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P26599

- PTBP1_HUMAN

UniProt

P26599 - PTBP1_HUMAN

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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

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. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP26599.
CleanExiHS_PTBP1.
ExpressionAtlasiP26599. baseline and differential.
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
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

Protein-protein interaction databases

BioGridi111697. 93 interactions.
IntActiP26599. 42 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.
GeneTreeiENSGT00550000074508.
HOGENOMiHOG000231699.
HOVERGENiHBG069548.
InParanoidiP26599.
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

        10         20         30         40         50
MDGIVPDIAV GTKRGSDELF STCVTNGPFI MSSNSASAAN GNDSKKFKGD
60 70 80 90 100
SRSAGVPSRV IHIRKLPIDV TEGEVISLGL PFGKVTNLLM LKGKNQAFIE
110 120 130 140 150
MNTEEAANTM VNYYTSVTPV LRGQPIYIQF SNHKELKTDS SPNQARAQAA
160 170 180 190 200
LQAVNSVQSG NLALAASAAA VDAGMAMAGQ SPVLRIIVEN LFYPVTLDVL
210 220 230 240 250
HQIFSKFGTV LKIITFTKNN QFQALLQYAD PVSAQHAKLS LDGQNIYNAC
260 270 280 290 300
CTLRIDFSKL TSLNVKYNND KSRDYTRPDL PSGDSQPSLD QTMAAAFGLS
310 320 330 340 350
VPNVHGALAP LAIPSAAAAA AAAGRIAIPG LAGAGNSVLL VSNLNPERVT
360 370 380 390 400
PQSLFILFGV YGDVQRVKIL FNKKENALVQ MADGNQAQLA MSHLNGHKLH
410 420 430 440 450
GKPIRITLSK HQNVQLPREG QEDQGLTKDY GNSPLHRFKK PGSKNFQNIF
460 470 480 490 500
PPSATLHLSN IPPSVSEEDL KVLFSSNGGV VKGFKFFQKD RKMALIQMGS
510 520 530
VEEAVQALID LHNHDLGENH HLRVSFSKST I
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. 42 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.
GeneTreei ENSGT00550000074508.
HOGENOMi HOG000231699.
HOVERGENi HBG069548.
InParanoidi P26599.
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

Bgeei P26599.
CleanExi HS_PTBP1.
ExpressionAtlasi P26599. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 172 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