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P09234 (RU1C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 108. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
U1 small nuclear ribonucleoprotein C

Short name=U1 snRNP C
Short name=U1-C
Short name=U1C
Gene names
Name:SNRPC
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length159 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates E complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region. Ref.4 Ref.5 Ref.6

Subunit structure

Component of the U1 snRNP particle, a subcomplex of the spliceosome. U1 snRNP is composed of the 7 core Sm proteins B/B', D1, D2, D3, E, F and G common to all spliceosomal snRNPs, and at least 3 particle-specific proteins U1-70K, U1-A and U1-C. U1-C interacts with U1 snRNA and the 5' splice-site region of the pre-mRNA. Ref.12

Subcellular location

Nucleus.

Sequence similarities

Belongs to the U1 small nuclear ribonucleoprotein C family.

Contains 1 matrin-type zinc finger.

Sequence caution

The sequence CAI20351.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 159159U1 small nuclear ribonucleoprotein C
PRO_0000097525

Regions

Zinc finger4 – 3633Matrin-type
Compositional bias63 – 15795Met/Pro-rich

Amino acid modifications

Modified residue81Phosphotyrosine Ref.8
Modified residue121Phosphotyrosine Ref.8
Modified residue171Phosphoserine Ref.9
Modified residue521N6-acetyllysine Ref.10

Experimental info

Mutagenesis61C → S: Abolishes the binding to U1 snRNP. Ref.5
Mutagenesis91C → S: Abolishes the binding to U1 snRNP. Ref.5
Mutagenesis241H → Q: Abolishes the binding to U1 snRNP. Ref.5
Mutagenesis251C → S: No effect. Ref.5
Mutagenesis301H → Q: Abolishes the binding to U1 snRNP. Ref.5
Sequence conflict25 – 273CSG → RSR in AAA36618. Ref.3
Sequence conflict94 – 985APHMG → TPIW in AAA36618. Ref.3
Sequence conflict1011P → S in AAA36618. Ref.3
Sequence conflict129 – 1313HMP → ICQ in AAA36618. Ref.3

Secondary structure

.......... 159
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09234 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: EC313A57DEC79D95

FASTA15917,394
        10         20         30         40         50         60 
MPKFYCDYCD TYLTHDSPSV RKTHCSGRKH KENVKDYYQK WMEEQAQSLI DKTTAAFQQG 

        70         80         90        100        110        120 
KIPPTPFSAP PPAGAMIPPP PSLPGPPRPG MMPAPHMGGP PMMPMMGPPP PGMMPVGPAP 

       130        140        150 
GMRPPMGGHM PMMPGPPMMR PPARPMMVPT RPGMTRPDR 

« Hide

References

« Hide 'large scale' references
[1]"Human U1 snRNP-specific C protein: complete cDNA and protein sequence and identification of a multigene family in mammals."
Sillekens P.T.G., Beijer R.P., Habets W.J., van Venrooij W.J.
Nucleic Acids Res. 16:8307-8321(1988) [PubMed: 2971157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Isolation and characterization of a complementary DNA expressing human U1 small nuclear ribonucleoprotein C polypeptide."
Yamamoto K., Miura H., Moroi Y., Yoshinoya S., Goto M., Nishioka K., Miyamoto T.
J. Immunol. 140:311-317(1988) [PubMed: 2961811] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-131.
[4]"U1-specific protein C needed for efficient complex formation of U1 snRNP with a 5' splice site."
Heinrichs V., Bach M., Winkelmann G., Luehrmann R.
Science 247:69-72(1990) [PubMed: 2136774] [Abstract]
Cited for: FUNCTION.
[5]"Zinc finger-like structure in U1-specific protein C is essential for specific binding to U1 snRNP."
Nelissen R.L.H., Heinrichs V., Habets W.J., Simons F., Luehrmann R., van Venrooij W.J.
Nucleic Acids Res. 19:449-454(1991) [PubMed: 1826349] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-6; CYS-9; HIS-24; CYS-25 AND HIS-30.
[6]"Involvement of U1 small nuclear ribonucleoproteins (snRNP) in 5' splice site-U1 snRNP interaction."
Rossi F., Forne T., Antoine E., Tazi J., Brunel C., Cathala G.
J. Biol. Chem. 271:23985-23991(1996) [PubMed: 8798632] [Abstract]
Cited for: FUNCTION.
[7]"Protein stoichiometry of a multiprotein complex, the human spliceosomal U1 small nuclear ribonucleoprotein: absolute quantification using isotope-coded tags and mass spectrometry."
Hochleitner E.O., Kastner B., Froehlich T., Schmidt A., Luehrmann R., Arnold G., Lottspeich F.
J. Biol. Chem. 280:2536-2542(2005) [PubMed: 15525645] [Abstract]
Cited for: IDENTIFICATION IN THE U1 SNRNP COMPLEX, MASS SPECTROMETRY.
[8]"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-8 AND TYR-12, MASS SPECTROMETRY.
[9]"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-17, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[10]"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-52, MASS SPECTROMETRY.
[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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"The structure and biochemical properties of the human spliceosomal protein U1C."
Muto Y., Pomeranz Krummel D., Oubridge C., Hernandez H., Robinson C.V., Neuhaus D., Nagai K.
J. Mol. Biol. 341:185-198(2004) [PubMed: 15312772] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-61, SUBUNIT, DOMAIN ZINC FINGER.
[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: 19325628] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) OF 1-77.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12517 mRNA. Translation: CAA31037.1.
AL139100 Genomic DNA. Translation: CAI20351.1. Sequence problems.
M18465 mRNA. Translation: AAA36618.1.
IPIIPI00013396.
IPI00641788.
PIRS01387.
RefSeqNP_003084.1. NM_003093.2.
UniGeneHs.1063.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VRDNMR-A1-61[»]
3CW1X-ray5.490/9/L/l1-77[»]
ProteinModelPortalP09234.
SMRP09234. Positions 1-61.
ModBaseSearch...

Protein-protein interaction databases

IntActP09234. 9 interactions.
MINTMINT-1366350.
STRINGP09234.

PTM databases

PhosphoSiteP09234.

Polymorphism databases

DMDM134093.

Proteomic databases

PeptideAtlasP09234.
PRIDEP09234.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000244520; ENSP00000244520; ENSG00000124562.
ENST00000374017; ENSP00000363129; ENSG00000124562.
GeneID6631.
KEGGhsa:6631.
UCSCuc003ojt.1. human.

Organism-specific databases

CTD6631.
GeneCardsGC06P034725.
H-InvDBHIX0026423.
HIX0032952.
HGNCHGNC:11157. SNRPC.
MIM603522. gene.
neXtProtNX_P09234.
PharmGKBPA35998.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG21331.
GeneTreeENSGT00600000084349.
HOVERGENHBG017763.
OrthoDBEOG4933KH.
PhylomeDBP09234.

Gene expression databases

ArrayExpressP09234.
BgeeP09234.
CleanExHS_SNRPC.
GenevestigatorP09234.
GermOnlineENSG00000124562. Homo sapiens.

Family and domain databases

InterProIPR017340. U1_snRNP-C.
IPR000690. Znf_C2H2_matrin.
IPR003604. Znf_U1.
IPR013085. Znf_U1-C.
[Graphical view]
KOK11095.
PfamPF06220. zf-U1. 1 hit.
[Graphical view]
PIRSFPIRSF037969. U1_snRNP-C. 1 hit.
SMARTSM00451. ZnF_U1. 1 hit.
[Graphical view]
PROSITEPS50171. ZF_MATRIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio25831.
PMAP-CutDBP09234.
SOURCESearch...

Entry information

Entry nameRU1C_HUMAN
AccessionPrimary (citable) accession number: P09234
Secondary accession number(s): Q5TAL3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: January 25, 2012
This is version 108 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

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families