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UniProtKB/Swiss-Prot entry P26599


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PTBP1_HUMAN
Primary accession number P26599
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 105)
Name and origin of the protein
Protein name Polypyrimidine tract-binding protein 1
Synonyms PTB
Heterogeneous nuclear ribonucleoprotein I
hnRNP I
57 kDa RNA-binding protein PPTB-1
Gene name
Name: PTBP1
Synonyms: PTB
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 123-130 AND 219-238.
TISSUE=Placenta;
PubMed=1906035 [NCBI, ExPASy, EBI, Israel, Japan]
Gil A., Sharp P.A., Jamison S.F., Garcia-Blanco M.A.;
"Characterization of cDNAs encoding the polypyrimidine tract-binding protein.";
Genes Dev. 5:1224-1236(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1906036 [NCBI, ExPASy, EBI, Israel, Japan]
Patton J.G., Mayer S.A., Tempst P., Nadal-Ginard B.;
"Characterization and molecular cloning of polypyrimidine tract-binding protein: a component of a complex necessary for pre-mRNA splicing.";
Genes Dev. 5:1237-1251(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
DOI=10.1093/nar/20.14.3671; PubMed=1641332 [NCBI, ExPASy, EBI, Israel, Japan]
Ghetti A., Pinol-Roma S., Michael W., Morandi C., Dreyfuss G.;
"hnRNP I, the polypyrimidine tract-binding protein: distinct nuclear localization and association with hnRNAs.";
Nucleic Acids Res. 20:3671-3678(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02399; PubMed=15057824 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 1-13; 65-92; 123-134; 219-238; 326-348; 411-418; 429-437 AND 472-482, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
TISSUE=Colon carcinoma, Hepatoma, and Mammary carcinoma;
Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E., Matallanas D., Cooper W.N., Boldt K., von Kriegsheim A.F., Kolch W.;
Submitted (JUL-2007) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 123-129; 399-405; 411-426 AND 429-437.
TISSUE=Keratinocyte;
PubMed=1286667 [NCBI, ExPASy, EBI, Israel, Japan]
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[8]
INTERACTION WITH SFPQ.
DOI=10.1002/(SICI)1097-4644(20000315)76:4<559::AID-JCB4>3.3.CO;2-L; PubMed=10653975 [NCBI, ExPASy, EBI, Israel, Japan]
Meissner M., Dechat T., Gerner C., Grimm R., Foisner R., Sauermann G.;
"Differential nuclear localization and nuclear matrix association of the splicing factors PSF and PTB.";
J. Cell. Biochem. 76:559-566(2000).
[9]
FUNCTION, AND INTERACTION WITH HNRPH1; PTBP2 AND KHSRP.
DOI=10.1128/MCB.20.20.7463-7479.2000; PubMed=11003644 [NCBI, ExPASy, EBI, Israel, Japan]
Markovtsov V., Nikolic J.M., Goldman J.A., Turck C.W., Chou M.-Y., Black D.L.;
"Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein.";
Mol. Cell. Biol. 20:7463-7479(2000).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-127, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-433, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"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.";
J. Proteome Res. 6:4150-4162(2007).
[12]
STRUCTURE BY NMR OF 335-531, AND RNA-BINDING.
DOI=10.1093/emboj/19.12.3132; PubMed=10856256 [NCBI, ExPASy, EBI, Israel, Japan]
Conte M.R., Gruene T., Ghuman J., Kelly G., Ladas A., Matthews S., Curry S.;
"Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold.";
EMBO J. 19:3132-3141(2000).
[13]
STRUCTURE BY NMR OF 55-301, SUBUNIT, AND RNA-BINDING.
DOI=10.1016/j.str.2004.07.008; PubMed=15341728 [NCBI, ExPASy, EBI, Israel, Japan]
Simpson P.J., Monie T.P., Szendroei A., Davydova N., Tyzack J.K., Conte M.R., Read C.M., Cary P.D., Svergun D.I., Konarev P.V., Curry S., Matthews S.;
"Structure and RNA interactions of the N-terminal RRM domains of PTB.";
Structure 12:1631-1643(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X62006; CAA43973.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X65371; CAA46443.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X65372; CAA46444.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X60648; CAA43056.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X66975; CAA47386.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC006273; AAC99798.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004383; AAH04383.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S23016; S23016.
RefSeq NP_114368.1; -.
UniGene Hs.172550
3D structure databases
PDB
1QM9; NMR; -; A=335-531.[ExPASy / RCSB / EBI]
1SJQ; NMR; -; A=55-147.[ExPASy / RCSB / EBI]
1SJR; NMR; -; A=147-301.[ExPASy / RCSB / EBI]
2AD9; NMR; -; A=49-146.[ExPASy / RCSB / EBI]
2ADB; NMR; -; A=172-298.[ExPASy / RCSB / EBI]
2ADC; NMR; -; A=324-531.[ExPASy / RCSB / EBI]
2EVZ; NMR; -; A=324-531.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1QM9; -.
1SJQ; -.
1SJR; -.
2AD9; -.
2ADB; -.
2ADC; -.
2EVZ; -.
ModBase P26599.
Protein-protein interaction databases
IntAct P26599; -.
PTM databases
PhosphoSite P26599; -.
Enzyme and pathway databases
Reactome REACT_1675; mRNA Processing.
REACT_6167; Influenza Infection.
REACT_71; Gene Expression.
2D gel databases
SWISS-2DPAGE P26599; -.
Aarhus/Ghent-2DPAGE 1505; NEPHGE.
Organism-specific databases
H-InvDB HIX0040348; -.
HGNC HGNC:9583; PTBP1.
GenAtlas PTBP1.
HPA CAB013507; -.
MIM 600693; gene. [NCBI / EBI]
PharmGKB PA33934; -.
GeneCards P26599.
Gene expression databases
ArrayExpress P26599; -.
CleanEx HS_PTBP1; -.
GermOnline ENSG00000011304; Homo sapiens.
Ontologies
GO
GO:0030530; Cellular component: heterogeneous nuclear ribonucleoprotein complex (traceable author statement from ProtInc).
GO:0005730; Cellular component: nucleolus (traceable author statement from ProtInc).
GO:0005654; Cellular component: nucleoplasm (traceable author statement from ProtInc).
GO:0008187; Molecular function: poly-pyrimidine tract binding (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0000398; Biological process: nuclear mRNA splicing, via spliceosome (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR012677; a_b_plait_nuc_bd.
IPR006536; HnRNP-L_PTB.
IPR000504; RRM_RNP1.
Graphical view of domain structure.
Gene3D G3DSA:3.30.70.330; a_b_plait_nuc_bd; 4.
Pfam PF00076; RRM_1; 3.
Pfam graphical view of domain structure.
SMART SM00360; RRM; 4.
SMART graphical view of domain structure.
TIGRFAMs TIGR01649; hnRNP-L_PTB; 1.
PROSITE PS50102; RRM; 4.
PROSITE graphical view of domain structure (profiles).
BLOCKS P26599.
Genome annotation databases
Ensembl ENSG00000011304; Homo sapiens. [Contig view]
GeneID 5725; -.
Phylogenomic databases
HOVERGEN P26599; -.
Other
LinkHub P26599; -.
SOURCE PTBP1; Homo sapiens.
ProtoNet P26599.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Repeat; RNA-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   531  531     Polypyrimidine tract-binding protein 1. PRO_0000081737
DOMAIN   59   143  85     RRM 1. 
DOMAIN   184   260  77     RRM 2. 
DOMAIN   337   411  75     RRM 3. 
DOMAIN   454   529  76     RRM 4. 
COMPBIAS   316   323  8     Poly-Ala. 
MOD_RES   1     1        N-acetylmethionine. 
MOD_RES   127   127        Phosphotyrosine. 
MOD_RES   141   141        Phosphoserine. 
MOD_RES   433   433        Phosphoserine. 
VAR_SEQ   297   297        F -> FASPYAGAGFPPTFAIPQAA (in isoform 2). VSP_005802
STRAND   60    63  4      
HELIX   72    82  11      
STRAND   85    91  7      
TURN   92    95  4      
STRAND   96   103  8      
HELIX   104   114  11      
STRAND   132   135  4      
STRAND   183   188  6      
HELIX   197   207  11      
STRAND   210   220  11      
STRAND   222   229  8      
HELIX   231   240  10      
STRAND   246   249  4      
STRAND   253   257  5      
STRAND   259   262  4      
STRAND   269   276  8      
HELIX   329   332  4      
STRAND   339   342  4      
STRAND   346   348  3      
HELIX   351   359  9      
STRAND   365   368  4      
STRAND   378   380  3      
TURN   382   384  3      
HELIX   385   394  10      
STRAND   405   408  4      
STRAND   417   425  9      
STRAND   427   431  5      
STRAND   437   440  4      
STRAND   455   458  4      
HELIX   467   476  10      
STRAND   483   488  6      
STRAND   494   497  4      
HELIX   501   511  11      
STRAND   524   527  4      
Sequence information
Length: 531 AA [This is the length of the unprocessed precursor] Molecular weight: 57221 Da [This is the MW of the unprocessed precursor] CRC64: BE12D5EA21537BED [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDGIVPDIAV GTKRGSDELF STCVTNGPFI MSSNSASAAN GNDSKKFKGD SRSAGVPSRV 

        70         80         90        100        110        120 
IHIRKLPIDV TEGEVISLGL PFGKVTNLLM LKGKNQAFIE MNTEEAANTM VNYYTSVTPV 

       130        140        150        160        170        180 
LRGQPIYIQF SNHKELKTDS SPNQARAQAA LQAVNSVQSG NLALAASAAA VDAGMAMAGQ 

       190        200        210        220        230        240 
SPVLRIIVEN LFYPVTLDVL HQIFSKFGTV LKIITFTKNN QFQALLQYAD PVSAQHAKLS 

       250        260        270        280        290        300 
LDGQNIYNAC CTLRIDFSKL TSLNVKYNND KSRDYTRPDL PSGDSQPSLD QTMAAAFGLS 

       310        320        330        340        350        360 
VPNVHGALAP LAIPSAAAAA AAAGRIAIPG LAGAGNSVLL VSNLNPERVT PQSLFILFGV 

       370        380        390        400        410        420 
YGDVQRVKIL FNKKENALVQ MADGNQAQLA MSHLNGHKLH GKPIRITLSK HQNVQLPREG 

       430        440        450        460        470        480 
QEDQGLTKDY GNSPLHRFKK PGSKNFQNIF PPSATLHLSN IPPSVSEEDL KVLFSSNGGV 

       490        500        510        520        530 
VKGFKFFQKD RKMALIQMGS VEEAVQALID LHNHDLGENH HLRVSFSKST I 

P26599 in FASTA format

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View entry in raw text format (no links)
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