Q15287 (RNPS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RNA-binding protein with serine-rich domain 1

Alternative name(s):
SR-related protein LDC2

Gene names

Name:	RNPS1
Synonyms:	LDC2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	305 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Part of pre- and post-splicing multiprotein mRNP complexes. 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. 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.23
Subunit structure	Found in a mRNA splicing-dependent exon junction complex (EJC), at least composed of ACIN1, CASC3, EIF4A3, MAGOH, PNN, RBM8A, RNPS1, SAP18 and ALYREF/THOC4. Forms heterodimers with ACIN1. Found in a heterotrimeric complex with ACIN1, RNPS1 and SAP18. Component of the active spliceosome. Associates with polysomes. Found in a mRNA splicing-dependent exon junction complex (EJC) with DEK, RBM8A, RNPS1, SRRM1 and ALYREF/THOC4. Found in a post-splicing complex with NXF1, RBM8A, UPF1, UPF2, UPF3A, UPF3B and RNPS1. Interacts with the cleaved p110 isoform of CDC2L1, 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.21
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.24
Tissue specificity	Ubiquitous. Ref.1
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 process	Nonsense-mediated mRNA decay mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA 3'-end processing Traceable author statement. Source: Reactome mRNA export from nucleus Traceable author statement. Source: Reactome mRNA splicing, via spliceosome Traceable author statement. Source: Reactome nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from direct assay Ref.12. Source: UniProtKB termination of RNA polymerase II transcription Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	mRNA 3'-UTR binding Inferred from direct assay Ref.12. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SART3	Q15020	5	EBI-395959,EBI-308619

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 305

305

RNA-binding protein with serine-rich domain 1

PRO_0000081816

Regions

Domain

161 – 240

80

RRM

Region

1 – 220

220

Necessary for interaction with the cleaved p110 isoform of CDC2L1

Region

1 – 161

161

Necessary for interaction with SRP54, nuclear localization and exon-skipping

Region

69 – 121

53

Necessary for interactions with UPF2 and UPF3B and UPF2-dependent NMD

Region

156 – 242

87

Necessary for interaction with PNN and exon-skipping

Region

238 – 305

68

Necessary for interaction with TRA2B, nuclear localization and exon-skipping

Compositional bias

7 – 64

58

Lys-rich

Compositional bias

67 – 141

75

Ser-rich

Compositional bias

128 – 154

27

Arg-rich

Compositional bias

241 – 298

58

Arg/Pro-rich

Amino acid modifications

Modified residue

53

1

Phosphoserine; by CK2 Ref.18

Modified residue

155

1

Phosphoserine Ref.27

Modified residue

157

1

Phosphoserine Ref.27

Modified residue

161

1

Phosphothreonine Ref.27

Modified residue

218

1

N6-acetyllysine Ref.25

Natural variations

Alternative sequence

2 – 24

23

Missing in isoform 2 and isoform 3.

VSP_016243

Alternative sequence

69 – 82

14

Missing in isoform 3.

VSP_037601

Experimental info

Mutagenesis

53

1

S → A: Abolishes phosphorylation by CSNK2A1 and partially reduces splicing stimulation. Does not abolish interaction with CSNK2A1 and subcellular localization. Ref.18

Mutagenesis

53

1

S → E: Partially reduces splicing stimulation. Does not abolish interaction with CSNK2A1 and subcellular localization. Ref.18

Mutagenesis

205

1

Y → A: Abolishes exon-skipping. Ref.17

Mutagenesis

207

1

Y → A: Abolishes exon-skipping. Ref.17

Sequence conflict

32

1

K → E in BAG56859. Ref.4

Sequence conflict

66

1

R → G in AAC39791. Ref.2

Sequence conflict

249

1

R → G in BAG56859. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

305

Helix Strand Turn

Details...

Beta strand

162 – 166

5

Helix

174 – 182

9

Beta strand

187 – 191

5

Beta strand

198 – 202

5

Beta strand

204 – 212

9

Helix

213 – 223

11

Beta strand

234 – 238

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 930C9D36C2486144	FASTA	305	34,208
	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
	Isoform 2 [UniParc]. Checksum: D3F7AAD16B6309F4	FASTA	282	31,709
	10 20 30 40 50 60 MAPSPTKRKD RSDEKSKDRS KDKGATKESS EKDRGRDKTR KRRSASSGSS STRSRSSSTS 70 80 90 100 110 120 SSGSSTSTGS SSGSSSSSAS SRSGSSSTSR SSSSSSSSGS PSPSRRRHDN RRRSRSKSKP 130 140 150 160 170 180 PKRDEKERKR RSPSPKPTKV HIGRLTRNVT KDHIMEIFST YGKIKMIDMP VERMHPHLSK 190 200 210 220 230 240 GYAYVEFENP DEAEKALKHM DGGQIDGQEI TATAVLAPWP RPPPRRFSPP RRMLPPPPMW 250 260 270 280 RRSPPRMRRR SRSPRRRSPV RRRSRSPGRR RHRSRSSSNS SR
	Isoform 3 [UniParc]. Checksum: 9058DEEC9B433103	FASTA	268	30,354
	10 20 30 40 50 60 MAPSPTKRKD RSDEKSKDRS KDKGATKESS EKDRGRDKTR KRRSASSSGS STSTGSSSGS 70 80 90 100 110 120 SSSSASSRSG SSSTSRSSSS SSSSGSPSPS RRRHDNRRRS RSKSKPPKRD EKERKRRSPS 130 140 150 160 170 180 PKPTKVHIGR LTRNVTKDHI MEIFSTYGKI KMIDMPVERM HPHLSKGYAY VEFENPDEAE 190 200 210 220 230 240 KALKHMDGGQ IDGQEITATA VLAPWPRPPP RRFSPPRRML PPPPMWRRSP PRMRRRSRSP 250 260 RRRSPVRRRS RSPGRRRHRS RSSSNSSR

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, 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 (NMD), IDENTIFICATION IN A COMPLEX WITH UPF2 AND UPF3B.
[20]	"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].
[21]	"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, HETERODIMERIZATION, IDENTIFICATION IN A HETEROTRIMERIC COMPLEX, MASS SPECTROMETRY.
[22]	"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.
[23]	"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).
[24]	"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.
[25]	"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, MASS SPECTROMETRY.
[26]	"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].
[27]	"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, MASS SPECTROMETRY.
+	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.

IPI

IPI00033561.
IPI00479871.
IPI00783594.

PIR

JC4525.

RefSeq

NP_006702.1. NM_006711.3.
NP_542161.1. NM_080594.2.

UniGene

Hs.355643.
Hs.507343.
Hs.733012.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4A8X	X-ray	1.90	A	159-244	[»]

ProteinModelPortal

Q15287.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32943N.

IntAct

Q15287. 12 interactions.

MINT

MINT-1474621.

Protein family/group databases

TCDB

3.A.18.1.1. nuclear mRNA exporter (mRNA-E) family.

PTM databases

PhosphoSite

Q15287.

Polymorphism databases

DMDM

74754492.

Proteomic databases

PaxDb

Q15287.

PRIDE

Q15287.

Protocols and materials databases

DNASU

10921.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000301730; ENSP00000301730; ENSG00000205937.
ENST00000320225; ENSP00000315859; ENSG00000205937.
ENST00000397086; ENSP00000380275; ENSG00000205937.
ENST00000565678; ENSP00000457723; ENSG00000205937.
ENST00000566458; ENSP00000456352; ENSG00000205937.
ENST00000568631; ENSP00000457820; ENSG00000205937.

GeneID

10921.

KEGG

hsa:10921.

UCSC

uc002cpt.3. human.
uc002cpx.3. human.

Organism-specific databases

CTD

10921.

GeneCards

GC16M002303.

H-InvDB

HIX0031789.

HGNC

HGNC:10080. RNPS1.

HPA

HPA044014.

MIM

606447. gene.

neXtProt

NX_Q15287.

PharmGKB

PA34453.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG331533.

HOVERGEN

HBG053138.

InParanoid

Q15287.

KO

K14325.

OMA

TKRKDRT.

OrthoDB

EOG44J2KM.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpress

Q15287.

Bgee

Q15287.

CleanEx

HS_RNPS1.

Genevestigator

Q15287.

GermOnline

ENSG00000205937. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 1 hit.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF00076. RRM_1. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 1 hit.
[Graphical view]

PROSITE

PS50102. RRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RNPS1. human.

GenomeRNAi

10921.

NextBio

41487.

SOURCE

Search...

Entry information

Entry name

RNPS1_HUMAN

Accession

Primary (citable) accession number: Q15287
Secondary accession number(s): A8K1P0 , 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:	May 1, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.