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Protein

Small nuclear ribonucleoprotein E

Gene

SNRPE

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

GO - Biological processi

  • gene expression Source: Reactome
  • hair cycle Source: UniProtKB
  • histone mRNA metabolic process Source: Reactome
  • mRNA 3'-end processing Source: Reactome
  • mRNA splicing, via spliceosome Source: UniProtKB
  • ncRNA metabolic process Source: Reactome
  • RNA splicing Source: Reactome
  • spliceosomal complex assembly Source: UniProtKB
  • spliceosomal snRNP assembly Source: UniProtKB
  • termination of RNA polymerase II transcription Source: Reactome
  • transcription from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_11066. snRNP Assembly.
REACT_1364. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_185. SLBP independent Processing of Histone Pre-mRNAs.
REACT_387. Cleavage of Growing Transcript in the Termination Region.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Small nuclear ribonucleoprotein E
Short name:
snRNP-E
Alternative name(s):
Sm protein E
Short name:
Sm-E
Short name:
SmE
Gene namesi
Name:SNRPE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:11161. SNRPE.

Subcellular locationi

  • 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.

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • methylosome Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • pICln-Sm protein complex Source: UniProtKB
  • precatalytic spliceosome Source: GO_Central
  • small nuclear ribonucleoprotein complex Source: UniProtKB
  • SMN-Sm protein complex Source: UniProtKB
  • spliceosomal complex Source: UniProtKB
  • U12-type spliceosomal complex Source: UniProtKB
  • U1 snRNP Source: UniProtKB
  • U2 snRNP Source: GO_Central
  • U4/U6 x U5 tri-snRNP complex Source: GO_Central
  • U4 snRNP Source: UniProtKB
  • U5 snRNP Source: GO_Central
  • U7 snRNP Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Involvement in diseasei

Hypotrichosis 11 (HYPT11)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:615059
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451G → S in HYPT11; does not affect subcellular localization. 1 Publication
VAR_069619

Keywords - Diseasei

Disease mutation, Hypotrichosis

Organism-specific databases

MIMi615059. phenotype.
Orphaneti55654. Hypotrichosis simplex.
PharmGKBiPA36002.

Polymorphism and mutation databases

BioMutaiSNRPE.
DMDMi61237380.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9292Small nuclear ribonucleoprotein EPRO_0000125529Add
BLAST

Proteomic databases

MaxQBiP62304.
PaxDbiP62304.
PRIDEiP62304.

PTM databases

PhosphoSiteiP62304.

Expressioni

Tissue specificityi

Widely expressed. In scalp skin, it is present in the hair follicle, the epidermis, and the dermis.1 Publication

Gene expression databases

BgeeiP62304.
CleanExiHS_SNRPE.
ExpressionAtlasiP62304. baseline.
GenevisibleiP62304. HS.

Interactioni

Subunit structurei

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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GEMIN5Q8TEQ62EBI-348082,EBI-443630
SNRPFP623064EBI-348082,EBI-356900
SNRPGP623084EBI-348082,EBI-624585

Protein-protein interaction databases

BioGridi112519. 54 interactions.
DIPiDIP-31220N.
IntActiP62304. 29 interactions.
MINTiMINT-225773.
STRINGi9606.ENSP00000400591.

Structurei

Secondary structure

1
92
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 2711Combined sources
Beta strandi30 – 389Combined sources
Beta strandi40 – 5011Combined sources
Beta strandi56 – 649Combined sources
Beta strandi66 – 683Combined sources
Beta strandi71 – 799Combined sources
Helixi81 – 833Combined sources
Beta strandi84 – 896Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CW1X-ray5.49E/W/X/Y1-92[»]
3PGWX-ray4.40E/H1-92[»]
3S6NX-ray2.50E1-92[»]
4F7UX-ray1.90E/H1-92[»]
4PJOX-ray3.30E/S/e/s1-92[»]
4V98X-ray3.10AC/AK/AS/Aa/Ai/Aq/Ay/BC/BK/BS/Ba/Bi/Bq/By/CC/CK/CS/Ca/Ci/Cq1-92[»]
4WZJX-ray3.60AE/AL/AS/BE/BL/BS/CE/CL/CS/DE/DL/DS1-92[»]
ProteinModelPortaliP62304.
SMRiP62304. Positions 14-91.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62304.

Family & Domainsi

Sequence similaritiesi

Belongs to the snRNP Sm proteins family.Curated

Phylogenomic databases

eggNOGiCOG1958.
GeneTreeiENSGT00390000012818.
HOVERGENiHBG003229.
InParanoidiP62304.
KOiK11097.
OMAiYDNIEMR.
OrthoDBiEOG7GFB5W.
PhylomeDBiP62304.
TreeFamiTF314419.

Family and domain databases

InterProiIPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
IPR027078. snRNP-E.
[Graphical view]
PANTHERiPTHR11193. PTHR11193. 1 hit.
PfamiPF01423. LSM. 1 hit.
[Graphical view]
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.

Sequencei

Sequence statusi: Complete.

P62304-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYRGQGQKV QKVMVQPINL IFRYLQNRSR IQVWLYEQVN MRIEGCIIGF
60 70 80 90
DEYMNLVLDD AEEIHSKTKS RKQLGRIMLK GDNITLLQSV SN
Length:92
Mass (Da):10,804
Last modified:July 5, 2004 - v1
Checksum:i7D8881CE1F4FA2FD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451G → S in HYPT11; does not affect subcellular localization. 1 Publication
VAR_069619

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS30979.1.
PIRiA32127.
RefSeqiNP_001291393.1. NM_001304464.1.
NP_003085.1. NM_003094.3.
UniGeneiHs.334612.
Hs.654418.

Genome annotation databases

EnsembliENST00000414487; ENSP00000400591; ENSG00000182004.
GeneIDi6635.
KEGGihsa:6635.
UCSCiuc001hai.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS30979.1.
PIRiA32127.
RefSeqiNP_001291393.1. NM_001304464.1.
NP_003085.1. NM_003094.3.
UniGeneiHs.334612.
Hs.654418.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CW1X-ray5.49E/W/X/Y1-92[»]
3PGWX-ray4.40E/H1-92[»]
3S6NX-ray2.50E1-92[»]
4F7UX-ray1.90E/H1-92[»]
4PJOX-ray3.30E/S/e/s1-92[»]
4V98X-ray3.10AC/AK/AS/Aa/Ai/Aq/Ay/BC/BK/BS/Ba/Bi/Bq/By/CC/CK/CS/Ca/Ci/Cq1-92[»]
4WZJX-ray3.60AE/AL/AS/BE/BL/BS/CE/CL/CS/DE/DL/DS1-92[»]
ProteinModelPortaliP62304.
SMRiP62304. Positions 14-91.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112519. 54 interactions.
DIPiDIP-31220N.
IntActiP62304. 29 interactions.
MINTiMINT-225773.
STRINGi9606.ENSP00000400591.

PTM databases

PhosphoSiteiP62304.

Polymorphism and mutation databases

BioMutaiSNRPE.
DMDMi61237380.

Proteomic databases

MaxQBiP62304.
PaxDbiP62304.
PRIDEiP62304.

Protocols and materials databases

DNASUi6635.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000414487; ENSP00000400591; ENSG00000182004.
GeneIDi6635.
KEGGihsa:6635.
UCSCiuc001hai.3. human.

Organism-specific databases

CTDi6635.
GeneCardsiGC01P203839.
HGNCiHGNC:11161. SNRPE.
MIMi128260. gene.
615059. phenotype.
neXtProtiNX_P62304.
Orphaneti55654. Hypotrichosis simplex.
PharmGKBiPA36002.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1958.
GeneTreeiENSGT00390000012818.
HOVERGENiHBG003229.
InParanoidiP62304.
KOiK11097.
OMAiYDNIEMR.
OrthoDBiEOG7GFB5W.
PhylomeDBiP62304.
TreeFamiTF314419.

Enzyme and pathway databases

ReactomeiREACT_11066. snRNP Assembly.
REACT_1364. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_185. SLBP independent Processing of Histone Pre-mRNAs.
REACT_387. Cleavage of Growing Transcript in the Termination Region.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiSNRPE. human.
EvolutionaryTraceiP62304.
GenomeRNAii6635.
NextBioi20816234.
PROiP62304.
SOURCEiSearch...

Gene expression databases

BgeeiP62304.
CleanExiHS_SNRPE.
ExpressionAtlasiP62304. baseline.
GenevisibleiP62304. HS.

Family and domain databases

InterProiIPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
IPR027078. snRNP-E.
[Graphical view]
PANTHERiPTHR11193. PTHR11193. 1 hit.
PfamiPF01423. LSM. 1 hit.
[Graphical view]
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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. 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. 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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "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.
  15. "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.
  16. "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.

Entry informationi

Entry nameiRUXE_HUMAN
AccessioniPrimary (citable) accession number: P62304
Secondary accession number(s): B2R5B9
, P08578, Q15498, Q5BKT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 5, 2004
Last modified: July 22, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.