SNU71_YEAST - dbPTM
SNU71_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNU71_YEAST
UniProt AC P53207
Protein Name U1 small nuclear ribonucleoprotein component SNU71
Gene Name SNU71
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 620
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Component of the U1 snRNP particle, which recognizes and binds the 5'-splice site of pre-mRNA. Together with other non-snRNP factors, U1 snRNP forms the spliceosomal commitment complex, that targets pre-mRNA to the splicing pathway..
Protein Sequence MRDIVFVSPQLYLSSQEGWKSDSAKSGFIPILKNDLQRFQDSLKHIVDARNSLSETLLNSNDDGSIHNSDQNTGLNKDKEASIADNNSANKCATSSSRYQELKQFLPISLDQQIHTVSLQGVSSSFSRGQIESLLDHCLNLALTETQSNSALKVEAWSSFSSFLDTQDIFIRFSKVDEDEAFVNTLNYCKALFAFIRKLHEDFKIELHLDLNTKEYVEDRTGTIPSVKPEKASEFYSVFKNIEDQTDERNSKKEQLDDSSTQYKVDTNTLSDLPSDALDQLCKDIIEFRTKVVSIEKEKKMKSTYEESRRQRHQMQKVFDQIRKNHSGAKGSANTEEEDTNMEDEDEEDDTEDDLALEKRKEERDLEESNRRYEDMLHQLHSNTEPKIKSIRADIMSAENYEEHLEKNRSLYLKELLHLANDVHYDHHRSFKEQEERRDEEDRAKNGNAKELAPIQLSDGKAISAGKAAAITLPEGTVKSENYNADKNVSESSEHVKIKFDFKKAIDHSVESSSEDEGYRESELPPTKPSERSAAEDRLPFTADELNIRLTNLKESRYVDELVREFLGVYEDELVEYILENIRVNQSKQALLNELRETFDEDGETIADRLWSRKEFRLGT
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
44AcetylationQRFQDSLKHIVDARN
HHHHHHHHHHHHHHH		34.9324489116
52PhosphorylationHIVDARNSLSETLLN
HHHHHHHHHHHHHHC		27.9327017623
60PhosphorylationLSETLLNSNDDGSIH
HHHHHHCCCCCCCCC		41.4222369663
65PhosphorylationLNSNDDGSIHNSDQN
HCCCCCCCCCCCCCC		27.8922369663
69PhosphorylationDDGSIHNSDQNTGLN
CCCCCCCCCCCCCCC		26.8122369663
73PhosphorylationIHNSDQNTGLNKDKE
CCCCCCCCCCCCCCC		37.1024961812
82PhosphorylationLNKDKEASIADNNSA
CCCCCCCHHCCCCCC		21.2828889911
109PhosphorylationLKQFLPISLDQQIHT
HHHHCCCCHHCCEEE		24.7730377154
116PhosphorylationSLDQQIHTVSLQGVS
CHHCCEEEEEEECCC		17.2630377154
123PhosphorylationTVSLQGVSSSFSRGQ
EEEEECCCCCCCHHH		27.3930377154
124PhosphorylationVSLQGVSSSFSRGQI
EEEECCCCCCCHHHH		32.7530377154
125PhosphorylationSLQGVSSSFSRGQIE
EEECCCCCCCHHHHH		21.5330377154
127PhosphorylationQGVSSSFSRGQIESL
ECCCCCCCHHHHHHH		37.1330377154
317AcetylationRQRHQMQKVFDQIRK
HHHHHHHHHHHHHHH		39.2624489116
335PhosphorylationGAKGSANTEEEDTNM
CCCCCCCCHHCCCCC		44.4821551504
340PhosphorylationANTEEEDTNMEDEDE
CCCHHCCCCCCCCCC		39.4821551504
458PhosphorylationELAPIQLSDGKAISA
CCCCEECCCCCEECC		28.1319779198
464PhosphorylationLSDGKAISAGKAAAI
CCCCCEECCCCCEEE		35.5120377248
509PhosphorylationFKKAIDHSVESSSED
HHHHHCCCCCCCCCC		24.6719795423
512PhosphorylationAIDHSVESSSEDEGY
HHCCCCCCCCCCCCC		36.6917330950
513PhosphorylationIDHSVESSSEDEGYR
HCCCCCCCCCCCCCC		25.0017330950
514PhosphorylationDHSVESSSEDEGYRE
CCCCCCCCCCCCCCC		59.3417330950
519PhosphorylationSSSEDEGYRESELPP
CCCCCCCCCCCCCCC		14.7924961812
522PhosphorylationEDEGYRESELPPTKP
CCCCCCCCCCCCCCC		35.1224961812
527PhosphorylationRESELPPTKPSERSA
CCCCCCCCCCCCCCC		54.3624961812
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 SNU71_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNU71_YEAST !!
Disease-associated PTM Sites based on SAP

* 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 SNU71_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRP40_YEASTPRP40physical
10504710
RU1A_YEASTMUD1physical
10504710
NAM8_YEASTNAM8physical
10504710
RU17_YEASTSNP1physical
10504710
RU1C_YEASTYHC1physical
10504710
PRP39_YEASTPRP39physical
10504710
SNU56_YEASTSNU56physical
10504710
SMD1_YEASTSMD1physical
10504710
SMD2_YEASTSMD2physical
10504710
SMD3_YEASTSMD3physical
10504710
NCBP2_YEASTCBC2physical
16429126
LUC7_YEASTLUC7physical
16429126
RU1A_YEASTMUD1physical
16429126
NAM8_YEASTNAM8physical
16429126
PHO80_YEASTPHO80physical
16429126
PRP39_YEASTPRP39physical
16429126
PRP40_YEASTPRP40physical
16429126
PRP42_YEASTPRP42physical
16429126
RSMB_YEASTSMB1physical
16429126
SMD1_YEASTSMD1physical
16429126
SMD2_YEASTSMD2physical
16429126
SMD3_YEASTSMD3physical
16429126
RU17_YEASTSNP1physical
16429126
SNU56_YEASTSNU56physical
16429126
NCBP1_YEASTSTO1physical
16429126
RU1C_YEASTYHC1physical
16429126
PRP40_YEASTPRP40physical
11283351
IF4F1_YEASTTIF4631physical
19838078
IF4F2_YEASTTIF4632physical
19838078
PRP40_YEASTPRP40physical
19014439
KSS1_YEASTKSS1physical
21460040
PRP39_YEASTPRP39physical
22020974
PRP40_YEASTPRP40physical
22020974
NAM8_YEASTNAM8physical
22020974
PRP42_YEASTPRP42physical
22020974
SNU56_YEASTSNU56physical
22020974
RU17_YEASTSNP1physical
22020974
RU1A_YEASTMUD1physical
22020974
LUC7_YEASTLUC7physical
22020974
RU1C_YEASTYHC1physical
22020974
PUT2_YEASTPUT2genetic
27708008
NDI1_YEASTNDI1genetic
27708008
RL21B_YEASTRPL21Bgenetic
27708008
LUC7_YEASTLUC7genetic
27708008
RPB1_YEASTRPO21genetic
27708008
RPN5_YEASTRPN5genetic
27708008
ERF3_YEASTSUP35genetic
27708008
SNU56_YEASTSNU56genetic
27708008
PRP28_YEASTPRP28genetic
27708008
GPI19_YEASTGPI19genetic
27708008
CDC12_YEASTCDC12genetic
27708008
BET3_YEASTBET3genetic
27708008
BOS1_YEASTBOS1genetic
27708008
BBP_YEASTMSL5genetic
27708008
SEC22_YEASTSEC22genetic
27708008
RU1C_YEASTYHC1genetic
27708008
MGR1_YEASTMGR1genetic
27708008
CRD1_YEASTCRD1genetic
27708008
PMP3_YEASTPMP3genetic
27708008
ASPG1_YEASTASP1genetic
27708008
YD514_YEASTYDR514Cgenetic
27708008
SWI4_YEASTSWI4genetic
27708008
MIC19_YEASTMIC19genetic
27708008
OSW7_YEASTOSW7genetic
27708008
YGZ2_YEASTYGL242Cgenetic
27708008
YG5Q_YEASTYGR273Cgenetic
27708008
NAM8_YEASTNAM8genetic
27708008
RPE_YEASTRPE1genetic
27708008
YJN2_YEASTYJL132Wgenetic
27708008
FRMSR_YEASTYKL069Wgenetic
27708008
MUD2_YEASTMUD2genetic
27708008
TPO1_YEASTTPO1genetic
27708008
UBI4P_YEASTUBI4genetic
27708008
SIC1_YEASTSIC1genetic
27708008
PEX13_YEASTPEX13genetic
27708008
NKP2_YEASTNKP2genetic
27708008
ORM2_YEASTORM2genetic
27708008
ELO3_YEASTELO3genetic
27708008
MLH1_YEASTMLH1genetic
27708008
PEX15_YEASTPEX15genetic
27708008
DCAM_YEASTSPE2genetic
27708008
LEO1_YEASTLEO1genetic
27708008
TGS1_YEASTTGS1genetic
27708008
TRE1_YEASTTRE1genetic
27708008
YP191_YEASTYPL191Cgenetic
27708008
UBA3_YEASTUBA3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNU71_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512 AND SER-514, ANDMASS SPECTROMETRY.

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