VTS1_SCHPO - dbPTM
VTS1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VTS1_SCHPO
UniProt AC Q9P6R7
Protein Name Protein vts1
Gene Name SPBC13E7.03c
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 713
Subcellular Localization Cytoplasm.
Protein Description RNA-binding protein involved in post-transcriptional regulation through transcript degradation. May be involved in vacuolar protein transport (By similarity)..
Protein Sequence MEVVEGRRKTCLDVVDSPSSRQKQTIAVSLVDGKNYPTRFLNSRTIDKLKQELNTSNLSTGEMSTNETLKNAQEVAGKLLSEENEDSISEHFDEYLGADKPGISFLTRLKTLESWFQSLSLQDRLTTLRTLLHHLPSQEISTLLSSSLTSSPSNSGLSLDKSLPSSPKGDSPSLSSSLPSLTTKSNLSGNLNMVTPASTQGPAFSSKHGFSNALSTASPIPVRTSSVSSTYLTQDREASSKNCLSKALAFSSIEPPASSASTSPRNTPTPSNNGTSINANVTSSLTSNSTGKTSKTTDLLIAASKKSLPSNSTPSKPNTSFFETPHNNIWDSRDRGAFSAPPAPFFPLGFSPHLNDESSRSRWSNISYSPPPPPPPPELLNHSPKSRPLGDKPYLFYRNNQIGPRTRTEGRSSITEGKPFLSSSLRFEHVPSANDLNSVVNARVEKSTGQPSTPLNRQHYFNELPHSTTPVTLPSLIHGSEIDRRRSGFCLNNFNSTPPFQPYHYEIGSGLPQQMHATNTILTNPIDPNSNISTPVGMHLCTLPYTYQPFSSVEKIETPPNNSKNQTYRRSSRGSNKTRKSISHSKNTDKHVGNELPQDIPSWLRSLRLHKYTNNLKDTDWDALVSLSDLDLQNRGIMALGARRKLLKSFQEVAPLVSSKKMNENLKAAKNQSSESLTSFKGHTDSEDLPSGSMSNEISSNSTKQDVSSSSMD
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
10PhosphorylationVVEGRRKTCLDVVDS
CCCCCCCCHHEECCC
19.2529996109
17PhosphorylationTCLDVVDSPSSRQKQ
CHHEECCCCCCCCCE
18.3121712547
20PhosphorylationDVVDSPSSRQKQTIA
EECCCCCCCCCEEEE
41.9629996109
25PhosphorylationPSSRQKQTIAVSLVD
CCCCCCEEEEEEECC
20.2428889911
38PhosphorylationVDGKNYPTRFLNSRT
CCCCCCCCCHHCHHH
24.5628889911
81PhosphorylationEVAGKLLSEENEDSI
HHHHHHHCCCCCCHH
53.9929996109
87PhosphorylationLSEENEDSISEHFDE
HCCCCCCHHHHHHHH
23.1029996109
89PhosphorylationEENEDSISEHFDEYL
CCCCCHHHHHHHHHH
29.0429996109
158PhosphorylationSPSNSGLSLDKSLPS
CCCCCCCCCCCCCCC
37.7429996109
162PhosphorylationSGLSLDKSLPSSPKG
CCCCCCCCCCCCCCC
45.2224763107
165PhosphorylationSLDKSLPSSPKGDSP
CCCCCCCCCCCCCCC
65.6524763107
166PhosphorylationLDKSLPSSPKGDSPS
CCCCCCCCCCCCCCC
28.7921712547
171PhosphorylationPSSPKGDSPSLSSSL
CCCCCCCCCCHHHCC
25.6728889911
173PhosphorylationSPKGDSPSLSSSLPS
CCCCCCCCHHHCCCC
44.8521712547
175PhosphorylationKGDSPSLSSSLPSLT
CCCCCCHHHCCCCCC
23.4024763107
177PhosphorylationDSPSLSSSLPSLTTK
CCCCHHHCCCCCCCC
40.7121712547
180PhosphorylationSLSSSLPSLTTKSNL
CHHHCCCCCCCCCCC
43.5721712547
211PhosphorylationFSSKHGFSNALSTAS
CCCCCCCCHHHCCCC
26.2829996109
215PhosphorylationHGFSNALSTASPIPV
CCCCHHHCCCCCCCC
21.3721712547
216PhosphorylationGFSNALSTASPIPVR
CCCHHHCCCCCCCCC
31.8225720772
218PhosphorylationSNALSTASPIPVRTS
CHHHCCCCCCCCCCC
24.3725720772
224PhosphorylationASPIPVRTSSVSSTY
CCCCCCCCCCCCCEE
26.1125720772
226PhosphorylationPIPVRTSSVSSTYLT
CCCCCCCCCCCEECC
25.9621712547
252PhosphorylationSKALAFSSIEPPASS
HHHHHHHCCCCCCCC
25.2329996109
258PhosphorylationSSIEPPASSASTSPR
HCCCCCCCCCCCCCC
32.0125720772
259PhosphorylationSIEPPASSASTSPRN
CCCCCCCCCCCCCCC
28.4829996109
261PhosphorylationEPPASSASTSPRNTP
CCCCCCCCCCCCCCC
31.2228889911
262PhosphorylationPPASSASTSPRNTPT
CCCCCCCCCCCCCCC
42.3329996109
263PhosphorylationPASSASTSPRNTPTP
CCCCCCCCCCCCCCC
21.2628889911
267PhosphorylationASTSPRNTPTPSNNG
CCCCCCCCCCCCCCC
29.8025720772
293PhosphorylationTSNSTGKTSKTTDLL
CCCCCCCCCCHHHHH
36.4825720772
294PhosphorylationSNSTGKTSKTTDLLI
CCCCCCCCCHHHHHH
31.3325720772
304PhosphorylationTDLLIAASKKSLPSN
HHHHHHHHCCCCCCC
31.4325720772
312PhosphorylationKKSLPSNSTPSKPNT
CCCCCCCCCCCCCCC
46.1429996109
315PhosphorylationLPSNSTPSKPNTSFF
CCCCCCCCCCCCCCC
61.9129996109
339PhosphorylationSRDRGAFSAPPAPFF
CCCCCCCCCCCCCCC
39.0529996109
351PhosphorylationPFFPLGFSPHLNDES
CCCCCCCCCCCCCCC
15.0425720772
358PhosphorylationSPHLNDESSRSRWSN
CCCCCCCCCCCCCCC
33.6429996109
369PhosphorylationRWSNISYSPPPPPPP
CCCCCCCCCCCCCCC
24.9229996109
383PhosphorylationPPELLNHSPKSRPLG
CHHHCCCCCCCCCCC
32.7129996109
412PhosphorylationRTRTEGRSSITEGKP
CCCCCCCCCCCCCCC
36.6329996109
413PhosphorylationTRTEGRSSITEGKPF
CCCCCCCCCCCCCCC
31.9729996109
415PhosphorylationTEGRSSITEGKPFLS
CCCCCCCCCCCCCCC
40.4029996109
452PhosphorylationEKSTGQPSTPLNRQH
HHCCCCCCCCCCHHH
34.4729996109
453PhosphorylationKSTGQPSTPLNRQHY
HCCCCCCCCCCHHHC
38.1829996109
468PhosphorylationFNELPHSTTPVTLPS
CCCCCCCCCCCCCHH
31.8929996109
469PhosphorylationNELPHSTTPVTLPSL
CCCCCCCCCCCCHHH
20.8329996109
558PhosphorylationSSVEKIETPPNNSKN
CCCEECCCCCCCCCC
47.7429996109
673PhosphorylationLKAAKNQSSESLTSF
HHHHHHCCCHHHHHC
45.5328889911
674PhosphorylationKAAKNQSSESLTSFK
HHHHHCCCHHHHHCC
22.8025720772
676PhosphorylationAKNQSSESLTSFKGH
HHHCCCHHHHHCCCC
38.6128889911
678PhosphorylationNQSSESLTSFKGHTD
HCCCHHHHHCCCCCC
41.2029996109
679PhosphorylationQSSESLTSFKGHTDS
CCCHHHHHCCCCCCC
30.1924763107
684PhosphorylationLTSFKGHTDSEDLPS
HHHCCCCCCCCCCCC
50.3021712547
686PhosphorylationSFKGHTDSEDLPSGS
HCCCCCCCCCCCCCC
33.8821712547

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 VTS1_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VTS1_SCHPO !!

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 VTS1_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YH7G_SCHPOSPBC16G5.16physical
26771498

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VTS1_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673, AND MASSSPECTROMETRY.

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