.1 .
    CH471058 Genomic DNA. Translation: EAX11377.1 .
    BC003388 mRNA. Translation: AAH03388.1 .
    CCDSi CCDS2215.1. [Q92844-1 ]
    CCDS46436.1. [Q92844-3 ]
    RefSeqi NP_001186064.1. NM_001199135.1. [Q92844-1 ]
    NP_004171.2. NM_004180.2. [Q92844-1 ]
    NP_597841.1. NM_133484.1. [Q92844-3 ]
    UniGenei Hs.132257.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KZZ X-ray 3.50 B 177-187 [» ]
    1L0A X-ray 2.90 B 178-195 [» ]
    ProteinModelPortali Q92844.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115328. 39 interactions.
    DIPi DIP-27516N.
    IntActi Q92844. 31 interactions.
    MINTi MINT-111947.
    STRINGi 9606.ENSP00000259075.

    PTM databases

    PhosphoSitei Q92844.

    Polymorphism databases

    DMDMi 143811466.

    Proteomic databases

    MaxQBi Q92844.
    PaxDbi Q92844.
    PeptideAtlasi Q92844.
    PRIDEi Q92844.

    Protocols and materials databases

    DNASUi 10010.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259075 ; ENSP00000259075 ; ENSG00000136560 . [Q92844-1 ]
    ENST00000392749 ; ENSP00000376505 ; ENSG00000136560 . [Q92844-1 ]
    ENST00000403609 ; ENSP00000385983 ; ENSG00000136560 . [Q92844-3 ]
    GeneIDi 10010.
    KEGGi hsa:10010.
    UCSCi uc002ubq.1. human. [Q92844-3 ]
    uc002ubr.2. human. [Q92844-1 ]

    Organism-specific databases

    CTDi 10010.
    GeneCardsi GC02P161957.
    HGNCi HGNC:11562. TANK.
    HPAi CAB010345.
    HPA037676.
    MIMi 603893. gene.
    neXtProti NX_Q92844.
    PharmGKBi PA36330.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG44252.
    HOGENOMi HOG000231816.
    HOVERGENi HBG019299.
    InParanoidi Q92844.
    KOi K12650.
    OMAi LHSTPER.
    OrthoDBi EOG7ZKSBN.
    PhylomeDBi Q92844.
    TreeFami TF336453.

    Enzyme and pathway databases

    Reactomei REACT_24938. TRAF6 mediated IRF7 activation.
    SignaLinki Q92844.

    Miscellaneous databases

    ChiTaRSi TANK. human.
    EvolutionaryTracei Q92844.
    GeneWikii TANK_(gene).
    GenomeRNAii 10010.
    NextBioi 37817.
    PROi Q92844.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92844.
    Bgeei Q92844.
    CleanExi HS_TANK.
    HS_TRAF2.
    Genevestigatori Q92844.

    Family and domain databases

    InterProi IPR024581. TBD.
    [Graphical view ]
    Pfami PF12845. TBD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "I-TRAF is a novel TRAF-interacting protein that regulates TRAF-mediated signal transduction."
      Rothe M., Xiong J., Shu H.-B., Williamson K., Goddard A., Goeddel D.V.
      Proc. Natl. Acad. Sci. U.S.A. 93:8241-8246(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    2. "Tumor necrosis factor receptor associated factor 2 is a mediator of NF-kappa B activation by latent infection membrane protein 1, the Epstein-Barr virus transforming protein."
      Kaye K.M., Devergne O., Harada J.N., Izumi K.M., Yalamanchili R., Kieff E., Mosialos G.
      Proc. Natl. Acad. Sci. U.S.A. 93:11085-11090(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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 SHORT).
      Tissue: Placenta.
    7. "NF-kB activation by a signaling complex containing TRAF2, TANK, and TBK1, a novel IKK-related kinase."
      Pomerantz J.L., Baltimore D.
      EMBO J. 18:6694-6704(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TBK1.
      Tissue: Spleen.
    8. "NF-kappaB activation through IKK-i-dependent I-TRAF/TANK phosphorylation."
      Nomura F., Kawai T., Nakanishi K., Akira S.
      Genes Cells 5:191-202(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF2, PHOSPHORYLATION BY IKBKE.
    9. "Association of the adaptor TANK with the I kappa B kinase (IKK) regulator NEMO connects IKK complexes with IKK epsilon and TBK1 kinases."
      Chariot A., Leonardi A., Muller J., Bonif M., Brown K., Siebenlist U.
      J. Biol. Chem. 277:37029-37036(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH IKBKG AND IKBKB.
    10. "SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-binding domain with NAP1 and TANK."
      Ryzhakov G., Randow F.
      EMBO J. 26:3180-3190(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IKBKE.
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND SER-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; SER-129; SER-341; SER-354 AND SER-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: FUNCTION, INTERACTION WITH TBK1.
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Downstream regulator TANK binds to the CD40 recognition site on TRAF3."
      Li C., Ni C.Z., Havert M.L., Cabezas E., He J., Kaiser D., Reed J.C., Satterthwait A.C., Cheng G., Ely K.R.
      Structure 10:403-411(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 174-194 IN COMPLEX WITH TRAF3, MUTAGENESIS OF GLN-182; THR-184; ASP-185; ASP-188 AND PHE-194.

    Entry informationi

    Entry nameiTANK_HUMAN
    AccessioniPrimary (citable) accession number: Q92844
    Secondary accession number(s): D3DPB5, Q7Z4J6, Q92885
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 141 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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