HRP1_YEAST - dbPTM
HRP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HRP1_YEAST
UniProt AC Q99383
Protein Name Nuclear polyadenylated RNA-binding protein 4
Gene Name HRP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 534
Subcellular Localization Cytoplasm. Nucleus.
Protein Description RNA-binding protein, which is involved in the polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor CFIA complex and the cleavage and polyadenylation factor (CPF) complex. May be involved in regulation of poly(A) site selection. Is involved in nonsense-mediated mRNA decay. Seems to bind to an RNA downstream sequence element (DSE) located 3' of a nonsense codon and may mark the transcript for decay..
Protein Sequence MSSDEEDFNDIYGDDKPTTTEEVKKEEEQNKAGSGTSQLDQLAALQALSSSLNKLNNPNSNNSSSNNSNQDTSSSKQDGTANDKEGSNEDTKNEKKQESATSANANANASSAGPSGLPWEQLQQTMSQFQQPSSQSPPQQQVTQTKEERSKADLSKESCKMFIGGLNWDTTEDNLREYFGKYGTVTDLKIMKDPATGRSRGFGFLSFEKPSSVDEVVKTQHILDGKVIDPKRAIPRDEQDKTGKIFVGGIGPDVRPKEFEEFFSQWGTIIDAQLMLDKDTGQSRGFGFVTYDSADAVDRVCQNKFIDFKDRKIEIKRAEPRHMQQKSSNNGGNNGGNNMNRRGGNFGNQGDFNQMYQNPMMGGYNPMMNPQAMTDYYQKMQEYYQQMQKQTGMDYTQMYQQQMQQMAMMMPGFAMPPNAMTLNQPQQDSNATQGSPAPSDSDNNKSNDVQTIGNTSNTDSGSPPLNLPNGPKGPSQYNDDHNSGYGYNRDRGDRDRNDRDRDYNHRSGGNHRRNGRGGRGGYNRRNNGYHPYNR
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
2Phosphorylation------MSSDEEDFN
------CCCCHHHHH		46.6322369663
3Phosphorylation-----MSSDEEDFND
-----CCCCHHHHHH		47.9822369663
12PhosphorylationEEDFNDIYGDDKPTT
HHHHHHHCCCCCCCC		19.8419823750
18PhosphorylationIYGDDKPTTTEEVKK
HCCCCCCCCHHHHHH		52.6819823750
19PhosphorylationYGDDKPTTTEEVKKE
CCCCCCCCHHHHHHH		40.5119823750
20PhosphorylationGDDKPTTTEEVKKEE
CCCCCCCHHHHHHHH		32.4019779198
34PhosphorylationEEQNKAGSGTSQLDQ
HHHHCCCCCCHHHHH		43.7022890988
36PhosphorylationQNKAGSGTSQLDQLA
HHCCCCCCHHHHHHH		18.2622890988
37PhosphorylationNKAGSGTSQLDQLAA
HCCCCCCHHHHHHHH		32.0722890988
49PhosphorylationLAALQALSSSLNKLN
HHHHHHHHHHHHHHC		22.3922890988
50PhosphorylationAALQALSSSLNKLNN
HHHHHHHHHHHHHCC		39.4322890988
51PhosphorylationALQALSSSLNKLNNP
HHHHHHHHHHHHCCC		32.3622890988
54AcetylationALSSSLNKLNNPNSN
HHHHHHHHHCCCCCC		58.8624489116
60PhosphorylationNKLNNPNSNNSSSNN
HHHCCCCCCCCCCCC		38.3522369663
63PhosphorylationNNPNSNNSSSNNSNQ
CCCCCCCCCCCCCCC		39.1222369663
64PhosphorylationNPNSNNSSSNNSNQD
CCCCCCCCCCCCCCC		38.9322369663
65PhosphorylationPNSNNSSSNNSNQDT
CCCCCCCCCCCCCCC		39.5920377248
68PhosphorylationNNSSSNNSNQDTSSS
CCCCCCCCCCCCCCC		39.8722369663
72PhosphorylationSNNSNQDTSSSKQDG
CCCCCCCCCCCCCCC		22.2721440633
73PhosphorylationNNSNQDTSSSKQDGT
CCCCCCCCCCCCCCC		40.6922369663
74PhosphorylationNSNQDTSSSKQDGTA
CCCCCCCCCCCCCCC		43.5822369663
75PhosphorylationSNQDTSSSKQDGTAN
CCCCCCCCCCCCCCC		33.8222369663
80PhosphorylationSSSKQDGTANDKEGS
CCCCCCCCCCCCCCC		30.4922369663
87PhosphorylationTANDKEGSNEDTKNE
CCCCCCCCCCHHHHH		37.8320377248
156AcetylationRSKADLSKESCKMFI
HHHHHHCHHHHHHHH		62.0325381059
170PhosphorylationIGGLNWDTTEDNLRE
HCCCCCCCCHHHHHH		24.5722369663
171PhosphorylationGGLNWDTTEDNLREY
CCCCCCCCHHHHHHH		38.5822369663
181AcetylationNLREYFGKYGTVTDL
HHHHHHHCCCCEEEE		30.5224489116
184PhosphorylationEYFGKYGTVTDLKIM
HHHHCCCCEEEEEEE		19.6922369663
186PhosphorylationFGKYGTVTDLKIMKD
HHCCCCEEEEEEEEC		35.1427017623
189AcetylationYGTVTDLKIMKDPAT
CCCEEEEEEEECCCC		43.4924489116
189SuccinylationYGTVTDLKIMKDPAT
CCCEEEEEEEECCCC		43.4923954790
192UbiquitinationVTDLKIMKDPATGRS
EEEEEEEECCCCCCC		65.1223749301
206PhosphorylationSRGFGFLSFEKPSSV
CCCCEEEEECCCCCH		29.1528889911
209UbiquitinationFGFLSFEKPSSVDEV
CEEEEECCCCCHHHH		48.4623749301
209AcetylationFGFLSFEKPSSVDEV
CEEEEECCCCCHHHH		48.4624489116
218AcetylationSSVDEVVKTQHILDG
CCHHHHHHHHHEECC		47.8722865919
226AcetylationTQHILDGKVIDPKRA
HHHEECCEECCHHCC		35.3724489116
304AcetylationVDRVCQNKFIDFKDR
HHHHHHCCCCCCCCC		20.1624489116
309AcetylationQNKFIDFKDRKIEIK
HCCCCCCCCCCEEEE		53.5324489116
328PhosphorylationRHMQQKSSNNGGNNG
CCCCCCCCCCCCCCC		41.1528889911
446PhosphorylationSDSDNNKSNDVQTIG
CCCCCCCCCCCEECC		40.1521126336
451PhosphorylationNKSNDVQTIGNTSNT
CCCCCCEECCCCCCC		30.6023749301
455PhosphorylationDVQTIGNTSNTDSGS
CCEECCCCCCCCCCC		20.3830377154
456PhosphorylationVQTIGNTSNTDSGSP
CEECCCCCCCCCCCC		41.5520377248
458PhosphorylationTIGNTSNTDSGSPPL
ECCCCCCCCCCCCCC		31.1727214570
460PhosphorylationGNTSNTDSGSPPLNL
CCCCCCCCCCCCCCC		38.8525752575
462PhosphorylationTSNTDSGSPPLNLPN
CCCCCCCCCCCCCCC		27.5725521595
483PhosphorylationQYNDDHNSGYGYNRD
HCCCCCCCCCCCCCC		29.9423749301
485PhosphorylationNDDHNSGYGYNRDRG
CCCCCCCCCCCCCCC		19.0930377154
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 HRP1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HRP1_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 HRP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AEP1_YEASTAEP1physical
11805826
AEP2_YEASTAEP2physical
11805826
SYSC_YEASTSES1physical
11805826
ATP22_YEASTATP22physical
11805826
TSR1_YEASTTSR1physical
11805826
NAB2_YEASTNAB2physical
10688190
NAM7_YEASTNAM7physical
10882134
IMB2_YEASTKAP104physical
10506153
XPO1_YEASTCRM1physical
12192043
RNA14_YEASTRNA14physical
9334319
RNA15_YEASTRNA15physical
9334319
NOP3_YEASTNPL3physical
15572678
RNA14_YEASTRNA14genetic
9334319
RNA15_YEASTRNA15genetic
9334319
AEP1_YEASTAEP1physical
16429126
RS11A_YEASTRPS11Aphysical
16429126
RS11B_YEASTRPS11Aphysical
16429126
RS24A_YEASTRPS24Bphysical
16429126
RS24B_YEASTRPS24Bphysical
16429126
RS8A_YEASTRPS8Aphysical
16429126
RS8B_YEASTRPS8Aphysical
16429126
RS9A_YEASTRPS9Aphysical
16429126
RLA0_YEASTRPP0physical
16429126
IMB2_YEASTKAP104physical
15894541
NAB2_YEASTNAB2physical
15894541
NAM7_YEASTNAM7physical
16611983
NMD2_YEASTNMD2physical
16611983
NAB2_YEASTNAB2physical
11283351
IMB2_YEASTKAP104physical
18532879
TRM10_YEASTTRM10genetic
19061648
NAB2_YEASTNAB2physical
18719252
RNQ1_YEASTRNQ1physical
18719252
HRP1_YEASTHRP1physical
19345193
RNA15_YEASTRNA15physical
20600122
NOT4_YEASTMOT2genetic
21464899
RNA14_YEASTRNA14physical
23236150
RAD7_YEASTRAD7genetic
24603480
DPOA2_YEASTPOL12genetic
27708008
ORC2_YEASTORC2genetic
27708008
RFC5_YEASTRFC5genetic
27708008
SLD5_YEASTSLD5genetic
27708008
ACT_YEASTACT1genetic
27708008
SLD3_YEASTSLD3genetic
27708008
CDC20_YEASTCDC20genetic
27708008
ORC6_YEASTORC6genetic
27708008
DNA2_YEASTDNA2genetic
27708008
CTF8_YEASTCTF8genetic
27708008
MCM10_YEASTMCM10genetic
27708008
PRI1_YEASTPRI1genetic
27708008
DPOD2_YEASTPOL31genetic
27708008
PRI2_YEASTPRI2genetic
27708008
IMB1_YEASTKAP95genetic
27708008
ORC1_YEASTORC1genetic
27708008
DPOA_YEASTPOL1genetic
27708008
RBY1F_HUMANRBMY1Fphysical
27107014
RBMX_HUMANRBMXphysical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HRP1_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-2; SER-3; SER-34;THR-184; SER-206; THR-458; SER-460 AND SER-462, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-3, 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-2 AND SER-3, AND MASSSPECTROMETRY.

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