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Q9UKA9

- PTBP2_HUMAN

UniProt

Q9UKA9 - PTBP2_HUMAN

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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

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
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

BgeeiQ9UKA9.
CleanExiHS_PTBP2.
ExpressionAtlasiQ9UKA9. baseline and differential.
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 – 657Combined sources
Helixi72 – 776Combined sources
Turni78 – 825Combined sources
Beta strandi85 – 917Combined sources
Turni92 – 954Combined sources
Beta strandi96 – 1038Combined sources
Helixi104 – 11613Combined sources
Beta strandi127 – 1304Combined sources
Beta strandi339 – 3446Combined sources
Turni347 – 3493Combined sources
Helixi352 – 3598Combined sources
Turni360 – 3623Combined sources
Beta strandi365 – 3717Combined sources
Beta strandi374 – 38411Combined sources
Helixi385 – 39511Combined sources
Beta strandi400 – 4034Combined sources
Beta strandi406 – 4094Combined sources
Beta strandi419 – 4224Combined sources
Turni423 – 4253Combined sources
Beta strandi428 – 4303Combined sources
Helixi431 – 4333Combined sources
Helixi444 – 4463Combined sources
Beta strandi447 – 4504Combined sources
Beta strandi455 – 4606Combined sources
Helixi468 – 4769Combined sources
Turni477 – 4793Combined sources
Beta strandi482 – 4876Combined sources
Beta strandi494 – 5007Combined sources
Helixi501 – 51111Combined sources
Beta strandi515 – 5173Combined sources
Beta strandi523 – 5264Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00550000074508.
HOVERGENiHBG069548.
InParanoidiQ9UKA9.
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

        10         20         30         40         50
MDGIVTEVAV GVKRGSDELL SGSVLSSPNS NMSSMVVTAN GNDSKKFKGE
60 70 80 90 100
DKMDGAPSRV LHIRKLPGEV TETEVIALGL PFGKVTNILM LKGKNQAFLE
110 120 130 140 150
LATEEAAITM VNYYSAVTPH LRNQPIYIQY SNHKELKTDN TLNQRAQAVL
160 170 180 190 200
QAVTAVQTAN TPLSGTTVSE SAVTPAQSPV LRIIIDNMYY PVTLDVLHQI
210 220 230 240 250
FSKFGAVLKI ITFTKNNQFQ ALLQYGDPVN AQQAKLALDG QNIYNACCTL
260 270 280 290 300
RIDFSKLVNL NVKYNNDKSR DYTRPDLPSG DGQPALDPAI AAAFAKETSL
310 320 330 340 350
LAVPGALSPL AIPNAAAAAA AAAAGRVGMP GVSAGGNTVL LVSNLNEEMV
360 370 380 390 400
TPQSLFTLFG VYGDVQRVKI LYNKKDSALI QMADGNQSQL AMNHLNGQKM
410 420 430 440 450
YGKIIRVTLS KHQTVQLPRE GLDDQGLTKD FGNSPLHRFK KPGSKNFQNI
460 470 480 490 500
FPPSATLHLS NIPPSVAEED LRTLFANTGG TVKAFKFFQD HKMALLQMAT
510 520 530
VEEAIQALID LHNYNLGENH HLRVSFSKST I
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:
EMBLi
GenBanki
DDBJi
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.
CCDSiCCDS72828.1. [Q9UKA9-3]
CCDS72829.1. [Q9UKA9-4]
CCDS72830.1. [Q9UKA9-2]
CCDS754.1. [Q9UKA9-1]
RefSeqiNP_001287914.1. NM_001300985.1. [Q9UKA9-3]
NP_001287915.1. NM_001300986.1.
NP_001287916.1. NM_001300987.1.
NP_001287917.1. NM_001300988.1. [Q9UKA9-4]
NP_001287918.1. NM_001300989.1. [Q9UKA9-2]
NP_001287919.1. NM_001300990.1.
NP_067013.1. NM_021190.3. [Q9UKA9-1]
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:
EMBLi
GenBanki
DDBJi
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 CCDS72828.1. [Q9UKA9-3 ]
CCDS72829.1. [Q9UKA9-4 ]
CCDS72830.1. [Q9UKA9-2 ]
CCDS754.1. [Q9UKA9-1 ]
RefSeqi NP_001287914.1. NM_001300985.1. [Q9UKA9-3 ]
NP_001287915.1. NM_001300986.1.
NP_001287916.1. NM_001300987.1.
NP_001287917.1. NM_001300988.1. [Q9UKA9-4 ]
NP_001287918.1. NM_001300989.1. [Q9UKA9-2 ]
NP_001287919.1. NM_001300990.1.
NP_067013.1. NM_021190.3. [Q9UKA9-1 ]
UniGenei Hs.596061.
Hs.743449.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00550000074508.
HOVERGENi HBG069548.
InParanoidi Q9UKA9.
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

Bgeei Q9UKA9.
CleanExi HS_PTBP2.
ExpressionAtlasi Q9UKA9. baseline and differential.
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: November 26, 2014
This is version 124 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