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P62304 (RUXE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Small nuclear ribonucleoprotein E

Short name=snRNP-E
Alternative name(s):
Sm protein E
Short name=Sm-E
Short name=SmE
Gene names
Name:SNRPE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length92 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. As part of the U7 snRNP it is involved in histone 3'-end processing. May indirectly play a role in hair development. Ref.10 Ref.12 Ref.15

Subunit structure

U1 snRNP is for instance composed of the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Component of the heptameric ring U7 snRNP complex, or U7 Sm protein core complex, at least composed of LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF, SNRPG and U7 snRNA. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP. Ref.7 Ref.8 Ref.9 Ref.10 Ref.15

Subcellular location

Cytoplasmcytosol. Nucleus. Note: SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. Ref.10 Ref.12

Tissue specificity

Widely expressed. In scalp skin, it is present in the hair follicle, the epidermis, and the dermis. Ref.12

Involvement in disease

Hypotrichosis 11 (HYPT11) [MIM:615059]: A form of hypotrichosis, a condition characterized by the presence of less than the normal amount of hair and abnormal hair follicles and shafts, which are thin and atrophic. The extent of scalp and body hair involvement can be very variable, within as well as between families. HYPT11 is characterized by scanty or absent eyebrows and a highly variable degree of alopecia since birth, ranging from slight thinning of scalp and axillary hair to complete loss of scalp and body hair. Pubic hair remains mainly unaffected.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Miscellaneous

Patients with systemic lupus erythematosus produce antibodies which interact with snRNP proteins.

Sequence similarities

Belongs to the snRNP Sm proteins family.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentCytoplasm
Nucleus
Spliceosome
   DiseaseDisease mutation
Hypotrichosis
   LigandRNA-binding
   Molecular functionRibonucleoprotein
   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

hair cycle

Inferred from mutant phenotype Ref.12. Source: UniProtKB

histone mRNA metabolic process

Traceable author statement. Source: Reactome

mRNA 3'-end processing

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Inferred by curator Ref.8. Source: UniProtKB

ncRNA metabolic process

Traceable author statement. Source: Reactome

spliceosomal complex assembly

Non-traceable author statement Ref.1. Source: UniProtKB

spliceosomal snRNP assembly

Inferred from direct assay Ref.10. Source: UniProtKB

termination of RNA polymerase II transcription

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentSMN-Sm protein complex

Inferred from direct assay Ref.10. Source: UniProtKB

U1 snRNP

Inferred from direct assay PubMed 21113136. Source: UniProtKB

U12-type spliceosomal complex

Inferred from direct assay Ref.9. Source: UniProtKB

U4 snRNP

Inferred from direct assay Ref.14. Source: UniProtKB

U7 snRNP

Inferred from direct assay Ref.7. Source: UniProtKB

catalytic step 2 spliceosome

Inferred from direct assay Ref.8. Source: UniProtKB

cytosol

Inferred from direct assay Ref.10. Source: UniProtKB

methylosome

Inferred from direct assay Ref.10. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.12. Source: UniProtKB

pICln-Sm protein complex

Inferred from direct assay Ref.10. Source: UniProtKB

small nuclear ribonucleoprotein complex

Non-traceable author statement Ref.1. Source: UniProtKB

spliceosomal complex

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9292Small nuclear ribonucleoprotein E
PRO_0000125529

Natural variations

Natural variant451G → S in HYPT11; does not affect subcellular localization. Ref.12
VAR_069619

Secondary structure

................ 92
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62304 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 7D8881CE1F4FA2FD

FASTA9210,804
        10         20         30         40         50         60 
MAYRGQGQKV QKVMVQPINL IFRYLQNRSR IQVWLYEQVN MRIEGCIIGF DEYMNLVLDD 

        70         80         90 
AEEIHSKTKS RKQLGRIMLK GDNITLLQSV SN 

« Hide

References

« Hide 'large scale' references
[1]"The complete primary structure of the human snRNP E protein."
Stanford D.R., Kehl M., Perry C.A., Holicky E., Harvey S.E., Rohleder A.M., Rehder K., Luehrmann R., Wieben E.D.
Nucleic Acids Res. 16:10593-10605(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The small nuclear ribonucleoprotein E protein gene contains four introns and has upstream similarities to genes for ribosomal proteins."
Stanford D.R., Perry C.A., Holicky E., Rohleder A.M., Wieben E.D.
J. Biol. Chem. 263:17772-17779(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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].
Tissue: Cerebellum.
[4]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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].
Tissue: Lung and Uterus.
[6]"DNA sequence of a human Sm autoimmune antigen. The multigene family contains a processed pseudogene."
Stanford D.R., Rohleder A., Neiswanger K., Wieben E.D.
J. Biol. Chem. 262:9931-9934(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-92.
[7]"Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein."
Pillai R.S., Will C.L., Luehrmann R., Schuemperli D., Mueller B.
EMBO J. 20:5470-5479(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE U7 SNRNP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[9]"The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome."
Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S., Tuschl T., Luehrmann R.
RNA 10:929-941(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN 6S PICLN-SM COMPLEX, IDENTIFICATION IN SMN-SM COMPLEX, SUBCELLULAR LOCATION.
[11]"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].
[12]"Mutations in SNRPE, which encodes a core protein of the spliceosome, cause autosomal-dominant hypotrichosis simplex."
Pasternack S.M., Refke M., Paknia E., Hennies H.C., Franz T., Schaefer N., Fryer A., van Steensel M., Sweeney E., Just M., Grimm C., Kruse R., Ferrandiz C., Noethen M.M., Fischer U., Betz R.C.
Am. J. Hum. Genet. 92:81-87(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT HYPT11 SER-45, CHARACTERIZATION OF VARIANT HYPT11 SER-45.
[13]"Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution."
Pomeranz Krummel D.A., Oubridge C., Leung A.K., Li J., Nagai K.
Nature 458:475-480(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) IN SPLICEOSOMAL U1 SNRNP.
[14]"Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis."
Leung A.K., Nagai K., Li J.
Nature 473:536-539(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN SPLICEOSOMAL CORE U4 SNRNP.
[15]"Structural basis of assembly chaperone-mediated snRNP formation."
Grimm C., Chari A., Pelz J.P., Kuper J., Kisker C., Diederichs K., Stark H., Schindelin H., Fischer U.
Mol. Cell 49:692-703(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN 6S PICLN-SM COMPLEX, IDENTIFICATION IN 6S PICLN-SM COMPLEX, FUNCTION IN CORE U1 SNRNP BIOGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M37716 mRNA. Translation: AAA90926.1.
M15919 mRNA. Translation: AAA36621.1.
X12466 mRNA. Translation: CAA31007.1.
AK312130 mRNA. Translation: BAG35066.1.
CH471067 Genomic DNA. Translation: EAW91494.1.
BC002639 mRNA. Translation: AAH02639.1.
BC090951 mRNA. Translation: AAH90951.1.
M21258, M21253 Genomic DNA. Translation: AAB59365.1. Sequence problems.
PIRA32127.
RefSeqNP_003085.1. NM_003094.2.
UniGeneHs.334612.
Hs.654418.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VU2X-ray3.10C/K/S/a/i/q/y1-92[»]
1VU3X-ray3.10C/K/S/a/i/q1-92[»]
2Y9AX-ray3.60E/L/S1-92[»]
2Y9BX-ray3.60E/L/S1-92[»]
2Y9CX-ray3.60E/L/S1-92[»]
2Y9DX-ray3.60E/L/S1-92[»]
3CW1X-ray5.49E/W/X/Y1-92[»]
3PGWX-ray4.40E/H1-92[»]
3S6NX-ray2.50E1-92[»]
4F77X-ray3.10C/K/S/a/i/q/y1-92[»]
4F7UX-ray1.90E/H1-92[»]
ProteinModelPortalP62304.
SMRP62304. Positions 14-91.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112519. 54 interactions.
DIPDIP-31220N.
IntActP62304. 29 interactions.
MINTMINT-225773.
STRING9606.ENSP00000400591.

PTM databases

PhosphoSiteP62304.

Polymorphism databases

DMDM61237380.

Proteomic databases

PaxDbP62304.
PRIDEP62304.

Protocols and materials databases

DNASU6635.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000414487; ENSP00000400591; ENSG00000182004.
GeneID6635.
KEGGhsa:6635.
UCSCuc001hai.3. human.

Organism-specific databases

CTD6635.
GeneCardsGC01P203834.
HGNCHGNC:11161. SNRPE.
MIM128260. gene.
615059. phenotype.
neXtProtNX_P62304.
Orphanet55654. Hypotrichosis simplex.
PharmGKBPA36002.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1958.
HOVERGENHBG003229.
InParanoidP62304.
KOK11097.
OMAKPRRELG.
OrthoDBEOG7GFB5W.
PhylomeDBP62304.
TreeFamTF314419.

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

ArrayExpressP62304.
BgeeP62304.
CleanExHS_SNRPE.
GenevestigatorP62304.

Family and domain databases

InterProIPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
IPR027078. snRNP-E.
[Graphical view]
PANTHERPTHR11193. PTHR11193. 1 hit.
PfamPF01423. LSM. 1 hit.
[Graphical view]
SMARTSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMSSF50182. SSF50182. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSNRPE. human.
EvolutionaryTraceP62304.
GenomeRNAi6635.
NextBio25849.
PROP62304.
SOURCESearch...

Entry information

Entry nameRUXE_HUMAN
AccessionPrimary (citable) accession number: P62304
Secondary accession number(s): B2R5B9 expand/collapse secondary AC list , P08578, Q15498, Q5BKT2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 102 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM