Reviewed, UniProtKB/Swiss-Prot Q15287 (RNPS1_HUMAN)

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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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 RENT2-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.19 Ref.20 Ref.24
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 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 THOC4. Found in a post-splicing complex with NXF1, RBM8A, RENT1, RENT2, RENT3A, RENT3B and RNPS1. Interacts with the cleaved p110 isoform of CDC2L1, CSNK2A1, PNN, SART3, SRP54, SRRM1 and TRA2B/SFRS10. Ref.13 Ref.17 Ref.19 Ref.2 Ref.11 Ref.14 Ref.22
Subcellular location	Nucleus. Nucleus speckle. Cytoplasm. Note: Nucleocytoplasmic shuttling protein. Colocalizes with the core EJC, THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles. Ref.9 Ref.12 Ref.17 Ref.19 Ref.2 Ref.11 Ref.14 Ref.28
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.19 Ref.18 Ref.21 Ref.23 Ref.25 Ref.26
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	Complete proteome
Gene Ontology (GO)
Biological process	RNA splicing Ref.2 Inferred from Experiment. Source: Reactome mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from electronic annotation. Source: UniProtKB-KW transcription Ref.2 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	RNA binding Ref.2 Traceable author statement. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Ref.11 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AP2B1	P63010	1	EBI-395959,EBI-432924
C14orf102	Q9H7Z3	1	EBI-395959,EBI-1042642
C20orf11	Q9NWU2	1	EBI-395959,EBI-1051077
CDC2L1	P21127	1	EBI-395959,EBI-1298
CPSF2	Q9P2I0	1	EBI-395959,EBI-1043224
CPSF6	Q16630	1	EBI-395959,EBI-358410
CSNK2A1	P68400	1	EBI-395959,EBI-347804
CSNK2A2	P19784	1	EBI-395959,EBI-347451
CSNK2B	P67870	1	EBI-395959,EBI-348169
DDX20	Q9UHI6	1	EBI-395959,EBI-347658
DDX23	Q9BUQ8	1	EBI-395959,EBI-540096
DDX41	Q9UJV9	1	EBI-395959,EBI-1046350
DHX38	Q92620	1	EBI-395959,EBI-1043041
EFTUD2	Q15029	1	EBI-395959,EBI-357897
GEMIN4	P57678	1	EBI-395959,EBI-356700
KHK	P50053	1	EBI-395959,EBI-1053974
LUC7L	Q9NQ29	1	EBI-395959,EBI-473747
LUC7L2	Q9Y383	1	EBI-395959,EBI-352851
LUC7L3	O95232	1	EBI-395959,EBI-395671
MKLN1	Q9UL63	1	EBI-395959,EBI-1048053
NUDT21	O43809	1	EBI-395959,EBI-355720
PNN	Q9H307	1	EBI-395959,EBI-681904
PRPF3	O43395	1	EBI-395959,EBI-744322
PRPF40A	O75400	1	EBI-395959,EBI-473291
PRPF6	O94906	1	EBI-395959,EBI-536755
PSME3	P61289	1	EBI-395959,EBI-355546
PUF60	Q9UHX1	1	EBI-395959,EBI-1053259
RANBP9	Q96S59	1	EBI-395959,EBI-636085
RARS	P54136	1	EBI-395959,EBI-355482
SART3	Q15020	4	EBI-395959,EBI-308619
SF3B1	O75533	1	EBI-395959,EBI-876542
SF3B3	Q15393	1	EBI-395959,EBI-346977
SFRS1	Q07955	1	EBI-395959,EBI-398920
SFRS12	Q8WXA9	1	EBI-395959,EBI-1044237
SFRS2	Q01130	1	EBI-395959,EBI-627047
SFRS8	Q12872	1	EBI-395959,EBI-1055938
SIP1	O14893	1	EBI-395959,EBI-443648
SNRNP200	O75643	1	EBI-395959,EBI-1045395
SNRNP70	P08621	1	EBI-395959,EBI-1049228
SNRPA	P09012	1	EBI-395959,EBI-607085
SRPK1	Q96SB4	1	EBI-395959,EBI-539478
SRPK2	P78362	1	EBI-395959,EBI-593303
SRRM1	Q8IYB3	1	EBI-395959,EBI-1055880
SRRM2	Q9UQ35	1	EBI-395959,EBI-1050142
SRRT	Q9BXP5	1	EBI-395959,EBI-712721
STRAP	Q9Y3F4	1	EBI-395959,EBI-727414
THRAP3	Q9Y2W1	1	EBI-395959,EBI-352039
TRA2B	P62995	1	EBI-395959,EBI-725485
U2AF2	P26368	1	EBI-395959,EBI-742339
USP7	Q93009	1	EBI-395959,EBI-302474
WDR33	Q9C0J8	1	EBI-395959,EBI-712637

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 RENT2 and REN3B and RENT2-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	27	1	Phosphoserine Ref.23
	Modified residue	53	1	Phosphoserine; by CK2 Ref.19
	Modified residue	125	1	Phosphoserine Ref.18
	Modified residue	155	1	Phosphoserine Ref.18 Ref.25
	Modified residue	157	1	Phosphoserine Ref.18 Ref.25
	Modified residue	205	1	Phosphotyrosine Ref.21
	Modified residue	218	1	N6-acetyllysine Ref.29
	Modified residue	251	1	Phosphoserine Ref.23 Ref.26
	Modified residue	266	1	Phosphoserine Ref.23
	Modified residue	287	1	Phosphoserine Ref.23
	Modified residue	289	1	Phosphoserine Ref.23
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.19
	Mutagenesis	53	1	S → E: Partially reduces splicing stimulation. Does not abolish interaction with CSNK2A1 and subcellular localization. Ref.19
	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

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. 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. 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: 8543184] [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: 9580558] [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: 14702039] [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: 15616553] [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: 15489334] [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: 10449421] [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: 11118221] [Abstract] Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH DEK; RBM8A; SRRM1 AND 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: 11477570] [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: 11546874] [Abstract] Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, IDENTIFICATION IN A POST-SPLICING COMPLEX WITH NXF1; RBM8A; RENT1; RENT2; RENT3A AND RENT3B, 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: 12944400] [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: 14517304] [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: 14752011] [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: 14625303] [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: 14729963] [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]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-155 AND SER-157, MASS SPECTROMETRY. Tissue: Epithelium.
[19]	"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: 15684395] [Abstract] Cited for: FUNCTION IN PRE-MRNA SPLICING, ASSOCIATION WITH THE ACTIVE SPLICEOSOME, PHOSPHORYLATION, PHOSPHORYLATION AT SER-53, MASS SPECTROMETRY, INTERACTION WITH CSNK2A1, MUTAGENESIS OF SER-53, SUBCELLULAR LOCATION.
[20]	"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: 16209946] [Abstract] Cited for: FUNCTION IN A RENT2-DEPENDENT NONSENSE-MEDIATED MRNA DECAY (NMD), IDENTIFICATION IN A COMPLEX WITH RENT2 AND RENT3B.
[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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-205, MASS SPECTROMETRY.
[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: 16314458] [Abstract] Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, HETERODIMERIZATION, IDENTIFICATION IN A HETEROTRIMERIC COMPLEX, 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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-251; SER-266; SER-287 AND SER-289, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 17586820] [Abstract] Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY (NMD).
[25]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-157, MASS SPECTROMETRY.
[26]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, MASS SPECTROMETRY.
[27]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[28]	"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: 19324961] [Abstract] Cited for: SUBCELLULAR LOCATION.
[29]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-218, 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. NP_542161.1.
UniGene	Hs.355643
3D structure databases
SMR	Q15287. Positions 157-235.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15287. 106 interactions.
STRING	Q15287.
Protein family/group databases
TCDB	3.A.18.1.1. nuclear mRNA exporter (mRNA-E) family.
PTM databases
PhosphoSite	Q15287.
Proteomic databases
PRIDE	Q15287.
Genome annotation databases
Ensembl	ENST00000320225; ENSP00000315859; ENSG00000205937; Homo sapiens. [Genome view] ENST00000397086; ENSP00000380275; ENSG00000205937; Homo sapiens. [Genome view]
GeneID	10921.
KEGG	hsa:10921.
UCSC	uc002cpt.1. human. uc002cpv.1. human.
Organism-specific databases
CTD	10921.
GeneCards	GC04P010979. GC16M002247.
H-InvDB	HIX0012719. HIX0031789.
HGNC	HGNC:10080. RNPS1.
MIM	606447. gene.
PharmGKB	PA34453.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG20034.
HOVERGEN	Q15287.
InParanoid	Q15287.
OMA	DHIQEIF.
OrthoDB	EOG96X1VN.
Enzyme and pathway databases
Reactome	REACT_125. Processing of Capped Intron-Containing Pre-mRNA. REACT_1788. Transcription. REACT_6167. Influenza Infection. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q15287.
Bgee	Q15287.
CleanEx	HS_RNPS1.
Genevestigator	Q15287.
GermOnline	ENSG00000205937. Homo sapiens.
Family and domain databases
InterPro	IPR012677. a_b_plait_nuc_bd. IPR000504. RRM_RNP1. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.
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 Resources
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:	February 9, 2010
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.