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Protein

Transforming growth factor beta regulator 1

Gene

TBRG1

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

Functioni

Acts as a growth inhibitor. Can activate p53/TP53, causes G1 arrest and collaborates with CDKN2A to restrict proliferation, but does not require either protein to inhibit DNA synthesis. Redistributes CDKN2A into the nucleoplasm. Involved in maintaining chromosomal stability.1 Publication

GO - Biological processi

  • cell cycle arrest Source: HGNC
  • DNA replication Source: HGNC
  • negative regulation of cell proliferation Source: HGNC
  • nucleolus to nucleoplasm transport Source: HGNC
  • protein stabilization Source: HGNC
Complete GO annotation...

Keywords - Biological processi

Cell cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Transforming growth factor beta regulator 1
Alternative name(s):
Nuclear interactor of ARF and Mdm2
Gene namesi
Name:TBRG1
Synonyms:NIAM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:29551. TBRG1.

Subcellular locationi

GO - Cellular componenti

  • intracellular membrane-bounded organelle Source: HPA
  • nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA134926528.

Polymorphism and mutation databases

BioMutaiTBRG1.
DMDMi121943045.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 411410Transforming growth factor beta regulator 1PRO_0000274218Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei10 – 101PhosphoserineCombined sources

Post-translational modificationi

Ubiquitinated; mediated by MDM2 and leading to its subsequent proteasomal degradation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ3YBR2.
MaxQBiQ3YBR2.
PaxDbiQ3YBR2.
PeptideAtlasiQ3YBR2.
PRIDEiQ3YBR2.

PTM databases

iPTMnetiQ3YBR2.
PhosphoSiteiQ3YBR2.

Expressioni

Tissue specificityi

Widely expressed at low levels in most tissues, with highest levels in pancreas, lung and liver. Expression is decreased in primary tumors including lung, liver, breast, pancreas and kidney carcinomas, chronic lymphocytic leukemia and diffuse large B-cell lymphoma.1 Publication

Gene expression databases

BgeeiQ3YBR2.
CleanExiHS_TBRG1.
ExpressionAtlasiQ3YBR2. baseline and differential.
GenevisibleiQ3YBR2. HS.

Interactioni

Subunit structurei

Interacts with CDKN2A and MDM2.2 Publications

Protein-protein interaction databases

BioGridi124337. 7 interactions.
IntActiQ3YBR2. 13 interactions.
STRINGi9606.ENSP00000409016.

Structurei

Secondary structure

1
411
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi185 – 1873Combined sources
Beta strandi190 – 1978Combined sources
Helixi203 – 2053Combined sources
Beta strandi214 – 22310Combined sources
Beta strandi230 – 24011Combined sources
Beta strandi242 – 25110Combined sources
Helixi255 – 2573Combined sources
Beta strandi259 – 2635Combined sources
Helixi264 – 27916Combined sources
Helixi290 – 2945Combined sources
Helixi299 – 3057Combined sources
Helixi311 – 3133Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WZOX-ray1.60A179-324[»]
ProteinModelPortaliQ3YBR2.
SMRiQ3YBR2. Positions 179-324.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ3YBR2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini182 – 24160FYR N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini242 – 32180FYR C-terminalPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi134 – 16128Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the TBRG1 family.Curated
Contains 1 FYR C-terminal domain.PROSITE-ProRule annotation
Contains 1 FYR N-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410ITPM. Eukaryota.
ENOG410XTBM. LUCA.
GeneTreeiENSGT00390000013374.
HOVERGENiHBG094027.
InParanoidiQ3YBR2.
OMAiTCKKKKM.
OrthoDBiEOG7GJ6DC.
PhylomeDBiQ3YBR2.
TreeFamiTF324736.

Family and domain databases

InterProiIPR003889. FYrich_C.
IPR003888. FYrich_N.
[Graphical view]
PfamiPF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
[Graphical view]
SMARTiSM00542. FYRC. 1 hit.
SM00541. FYRN. 1 hit.
[Graphical view]
PROSITEiPS51543. FYRC. 1 hit.
PS51542. FYRN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q3YBR2-1) [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

        10         20         30         40         50
MSLLDGLASS PRAPLQSSKA RMKKLPKKSQ NEKYRLKYLR LRKAAKATVF
60 70 80 90 100
ENAAICDEIA RLEEKFLKAK EERRYLLKKL LQLQALTEGE VQAAAPSHSS
110 120 130 140 150
SLPLTYGVAS SVGTIQGAGP ISGPSTGAEE PFGKKTKKEK KEKGKENNKL
160 170 180 190 200
EVLKKTCKKK KMAGGARKLV QPIALDPSGR PVFPIGLGGL TVYSLGEIIT
210 220 230 240 250
DRPGFHDESA IYPVGYCSTR IYASMKCPDQ KCLYTCQIKD GGVQPQFEIV
260 270 280 290 300
PEDDPQNAIV SSSADACHAE LLRTISTTMG KLMPNLLPAG ADFFGFSHPA
310 320 330 340 350
IHNLIQSCPG ARKCINYQWV KFDVCKPGDG QLPEGLPEND AAMSFEAFQR
360 370 380 390 400
QIFDEDQNDP LLPGSLDLPE LQPAAFVSSY QPMYLTHEPL VDTHLQHLKS
410
PSQGSPIQSS D
Length:411
Mass (Da):44,946
Last modified:September 27, 2005 - v1
Checksum:iC6FDE7D7961E78C4
GO
Isoform 2 (identifier: Q3YBR2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-197: MSLLDGLASS...GGLTVYSLGE → MVWPALWELY...KKAKRTTNWK

Show »
Length:260
Mass (Da):29,157
Checksum:i8F7E21F0ACF41A68
GO
Isoform 3 (identifier: Q3YBR2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-224: Missing.

Show »
Length:187
Mass (Da):20,558
Checksum:iDAF7DAC71DF246C1
GO

Sequence cautioni

The sequence BAB84966.1 differs from that shown. Reason: Frameshift at position 229. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti406 – 4061P → S in BAD96656 (Ref. 4) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 224224Missing in isoform 3. 1 PublicationVSP_022644Add
BLAST
Alternative sequencei1 – 197197MSLLD…YSLGE → MVWPALWELYRELGLFQGPA LGLRNHLGRKLRRRKKKKAK RTTNWK in isoform 2. 3 PublicationsVSP_022645Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ144542 mRNA. Translation: AAZ76016.1.
AK027527 mRNA. Translation: BAB55177.1.
AK074140 mRNA. Translation: BAB84966.1. Frameshift.
AY696294 mRNA. Translation: AAU10523.1.
AK222936 mRNA. Translation: BAD96656.1.
BC109269 mRNA. Translation: AAI09270.1.
AL713631 mRNA. Translation: CAD28450.1.
AL831881 mRNA. Translation: CAH10595.1.
CCDSiCCDS8448.2. [Q3YBR2-1]
RefSeqiNP_116200.2. NM_032811.2. [Q3YBR2-1]
UniGeneiHs.436410.

Genome annotation databases

EnsembliENST00000441174; ENSP00000409016; ENSG00000154144. [Q3YBR2-1]
GeneIDi84897.
KEGGihsa:84897.
UCSCiuc001qak.5. human. [Q3YBR2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ144542 mRNA. Translation: AAZ76016.1.
AK027527 mRNA. Translation: BAB55177.1.
AK074140 mRNA. Translation: BAB84966.1. Frameshift.
AY696294 mRNA. Translation: AAU10523.1.
AK222936 mRNA. Translation: BAD96656.1.
BC109269 mRNA. Translation: AAI09270.1.
AL713631 mRNA. Translation: CAD28450.1.
AL831881 mRNA. Translation: CAH10595.1.
CCDSiCCDS8448.2. [Q3YBR2-1]
RefSeqiNP_116200.2. NM_032811.2. [Q3YBR2-1]
UniGeneiHs.436410.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WZOX-ray1.60A179-324[»]
ProteinModelPortaliQ3YBR2.
SMRiQ3YBR2. Positions 179-324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124337. 7 interactions.
IntActiQ3YBR2. 13 interactions.
STRINGi9606.ENSP00000409016.

PTM databases

iPTMnetiQ3YBR2.
PhosphoSiteiQ3YBR2.

Polymorphism and mutation databases

BioMutaiTBRG1.
DMDMi121943045.

Proteomic databases

EPDiQ3YBR2.
MaxQBiQ3YBR2.
PaxDbiQ3YBR2.
PeptideAtlasiQ3YBR2.
PRIDEiQ3YBR2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000441174; ENSP00000409016; ENSG00000154144. [Q3YBR2-1]
GeneIDi84897.
KEGGihsa:84897.
UCSCiuc001qak.5. human. [Q3YBR2-1]

Organism-specific databases

CTDi84897.
GeneCardsiTBRG1.
HGNCiHGNC:29551. TBRG1.
MIMi610614. gene.
neXtProtiNX_Q3YBR2.
PharmGKBiPA134926528.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITPM. Eukaryota.
ENOG410XTBM. LUCA.
GeneTreeiENSGT00390000013374.
HOVERGENiHBG094027.
InParanoidiQ3YBR2.
OMAiTCKKKKM.
OrthoDBiEOG7GJ6DC.
PhylomeDBiQ3YBR2.
TreeFamiTF324736.

Miscellaneous databases

ChiTaRSiTBRG1. human.
EvolutionaryTraceiQ3YBR2.
GeneWikiiTBRG1.
GenomeRNAii84897.
PROiQ3YBR2.
SOURCEiSearch...

Gene expression databases

BgeeiQ3YBR2.
CleanExiHS_TBRG1.
ExpressionAtlasiQ3YBR2. baseline and differential.
GenevisibleiQ3YBR2. HS.

Family and domain databases

InterProiIPR003889. FYrich_C.
IPR003888. FYrich_N.
[Graphical view]
PfamiPF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
[Graphical view]
SMARTiSM00542. FYRC. 1 hit.
SM00541. FYRN. 1 hit.
[Graphical view]
PROSITEiPS51543. FYRC. 1 hit.
PS51542. FYRN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH CDKN2A AND MDM2, UBIQUITINATION.
    Tissue: Pancreas.
  2. "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: Spleen.
  3. Zhou G., Li M., Li H., Shen C., Zhong G., Lin L., Yang S.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Kidney.
  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] (ISOFORM 3).
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 220-411.
    Tissue: Amygdala and Brain.
  7. "Identification of novel ARF binding proteins by two-hybrid screening."
    Tompkins V., Hagen J., Zediak V.P., Quelle D.E.
    Cell Cycle 5:641-646(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDKN2A.
  8. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  10. "The structure of the FYR domain of transforming growth factor beta regulator 1."
    Garcia-Alai M.M., Allen M.D., Joerger A.C., Bycroft M.
    Protein Sci. 19:1432-1438(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 179-324.

Entry informationi

Entry nameiTBRG1_HUMAN
AccessioniPrimary (citable) accession number: Q3YBR2
Secondary accession number(s): Q53GJ5
, Q66ZJ6, Q69YS7, Q8TCS4, Q8TEI4, Q96SV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: September 27, 2005
Last modified: July 6, 2016
This is version 94 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 11
    Human chromosome 11: 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

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 one 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.