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Q9UKA9

- PTBP2_HUMAN

UniProt

Q9UKA9 - PTBP2_HUMAN

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Protein

Polypyrimidine tract-binding protein 2

Gene
PTBP2, NPTB, PTB, PTBLP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. Beside 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
Complete GO annotation...

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
Complete GO annotation...

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 HNRPH1.2 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.

Miscellaneous databases

EvolutionaryTraceiQ9UKA9.

Family & Domainsi

Domains and Repeats

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

Compositional bias

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

Sequence similaritiesi

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. VSP_018015
Alternative sequencei349 – 3568MVTPQSLF → VFMEMCSV in isoform 5 and isoform 6. VSP_018016
Alternative sequencei357 – 531175Missing in isoform 5 and isoform 6. VSP_018017Add
BLAST
Alternative sequencei489 – 4891Q → QR in isoform 2 and isoform 3. VSP_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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 121 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

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