P09234 (RU1C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
U1 small nuclear ribonucleoprotein C
Short name=U1 snRNP C
Short name=U1-C
Short name=U1C

Gene names

Name:

SNRPC

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	159 AA.
Sequence status	Complete.
Protein existence	Evidence 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.7 Ref.13
Subcellular location	Nucleus HAMAP-Rule MF_03153.
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

Keywords
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	Metal-binding RNA-binding Zinc
Molecular function	Ribonucleoprotein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	spliceosomal snRNP assembly Inferred from direct assay PubMed 8972845. Source: UniProtKB
Cellular_component	Cajal body Inferred from direct assay PubMed 10068039. Source: UniProtKB U1 snRNP Inferred from direct assay Ref.13Ref.7. Source: UniProtKB
Molecular_function	single-stranded RNA binding Inferred from direct assay Ref.6. Source: UniProtKB zinc ion binding Inferred from direct assay Ref.13. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 159

159

U1 small nuclear ribonucleoprotein C HAMAP-Rule MF_03153

PRO_0000097525

Regions

Zinc finger

4 – 36

33

Matrin-type HAMAP-Rule MF_03153

Compositional bias

63 – 157

95

Met/Pro-rich HAMAP-Rule MF_03153

Amino acid modifications

Modified residue

8

1

Phosphotyrosine Ref.8

Modified residue

17

1

Phosphoserine Ref.9

Modified residue

52

1

N6-acetyllysine Ref.10

Experimental info

Mutagenesis

6

1

C → S: Abolishes the binding to U1 snRNP. Ref.5

Mutagenesis

9

1

C → S: Abolishes the binding to U1 snRNP. Ref.5

Mutagenesis

24

1

H → Q: Abolishes the binding to U1 snRNP. Ref.5

Mutagenesis

25

1

C → S: No effect. Ref.5

Mutagenesis

30

1

H → Q: Abolishes the binding to U1 snRNP. Ref.5

Sequence conflict

25 – 27

3

CSG → RSR in AAA36618. Ref.3

Sequence conflict

94 – 98

5

APHMG → TPIW in AAA36618. Ref.3

Sequence conflict

101

1

P → S in AAA36618. Ref.3

Sequence conflict

129 – 131

3

HMP → ICQ in AAA36618. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

159

Helix Strand Turn

Details...

Turn

7 – 9

3

Helix

18 – 24

7

Helix

29 – 37

9

Beta strand

39 – 44

6

Helix

49 – 55

7

Beta strand

56 – 59

4

Sequences

	Sequence		Length	Mass (Da)
	P09234 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: EC313A57DEC79D95	FASTA	159	17,394
	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

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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. , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-8, 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] [Europe PMC] [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.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52, MASS SPECTROMETRY.
[11]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[12]	"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].
[13]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-61, SUBUNIT, DOMAIN ZINC FINGER.
[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) 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.

IPI

IPI00013396.
IPI00641788.

PIR

S01387.

RefSeq

NP_003084.1. NM_003093.2.

UniGene

Hs.1063.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VRD	NMR	-	A	1-61	[»]
3CW1	X-ray	5.49	0/9/L/l	1-77	[»]

ProteinModelPortal

P09234.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34235N.

IntAct

P09234. 9 interactions.

MINT

MINT-1366350.

STRING

9606.ENSP00000244520.

PTM databases

PhosphoSite

P09234.

Polymorphism databases

DMDM

134093.

Proteomic databases

PaxDb

P09234.

PeptideAtlas

P09234.

PRIDE

P09234.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000244520; ENSP00000244520; ENSG00000124562.
ENST00000374017; ENSP00000363129; ENSG00000124562.

GeneID

6631.

KEGG

hsa:6631.

UCSC

uc003ojt.2. human.

Organism-specific databases

CTD

6631.

GeneCards

GC06P034825.

H-InvDB

HIX0010405.
HIX0171661.

HGNC

HGNC:11157. SNRPC.

HPA

CAB034338.

MIM

603522. gene.

neXtProt

NX_P09234.

PharmGKB

PA35998.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5136.

HOGENOM

HOG000238970.

HOVERGEN

HBG017763.

KO

K11095.

OrthoDB

EOG4933KH.

Gene expression databases

ArrayExpress

P09234.

Bgee

P09234.

CleanEx

HS_SNRPC.

Genevestigator

P09234.

GermOnline

ENSG00000124562. Homo sapiens.

Family and domain databases

HAMAP

MF_03153. U1-C.

InterPro

IPR017340. U1_snRNP-C.
IPR000690. Znf_C2H2_matrin.
IPR003604. Znf_U1.
IPR013085. Znf_U1-C.
[Graphical view]

Pfam

PF06220. zf-U1. 1 hit.
[Graphical view]

PIRSF

PIRSF037969. U1_snRNP-C. 1 hit.

SMART

SM00451. ZnF_U1. 1 hit.
[Graphical view]

PROSITE

PS50171. ZF_MATRIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P09234.

GenomeRNAi

6631.

NextBio

25831.

PMAP-CutDB

P09234.

SOURCE

Search...

Entry information

Entry name

RU1C_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 122 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.