Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  U1 small nuclear ribonucleoprotein A  

UniProtKB / Swiss-Prot ID :  SNRPA_HUMAN

Gene Name (Synonyms) : 
SNRPA  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  Binds stem loop II of U1 snRNA. It is the first snRNP to interact with pre-mRNA. This interaction is required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP. In a snRNP-free form (SF-A) may be involved in coupled pre-mRNA splicing and polyadenylation process. Binds preferentially to the 5'-UGCAC-3' motif in vitro. 

Protein Sequence MAVPETRPNHTIYINNLNEKIKKDELKKSLYAIFSQFGQILDILVSRSLKMRGQAFVIFKEVSSATNALR...
Predicted Secondary Structure CCCCCCCCCCEEEEECCCCCCCHHHHHHHHHHHHHCCCCEEEEEEECCCCCCCEEEEEECCHHHHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAVPET
---CCCCCC
26.10UniProtKB
Link
20Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NLNEKIKKD
CCCCCCCHH
59.77Phosphositeplus
Link
60Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FVIFKEVSS
EEEECCHHH
46.19Phosphositeplus
Link
60N6-acetyllysineFVIFKEVSS
EEEECCHHH
46.19HPRD
Link
60N6-acetyllysineFVIFKEVSS
EEEECCHHH
46.19Phosphositeplus
Link
60N6-acetyllysine.FVIFKEVSS
EEEECCHHH
46.19UniProtKB
Link
88Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IQYAKTDSD
EEECCCCHH
48.18Phosphositeplus
Link
96Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DIIAKMKGT
HHHHHHCCC
30.64Phosphositeplus
Link
98Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IAKMKGTFV
HHHHCCCCC
54.84Phosphositeplus
Link
131PhosphothreonineGGGATPVVG
CCCCCCCCC
21.64HPRD
Link-
131PhosphothreonineGGGATPVVG
CCCCCCCCC
21.64PhosphoELM
Link-
131PhosphothreonineGGGATPVVG
CCCCCCCCC
21.64Phosphositeplus
Link-
131PhosphothreonineGGGATPVVG
CCCCCCCCC
21.64SysPTM
Link-
131Phosphothreonine.GGGATPVVG
CCCCCCCCC
21.64UniProtKB
Link-
268Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LQGFKITQN
HCCEEECCC
52.23Phosphositeplus
Link-
276Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NNAMKISFA
CCEEEEEEC
32.56Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PERQ2_HUMANphysical interactionMINT-65909MINT16120600
CD2B2_HUMANphysical interactionMINT-62838MINT15105431
SNRPA_HUMANphysical interactionMINT-68459MINT16189514
PAPOA_HUMANphysical interactionMINT-49769MINT10742179
SF3A2_HUMANphysical interactionMINT-5205386MINT17332742
SMAD5_HUMANphysical interactionMINT-61830MINT15231748
Q9BUQ0_HUMANphysical interactionMINT-66535MINT16189514
PPM1G_HUMANdirect interactionDIP:58779EDIP17572683
SNRPA_HUMANphysical interactionEBI-760387
intact16189514
CS043_HUMANphysical interactionEBI-754237
intact16189514
SNRPA_HUMANin vitro
yeast 2-hybrid
HPRD:01658HPRD10742179
7984237
16189514
PTBP1_HUMANyeast 2-hybridHPRD:01658HPRD16189514
CS043_HUMANyeast 2-hybridHPRD:01658HPRD16189514
RPAB1_HUMANENSP00000243563STRING
SF3A1_HUMANENSP00000243563STRING
SMD3_HUMANENSP00000243563STRING
NH2L1_HUMANENSP00000243563STRING
RPAB2_HUMANENSP00000243563STRING
PHF5A_HUMANENSP00000243563STRING
PAPOA_HUMANENSP00000243563STRING
SFRS5_HUMANENSP00000243563STRING
PABP2_HUMANENSP00000243563STRING
CSTF1_HUMANENSP00000243563STRING
RPB3_HUMANENSP00000243563STRING
HNRPL_HUMANENSP00000243563STRING
RU17_HUMANENSP00000243563STRING
SF3A2_HUMANENSP00000243563STRING
RPB9_HUMANENSP00000243563STRING
SFRS9_HUMANENSP00000243563STRING
LSM2_HUMANENSP00000243563STRING
PM14_HUMANENSP00000243563STRING
CPSF3_HUMANENSP00000243563STRING
SFRS6_HUMANENSP00000243563STRING
T2FA_HUMANENSP00000243563STRING
RU2B_HUMANENSP00000243563STRING
SF04_HUMANENSP00000243563STRING
FUS_HUMANENSP00000243563STRING
RU2A_HUMANENSP00000243563STRING
SFRS1_HUMANENSP00000243563STRING
U5S1_HUMANENSP00000243563STRING
WDR57_HUMANENSP00000243563STRING
DNJC8_HUMANENSP00000243563STRING
PRP6_HUMANENSP00000243563STRING
RUXF_HUMANENSP00000243563STRING
RUXF_HUMANENSP00000243563STRING
RUXF_HUMANENSP00000243563STRING
PRP16_HUMANENSP00000243563STRING
TXN4A_HUMANENSP00000243563STRING
SF3B4_HUMANENSP00000243563STRING
RUXG_HUMANENSP00000243563STRING
RPB4_HUMANENSP00000243563STRING
U2AF1_HUMANENSP00000243563STRING
SFRS2_HUMANENSP00000243563STRING
RPAB3_HUMANENSP00000243563STRING
PCF11_HUMANENSP00000243563STRING
CPSF2_HUMANENSP00000243563STRING
CPSF5_HUMANENSP00000243563STRING
SMD1_HUMANENSP00000243563STRING
RPB7_HUMANENSP00000243563STRING
PRP8_HUMANENSP00000243563STRING
PRP17_HUMANENSP00000243563STRING
HNRPR_HUMANENSP00000243563STRING
CLP1_HUMANENSP00000243563STRING
CD2B2_HUMANENSP00000243563STRING
PCBP1_HUMANENSP00000243563STRING
SF3B3_HUMANENSP00000243563STRING
U2AF2_HUMANENSP00000243563STRING
DDX23_HUMANENSP00000243563STRING
RPB2_HUMANENSP00000243563STRING
HNRPD_HUMANENSP00000243563STRING
RPB1_HUMANENSP00000243563STRING
CSTF3_HUMANENSP00000243563STRING
ROA0_HUMANENSP00000243563STRING
U520_HUMANENSP00000243563STRING
SF3B2_HUMANENSP00000243563STRING
SMC1A_HUMANENSP00000243563STRING
RPAB5_HUMANENSP00000243563STRING
HNRPM_HUMANENSP00000243563STRING
SFRS7_HUMANENSP00000243563STRING
NCBP2_HUMANENSP00000243563STRING
THOC4_HUMANENSP00000243563STRING
SF3B1_HUMANENSP00000243563STRING
HNRPC_HUMANENSP00000243563STRING
CPSF1_HUMANENSP00000243563STRING
ROA1_HUMANENSP00000243563STRING
SMD2_HUMANENSP00000243563STRING
RPAB4_HUMANENSP00000243563STRING
RBM5_HUMANENSP00000243563STRING
CPSF7_HUMANENSP00000243563STRING
HNRPF_HUMANENSP00000243563STRING
T2FB_HUMANENSP00000243563STRING
PCBP2_HUMANENSP00000243563STRING
HNRPK_HUMANENSP00000243563STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures