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P26599

- PTBP1_HUMAN

UniProt

P26599 - PTBP1_HUMAN

Protein

Polypyrimidine tract-binding protein 1

Gene

PTBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Plays a role in pre-mRNA splicing and in the regulation of alternative splicing events. Activates exon skipping of its own pre-mRNA during muscle cell differentiation. Binds to the polypyrimidine tract of introns. May promote RNA looping when bound to two separate polypyrimidine tracts in the same pre-mRNA. May promote the binding of U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA. Represses the splicing of MAPT/Tau exon 10.5 Publications

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. poly-pyrimidine tract binding Source: ProtInc
    4. pre-mRNA binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. RNA binding Source: ProtInc

    GO - Biological processi

    1. alternative mRNA splicing, via spliceosome Source: Ensembl
    2. gene expression Source: Reactome
    3. mRNA processing Source: ProtInc
    4. mRNA splicing, via spliceosome Source: Reactome
    5. negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
    6. negative regulation of muscle cell differentiation Source: UniProtKB
    7. negative regulation of RNA splicing Source: UniProtKB
    8. regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
    9. RNA splicing Source: Reactome

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polypyrimidine tract-binding protein 1
    Short name:
    PTB
    Alternative name(s):
    57 kDa RNA-binding protein PPTB-1
    Heterogeneous nuclear ribonucleoprotein I
    Short name:
    hnRNP I
    Gene namesi
    Name:PTBP1
    Synonyms:PTB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9583. PTBP1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. membrane Source: UniProtKB
    3. nucleolus Source: ProtInc
    4. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33934.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 531531Polypyrimidine tract-binding protein 1PRO_0000081737Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei16 – 161Phosphoserine1 Publication
    Modified residuei138 – 1381Phosphothreonine1 Publication
    Modified residuei141 – 1411Phosphoserine3 Publications
    Modified residuei433 – 4331Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP26599.
    PaxDbiP26599.
    PRIDEiP26599.

    2D gel databases

    SWISS-2DPAGEP26599.

    PTM databases

    PhosphoSiteiP26599.

    Miscellaneous databases

    PMAP-CutDBP26599.

    Expressioni

    Gene expression databases

    ArrayExpressiP26599.
    BgeeiP26599.
    CleanExiHS_PTBP1.
    GenevestigatoriP26599.

    Organism-specific databases

    HPAiCAB013507.

    Interactioni

    Subunit structurei

    Monomer. Part of a ternary complex containing KHSRP, PTBP1, PTBP2 and HNRPH1. Interacts with RAVER1 and SFPQ.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P299915EBI-350540,EBI-8826689From a different organism.
    hnrnpabQ7ZYE94EBI-350540,EBI-1086317From a different organism.
    PCBP1Q153652EBI-350540,EBI-946095
    QKIQ96PU83EBI-350540,EBI-945792
    SFPQP232462EBI-350540,EBI-355453

    Protein-protein interaction databases

    BioGridi111697. 93 interactions.
    IntActiP26599. 41 interactions.
    MINTiMINT-1348690.
    STRINGi9606.ENSP00000349428.

    Structurei

    Secondary structure

    1
    531
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi60 – 634
    Helixi72 – 8211
    Beta strandi85 – 917
    Turni92 – 954
    Beta strandi96 – 1038
    Helixi104 – 11411
    Beta strandi127 – 1304
    Beta strandi132 – 1354
    Turni142 – 1454
    Beta strandi182 – 1909
    Helixi197 – 2048
    Helixi205 – 2073
    Beta strandi210 – 2189
    Beta strandi221 – 2299
    Helixi231 – 24111
    Beta strandi245 – 2473
    Beta strandi250 – 2578
    Beta strandi259 – 2624
    Beta strandi269 – 2746
    Turni289 – 2913
    Turni294 – 2963
    Helixi329 – 3324
    Beta strandi339 – 3424
    Beta strandi346 – 3483
    Helixi351 – 3599
    Beta strandi365 – 3684
    Turni371 – 3733
    Beta strandi378 – 3803
    Turni382 – 3843
    Helixi385 – 39410
    Beta strandi400 – 4034
    Beta strandi405 – 4084
    Beta strandi417 – 4259
    Beta strandi427 – 4315
    Beta strandi437 – 4404
    Helixi444 – 4463
    Beta strandi455 – 4584
    Helixi467 – 47610
    Beta strandi483 – 4886
    Beta strandi494 – 4974
    Helixi501 – 51111
    Beta strandi515 – 5195
    Beta strandi524 – 5274

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QM9NMR-A335-531[»]
    1SJQNMR-A55-147[»]
    1SJRNMR-A147-301[»]
    2AD9NMR-A49-146[»]
    2ADBNMR-A172-298[»]
    2ADCNMR-A324-531[»]
    2EVZNMR-A324-531[»]
    3ZZYX-ray1.40A/B156-285[»]
    3ZZZX-ray1.55A/B156-285[»]
    ProteinModelPortaliP26599.
    SMRiP26599. Positions 49-146, 172-298, 324-531.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26599.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini59 – 14385RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini184 – 26077RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini337 – 41175RRM 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini454 – 52976RRM 4PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi316 – 3238Poly-Ala

    Sequence similaritiesi

    Contains 4 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG263741.
    HOGENOMiHOG000231699.
    HOVERGENiHBG069548.
    KOiK13218.
    OMAiMSAQHAK.
    OrthoDBiEOG7V7691.
    PhylomeDBiP26599.
    TreeFamiTF319824.

    Family and domain databases

    Gene3Di3.30.70.330. 4 hits.
    InterProiIPR006536. HnRNP-L_PTB.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 4 hits.
    [Graphical view]
    TIGRFAMsiTIGR01649. hnRNP-L_PTB. 1 hit.
    PROSITEiPS50102. RRM. 4 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P26599-1) [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

    MDGIVPDIAV GTKRGSDELF STCVTNGPFI MSSNSASAAN GNDSKKFKGD    50
    SRSAGVPSRV IHIRKLPIDV TEGEVISLGL PFGKVTNLLM LKGKNQAFIE 100
    MNTEEAANTM VNYYTSVTPV LRGQPIYIQF SNHKELKTDS SPNQARAQAA 150
    LQAVNSVQSG NLALAASAAA VDAGMAMAGQ SPVLRIIVEN LFYPVTLDVL 200
    HQIFSKFGTV LKIITFTKNN QFQALLQYAD PVSAQHAKLS LDGQNIYNAC 250
    CTLRIDFSKL TSLNVKYNND KSRDYTRPDL PSGDSQPSLD QTMAAAFGLS 300
    VPNVHGALAP LAIPSAAAAA AAAGRIAIPG LAGAGNSVLL VSNLNPERVT 350
    PQSLFILFGV YGDVQRVKIL FNKKENALVQ MADGNQAQLA MSHLNGHKLH 400
    GKPIRITLSK HQNVQLPREG QEDQGLTKDY GNSPLHRFKK PGSKNFQNIF 450
    PPSATLHLSN IPPSVSEEDL KVLFSSNGGV VKGFKFFQKD RKMALIQMGS 500
    VEEAVQALID LHNHDLGENH HLRVSFSKST I 531
    Length:531
    Mass (Da):57,221
    Last modified:August 1, 1992 - v1
    Checksum:iBE12D5EA21537BED
    GO
    Isoform 2 (identifier: P26599-2) [UniParc]FASTAAdd to Basket

    Also known as: PTB2

    The sequence of this isoform differs from the canonical sequence as follows:
         297-297: F → FASPYAGAGFPPTFAIPQAA

    Show »
    Length:550
    Mass (Da):59,037
    Checksum:i70CB96D0530CA091
    GO
    Isoform 3 (identifier: P26599-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         297-297: F → FGAPGIISASPYAGAGFPPTFAIPQAA

    Show »
    Length:557
    Mass (Da):59,633
    Checksum:iDAFE52BAC0E4BE5C
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei297 – 2971F → FASPYAGAGFPPTFAIPQAA in isoform 2. CuratedVSP_005802
    Alternative sequencei297 – 2971F → FGAPGIISASPYAGAGFPPT FAIPQAA in isoform 3. 2 PublicationsVSP_043649

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62006 mRNA. Translation: CAA43973.1.
    X65371 mRNA. Translation: CAA46443.1.
    X65372 mRNA. Translation: CAA46444.1.
    X60648 mRNA. Translation: CAA43056.1.
    X66975 mRNA. Translation: CAA47386.1.
    BT006819 mRNA. Translation: AAP35465.1.
    AC006273 Genomic DNA. Translation: AAC99798.1.
    CH471242 Genomic DNA. Translation: EAW61154.1.
    BC002397 mRNA. Translation: AAH02397.1.
    BC004383 mRNA. Translation: AAH04383.1.
    BC013694 mRNA. Translation: AAH13694.1.
    CCDSiCCDS32859.1. [P26599-1]
    CCDS42456.1. [P26599-3]
    CCDS45892.1. [P26599-2]
    PIRiS23016.
    RefSeqiNP_002810.1. NM_002819.4. [P26599-3]
    NP_114367.1. NM_031990.3. [P26599-2]
    NP_114368.1. NM_031991.3. [P26599-1]
    UniGeneiHs.172550.

    Genome annotation databases

    EnsembliENST00000349038; ENSP00000014112; ENSG00000011304. [P26599-1]
    ENST00000356948; ENSP00000349428; ENSG00000011304. [P26599-3]
    ENST00000394601; ENSP00000408096; ENSG00000011304. [P26599-2]
    GeneIDi5725.
    KEGGihsa:5725.
    UCSCiuc002lpp.2. human. [P26599-3]
    uc002lpq.2. human. [P26599-2]
    uc002lpr.2. human. [P26599-1]

    Polymorphism databases

    DMDMi131528.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62006 mRNA. Translation: CAA43973.1 .
    X65371 mRNA. Translation: CAA46443.1 .
    X65372 mRNA. Translation: CAA46444.1 .
    X60648 mRNA. Translation: CAA43056.1 .
    X66975 mRNA. Translation: CAA47386.1 .
    BT006819 mRNA. Translation: AAP35465.1 .
    AC006273 Genomic DNA. Translation: AAC99798.1 .
    CH471242 Genomic DNA. Translation: EAW61154.1 .
    BC002397 mRNA. Translation: AAH02397.1 .
    BC004383 mRNA. Translation: AAH04383.1 .
    BC013694 mRNA. Translation: AAH13694.1 .
    CCDSi CCDS32859.1. [P26599-1 ]
    CCDS42456.1. [P26599-3 ]
    CCDS45892.1. [P26599-2 ]
    PIRi S23016.
    RefSeqi NP_002810.1. NM_002819.4. [P26599-3 ]
    NP_114367.1. NM_031990.3. [P26599-2 ]
    NP_114368.1. NM_031991.3. [P26599-1 ]
    UniGenei Hs.172550.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QM9 NMR - A 335-531 [» ]
    1SJQ NMR - A 55-147 [» ]
    1SJR NMR - A 147-301 [» ]
    2AD9 NMR - A 49-146 [» ]
    2ADB NMR - A 172-298 [» ]
    2ADC NMR - A 324-531 [» ]
    2EVZ NMR - A 324-531 [» ]
    3ZZY X-ray 1.40 A/B 156-285 [» ]
    3ZZZ X-ray 1.55 A/B 156-285 [» ]
    ProteinModelPortali P26599.
    SMRi P26599. Positions 49-146, 172-298, 324-531.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111697. 93 interactions.
    IntActi P26599. 41 interactions.
    MINTi MINT-1348690.
    STRINGi 9606.ENSP00000349428.

    Chemistry

    ChEMBLi CHEMBL1293230.

    PTM databases

    PhosphoSitei P26599.

    Polymorphism databases

    DMDMi 131528.

    2D gel databases

    SWISS-2DPAGE P26599.

    Proteomic databases

    MaxQBi P26599.
    PaxDbi P26599.
    PRIDEi P26599.

    Protocols and materials databases

    DNASUi 5725.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000349038 ; ENSP00000014112 ; ENSG00000011304 . [P26599-1 ]
    ENST00000356948 ; ENSP00000349428 ; ENSG00000011304 . [P26599-3 ]
    ENST00000394601 ; ENSP00000408096 ; ENSG00000011304 . [P26599-2 ]
    GeneIDi 5725.
    KEGGi hsa:5725.
    UCSCi uc002lpp.2. human. [P26599-3 ]
    uc002lpq.2. human. [P26599-2 ]
    uc002lpr.2. human. [P26599-1 ]

    Organism-specific databases

    CTDi 5725.
    GeneCardsi GC19P000797.
    H-InvDB HIX0137476.
    HGNCi HGNC:9583. PTBP1.
    HPAi CAB013507.
    MIMi 600693. gene.
    neXtProti NX_P26599.
    PharmGKBi PA33934.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG263741.
    HOGENOMi HOG000231699.
    HOVERGENi HBG069548.
    KOi K13218.
    OMAi MSAQHAK.
    OrthoDBi EOG7V7691.
    PhylomeDBi P26599.
    TreeFami TF319824.

    Enzyme and pathway databases

    Reactomei REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    EvolutionaryTracei P26599.
    GeneWikii PTBP1.
    GenomeRNAii 5725.
    NextBioi 22252.
    PMAP-CutDB P26599.
    PROi P26599.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26599.
    Bgeei P26599.
    CleanExi HS_PTBP1.
    Genevestigatori P26599.

    Family and domain databases

    Gene3Di 3.30.70.330. 4 hits.
    InterProi IPR006536. HnRNP-L_PTB.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 4 hits.
    [Graphical view ]
    TIGRFAMsi TIGR01649. hnRNP-L_PTB. 1 hit.
    PROSITEi PS50102. RRM. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of cDNAs encoding the polypyrimidine tract-binding protein."
      Gil A., Sharp P.A., Jamison S.F., Garcia-Blanco M.A.
      Genes Dev. 5:1224-1236(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 123-130 AND 219-238.
      Tissue: Placenta.
    2. "Characterization and molecular cloning of polypyrimidine tract-binding protein: a component of a complex necessary for pre-mRNA splicing."
      Patton J.G., Mayer S.A., Tempst P., Nadal-Ginard B.
      Genes Dev. 5:1237-1251(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "hnRNP I, the polypyrimidine tract-binding protein: distinct nuclear localization and association with hnRNAs."
      Ghetti A., Pinol-Roma S., Michael W., Morandi C., Dreyfuss G.
      Nucleic Acids Res. 20:3671-3678(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    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 3).
    5. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS 1 AND 3).
      Tissue: Lung, Ovary and Skin.
    8. Cited for: PROTEIN SEQUENCE OF 1-13; 65-92; 123-134; 219-238; 326-348; 411-418; 429-437 AND 472-482, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma, Hepatoma and Mammary carcinoma.
    9. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
      Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 123-129; 399-405; 411-426 AND 429-437.
      Tissue: Keratinocyte.
    10. "Differential nuclear localization and nuclear matrix association of the splicing factors PSF and PTB."
      Meissner M., Dechat T., Gerner C., Grimm R., Foisner R., Sauermann G.
      J. Cell. Biochem. 76:559-566(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SFPQ.
    11. "Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein."
      Markovtsov V., Nikolic J.M., Goldman J.A., Turck C.W., Chou M.-Y., Black D.L.
      Mol. Cell. Biol. 20:7463-7479(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HNRPH1; PTBP2 AND KHSRP.
    12. "Tau exon 10, whose missplicing causes frontotemporal dementia, is regulated by an intricate interplay of cis elements and trans factors."
      Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A.
      J. Neurochem. 88:1078-1090(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Exon selection in alpha-tropomyosin mRNA is regulated by the antagonistic action of RBM4 and PTB."
      Lin J.C., Tarn W.Y.
      Mol. Cell. Biol. 25:10111-10121(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING.
    14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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 THR-138 AND SER-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "RBM4 down-regulates PTB and antagonizes its activity in muscle cell-specific alternative splicing."
      Lin J.C., Tarn W.Y.
      J. Cell Biol. 193:509-520(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold."
      Conte M.R., Gruene T., Ghuman J., Kelly G., Ladas A., Matthews S., Curry S.
      EMBO J. 19:3132-3141(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 335-531, RNA-BINDING.
    25. Cited for: STRUCTURE BY NMR OF 55-301, SUBUNIT, RNA-BINDING.
    26. "Structure of PTB bound to RNA: specific binding and implications for splicing regulation."
      Oberstrass F.C., Auweter S.D., Erat M., Hargous Y., Henning A., Wenter P., Reymond L., Amir-Ahmady B., Pitsch S., Black D.L., Allain F.H.
      Science 309:2054-2057(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 49-531 IN COMPLEXES WITH RNA, FUNCTION.
    27. "Structure of the two most C-terminal RNA recognition motifs of PTB using segmental isotope labeling."
      Vitali F., Henning A., Oberstrass F.C., Hargous Y., Auweter S.D., Erat M., Allain F.H.
      EMBO J. 25:150-162(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 324-531.

    Entry informationi

    Entry nameiPTBP1_HUMAN
    AccessioniPrimary (citable) accession number: P26599
    Secondary accession number(s): Q9BUQ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 171 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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