PUB1_SCHPO - dbPTM
PUB1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PUB1_SCHPO
UniProt AC Q92462
Protein Name E3 ubiquitin-protein ligase pub1
Gene Name pub1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 767
Subcellular Localization Membrane
Peripheral membrane protein . Cytoplasm .
Protein Description E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Regulates ubiquitination of cdc25..
Protein Sequence MSNSAQSRRIRVTIVAADGLYKRDVFRFPDPFAVLTVDGEQTHTTTAIKKTLNPYWNETFEVNVTDNSTIAIQVFDQKKFKKKGQGFLGVINLRVGDVLDLAIGGDEMLTRDLKKSNENTVVHGKIIINLSTTAQSTLQVPSSAASGARTQRTSITNDPQSSQSSSVSRNPASSRAGSPTRDNAPAASPASSEPRTFSSFEDQYGRLPPGWERRTDNLGRTYYVDHNTRSTTWIRPNLSSVAGAAAAELHSSASSANVTEGVQPSSSNAARRTEASVLTSNATTAGSGELPPGWEQRYTPEGRPYFVDHNTRTTTWVDPRRQQYIRSYGGPNNATIQQQPVSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQNVPQYKRDFRRKLIYFLSQPALHPLPGQCHIKVRRNHIFEDSYAEIMRQSATDLKKRLMIKFDGEDGLDYGGLSREYFFLLSHEMFNPFYCLFEYSSVDNYTLQINPHSGINPEHLNYFKFIGRVIGLAIFHRRFVDAFFVVSFYKMILQKKVTLQDMESMDAEYYRSLVWILDNDITGVLDLTFSVEDNCFGEVVTIDLKPNGRNIEVTEENKREYVDLVTVWRIQKRIEEQFNAFHEGFSELIPQELINVFDERELELLIGGISEIDMEDWKKHTDYRSYSENDQIIKWFWELMDEWSNEKKSRLLQFTTGTSRIPVNGFKDLQGSDGPRKFTIEKAGEPNKLPKAHTCFNRLDLPPYTSKKDLDHKLSIAVEETIGFGQE
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
150PhosphorylationSAASGARTQRTSITN
CCCCCCCCCCEECCC		23.1325720772
153PhosphorylationSGARTQRTSITNDPQ
CCCCCCCEECCCCCC		18.0525720772
154PhosphorylationGARTQRTSITNDPQS
CCCCCCEECCCCCCC		29.6029996109
156PhosphorylationRTQRTSITNDPQSSQ
CCCCEECCCCCCCCC		33.0828889911
161PhosphorylationSITNDPQSSQSSSVS
ECCCCCCCCCCCCCC		35.4125720772
164PhosphorylationNDPQSSQSSSVSRNP
CCCCCCCCCCCCCCC		26.9125720772
166PhosphorylationPQSSQSSSVSRNPAS
CCCCCCCCCCCCCCH		29.3829996109
168PhosphorylationSSQSSSVSRNPASSR
CCCCCCCCCCCCHHC		28.4325720772
173PhosphorylationSVSRNPASSRAGSPT
CCCCCCCHHCCCCCC		22.9329996109
174PhosphorylationVSRNPASSRAGSPTR
CCCCCCHHCCCCCCC		28.4025720772
178PhosphorylationPASSRAGSPTRDNAP
CCHHCCCCCCCCCCC		23.3228889911
180PhosphorylationSSRAGSPTRDNAPAA
HHCCCCCCCCCCCCC		52.9628889911
188PhosphorylationRDNAPAASPASSEPR
CCCCCCCCCCCCCCC		24.0929996109
191PhosphorylationAPAASPASSEPRTFS
CCCCCCCCCCCCCCC		38.3229996109
192PhosphorylationPAASPASSEPRTFSS
CCCCCCCCCCCCCCC		54.4429996109
198PhosphorylationSSEPRTFSSFEDQYG
CCCCCCCCCHHHHCC		33.2429996109
199PhosphorylationSEPRTFSSFEDQYGR
CCCCCCCCHHHHCCC		28.5928889911
239PhosphorylationTWIRPNLSSVAGAAA
EEECCCHHHHHHHHH		29.4327738172
254PhosphorylationAELHSSASSANVTEG
HHHHHCCCCCCCCCC		31.7527738172
255PhosphorylationELHSSASSANVTEGV
HHHHCCCCCCCCCCC		24.4727738172
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 PUB1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PUB1_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 PUB1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HOG1_SCHPOsty1genetic
10467003
PUB2_SCHPOpub2genetic
11956316
MPIP_SCHPOcdc25genetic
8635463
SPO11_SCHPOrec12genetic
18818364
MAL3_SCHPOmal3genetic
18818364
FFT3_SCHPOfft3genetic
18818364
SNT2_SCHPOsnt2genetic
18818364
MPH1L_SCHPOmph1genetic
18818364
REB1_SCHPOreb1genetic
18818364
CSK2C_SCHPOckb2genetic
18818364
TSC2_SCHPOtsc2genetic
23813957
TSC1_SCHPOtsc1genetic
23813957
YNSK_SCHPOany1physical
23813957
CIS4_SCHPOcis4genetic
24454826
AP1M1_SCHPOapm1genetic
24454826
YNSK_SCHPOany1physical
24876389
HUA1_SCHPOSPAC17A5.10physical
26771498
YDA5_SCHPOSPAC1F12.05physical
26771498
YF75_SCHPOspa2physical
26771498
YNSK_SCHPOany1physical
26771498
YHK5_SCHPOSPBC660.05physical
26771498
ALY1_SCHPOSPBC839.02physical
26771498
YHP4_SCHPOrmn1physical
26771498
YORQ_SCHPOSPBP8B7.26physical
26771498
PUB2_SCHPOpub2genetic
26365378
UBC13_SCHPOubc13genetic
26365378
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PUB1_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 THR-156; SER-178 ANDTHR-180, AND MASS SPECTROMETRY.

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