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Q9BZK7 - TBL1R_HUMAN

UniProt

Q9BZK7 - TBL1R_HUMAN

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Protein

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

Gene

TBL1XR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 N-terminus binding Source: UniProtKB
  4. transcription corepressor activity Source: UniProtKB
  5. 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. histone deacetylation Source: GO_Central
  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
Complete GO annotation...

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_228222. HDACs deacetylate histones.
REACT_24941. Circadian Clock.
REACT_267716. Orphan transporters.
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
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
Complete GO annotation...

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

BgeeiQ9BZK7.
CleanExiHS_TBL1XR1.
ExpressionAtlasiQ9BZK7. baseline and differential.
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. 39 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 – 1613Combined sources
Beta strandi162 – 1654Combined sources
Beta strandi172 – 1776Combined sources
Beta strandi179 – 18810Combined sources
Beta strandi191 – 1977Combined sources
Beta strandi208 – 2125Combined sources
Beta strandi228 – 2336Combined sources
Beta strandi237 – 2448Combined sources
Beta strandi247 – 2537Combined sources
Beta strandi258 – 2647Combined sources
Beta strandi269 – 2746Combined sources
Beta strandi276 – 28510Combined sources
Beta strandi290 – 2945Combined sources
Turni295 – 2984Combined sources
Beta strandi299 – 3046Combined sources
Beta strandi311 – 32616Combined sources
Beta strandi331 – 3355Combined sources
Beta strandi342 – 3454Combined sources
Beta strandi352 – 3576Combined sources
Beta strandi361 – 3688Combined sources
Beta strandi371 – 3777Combined sources
Beta strandi384 – 3885Combined sources
Beta strandi394 – 3996Combined sources
Beta strandi406 – 4083Combined sources
Beta strandi415 – 4195Combined sources
Beta strandi424 – 4285Combined sources
Turni429 – 4324Combined sources
Beta strandi433 – 4386Combined sources
Beta strandi445 – 4506Combined sources
Beta strandi454 – 4618Combined sources
Beta strandi464 – 4707Combined sources
Turni471 – 4733Combined sources
Beta strandi476 – 4816Combined sources
Beta strandi486 – 4916Combined sources
Beta strandi495 – 5028Combined sources
Beta strandi507 – 5115Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LG9X-ray2.28A134-514[»]
ProteinModelPortaliQ9BZK7.
SMRiQ9BZK7. Positions 1-68, 124-513.
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.
GeneTreeiENSGT00750000117536.
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

« Hide

        10         20         30         40         50
MSISSDEVNF LVYRYLQESG FSHSAFTFGI ESHISQSNIN GALVPPAALI 
        60         70         80         90        100
SIIQKGLQYV EAEVSINEDG TLFDGRPIES LSLIDAVMPD VVQTRQQAYR 
       110        120        130        140        150
DKLAQQQAAA AAAAAAAASQ QGSAKNGENT ANGEENGAHT IANNHTDMME 
       160        170        180        190        200
VDGDVEIPPN KAVVLRGHES EVFICAWNPV SDLLASGSGD STARIWNLSE 
       210        220        230        240        250
NSTSGSTQLV LRHCIREGGQ DVPSNKDVTS LDWNSEGTLL ATGSYDGFAR 
       260        270        280        290        300
IWTKDGNLAS TLGQHKGPIF ALKWNKKGNF ILSAGVDKTT IIWDAHTGEA 
       310        320        330        340        350
KQQFPFHSAP ALDVDWQSNN TFASCSTDMC IHVCKLGQDR PIKTFQGHTN 
       360        370        380        390        400
EVNAIKWDPT GNLLASCSDD MTLKIWSMKQ DNCVHDLQAH NKEIYTIKWS 
       410        420        430        440        450
PTGPGTNNPN ANLMLASASF DSTVRLWDVD RGICIHTLTK HQEPVYSVAF 
       460        470        480        490        500
SPDGRYLASG SFDKCVHIWN TQTGALVHSY RGTGGIFEVC WNAAGDKVGA 
       510 
SASDGSVCVL DLRK
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.Contaminating sequence. Potential poly-A sequence.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LG9X-ray2.28A134-514[»]
ProteinModelPortaliQ9BZK7.
SMRiQ9BZK7. Positions 1-68, 124-513.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122834. 39 interactions.
IntActiQ9BZK7. 17 interactions.
MINTiMINT-2816883.
STRINGi9606.ENSP00000405574.

PTM databases

PhosphoSiteiQ9BZK7.

Polymorphism databases

DMDMi23396874.

Proteomic databases

MaxQBiQ9BZK7.
PaxDbiQ9BZK7.
PRIDEiQ9BZK7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi79718.
GeneCardsiGC03M176737.
H-InvDBHIX0147994.
HGNCiHGNC:29529. TBL1XR1.
HPAiHPA019182.
MIMi608628. gene.
neXtProtiNX_Q9BZK7.
PharmGKBiPA134928556.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00750000117536.
HOGENOMiHOG000220902.
HOVERGENiHBG050240.
InParanoidiQ9BZK7.
KOiK04508.
OMAiLANNHAD.
OrthoDBiEOG79CXZ3.
PhylomeDBiQ9BZK7.
TreeFamiTF323190.

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_228222. HDACs deacetylate histones.
REACT_24941. Circadian Clock.
REACT_267716. Orphan transporters.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiQ9BZK7.

Miscellaneous databases

ChiTaRSiTBL1XR1. human.
GeneWikiiTBL1XR1.
GenomeRNAii79718.
NextBioi69065.
PMAP-CutDBQ9BZK7.
PROiQ9BZK7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BZK7.
CleanExiHS_TBL1XR1.
ExpressionAtlasiQ9BZK7. baseline and differential.
GenevestigatoriQ9BZK7.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].
+Additional computationally mapped references.

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: February 4, 2015
This is version 135 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.