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P26599 (PTBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 169. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PTBP1
Synonyms:PTB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length531 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11 Ref.12 Ref.13 Ref.20 Ref.26

Subunit structure

Monomer. Part of a ternary complex containing KHSRP, PTBP1, PTBP2 and HNRPH1. Interacts with RAVER1 and SFPQ. Ref.10 Ref.11 Ref.25

Subcellular location

Nucleus.

Sequence similarities

Contains 4 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandRNA-binding
   Molecular functionActivator
Repressor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Traceable author statement. Source: Reactome

alternative mRNA splicing, via spliceosome

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

mRNA processing

Traceable author statement Ref.2. Source: ProtInc

mRNA splicing, via spliceosome

Traceable author statement. Source: Reactome

negative regulation of RNA splicing

Inferred from direct assay PubMed 18335065. Source: UniProtKB

negative regulation of mRNA splicing, via spliceosome

Inferred from direct assay Ref.12. Source: UniProtKB

negative regulation of muscle cell differentiation

Inferred from direct assay Ref.20. Source: UniProtKB

regulation of alternative mRNA splicing, via spliceosome

Inferred from direct assay Ref.13Ref.20. Source: UniProtKB

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nucleolus

Traceable author statement Ref.3. Source: ProtInc

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionRNA binding

Traceable author statement Ref.2. Source: ProtInc

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

poly-pyrimidine tract binding

Traceable author statement Ref.2. Source: ProtInc

pre-mRNA binding

Inferred from direct assay Ref.13. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.10PubMed 11514619PubMed 16373488PubMed 16713569PubMed 21911577PubMed 22365833. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P299913EBI-350540,EBI-8826747From a different organism.
hnrnpabQ7ZYE94EBI-350540,EBI-1086317From a different organism.
PCBP1Q153652EBI-350540,EBI-946095
QKIQ96PU83EBI-350540,EBI-945792
SFPQP232462EBI-350540,EBI-355453

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P26599-1)

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.
Isoform 2 (identifier: P26599-2)

Also known as: PTB2;

The sequence of this isoform differs from the canonical sequence as follows:
     297-297: F → FASPYAGAGFPPTFAIPQAA
Isoform 3 (identifier: P26599-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 531531Polypyrimidine tract-binding protein 1
PRO_0000081737

Regions

Domain59 – 14385RRM 1
Domain184 – 26077RRM 2
Domain337 – 41175RRM 3
Domain454 – 52976RRM 4
Compositional bias316 – 3238Poly-Ala

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8 Ref.17 Ref.23
Modified residue161Phosphoserine Ref.16
Modified residue1381Phosphothreonine Ref.18
Modified residue1411Phosphoserine Ref.16 Ref.18 Ref.21
Modified residue4331Phosphoserine Ref.15 Ref.21

Natural variations

Alternative sequence2971F → FASPYAGAGFPPTFAIPQAA in isoform 2.
VSP_005802
Alternative sequence2971F → FGAPGIISASPYAGAGFPPT FAIPQAA in isoform 3.
VSP_043649

Secondary structure

.................................................................................. 531
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: BE12D5EA21537BED

FASTA53157,221
        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 

« Hide

Isoform 2 (PTB2) [UniParc].

Checksum: 70CB96D0530CA091
Show »

FASTA55059,037
Isoform 3 [UniParc].

Checksum: DAFE52BAC0E4BE5C
Show »

FASTA55759,633

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]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
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"Structure and RNA interactions of the N-terminal RRM domains of PTB."
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 12:1631-1643(2004) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS32859.1. [P26599-1]
CCDS42456.1. [P26599-3]
CCDS45892.1. [P26599-2]
PIRS23016.
RefSeqNP_002810.1. NM_002819.4. [P26599-3]
NP_114367.1. NM_031990.3. [P26599-2]
NP_114368.1. NM_031991.3. [P26599-1]
UniGeneHs.172550.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP26599.
SMRP26599. Positions 49-146, 172-298, 324-531.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111697. 91 interactions.
IntActP26599. 41 interactions.
MINTMINT-1348690.
STRING9606.ENSP00000349428.

Chemistry

ChEMBLCHEMBL1293230.

PTM databases

PhosphoSiteP26599.

Polymorphism databases

DMDM131528.

2D gel databases

SWISS-2DPAGEP26599.

Proteomic databases

MaxQBP26599.
PaxDbP26599.
PRIDEP26599.

Protocols and materials databases

DNASU5725.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000349038; ENSP00000014112; ENSG00000011304. [P26599-1]
ENST00000356948; ENSP00000349428; ENSG00000011304. [P26599-3]
ENST00000394601; ENSP00000408096; ENSG00000011304. [P26599-2]
GeneID5725.
KEGGhsa:5725.
UCSCuc002lpp.2. human. [P26599-3]
uc002lpq.2. human. [P26599-2]
uc002lpr.2. human. [P26599-1]

Organism-specific databases

CTD5725.
GeneCardsGC19P000797.
H-InvDBHIX0137476.
HGNCHGNC:9583. PTBP1.
HPACAB013507.
MIM600693. gene.
neXtProtNX_P26599.
PharmGKBPA33934.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG263741.
HOGENOMHOG000231699.
HOVERGENHBG069548.
KOK13218.
OMAMSAQHAK.
OrthoDBEOG7V7691.
PhylomeDBP26599.
TreeFamTF319824.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP26599.
BgeeP26599.
CleanExHS_PTBP1.
GenevestigatorP26599.

Family and domain databases

Gene3D3.30.70.330. 4 hits.
InterProIPR006536. HnRNP-L_PTB.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 4 hits.
[Graphical view]
TIGRFAMsTIGR01649. hnRNP-L_PTB. 1 hit.
PROSITEPS50102. RRM. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26599.
GeneWikiPTBP1.
GenomeRNAi5725.
NextBio22252.
PMAP-CutDBP26599.
PROP26599.
SOURCESearch...

Entry information

Entry namePTBP1_HUMAN
AccessionPrimary (citable) accession number: P26599
Secondary accession number(s): Q9BUQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 9, 2014
This is version 169 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM