UniProt ID | RU2A_HUMAN | |
---|---|---|
UniProt AC | P09661 | |
Protein Name | U2 small nuclear ribonucleoprotein A' | |
Gene Name | SNRPA1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 255 | |
Subcellular Localization | Nucleus . | |
Protein Description | Involved in pre-mRNA splicing as component of the spliceosome. [PubMed: 11991638] | |
Protein Sequence | MVKLTAELIEQAAQYTNAVRDRELDLRGYKIPVIENLGATLDQFDAIDFSDNEIRKLDGFPLLRRLKTLLVNNNRICRIGEGLDQALPCLTELILTNNSLVELGDLDPLASLKSLTYLSILRNPVTNKKHYRLYVIYKVPQVRVLDFQKVKLKERQEAEKMFKGKRGAQLAKDIARRSKTFNPGAGLPTDKKKGGPSPGDVEAIKNAIANASTLAEVERLKGLLQSGQIPGRERRSGPTDDGEEEMEEDTVTNGS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
5 | Phosphorylation | ---MVKLTAELIEQA ---CCHHHHHHHHHH | 16.62 | - | |
15 | Phosphorylation | LIEQAAQYTNAVRDR HHHHHHHHHHHHCCH | 9.38 | 28796482 | |
16 | Phosphorylation | IEQAAQYTNAVRDRE HHHHHHHHHHHCCHH | 12.48 | 28796482 | |
27 | Methylation | RDRELDLRGYKIPVI CCHHCCCCCCCCCEE | 46.17 | 115917373 | |
30 | Ubiquitination | ELDLRGYKIPVIENL HCCCCCCCCCEEECC | 43.27 | 29967540 | |
56 | 2-Hydroxyisobutyrylation | FSDNEIRKLDGFPLL CCHHHHHHCCCCHHH | 57.50 | - | |
56 | Ubiquitination | FSDNEIRKLDGFPLL CCHHHHHHCCCCHHH | 57.50 | 33845483 | |
67 | Ubiquitination | FPLLRRLKTLLVNNN CHHHHHHHHHHHCCC | 35.00 | 24816145 | |
67 | 2-Hydroxyisobutyrylation | FPLLRRLKTLLVNNN CHHHHHHHHHHHCCC | 35.00 | - | |
68 | O-linked_Glycosylation | PLLRRLKTLLVNNNR HHHHHHHHHHHCCCC | 29.89 | 28510447 | |
114 | Phosphorylation | DPLASLKSLTYLSIL CHHHHCCCCHHHHHH | 31.10 | 28152594 | |
116 | Phosphorylation | LASLKSLTYLSILRN HHHCCCCHHHHHHCC | 29.52 | 28152594 | |
117 | Phosphorylation | ASLKSLTYLSILRNP HHCCCCHHHHHHCCC | 12.07 | 28152594 | |
119 | Phosphorylation | LKSLTYLSILRNPVT CCCCHHHHHHCCCCC | 14.79 | 28152594 | |
126 | Phosphorylation | SILRNPVTNKKHYRL HHHCCCCCCCCEEEE | 42.45 | 20068231 | |
128 | 2-Hydroxyisobutyrylation | LRNPVTNKKHYRLYV HCCCCCCCCEEEEEE | 31.40 | - | |
131 | Phosphorylation | PVTNKKHYRLYVIYK CCCCCCEEEEEEEEE | 15.93 | - | |
134 | Phosphorylation | NKKHYRLYVIYKVPQ CCCEEEEEEEEECCC | 3.93 | 28152594 | |
137 | Phosphorylation | HYRLYVIYKVPQVRV EEEEEEEEECCCEEE | 8.90 | 28152594 | |
138 | Acetylation | YRLYVIYKVPQVRVL EEEEEEEECCCEEEE | 35.99 | 25953088 | |
138 | Ubiquitination | YRLYVIYKVPQVRVL EEEEEEEECCCEEEE | 35.99 | - | |
149 | Acetylation | VRVLDFQKVKLKERQ EEEECCEEECHHHHH | 41.13 | 26051181 | |
149 | Methylation | VRVLDFQKVKLKERQ EEEECCEEECHHHHH | 41.13 | - | |
149 | Ubiquitination | VRVLDFQKVKLKERQ EEEECCEEECHHHHH | 41.13 | 33845483 | |
151 | Ubiquitination | VLDFQKVKLKERQEA EECCEEECHHHHHHH | 61.96 | - | |
160 | Acetylation | KERQEAEKMFKGKRG HHHHHHHHHHCCHHH | 57.60 | 23749302 | |
160 | Ubiquitination | KERQEAEKMFKGKRG HHHHHHHHHHCCHHH | 57.60 | 32015554 | |
160 | 2-Hydroxyisobutyrylation | KERQEAEKMFKGKRG HHHHHHHHHHCCHHH | 57.60 | - | |
163 | Ubiquitination | QEAEKMFKGKRGAQL HHHHHHHCCHHHHHH | 61.08 | 24816145 | |
172 | Malonylation | KRGAQLAKDIARRSK HHHHHHHHHHHHHCC | 59.25 | 26320211 | |
172 | Ubiquitination | KRGAQLAKDIARRSK HHHHHHHHHHHHHCC | 59.25 | 33845483 | |
172 | Sumoylation | KRGAQLAKDIARRSK HHHHHHHHHHHHHCC | 59.25 | 28112733 | |
172 | Methylation | KRGAQLAKDIARRSK HHHHHHHHHHHHHCC | 59.25 | 23644510 | |
172 | Acetylation | KRGAQLAKDIARRSK HHHHHHHHHHHHHCC | 59.25 | 19608861 | |
178 | Phosphorylation | AKDIARRSKTFNPGA HHHHHHHCCCCCCCC | 30.41 | 30266825 | |
179 | Ubiquitination | KDIARRSKTFNPGAG HHHHHHCCCCCCCCC | 56.15 | 23000965 | |
179 | Acetylation | KDIARRSKTFNPGAG HHHHHHCCCCCCCCC | 56.15 | 26051181 | |
180 | Phosphorylation | DIARRSKTFNPGAGL HHHHHCCCCCCCCCC | 29.86 | 30266825 | |
189 | Phosphorylation | NPGAGLPTDKKKGGP CCCCCCCCCCCCCCC | 66.55 | 24732914 | |
191 | Ubiquitination | GAGLPTDKKKGGPSP CCCCCCCCCCCCCCH | 59.88 | 21906983 | |
191 | 2-Hydroxyisobutyrylation | GAGLPTDKKKGGPSP CCCCCCCCCCCCCCH | 59.88 | - | |
191 | Acetylation | GAGLPTDKKKGGPSP CCCCCCCCCCCCCCH | 59.88 | 25953088 | |
192 | Ubiquitination | AGLPTDKKKGGPSPG CCCCCCCCCCCCCHH | 60.50 | 21906983 | |
193 | Ubiquitination | GLPTDKKKGGPSPGD CCCCCCCCCCCCHHH | 74.88 | 21963094 | |
197 | Phosphorylation | DKKKGGPSPGDVEAI CCCCCCCCHHHHHHH | 44.80 | 29255136 | |
205 | Ubiquitination | PGDVEAIKNAIANAS HHHHHHHHHHHHCCH | 47.58 | 23000965 | |
212 | Phosphorylation | KNAIANASTLAEVER HHHHHCCHHHHHHHH | 24.62 | 25627689 | |
213 | Phosphorylation | NAIANASTLAEVERL HHHHCCHHHHHHHHH | 27.81 | 21712546 | |
221 | Sumoylation | LAEVERLKGLLQSGQ HHHHHHHHHHHHCCC | 54.45 | 28112733 | |
221 | Malonylation | LAEVERLKGLLQSGQ HHHHHHHHHHHHCCC | 54.45 | 26320211 | |
221 | Ubiquitination | LAEVERLKGLLQSGQ HHHHHHHHHHHHCCC | 54.45 | 23000965 | |
226 | Phosphorylation | RLKGLLQSGQIPGRE HHHHHHHCCCCCCCC | 32.41 | 20068231 | |
236 | Phosphorylation | IPGRERRSGPTDDGE CCCCCCCCCCCCCCC | 56.18 | 25159151 | |
239 | Phosphorylation | RERRSGPTDDGEEEM CCCCCCCCCCCCHHH | 50.69 | 21955146 | |
246 | Sulfoxidation | TDDGEEEMEEDTVTN CCCCCHHHHHHCCCC | 8.48 | 21406390 | |
250 | Phosphorylation | EEEMEEDTVTNGS-- CHHHHHHCCCCCC-- | 32.29 | 27251275 | |
252 | Phosphorylation | EMEEDTVTNGS---- HHHHHCCCCCC---- | 35.63 | 28450419 | |
255 | Phosphorylation | EDTVTNGS------- HHCCCCCC------- | 38.83 | 28112733 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of RU2A_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RU2A_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of RU2A_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"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-172, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND MASSSPECTROMETRY. | |
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178 AND SER-197, ANDMASS SPECTROMETRY. | |
"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 SER-197, AND MASSSPECTROMETRY. | |
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND MASSSPECTROMETRY. |