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3.A.18.1.1
The nuclear mRNA Export Complex (mRNA-E also called TREX) (including the exon junction complex) [TAP+p15 interact as a complex with the nuclear pore to facilitate mRNA transport to the cytoplasm] (Nojimma et al. 2007; Cheng et al., 2006)

Accession Number:Q9H307
Protein Name:Pinin
Length:717
Molecular Weight:81614.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Nucleus speckle1
Substrate mRNA

Cross database links:

Genevestigator: Q9H307
eggNOG: prNOG16657
RefSeq: NP_002678.2   
Entrez Gene ID: 5411   
Pfam: PF04696    PF04697   
OMIM: 603154  gene
KEGG: hsa:5411   

Gene Ontology

GO:0030057 C:desmosome
GO:0005882 C:intermediate filament
GO:0016607 C:nuclear speck
GO:0005681 C:spliceosomal complex
GO:0003677 F:DNA binding
GO:0005515 F:protein binding
GO:0005198 F:structural molecule activity
GO:0007155 P:cell adhesion
GO:0006397 P:mRNA processing
GO:0045449 P:regulation of transcription
GO:0008380 P:RNA splicing
GO:0006350 P:transcription

References (30)

[1] “Characterization of pinin, a novel protein associated with the desmosome-intermediate filament complex.”  Ouyang P.et.al.   8922384
[2] “memA/DRS, a putative mediator of multiprotein complexes, is overexpressed in the metastasizing human melanoma cell lines BLM and MV3.”  Degen W.G.J.et.al.   10095061
[3] “Characterization of the gene encoding pinin/DRS/memA and evidence for its potential tumor suppressor function.”  Shi Y.et.al.   10645008
[4] “Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning.”  Hu R.-M.et.al.   10931946
[5] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[6] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[7] “Evidence that 'pinin', reportedly a differentiation-specific desmosomal protein, is actually a widespread nuclear protein.”  Brandner J.et.al.   9447706
[8] “Antibodies differentiate desmosome-form and nucleus-form pinin: evidence that pinin is a moonlighting protein with dual location at the desmosome and within the nucleus.”  Ouyang P.et.al.   10486276
[9] “Dissection of protein linkage between keratins and pinin, a protein with dual location at desmosome-intermediate filament complex and in the nucleus.”  Shi J.et.al.   10809736
[10] “Modulation of alternative pre-mRNA splicing in vivo by pinin.”  Wang P.et.al.   12051732
[11] “Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.”  Jurica M.S.et.al.   11991638
[12] “Molecular characterization of a novel nucleolar protein, pNO40.”  Chang W.-L.et.al.   12893261
[13] “Pinin/DRS/memA interacts with SRp75, SRm300 and SRrp130 in corneal epithelial cells.”  Zimowska G.et.al.   14578391
[14] “Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in mRNA processing and export via interaction with RNPS1.”  Li C.et.al.   14517304
[15] “Over-expression of SR-cyclophilin, an interaction partner of nuclear pinin, releases SR family splicing factors from nuclear speckles.”  Lin C.L.et.al.   15358154
[16] “Human RNPS1 and its associated factors: a versatile alternative pre-mRNA splicing regulator in vivo.”  Sakashita E.et.al.   14729963
[17] “Nuclear speckle-associated protein Pnn/DRS binds to the transcriptional corepressor CtBP and relieves CtBP-mediated repression of the E-cadherin gene.”  Alpatov R.et.al.   15542832
[18] “Reduction of Pnn by RNAi induces loss of cell-cell adhesion between human corneal epithelial cells.”  Joo J.-H.et.al.   15735603
[19] “Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core.”  Tange T.O.et.al.   16314458
[20] “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.”  Olsen J.V.et.al.   17081983
[21] “A probability-based approach for high-throughput protein phosphorylation analysis and site localization.”  Beausoleil S.A.et.al.   16964243
[22] “Phosphoproteome analysis of the human mitotic spindle.”  Nousiainen M.et.al.   16565220
[23] “Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.”  Molina H.et.al.   17287340
[24] “ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.”  Matsuoka S.et.al.   17525332
[25] “Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis.”  Wang B.et.al.   19007248
[26] “Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.”  Daub H.et.al.   18691976
[27] “A quantitative atlas of mitotic phosphorylation.”  Dephoure N.et.al.   18669648
[28] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330
[29] “Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.”  Mayya V.et.al.   19690332
[30] “Lysine acetylation targets protein complexes and co-regulates major cellular functions.”  Choudhary C.et.al.   19608861

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FASTA formatted sequence
1:	MAVAVRTLQE QLEKAKESLK NVDENIRKLT GRDPNDVRPI QARLLALSGP GGGRGRGSLL 
61:	LRRGFSDSGG GPPAKQRDLE GAVSRLGGER RTRRESRQES DPEDDDVKKP ALQSSVVATS 
121:	KERTRRDLIQ DQNMDEKGKQ RNRRIFGLLM GTLQKFKQES TVATERQKRR QEIEQKLEVQ 
181:	AEEERKQVEN ERRELFEERR AKQTELRLLE QKVELAQLQE EWNEHNAKII KYIRTKTKPH 
241:	LFYIPGRMCP ATQKLIEESQ RKMNALFEGR RIEFAEQINK MEARPRRQSM KEKEHQVVRN 
301:	EEQKAEQEEG KVAQREEELE ETGNQHNDVE IEEAGEEEEK EIAIVHSDAE KEQEEEEQKQ 
361:	EMEVKMEEET EVRESEKQQD SQPEEVMDVL EMVENVKHVI ADQEVMETNR VESVEPSENE 
421:	ASKELEPEME FEIEPDKECK SLSPGKENVS ALDMEKESEE KEEKESEPQP EPVAQPQPQS 
481:	QPQLQLQSQS QPVLQSQPPS QPEDLSLAVL QPTPQVTQEQ GHLLPERKDF PVESVKLTEV 
541:	PVEPVLTVHP ESKSKTKTRS RSRGRARNKT SKSRSRSSSS SSSSSSSTSS SSGSSSSSGS 
601:	SSSRSSSSSS SSTSGSSSRD SSSSTSSSSE SRSRSRGRGH NRDRKHRRSV DRKRRDTSGL 
661:	ERSHKSSKGG SSRDTKGSKD KNSRSDRKRS ISESSRSGKR SSRSERDRKS DRKDKRR