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Q9UKA9

- PTBP2_HUMAN

UniProt

Q9UKA9 - PTBP2_HUMAN

Protein

Polypyrimidine tract-binding protein 2

Gene

PTBP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    RNA-binding protein which binds to intronic polypyrimidine tracts and mediates negative regulation of exons splicing. May antagonize in a tissue-specific manner the ability of NOVA1 to activate exon selection. In addition to its function in pre-mRNA splicing, plays also a role in the regulation of translation. Isoform 5 has a reduced affinity for RNA.2 Publications

    GO - Molecular functioni

    1. mRNA binding Source: Ensembl
    2. nucleotide binding Source: InterPro
    3. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. mRNA splice site selection Source: Ensembl
    2. negative regulation of RNA splicing Source: UniProtKB
    3. regulation of neural precursor cell proliferation Source: Ensembl

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polypyrimidine tract-binding protein 2
    Alternative name(s):
    Neural polypyrimidine tract-binding protein
    Neurally-enriched homolog of PTB
    PTB-like protein
    Gene namesi
    Name:PTBP2
    Synonyms:NPTB, PTB, PTBLP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:17662. PTBP2.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. spliceosomal complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33935.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 531531Polypyrimidine tract-binding protein 2PRO_0000232928Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei308 – 3081Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UKA9.
    PaxDbiQ9UKA9.
    PRIDEiQ9UKA9.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00647067.

    PTM databases

    PhosphoSiteiQ9UKA9.

    Expressioni

    Tissue specificityi

    Mainly expressed in brain although also detected in other tissues like heart and skeletal muscle. Isoform 1 and isoform 2 are specifically expressed in neuronal tissues. Isoform 3 and isoform 4 are expressed in non-neuronal tissues. Isoform 5 and isoform 6 are truncated forms expressed in non-neuronal tissues.2 Publications

    Gene expression databases

    ArrayExpressiQ9UKA9.
    BgeeiQ9UKA9.
    CleanExiHS_PTBP2.
    GenevestigatoriQ9UKA9.

    Organism-specific databases

    HPAiHPA047420.

    Interactioni

    Subunit structurei

    Monomer. Interacts with NOVA1; the interaction is direct. Interacts with NOVA2; the interaction is direct By similarity. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Part of a ternary complex containing KHSRP and HNRPH1.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi121796. 21 interactions.
    IntActiQ9UKA9. 19 interactions.
    MINTiMINT-1483252.
    STRINGi9606.ENSP00000412788.

    Structurei

    Secondary structure

    1
    531
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi59 – 657
    Helixi72 – 776
    Turni78 – 825
    Beta strandi85 – 917
    Turni92 – 954
    Beta strandi96 – 1038
    Helixi104 – 11613
    Beta strandi127 – 1304
    Beta strandi339 – 3446
    Turni347 – 3493
    Helixi352 – 3598
    Turni360 – 3623
    Beta strandi365 – 3717
    Beta strandi374 – 38411
    Helixi385 – 39511
    Beta strandi400 – 4034
    Beta strandi406 – 4094
    Beta strandi419 – 4224
    Turni423 – 4253
    Beta strandi428 – 4303
    Helixi431 – 4333
    Helixi444 – 4463
    Beta strandi447 – 4504
    Beta strandi455 – 4606
    Helixi468 – 4769
    Turni477 – 4793
    Beta strandi482 – 4876
    Beta strandi494 – 5007
    Helixi501 – 51111
    Beta strandi515 – 5173
    Beta strandi523 – 5264

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CQ1NMR-A51-138[»]
    2MJUNMR-A325-531[»]
    4CQ1X-ray1.69A/B/C/D/E/F/G/H336-531[»]
    ProteinModelPortaliQ9UKA9.
    SMRiQ9UKA9. Positions 51-138, 177-281, 325-531.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UKA9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini59 – 13375RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini181 – 25777RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini338 – 41275RRM 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini455 – 52975RRM 4PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi315 – 32410Poly-Ala

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG263741.
    HOVERGENiHBG069548.
    KOiK14948.
    PhylomeDBiQ9UKA9.
    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]
    SMARTiSM00360. RRM. 4 hits.
    [Graphical view]
    TIGRFAMsiTIGR01649. hnRNP-L_PTB. 1 hit.
    PROSITEiPS50102. RRM. 4 hits.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UKA9-1) [UniParc]FASTAAdd to Basket

    Also known as: nPTB1

    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

    MDGIVTEVAV GVKRGSDELL SGSVLSSPNS NMSSMVVTAN GNDSKKFKGE    50
    DKMDGAPSRV LHIRKLPGEV TETEVIALGL PFGKVTNILM LKGKNQAFLE 100
    LATEEAAITM VNYYSAVTPH LRNQPIYIQY SNHKELKTDN TLNQRAQAVL 150
    QAVTAVQTAN TPLSGTTVSE SAVTPAQSPV LRIIIDNMYY PVTLDVLHQI 200
    FSKFGAVLKI ITFTKNNQFQ ALLQYGDPVN AQQAKLALDG QNIYNACCTL 250
    RIDFSKLVNL NVKYNNDKSR DYTRPDLPSG DGQPALDPAI AAAFAKETSL 300
    LAVPGALSPL AIPNAAAAAA AAAAGRVGMP GVSAGGNTVL LVSNLNEEMV 350
    TPQSLFTLFG VYGDVQRVKI LYNKKDSALI QMADGNQSQL AMNHLNGQKM 400
    YGKIIRVTLS KHQTVQLPRE GLDDQGLTKD FGNSPLHRFK KPGSKNFQNI 450
    FPPSATLHLS NIPPSVAEED LRTLFANTGG TVKAFKFFQD HKMALLQMAT 500
    VEEAIQALID LHNYNLGENH HLRVSFSKST I 531
    Length:531
    Mass (Da):57,491
    Last modified:May 1, 2000 - v1
    Checksum:i57ADA23F422AE02A
    GO
    Isoform 2 (identifier: Q9UKA9-2) [UniParc]FASTAAdd to Basket

    Also known as: nPTB2, PTBPLP-L

    The sequence of this isoform differs from the canonical sequence as follows:
         489-489: Q → QR

    Show »
    Length:532
    Mass (Da):57,647
    Checksum:iA77702A0B7A84298
    GO
    Isoform 3 (identifier: Q9UKA9-3) [UniParc]FASTAAdd to Basket

    Also known as: nPTB3, PTBPLP-L'

    The sequence of this isoform differs from the canonical sequence as follows:
         302-302: A → GLPVAA
         489-489: Q → QR

    Show »
    Length:537
    Mass (Da):58,084
    Checksum:i35F5BFD2614647B3
    GO
    Isoform 4 (identifier: Q9UKA9-4) [UniParc]FASTAAdd to Basket

    Also known as: nPTB4

    The sequence of this isoform differs from the canonical sequence as follows:
         302-302: A → GLPVAA

    Show »
    Length:536
    Mass (Da):57,928
    Checksum:i9510D0E9AC2FCBD6
    GO
    Isoform 5 (identifier: Q9UKA9-5) [UniParc]FASTAAdd to Basket

    Also known as: nPTB5, nPTB7, PTBPLP-S

    The sequence of this isoform differs from the canonical sequence as follows:
         349-356: MVTPQSLF → VFMEMCSV
         357-531: Missing.

    Show »
    Length:356
    Mass (Da):37,898
    Checksum:iC1D3D2E104207E27
    GO
    Isoform 6 (identifier: Q9UKA9-6) [UniParc]FASTAAdd to Basket

    Also known as: nPTB6, nPTB8, PTBPLP-S'

    The sequence of this isoform differs from the canonical sequence as follows:
         302-302: A → GLPVAA
         349-356: MVTPQSLF → VFMEMCSV
         357-531: Missing.

    Show »
    Length:361
    Mass (Da):38,336
    Checksum:iC47DB1BA2B404A03
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei302 – 3021A → GLPVAA in isoform 3, isoform 4 and isoform 6. 1 PublicationVSP_018015
    Alternative sequencei349 – 3568MVTPQSLF → VFMEMCSV in isoform 5 and isoform 6. 2 PublicationsVSP_018016
    Alternative sequencei357 – 531175Missing in isoform 5 and isoform 6. 2 PublicationsVSP_018017Add
    BLAST
    Alternative sequencei489 – 4891Q → QR in isoform 2 and isoform 3. 3 PublicationsVSP_018018

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF176085 mRNA. Translation: AAF14284.1.
    AB051232 mRNA. Translation: BAB71742.1.
    AB051233 mRNA. Translation: BAB71743.1.
    AF530580 mRNA. Translation: AAM94624.1.
    AF530581 mRNA. Translation: AAM94625.1.
    AF530582 mRNA. Translation: AAM94626.1.
    AF530583 mRNA. Translation: AAM94627.1.
    BK000526 mRNA. Translation: DAA00060.1.
    AL357150 Genomic DNA. Translation: CAH70266.1.
    AL357150 Genomic DNA. Translation: CAH70267.1.
    AL357150 Genomic DNA. Translation: CAH70268.1.
    AL357150 Genomic DNA. Translation: CAH70269.1.
    BC016582 mRNA. Translation: AAH16582.1.
    CCDSiCCDS754.1. [Q9UKA9-1]
    RefSeqiNP_067013.1. NM_021190.2. [Q9UKA9-1]
    XP_005271141.1. XM_005271084.1. [Q9UKA9-3]
    XP_005271142.1. XM_005271085.1. [Q9UKA9-4]
    XP_005271143.1. XM_005271086.1. [Q9UKA9-2]
    UniGeneiHs.596061.
    Hs.743449.

    Genome annotation databases

    EnsembliENST00000370197; ENSP00000359216; ENSG00000117569. [Q9UKA9-3]
    ENST00000370198; ENSP00000359217; ENSG00000117569. [Q9UKA9-4]
    ENST00000426398; ENSP00000412788; ENSG00000117569. [Q9UKA9-1]
    ENST00000609116; ENSP00000477024; ENSG00000117569. [Q9UKA9-2]
    GeneIDi58155.
    KEGGihsa:58155.
    UCSCiuc001drn.2. human. [Q9UKA9-3]
    uc001dro.2. human. [Q9UKA9-2]
    uc001drq.3. human. [Q9UKA9-1]
    uc001drr.3. human. [Q9UKA9-4]

    Polymorphism databases

    DMDMi74761983.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF176085 mRNA. Translation: AAF14284.1 .
    AB051232 mRNA. Translation: BAB71742.1 .
    AB051233 mRNA. Translation: BAB71743.1 .
    AF530580 mRNA. Translation: AAM94624.1 .
    AF530581 mRNA. Translation: AAM94625.1 .
    AF530582 mRNA. Translation: AAM94626.1 .
    AF530583 mRNA. Translation: AAM94627.1 .
    BK000526 mRNA. Translation: DAA00060.1 .
    AL357150 Genomic DNA. Translation: CAH70266.1 .
    AL357150 Genomic DNA. Translation: CAH70267.1 .
    AL357150 Genomic DNA. Translation: CAH70268.1 .
    AL357150 Genomic DNA. Translation: CAH70269.1 .
    BC016582 mRNA. Translation: AAH16582.1 .
    CCDSi CCDS754.1. [Q9UKA9-1 ]
    RefSeqi NP_067013.1. NM_021190.2. [Q9UKA9-1 ]
    XP_005271141.1. XM_005271084.1. [Q9UKA9-3 ]
    XP_005271142.1. XM_005271085.1. [Q9UKA9-4 ]
    XP_005271143.1. XM_005271086.1. [Q9UKA9-2 ]
    UniGenei Hs.596061.
    Hs.743449.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CQ1 NMR - A 51-138 [» ]
    2MJU NMR - A 325-531 [» ]
    4CQ1 X-ray 1.69 A/B/C/D/E/F/G/H 336-531 [» ]
    ProteinModelPortali Q9UKA9.
    SMRi Q9UKA9. Positions 51-138, 177-281, 325-531.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121796. 21 interactions.
    IntActi Q9UKA9. 19 interactions.
    MINTi MINT-1483252.
    STRINGi 9606.ENSP00000412788.

    PTM databases

    PhosphoSitei Q9UKA9.

    Polymorphism databases

    DMDMi 74761983.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00647067.

    Proteomic databases

    MaxQBi Q9UKA9.
    PaxDbi Q9UKA9.
    PRIDEi Q9UKA9.

    Protocols and materials databases

    DNASUi 58155.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370197 ; ENSP00000359216 ; ENSG00000117569 . [Q9UKA9-3 ]
    ENST00000370198 ; ENSP00000359217 ; ENSG00000117569 . [Q9UKA9-4 ]
    ENST00000426398 ; ENSP00000412788 ; ENSG00000117569 . [Q9UKA9-1 ]
    ENST00000609116 ; ENSP00000477024 ; ENSG00000117569 . [Q9UKA9-2 ]
    GeneIDi 58155.
    KEGGi hsa:58155.
    UCSCi uc001drn.2. human. [Q9UKA9-3 ]
    uc001dro.2. human. [Q9UKA9-2 ]
    uc001drq.3. human. [Q9UKA9-1 ]
    uc001drr.3. human. [Q9UKA9-4 ]

    Organism-specific databases

    CTDi 58155.
    GeneCardsi GC01P097187.
    HGNCi HGNC:17662. PTBP2.
    HPAi HPA047420.
    MIMi 608449. gene.
    neXtProti NX_Q9UKA9.
    PharmGKBi PA33935.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG263741.
    HOVERGENi HBG069548.
    KOi K14948.
    PhylomeDBi Q9UKA9.
    TreeFami TF319824.

    Miscellaneous databases

    ChiTaRSi PTBP2. human.
    EvolutionaryTracei Q9UKA9.
    GeneWikii PTBP2.
    GenomeRNAii 58155.
    NextBioi 64859.
    PROi Q9UKA9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UKA9.
    Bgeei Q9UKA9.
    CleanExi HS_PTBP2.
    Genevestigatori Q9UKA9.

    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 ]
    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. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 55-65; 210-215; 216-235; 370-374; 404-411; 431-440 AND 487-492, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH HNRPH1 AND KHSRP.
      Tissue: Retinoblastoma.
    2. "Molecular cloning and characterization of human PTB-like protein: a possible retinal autoantigen of cancer-associated retinopathy."
      Tateiwa H., Gotoh N., Ichikawa M., Kikuchi T., Yoshimura N.
      J. Neuroimmunol. 120:161-169(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), ALTERNATIVE SPLICING (ISOFORMS 3 AND 6).
      Tissue: Retina.
    3. "Alternative splicing of brain-specific PTB defines a tissue-specific isoform pattern that predicts distinct functional roles."
      Rahman L., Bliskovski V., Reinhold W., Zajac-Kaye M.
      Genomics 80:245-249(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), NUCLEOTIDE SEQUENCE [MRNA] OF 282-531 (ISOFORMS 5 AND 6), ALTERNATIVE SPLICING (ISOFORM 2), TISSUE SPECIFICITY.
      Tissue: Cervix carcinoma, Lung and Retinoblastoma.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 2).
      Tissue: Eye.
    6. "The Apaf-1 internal ribosome entry segment attains the correct structural conformation for function via interactions with PTB and unr."
      Mitchell S.A., Spriggs K.A., Coldwell M.J., Jackson R.J., Willis A.E.
      Mol. Cell 11:757-771(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "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].
    8. "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."
      Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
      RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A MRNP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    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-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Solution structure of RNA-binding domain in PTB-like protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 51-138.

    Entry informationi

    Entry nameiPTBP2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKA9
    Secondary accession number(s): Q8N0Z1
    , Q8N160, Q8NFB0, Q8NFB1, Q969N9, Q96Q76
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 18, 2006
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 122 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 1
      Human chromosome 1: 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