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Q15287 (RNPS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA-binding protein with serine-rich domain 1
Alternative name(s):
SR-related protein LDC2
Gene names
Name:RNPS1
Synonyms:LDC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length305 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of pre- and post-splicing multiprotein mRNP complexes. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Enhances the formation of the ATP-dependent A complex of the spliceosome. Involved in both constitutive splicing and, in association with SRP54 and TRA2B/SFRS10, in distinctive modulation of alternative splicing in a substrate-dependent manner. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Participates in mRNA 3'-end cleavage. Involved in UPF2-dependent nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Also mediates increase of mRNA abundance and translational efficiency. Binds spliced mRNA 20-25 nt upstream of exon-exon junctions. Ref.9 Ref.12 Ref.13 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.24 Ref.30

Subunit structure

Found in mRNA splicing-dependent exon junction complexes (EJC). Found in a post-splicing complex with NXF1, RBM8A, UPF1, UPF2, UPF3A, UPF3B and RNPS1. Component of the heterotrimeric ASAP (apoptosis- and splicing-associated protein) and PSAP complexes consisting of RNPS1, SAP18 and either ACIN1 or PNN, respectively; the ASAP and PSAP complexes probably are formed mutually exclusive. Component of the active spliceosome. Associates with polysomes. Interacts with the cleaved p110 isoform ofCDC2L1, CSNK2A1, PNN, SART3, SRP54, SRRM1 and TRA2B/SFRS10. Ref.2 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.27 Ref.31

Subcellular location

Nucleus. Nucleus speckle. Cytoplasm. Note: Nucleocytoplasmic shuttling protein. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles. Ref.2 Ref.9 Ref.11 Ref.12 Ref.14 Ref.17 Ref.18 Ref.25

Tissue specificity

Ubiquitous. Ref.1

Domain

The RRM domain is required for the formation of the ASAP complex.

Post-translational modification

Phosphorylated on one or more of the four Ser/Thr residues (Ser-43, Thr-49, Ser-52 or Ser-53). Ser-53 phosphorylation site is important for splicing and translation stimulation activity in vitro. Ref.18

Sequence similarities

Belongs to the splicing factor SR family.

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
Nonsense-mediated mRNA decay
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

RNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA 3'-end processing

Traceable author statement. Source: Reactome

mRNA export from nucleus

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Traceable author statement. Source: Reactome

negative regulation of mRNA splicing, via spliceosome

Inferred from direct assay Ref.20. Source: UniProtKB

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from direct assay Ref.12. Source: UniProtKB

positive regulation of apoptotic process

Inferred from direct assay Ref.20. Source: UniProtKB

regulation of alternative mRNA splicing, via spliceosome

Inferred from mutant phenotype Ref.30. Source: UniProtKB

termination of RNA polymerase II transcription

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement Ref.2. Source: ProtInc

   Cellular_componentASAP complex

Inferred from direct assay Ref.20. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.12. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.12. Source: UniProtKB

   Molecular_functionRNA binding

Traceable author statement Ref.2. Source: ProtInc

mRNA 3'-UTR binding

Inferred from direct assay Ref.12. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

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

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SART3Q150205EBI-395959,EBI-308619
SRPK1Q96SB42EBI-395959,EBI-539478

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15287-1)

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: Q15287-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2-24: Missing.
Isoform 3 (identifier: Q15287-3)

The sequence of this isoform differs from the canonical sequence as follows:
     2-24: Missing.
     69-82: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 305305RNA-binding protein with serine-rich domain 1
PRO_0000081816

Regions

Domain161 – 24080RRM
Region1 – 220220Necessary for interaction with the cleaved p110 isoform of CDC2L1
Region1 – 161161Necessary for interaction with SRP54, nuclear localization and exon-skipping
Region69 – 12153Necessary for interactions with UPF2 and UPF3B and UPF2-dependent NMD
Region156 – 24287Necessary for interaction with PNN and exon-skipping
Region159 – 24486Interaction with SAP18 and ACIN1
Region238 – 30568Necessary for interaction with TRA2B, nuclear localization and exon-skipping
Compositional bias7 – 6458Lys-rich
Compositional bias67 – 14175Ser-rich
Compositional bias128 – 15427Arg-rich
Compositional bias241 – 29858Arg/Pro-rich

Amino acid modifications

Modified residue531Phosphoserine; by CK2 Ref.18
Modified residue1551Phosphoserine Ref.29
Modified residue1571Phosphoserine Ref.29
Modified residue1611Phosphothreonine Ref.29
Modified residue2181N6-acetyllysine Ref.26

Natural variations

Alternative sequence2 – 2423Missing in isoform 2 and isoform 3.
VSP_016243
Alternative sequence69 – 8214Missing in isoform 3.
VSP_037601

Experimental info

Mutagenesis531S → A: Abolishes phosphorylation by CSNK2A1 and partially reduces splicing stimulation. Does not abolish interaction with CSNK2A1 and subcellular localization. Ref.18
Mutagenesis531S → E: Partially reduces splicing stimulation. Does not abolish interaction with CSNK2A1 and subcellular localization. Ref.18
Mutagenesis1711N → R: Impairs interaction with SAP18. Ref.31
Mutagenesis2051Y → A: Abolishes exon-skipping. Ref.17
Mutagenesis2071Y → A: Abolishes exon-skipping. Ref.17
Sequence conflict321K → E in BAG56859. Ref.4
Sequence conflict661R → G in AAC39791. Ref.2
Sequence conflict2491R → G in BAG56859. Ref.4

Secondary structure

.............. 305
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: 930C9D36C2486144

FASTA30534,208
        10         20         30         40         50         60 
MDLSGVKKKS LLGVKENNKK SSTRAPSPTK RKDRSDEKSK DRSKDKGATK ESSEKDRGRD 

        70         80         90        100        110        120 
KTRKRRSASS GSSSTRSRSS STSSSGSSTS TGSSSGSSSS SASSRSGSSS TSRSSSSSSS 

       130        140        150        160        170        180 
SGSPSPSRRR HDNRRRSRSK SKPPKRDEKE RKRRSPSPKP TKVHIGRLTR NVTKDHIMEI 

       190        200        210        220        230        240 
FSTYGKIKMI DMPVERMHPH LSKGYAYVEF ENPDEAEKAL KHMDGGQIDG QEITATAVLA 

       250        260        270        280        290        300 
PWPRPPPRRF SPPRRMLPPP PMWRRSPPRM RRRSRSPRRR SPVRRRSRSP GRRRHRSRSS 


SNSSR 

« Hide

Isoform 2 [UniParc].

Checksum: D3F7AAD16B6309F4
Show »

FASTA28231,709
Isoform 3 [UniParc].

Checksum: 9058DEEC9B433103
Show »

FASTA26830,354

References

« Hide 'large scale' references
[1]"Identification and characterisation of a novel human RNA-binding protein."
Badolato J., Gardiner E., Morrison N., Eisman J.
Gene 166:323-327(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Brain.
[2]"The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinases in vivo."
Loyer P., Trembley J.H., Lahti J.M., Kidd V.J.
J. Cell Sci. 111:1495-1506(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CDC2L1, SUBCELLULAR LOCATION.
Tissue: B-cell.
[3]"Identification of an alternatively spliced form of RNPS1."
Harada K., Yang D., Yamada A., Shichijo S., Itoh K.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Thymus.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
Tissue: Hippocampus and Tongue.
[5]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.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 (SEP-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] (ISOFORM 1).
Tissue: Muscle and Skin.
[8]"Direct interaction of LDC2, a SR-related protein with pinin."
Lee D.-C., Ouyang P.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 78-305.
Tissue: Kidney.
[9]"Purification and characterization of human RNPS1: a general activator of pre-mRNA splicing."
Mayeda A., Badolato J., Kobayashi R., Zhang M.Q., Gardiner E.M., Krainer A.R.
EMBO J. 18:4560-4570(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PRE-MRNA SPLICING, ASSOCIATION WITH THE SPLICEOSOME, SUBCELLULAR LOCATION.
[10]"The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions."
Le Hir H., Izaurralde E., Maquat L.E., Moore M.J.
EMBO J. 19:6860-6869(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH DEK; RBM8A; SRRM1 AND ALYREF/THOC4.
[11]"Binding of a SART3 tumor-rejection antigen to a pre-mRNA splicing factor RNPS1: a possible regulation of splicing by a complex formation."
Harada K., Yamada A., Yang D., Itoh K., Shichijo S.
Int. J. Cancer 93:623-628(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SART3, SUBCELLULAR LOCATION.
[12]"Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1."
Lykke-Andersen J., Shu M.-D., Steitz J.A.
Science 293:1836-1839(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, IDENTIFICATION IN A POST-SPLICING COMPLEX WITH NXF1; RBM8A; UPF1; UPF2; UPF3A AND UPF3B, RNA-BINDING, SUBCELLULAR LOCATION.
[13]"An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation."
McCracken S., Longman D., Johnstone I.L., Caceres J.F., Blencowe B.J.
J. Biol. Chem. 278:44153-44160(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MRNA 3'-END FORMATION, INTERACTION WITH SRRM1.
[14]"Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in mRNA processing and export via interaction with RNPS1."
Li C., Lin R.-I., Lai M.-C., Ouyang P., Tarn W.-Y.
Mol. Cell. Biol. 23:7363-7376(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH PNN, INTERACTION WITH PNN, SUBCELLULAR LOCATION.
[15]"Splicing enhances translation in mammalian cells: an additional function of the exon junction complex."
Nott A., Le Hir H., Moore M.J.
Genes Dev. 18:210-222(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSLATIONAL ACTIVITY AND NONSENSE-MEDIATED MRNA DECAY, ASSOCIATION WITH POLYSOMES.
[16]"A simple whole cell lysate system for in vitro splicing reveals a stepwise assembly of the exon-exon junction complex."
Kataoka N., Dreyfuss G.
J. Biol. Chem. 279:7009-7013(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH RBM8A AND SRRM1.
[17]"Human RNPS1 and its associated factors: a versatile alternative pre-mRNA splicing regulator in vivo."
Sakashita E., Tatsumi S., Werner D., Endo H., Mayeda A.
Mol. Cell. Biol. 24:1174-1187(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ALTERNATIVE PRE-MRNA SPLICING, INTERACTION WITH PNN; SRP54 AND TRA2B, MUTAGENESIS OF TYR-205 AND TYR-207, SUBCELLULAR LOCATION.
[18]"Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2 phosphorylation."
Trembley J.H., Tatsumi S., Sakashita E., Loyer P., Slaughter C.A., Suzuki H., Endo H., Kidd V.J., Mayeda A.
Mol. Cell. Biol. 25:1446-1457(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PRE-MRNA SPLICING, ASSOCIATION WITH THE ACTIVE SPLICEOSOME, PHOSPHORYLATION AT SER-53, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CSNK2A1, MUTAGENESIS OF SER-53, SUBCELLULAR LOCATION.
[19]"Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements."
Gehring N.H., Kunz J.B., Neu-Yilik G., Breit S., Viegas M.H., Hentze M.W., Kulozik A.E.
Mol. Cell 20:65-75(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN A RENT2-DEPENDENT NONSENSE-MEDIATED MRNA DECAY, IDENTIFICATION IN A COMPLEX WITH UPF2 AND UPF3B.
[20]"ASAP, a novel protein complex involved in RNA processing and apoptosis."
Schwerk C., Prasad J., Degenhardt K., Erdjument-Bromage H., White E., Tempst P., Kidd V.J., Manley J.L., Lahti J.M., Reinberg D.
Mol. Cell. Biol. 23:2981-2990(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE ASAP COMPLEX, FUNCTION OF THE ASAP COMPLEX.
[21]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core."
Tange T.O., Shibuya T., Jurica M.S., Moore M.J.
RNA 11:1869-1883(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, IDENTIFICATION IN THE ASAP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[23]"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.
[24]"The abundance of RNPS1, a protein component of the exon junction complex, can determine the variability in efficiency of the nonsense mediated decay pathway."
Viegas M.H., Gehring N.H., Breit S., Hentze M.W., Kulozik A.E.
Nucleic Acids Res. 35:4542-4551(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY (NMD).
[25]"Assembly and mobility of exon-exon junction complexes in living cells."
Schmidt U., Im K.-B., Benzing C., Janjetovic S., Rippe K., Lichter P., Wachsmuth M.
RNA 15:862-876(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[26]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Human SAP18 mediates assembly of a splicing regulatory multiprotein complex via its ubiquitin-like fold."
Singh K.K., Erkelenz S., Rattay S., Dehof A.K., Hildebrandt A., Schulze-Osthoff K., Schaal H., Schwerk C.
RNA 16:2442-2454(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SAP18 AND ACIN1.
[28]"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].
[29]"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-155; SER-157 AND THR-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"Proteins associated with the exon junction complex also control the alternative splicing of apoptotic regulators."
Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P., Durand M., Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H., Klinck R., Elela S.A., Prinos P., Chabot B.
Mol. Cell. Biol. 32:954-967(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[31]"The structure of the ASAP core complex reveals the existence of a Pinin-containing PSAP complex."
Murachelli A.G., Ebert J., Basquin C., Le Hir H., Conti E.
Nat. Struct. Mol. Biol. 19:378-386(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF THE ASAP COMPLEX, IDENTIFICATION IN THE PSAP COMPLEX, INTERACTION WITH SAP18, MUTAGENESIS OF ASN-171.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L37368 mRNA. Translation: AAA92859.1.
AF015608 mRNA. Translation: AAC39791.1.
AF274003 mRNA. Translation: AAL56665.1.
AK289955 mRNA. Translation: BAF82644.1.
AK293343 mRNA. Translation: BAG56859.1.
AK303100 mRNA. Translation: BAG64209.1.
AK316132 mRNA. Translation: BAH14503.1.
AC009065 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85516.1.
BC001659 mRNA. Translation: AAH01659.1.
BC001838 mRNA. Translation: AAH01838.1.
BC108316 mRNA. Translation: AAI08317.1.
AF247662 mRNA. Translation: AAF72519.1.
PIRJC4525.
RefSeqNP_001273554.1. NM_001286625.1.
NP_001273555.1. NM_001286626.1.
NP_001273556.1. NM_001286627.1.
NP_006702.1. NM_006711.4.
NP_542161.1. NM_080594.3.
XP_005255105.1. XM_005255048.1.
XP_005255106.1. XM_005255049.1.
UniGeneHs.355643.
Hs.507343.
Hs.733012.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4A8XX-ray1.90A159-244[»]
ProteinModelPortalQ15287.
SMRQ15287. Positions 157-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116125. 111 interactions.
DIPDIP-32943N.
IntActQ15287. 26 interactions.
MINTMINT-1474621.

Protein family/group databases

TCDB3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

PhosphoSiteQ15287.

Polymorphism databases

DMDM74754492.

Proteomic databases

PaxDbQ15287.
PRIDEQ15287.

Protocols and materials databases

DNASU10921.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301730; ENSP00000301730; ENSG00000205937. [Q15287-1]
ENST00000320225; ENSP00000315859; ENSG00000205937. [Q15287-1]
ENST00000397086; ENSP00000380275; ENSG00000205937. [Q15287-1]
ENST00000565678; ENSP00000457723; ENSG00000205937. [Q15287-1]
ENST00000566458; ENSP00000456352; ENSG00000205937. [Q15287-2]
ENST00000568631; ENSP00000457820; ENSG00000205937. [Q15287-1]
GeneID10921.
KEGGhsa:10921.
UCSCuc002cpt.3. human. [Q15287-1]
uc002cpx.3. human. [Q15287-2]

Organism-specific databases

CTD10921.
GeneCardsGC16M002303.
H-InvDBHIX0031789.
HGNCHGNC:10080. RNPS1.
HPAHPA044014.
MIM606447. gene.
neXtProtNX_Q15287.
PharmGKBPA34453.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG331533.
HOVERGENHBG053138.
InParanoidQ15287.
KOK14325.
OMAMIDMPAD.
OrthoDBEOG7Q5HGF.
PhylomeDBQ15287.
TreeFamTF314165.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpressQ15287.
BgeeQ15287.
CleanExHS_RNPS1.
GenevestigatorQ15287.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRNPS1. human.
GeneWikiRNPS1.
GenomeRNAi10921.
NextBio41487.
PROQ15287.
SOURCESearch...

Entry information

Entry nameRNPS1_HUMAN
AccessionPrimary (citable) accession number: Q15287
Secondary accession number(s): A8K1P0 expand/collapse secondary AC list , B4DDU8, B4DZU7, B7ZA17, O75308, Q32P25, Q8WY42, Q9NYG3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 137 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 16

Human chromosome 16: entries, gene names and cross-references to MIM