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Q9BZK7

- TBL1R_HUMAN

UniProt

Q9BZK7 - TBL1R_HUMAN

Protein

F-box-like/WD repeat-containing protein TBL1XR1

Gene

TBL1XR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    F-box-like protein involved in the recruitment of the ubiquitin/19S proteasome complex to nuclear receptor-regulated transcription units. Plays an essential role in transcription activation mediated by nuclear receptors. Probably acts as integral component of the N-Cor corepressor complex that mediates the recruitment of the 19S proteasome complex, leading to the subsequent proteasomal degradation of N-Cor complex, thereby allowing cofactor exchange, and transcription activation.1 Publication

    GO - Molecular functioni

    1. beta-catenin binding Source: UniProtKB
    2. histone binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein N-terminus binding Source: UniProtKB
    5. transcription corepressor activity Source: UniProtKB
    6. transcription regulatory region DNA binding Source: UniProtKB

    GO - Biological processi

    1. canonical Wnt signaling pathway Source: UniProtKB
    2. cellular lipid metabolic process Source: Reactome
    3. chromatin modification Source: UniProtKB-KW
    4. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    5. Notch signaling pathway Source: Reactome
    6. positive regulation of transcription, DNA-templated Source: UniProtKB
    7. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    8. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    9. small molecule metabolic process Source: Reactome
    10. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates circadian gene expression.
    REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_118789. REV-ERBA represses gene expression.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_24941. Circadian Clock.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinkiQ9BZK7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    F-box-like/WD repeat-containing protein TBL1XR1
    Alternative name(s):
    Nuclear receptor corepressor/HDAC3 complex subunit TBLR1
    TBL1-related protein 1
    Transducin beta-like 1X-related protein 1
    Gene namesi
    Name:TBL1XR1
    Synonyms:IRA1, TBLR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:29529. TBL1XR1.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: UniProtKB
    3. spindle microtubule Source: UniProtKB
    4. transcriptional repressor complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134928556.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 514513F-box-like/WD repeat-containing protein TBL1XR1PRO_0000051266Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei102 – 1021N6-acetyllysineBy similarity
    Modified residuei119 – 1191Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BZK7.
    PaxDbiQ9BZK7.
    PRIDEiQ9BZK7.

    PTM databases

    PhosphoSiteiQ9BZK7.

    Miscellaneous databases

    PMAP-CutDBQ9BZK7.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ9BZK7.
    BgeeiQ9BZK7.
    CleanExiHS_TBL1XR1.
    GenevestigatoriQ9BZK7.

    Organism-specific databases

    HPAiHPA019182.

    Interactioni

    Subunit structurei

    Component of the N-Cor repressor complex, at least composed of NCOR1, NCOR2, HDAC3, TBL1X, TBL1XR1, CORO2A and GPS2. Probable component of some E3 ubiquitin ligase complex. Interacts with histones H2B and H4.

    Protein-protein interaction databases

    BioGridi122834. 33 interactions.
    IntActiQ9BZK7. 17 interactions.
    MINTiMINT-2816883.
    STRINGi9606.ENSP00000405574.

    Structurei

    Secondary structure

    1
    514
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi159 – 1613
    Beta strandi162 – 1654
    Beta strandi172 – 1776
    Beta strandi179 – 18810
    Beta strandi191 – 1977
    Beta strandi208 – 2125
    Beta strandi228 – 2336
    Beta strandi237 – 2448
    Beta strandi247 – 2537
    Beta strandi258 – 2647
    Beta strandi269 – 2746
    Beta strandi276 – 28510
    Beta strandi290 – 2945
    Turni295 – 2984
    Beta strandi299 – 3046
    Beta strandi311 – 32616
    Beta strandi331 – 3355
    Beta strandi342 – 3454
    Beta strandi352 – 3576
    Beta strandi361 – 3688
    Beta strandi371 – 3777
    Beta strandi384 – 3885
    Beta strandi394 – 3996
    Beta strandi406 – 4083
    Beta strandi415 – 4195
    Beta strandi424 – 4285
    Turni429 – 4324
    Beta strandi433 – 4386
    Beta strandi445 – 4506
    Beta strandi454 – 4618
    Beta strandi464 – 4707
    Turni471 – 4733
    Beta strandi476 – 4816
    Beta strandi486 – 4916
    Beta strandi495 – 5028
    Beta strandi507 – 5115

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4LG9X-ray2.28A134-514[»]
    ProteinModelPortaliQ9BZK7.
    SMRiQ9BZK7. Positions 1-68, 124-514.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 3633LisHPROSITE-ProRule annotationAdd
    BLAST
    Domaini41 – 8646F-box-likeAdd
    BLAST
    Repeati167 – 20640WD 1Add
    BLAST
    Repeati223 – 26240WD 2Add
    BLAST
    Repeati264 – 30340WD 3Add
    BLAST
    Repeati306 – 34439WD 4Add
    BLAST
    Repeati347 – 38640WD 5Add
    BLAST
    Repeati389 – 43749WD 6Add
    BLAST
    Repeati440 – 47940WD 7Add
    BLAST
    Repeati481 – 51333WD 8Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi108 – 11811Poly-AlaAdd
    BLAST

    Domaini

    The F-box-like domain is related to the F-box domain, and apparently displays the same function as component of ubiquitin E3 ligase complexes.By similarity

    Sequence similaritiesi

    Belongs to the WD repeat EBI family.Curated
    Contains 1 F-box-like domain.Curated
    Contains 1 LisH domain.PROSITE-ProRule annotation
    Contains 8 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOGENOMiHOG000220902.
    HOVERGENiHBG050240.
    InParanoidiQ9BZK7.
    KOiK04508.
    OMAiLANNHAD.
    OrthoDBiEOG79CXZ3.
    PhylomeDBiQ9BZK7.
    TreeFamiTF323190.

    Family and domain databases

    Gene3Di2.130.10.10. 2 hits.
    InterProiIPR020472. G-protein_beta_WD-40_rep.
    IPR006594. LisH_dimerisation.
    IPR013720. LisH_dimerisation_subgr.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF08513. LisH. 1 hit.
    PF00400. WD40. 7 hits.
    [Graphical view]
    PRINTSiPR00320. GPROTEINBRPT.
    SMARTiSM00667. LisH. 1 hit.
    SM00320. WD40. 8 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 2 hits.
    PROSITEiPS50896. LISH. 1 hit.
    PS00678. WD_REPEATS_1. 4 hits.
    PS50082. WD_REPEATS_2. 6 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9BZK7-1 [UniParc]FASTAAdd to Basket

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    MSISSDEVNF LVYRYLQESG FSHSAFTFGI ESHISQSNIN GALVPPAALI    50
    SIIQKGLQYV EAEVSINEDG TLFDGRPIES LSLIDAVMPD VVQTRQQAYR 100
    DKLAQQQAAA AAAAAAAASQ QGSAKNGENT ANGEENGAHT IANNHTDMME 150
    VDGDVEIPPN KAVVLRGHES EVFICAWNPV SDLLASGSGD STARIWNLSE 200
    NSTSGSTQLV LRHCIREGGQ DVPSNKDVTS LDWNSEGTLL ATGSYDGFAR 250
    IWTKDGNLAS TLGQHKGPIF ALKWNKKGNF ILSAGVDKTT IIWDAHTGEA 300
    KQQFPFHSAP ALDVDWQSNN TFASCSTDMC IHVCKLGQDR PIKTFQGHTN 350
    EVNAIKWDPT GNLLASCSDD MTLKIWSMKQ DNCVHDLQAH NKEIYTIKWS 400
    PTGPGTNNPN ANLMLASASF DSTVRLWDVD RGICIHTLTK HQEPVYSVAF 450
    SPDGRYLASG SFDKCVHIWN TQTGALVHSY RGTGGIFEVC WNAAGDKVGA 500
    SASDGSVCVL DLRK 514
    Length:514
    Mass (Da):55,595
    Last modified:June 1, 2001 - v1
    Checksum:i0B556D2EE4BA796D
    GO

    Sequence cautioni

    The sequence AAH60320.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311E → K in AAG44736. (PubMed:11063877)Curated
    Sequence conflicti59 – 591Y → H in BAB14331. (PubMed:14702039)Curated
    Sequence conflicti389 – 3891A → Q in AAG44736. (PubMed:11063877)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF314544 mRNA. Translation: AAK00301.1.
    AF268193 mRNA. Translation: AAG44736.1.
    AK022956 mRNA. Translation: BAB14331.1.
    CH471052 Genomic DNA. Translation: EAW78438.1.
    BC060320 mRNA. Translation: AAH60320.1. Sequence problems.
    BC113421 mRNA. Translation: AAI13422.1.
    CCDSiCCDS46961.1.
    RefSeqiNP_078941.2. NM_024665.4.
    XP_005247829.1. XM_005247772.1.
    XP_005247832.1. XM_005247775.1.
    XP_006713808.1. XM_006713745.1.
    XP_006713809.1. XM_006713746.1.
    UniGeneiHs.715026.

    Genome annotation databases

    EnsembliENST00000430069; ENSP00000405574; ENSG00000177565.
    ENST00000457928; ENSP00000413251; ENSG00000177565.
    GeneIDi79718.
    KEGGihsa:79718.
    UCSCiuc003fiw.4. human.

    Polymorphism databases

    DMDMi23396874.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF314544 mRNA. Translation: AAK00301.1 .
    AF268193 mRNA. Translation: AAG44736.1 .
    AK022956 mRNA. Translation: BAB14331.1 .
    CH471052 Genomic DNA. Translation: EAW78438.1 .
    BC060320 mRNA. Translation: AAH60320.1 . Sequence problems.
    BC113421 mRNA. Translation: AAI13422.1 .
    CCDSi CCDS46961.1.
    RefSeqi NP_078941.2. NM_024665.4.
    XP_005247829.1. XM_005247772.1.
    XP_005247832.1. XM_005247775.1.
    XP_006713808.1. XM_006713745.1.
    XP_006713809.1. XM_006713746.1.
    UniGenei Hs.715026.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4LG9 X-ray 2.28 A 134-514 [» ]
    ProteinModelPortali Q9BZK7.
    SMRi Q9BZK7. Positions 1-68, 124-514.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122834. 33 interactions.
    IntActi Q9BZK7. 17 interactions.
    MINTi MINT-2816883.
    STRINGi 9606.ENSP00000405574.

    PTM databases

    PhosphoSitei Q9BZK7.

    Polymorphism databases

    DMDMi 23396874.

    Proteomic databases

    MaxQBi Q9BZK7.
    PaxDbi Q9BZK7.
    PRIDEi Q9BZK7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000430069 ; ENSP00000405574 ; ENSG00000177565 .
    ENST00000457928 ; ENSP00000413251 ; ENSG00000177565 .
    GeneIDi 79718.
    KEGGi hsa:79718.
    UCSCi uc003fiw.4. human.

    Organism-specific databases

    CTDi 79718.
    GeneCardsi GC03M176737.
    H-InvDB HIX0147994.
    HGNCi HGNC:29529. TBL1XR1.
    HPAi HPA019182.
    MIMi 608628. gene.
    neXtProti NX_Q9BZK7.
    PharmGKBi PA134928556.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000220902.
    HOVERGENi HBG050240.
    InParanoidi Q9BZK7.
    KOi K04508.
    OMAi LANNHAD.
    OrthoDBi EOG79CXZ3.
    PhylomeDBi Q9BZK7.
    TreeFami TF323190.

    Enzyme and pathway databases

    Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates circadian gene expression.
    REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_118789. REV-ERBA represses gene expression.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_24941. Circadian Clock.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinki Q9BZK7.

    Miscellaneous databases

    ChiTaRSi TBL1XR1. human.
    GeneWikii TBL1XR1.
    GenomeRNAii 79718.
    NextBioi 69065.
    PMAP-CutDB Q9BZK7.
    PROi Q9BZK7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BZK7.
    Bgeei Q9BZK7.
    CleanExi HS_TBL1XR1.
    Genevestigatori Q9BZK7.

    Family and domain databases

    Gene3Di 2.130.10.10. 2 hits.
    InterProi IPR020472. G-protein_beta_WD-40_rep.
    IPR006594. LisH_dimerisation.
    IPR013720. LisH_dimerisation_subgr.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF08513. LisH. 1 hit.
    PF00400. WD40. 7 hits.
    [Graphical view ]
    PRINTSi PR00320. GPROTEINBRPT.
    SMARTi SM00667. LisH. 1 hit.
    SM00320. WD40. 8 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 2 hits.
    PROSITEi PS50896. LISH. 1 hit.
    PS00678. WD_REPEATS_1. 4 hits.
    PS50082. WD_REPEATS_2. 6 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2."
      Zhang J., Kalkum M., Chait B.T., Roeder R.G.
      Mol. Cell 9:611-623(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, COMPONENT OF THE N-COR COMPLEX WITH NCOR1; NCOR2; GPS2; TBL1X AND HDAC3.
    2. "Identification of four human cDNAs that are differentially expressed by early hematopoietic progenitors."
      Zhang X., Dormady S.P., Basch R.S.
      Exp. Hematol. 28:1286-1296(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Adrenal cortex and Liver.
    6. "Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1."
      Yoon H.-G., Chan D.W., Huang Z.-Q., Li J., Fondell J.D., Qin J., Wong J.
      EMBO J. 22:1336-1346(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPONENT OF THE N-COR COMPLEX WITH TBL1X; CORO2A AND HDAC3, HISTONE-BINDING.
    7. "A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors."
      Perissi V., Aggarwal A., Glass C.K., Rose D.W., Rosenfeld M.G.
      Cell 116:511-526(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RECRUITMENT OF 19S PROTEASOME COMPLEX.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    9. "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-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTBL1R_HUMAN
    AccessioniPrimary (citable) accession number: Q9BZK7
    Secondary accession number(s): D3DNQ9
    , Q14DC3, Q9H2I1, Q9H9A1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 131 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 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3