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Q15633

- TRBP2_HUMAN

UniProt

Q15633 - TRBP2_HUMAN

Protein

RISC-loading complex subunit TARBP2

Gene

TARBP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 3 (14 Oct 2008)
      Previous versions | rss
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    Functioni

    Required for formation of the RNA induced silencing complex (RISC). Component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2. Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. May also play a role in the production of short interfering RNAs (siRNAs) from double-stranded RNA (dsRNA) by DICER1. Binds to the HIV-1 TAR RNA which is located in the long terminal repeat (LTR) of HIV-1, and stimulates translation of TAR-containing RNAs. This is achieved in part at least by binding to and inhibiting EIF2AK2/PKR, thereby reducing phosphorylation and inhibition of EIF2S1/eIF-2-alpha. May also promote translation of TAR-containing RNAs independently of EIF2AK2/PKR.9 Publications

    GO - Molecular functioni

    1. double-stranded RNA binding Source: InterPro
    2. miRNA binding Source: UniProtKB-HAMAP
    3. protein binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB
    5. siRNA binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. miRNA loading onto RISC involved in gene silencing by miRNA Source: UniProtKB
    3. negative regulation of defense response to virus by host Source: UniProtKB
    4. negative regulation of protein kinase activity Source: UniProtKB
    5. positive regulation of viral genome replication Source: UniProtKB
    6. pre-miRNA processing Source: UniProtKB
    7. production of siRNA involved in RNA interference Source: UniProtKB
    8. regulation of transcription, DNA-templated Source: ProtInc
    9. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    10. regulation of translation Source: UniProtKB-KW
    11. regulation of viral transcription Source: UniProtKB
    12. targeting of mRNA for destruction involved in RNA interference Source: UniProtKB

    Keywords - Biological processi

    RNA-mediated gene silencing, Translation regulation

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_118560. Small interfering RNA (siRNA) biogenesis.
    REACT_12417. MicroRNA (miRNA) biogenesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RISC-loading complex subunit TARBP2UniRule annotation
    Alternative name(s):
    TAR RNA-binding protein 2
    Trans-activation-responsive RNA-binding protein
    Gene namesi
    Name:TARBP2UniRule annotation
    Synonyms:TRBP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:11569. TARBP2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleus Source: HPA
    4. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    5. RISC complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36334.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 366366RISC-loading complex subunit TARBP2PRO_0000065622Add
    BLAST

    Proteomic databases

    MaxQBiQ15633.
    PaxDbiQ15633.
    PRIDEiQ15633.

    PTM databases

    PhosphoSiteiQ15633.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15633.
    BgeeiQ15633.
    CleanExiHS_TARBP2.
    GenevestigatoriQ15633.

    Organism-specific databases

    HPAiHPA051181.

    Interactioni

    Subunit structurei

    Self-associates. Component of the RISC loading complex (RLC), or micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2. Note that the trimeric RLC/miRLC is also referred to as RISC. Interacts with EIF2AK2/PKR and inhibits its protein kinase activity. Interacts with DHX9, EIF6, MOV10 and PRKRA. Associates with the 60S ribosome.11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADARP55265-12EBI-978581,EBI-6913056
    ADARP55265-53EBI-978581,EBI-6913210
    AGO2Q9UKV85EBI-978581,EBI-528269
    DICER1Q9UPY315EBI-978581,EBI-395506
    EIF2AK2P195252EBI-978581,EBI-640775
    PRKRAO755692EBI-978581,EBI-713955

    Protein-protein interaction databases

    BioGridi112758. 39 interactions.
    DIPiDIP-29665N.
    IntActiQ15633. 10 interactions.
    MINTiMINT-92451.
    STRINGi9606.ENSP00000266987.

    Structurei

    Secondary structure

    1
    366
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi31 – 4111
    Beta strandi47 – 537
    Beta strandi62 – 687
    Beta strandi71 – 799
    Helixi80 – 9516
    Helixi161 – 17010
    Beta strandi177 – 1859
    Beta strandi187 – 1893
    Beta strandi191 – 1988
    Beta strandi201 – 2099
    Helixi210 – 22617

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CPNNMR-A150-225[»]
    3ADLX-ray2.20A161-231[»]
    3LLHX-ray2.14A/B22-105[»]
    ProteinModelPortaliQ15633.
    SMRiQ15633. Positions 28-225, 293-360.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15633.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 9768DRBM 1UniRule annotationAdd
    BLAST
    Domaini159 – 22769DRBM 2UniRule annotationAdd
    BLAST
    Domaini293 – 36169DRBM 3UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni22 – 10584Sufficient for interaction with PRKRAAdd
    BLAST
    Regioni152 – 23483Sufficient for interaction with PRKRAAdd
    BLAST
    Regioni228 – 366139Sufficient for interaction with DICER1Add
    BLAST
    Regioni287 – 36680Sufficient for interaction with PRKRAAdd
    BLAST

    Sequence similaritiesi

    Belongs to the TARBP2 family.UniRule annotation
    Contains 3 DRBM (double-stranded RNA-binding) domains.UniRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG245126.
    HOGENOMiHOG000231919.
    HOVERGENiHBG001700.
    InParanoidiQ15633.
    OMAiIEQMLAV.
    PhylomeDBiQ15633.
    TreeFamiTF315953.

    Family and domain databases

    Gene3Di3.30.160.20. 3 hits.
    HAMAPiMF_03034. TRBP2.
    InterProiIPR014720. dsRNA-bd_dom.
    IPR028605. TRBP2.
    [Graphical view]
    PANTHERiPTHR10910:SF61. PTHR10910:SF61. 1 hit.
    PfamiPF00035. dsrm. 2 hits.
    [Graphical view]
    SMARTiSM00358. DSRM. 3 hits.
    [Graphical view]
    PROSITEiPS50137. DS_RBD. 3 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative promoter usage. Align

    Isoform 1 (identifier: Q15633-1) [UniParc]FASTAAdd to Basket

    Also known as: TRBP2

    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

    MSEEEQGSGT TTGCGLPSIE QMLAANPGKT PISLLQEYGT RIGKTPVYDL    50
    LKAEGQAHQP NFTFRVTVGD TSCTGQGPSK KAAKHKAAEV ALKHLKGGSM 100
    LEPALEDSSS FSPLDSSLPE DIPVFTAAAA ATPVPSVVLT RSPPMELQPP 150
    VSPQQSECNP VGALQELVVQ KGWRLPEYTV TQESGPAHRK EFTMTCRVER 200
    FIEIGSGTSK KLAKRNAAAK MLLRVHTVPL DARDGNEVEP DDDHFSIGVG 250
    SRLDGLRNRG PGCTWDSLRN SVGEKILSLR SCSLGSLGAL GPACCRVLSE 300
    LSEEQAFHVS YLDIEELSLS GLCQCLVELS TQPATVCHGS ATTREAARGE 350
    AARRALQYLK IMAGSK 366
    Length:366
    Mass (Da):39,039
    Last modified:October 14, 2008 - v3
    Checksum:i768BA11751DA4912
    GO
    Isoform 2 (identifier: Q15633-2) [UniParc]FASTAAdd to Basket

    Also known as: TRBP1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: Missing.

    Show »
    Length:345
    Mass (Da):36,916
    Checksum:i7506A9324E9D0596
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti144 – 1441P → A in AAA36765. (PubMed:2011739)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti251 – 2511S → F.2 Publications
    Corresponds to variant rs1126500 [ dbSNP | Ensembl ].
    VAR_046992

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2121Missing in isoform 2. 1 PublicationVSP_035584Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60801 mRNA. Translation: AAA36765.1.
    U08998 mRNA. Translation: AAB50581.2.
    BT007140 mRNA. Translation: AAP35804.1.
    CH471054 Genomic DNA. Translation: EAW96720.1.
    BC005860 mRNA. Translation: AAH05860.1.
    AF281068 Genomic DNA. Translation: AAL55730.1.
    AF281068 Genomic DNA. Translation: AAL55731.1.
    CCDSiCCDS41791.1. [Q15633-2]
    CCDS8861.1. [Q15633-1]
    PIRiG01420.
    RefSeqiNP_004169.3. NM_004178.4. [Q15633-2]
    NP_599150.1. NM_134323.1. [Q15633-1]
    NP_599151.2. NM_134324.2. [Q15633-2]
    XP_005269171.1. XM_005269114.1. [Q15633-2]
    XP_005269172.1. XM_005269115.2. [Q15633-2]
    UniGeneiHs.326.
    Hs.604255.

    Genome annotation databases

    EnsembliENST00000266987; ENSP00000266987; ENSG00000139546. [Q15633-1]
    ENST00000394357; ENSP00000377885; ENSG00000139546. [Q15633-2]
    ENST00000456234; ENSP00000416077; ENSG00000139546. [Q15633-2]
    GeneIDi6895.
    KEGGihsa:6895.
    UCSCiuc001sdo.3. human. [Q15633-1]

    Polymorphism databases

    DMDMi209572714.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60801 mRNA. Translation: AAA36765.1 .
    U08998 mRNA. Translation: AAB50581.2 .
    BT007140 mRNA. Translation: AAP35804.1 .
    CH471054 Genomic DNA. Translation: EAW96720.1 .
    BC005860 mRNA. Translation: AAH05860.1 .
    AF281068 Genomic DNA. Translation: AAL55730.1 .
    AF281068 Genomic DNA. Translation: AAL55731.1 .
    CCDSi CCDS41791.1. [Q15633-2 ]
    CCDS8861.1. [Q15633-1 ]
    PIRi G01420.
    RefSeqi NP_004169.3. NM_004178.4. [Q15633-2 ]
    NP_599150.1. NM_134323.1. [Q15633-1 ]
    NP_599151.2. NM_134324.2. [Q15633-2 ]
    XP_005269171.1. XM_005269114.1. [Q15633-2 ]
    XP_005269172.1. XM_005269115.2. [Q15633-2 ]
    UniGenei Hs.326.
    Hs.604255.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CPN NMR - A 150-225 [» ]
    3ADL X-ray 2.20 A 161-231 [» ]
    3LLH X-ray 2.14 A/B 22-105 [» ]
    ProteinModelPortali Q15633.
    SMRi Q15633. Positions 28-225, 293-360.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112758. 39 interactions.
    DIPi DIP-29665N.
    IntActi Q15633. 10 interactions.
    MINTi MINT-92451.
    STRINGi 9606.ENSP00000266987.

    Chemistry

    BindingDBi Q15633.

    PTM databases

    PhosphoSitei Q15633.

    Polymorphism databases

    DMDMi 209572714.

    Proteomic databases

    MaxQBi Q15633.
    PaxDbi Q15633.
    PRIDEi Q15633.

    Protocols and materials databases

    DNASUi 6895.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000266987 ; ENSP00000266987 ; ENSG00000139546 . [Q15633-1 ]
    ENST00000394357 ; ENSP00000377885 ; ENSG00000139546 . [Q15633-2 ]
    ENST00000456234 ; ENSP00000416077 ; ENSG00000139546 . [Q15633-2 ]
    GeneIDi 6895.
    KEGGi hsa:6895.
    UCSCi uc001sdo.3. human. [Q15633-1 ]

    Organism-specific databases

    CTDi 6895.
    GeneCardsi GC12P053890.
    HGNCi HGNC:11569. TARBP2.
    HPAi HPA051181.
    MIMi 605053. gene.
    neXtProti NX_Q15633.
    PharmGKBi PA36334.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG245126.
    HOGENOMi HOG000231919.
    HOVERGENi HBG001700.
    InParanoidi Q15633.
    OMAi IEQMLAV.
    PhylomeDBi Q15633.
    TreeFami TF315953.

    Enzyme and pathway databases

    Reactomei REACT_118560. Small interfering RNA (siRNA) biogenesis.
    REACT_12417. MicroRNA (miRNA) biogenesis.

    Miscellaneous databases

    EvolutionaryTracei Q15633.
    GeneWikii TARBP2.
    GenomeRNAii 6895.
    NextBioi 26949.
    PROi Q15633.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15633.
    Bgeei Q15633.
    CleanExi HS_TARBP2.
    Genevestigatori Q15633.

    Family and domain databases

    Gene3Di 3.30.160.20. 3 hits.
    HAMAPi MF_03034. TRBP2.
    InterProi IPR014720. dsRNA-bd_dom.
    IPR028605. TRBP2.
    [Graphical view ]
    PANTHERi PTHR10910:SF61. PTHR10910:SF61. 1 hit.
    Pfami PF00035. dsrm. 2 hits.
    [Graphical view ]
    SMARTi SM00358. DSRM. 3 hits.
    [Graphical view ]
    PROSITEi PS50137. DS_RBD. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of a human TAR RNA-binding protein that activates the HIV-1 LTR."
      Gatignol A., Buckler-White A.J., Berkhout B., Jeang K.T.
      Science 251:1597-1600(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT PHE-251.
    2. Gatignol A., Duarte M.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Genetic mapping in human and mouse of the locus encoding TRBP, a protein that binds the TAR region of the human immunodeficiency virus (HIV-1)."
      Kozak C.A., Gatignol A., Graham K., Jeang K.T., McBride O.W.
      Genomics 25:66-72(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PHE-251.
    4. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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 1).
      Tissue: Muscle.
    7. "Organization of the human tarbp2 gene reveals two promoters that are repressed in an astrocytic cell line."
      Bannwarth S., Talakoub L., Letourneur F., Duarte M., Purcell D.F., Hiscott J., Gatignol A.
      J. Biol. Chem. 276:48803-48813(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74, ALTERNATIVE PROMOTER USAGE.
    8. "Relatedness of an RNA-binding motif in human immunodeficiency virus type 1 TAR RNA-binding protein TRBP to human P1/dsI kinase and Drosophila staufen."
      Gatignol A., Buckler C., Jeang K.T.
      Mol. Cell. Biol. 13:2193-2202(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF RNA-BINDING.
    9. "Two dimerization domains in the trans-activation response RNA-binding protein (TRBP) individually reverse the protein kinase R inhibition of HIV-1 long terminal repeat expression."
      Daher A., Longuet M., Dorin D., Bois F., Segeral E., Bannwarth S., Battisti P.-L., Purcell D.F., Benarous R., Vaquero C., Meurs E.F., Gatignol A.
      J. Biol. Chem. 276:33899-33905(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SELF-ASSOCIATION, INTERACTION WITH EIF2AK2.
    10. "The TAR RNA-binding protein, TRBP, stimulates the expression of TAR-containing RNAs in vitro and in vivo independently of its ability to inhibit the dsRNA-dependent kinase PKR."
      Dorin D., Bonnet M.C., Bannwarth S., Gatignol A., Meurs E.F., Vaquero C.
      J. Biol. Chem. 278:4440-4448(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Human RISC couples microRNA biogenesis and posttranscriptional gene silencing."
      Gregory R.I., Chendrimada T.P., Cooch N., Shiekhattar R.
      Cell 123:631-640(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DICER1 AND AGO2.
    12. "TRBP, a regulator of cellular PKR and HIV-1 virus expression, interacts with Dicer and functions in RNA silencing."
      Haase A.D., Jaskiewicz L., Zhang H., Laine S., Sack R., Gatignol A., Filipowicz W.
      EMBO Rep. 6:961-967(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SELF-ASSOCIATION, INTERACTION WITH DICER1.
    13. "A human, ATP-independent, RISC assembly machine fueled by pre-miRNA."
      Maniataki E., Mourelatos Z.
      Genes Dev. 19:2979-2990(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DICER1 AND AGO2.
    14. "TRBP recruits the Dicer complex to Ago2 for microRNA processing and gene silencing."
      Chendrimada T.P., Gregory R.I., Kumaraswamy E., Norman J., Cooch N., Nishikura K., Shiekhattar R.
      Nature 436:740-744(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH DICER1 AND AGO2, RNA-BINDING.
    15. "The role of PACT in the RNA silencing pathway."
      Lee Y., Hur I., Park S.-Y., Kim Y.-K., Suh M.R., Kim V.N.
      EMBO J. 25:522-532(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DICER1; AGO2 AND PRKRA, SUBCELLULAR LOCATION.
    16. "Human TRBP and PACT directly interact with each other and associate with dicer to facilitate the production of small interfering RNA."
      Kok K.H., Ng M.-H., Ching Y.-P., Jin D.-Y.
      J. Biol. Chem. 282:17649-17657(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SELF-ASSOCIATION, INTERACTION WITH DICER1 AND PRKRA, SUBCELLULAR LOCATION.
    17. "RNA helicase A interacts with RISC in human cells and functions in RISC loading."
      Robb G.B., Rana T.M.
      Mol. Cell 26:523-537(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DHX9.
    18. Cited for: INTERACTION WITH DICER1; AGO2; EIF6 AND MOV10, ASSOCIATION WITH THE 60S RIBOSOME.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH DICER1 AND AGO2.
    21. "Interactions between the double-stranded RNA-binding proteins TRBP and PACT define the Medipal domain that mediates protein-protein interactions."
      Laraki G., Clerzius G., Daher A., Melendez-Pena C., Daniels S., Gatignol A.
      RNA Biol. 5:92-103(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SELF-ASSOCIATION, INTERACTION WITH EIF2AK2 AND PRKRA, SUBCELLULAR LOCATION.
    22. Cited for: FUNCTION.
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Solution structure of the second DSRBD of TAR RNA-binding protein 2."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 150-225.

    Entry informationi

    Entry nameiTRBP2_HUMAN
    AccessioniPrimary (citable) accession number: Q15633
    Secondary accession number(s): Q12878
    , Q8WY32, Q8WY33, Q9BRY2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 137 of the entry and version 3 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 12
      Human chromosome 12: 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