SPT5_SCHPO - dbPTM
SPT5_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPT5_SCHPO
UniProt AC O13936
Protein Name Transcription elongation factor spt5
Gene Name spt5
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 990
Subcellular Localization Nucleus .
Protein Description The spt4-spt5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene (By similarity)..
Protein Sequence MDTNSPKSIDKDANSTEVDAAEQDAASVKINSTRASPNGSDLLNDDSEAAKITTNEKQSSPVDSHNESPNDTTINKGEDGNENEVDNVNNNDKKEDEDNVEENEEEADANEEEEEDEEDDEEDEEDEDESGGGRRKRARHDRRNQFLDIEAEVDEDEEELEDEEDEIGREDGFIEEEVGADYVGDDRRHRELDRQRQELQSVDAERLAEEYREKYGRSQTVVGDTSNVPQRLLLPSVNDPNIWAVRCKIGKEKDIVFTIMRKAMDLQYTSSPLEIISAFQRDSLVGYIYVEARKQSHVLDALNGVLNVYTNNMILVPIKEMPDLLKVQKQVVELLPGAYVRIRRGKYAGDLAQVDNLSENGLTARVRIVPRIDYSDGLKRKNSATRPQARLFNESEAFKSNPSKFSKRGPRLFLFNNEEFEDGFLVKDIRISSLITEGVNPTLDEVSKFNPNNEDLDLSSLALSVKGGHAEFQPGDHVEVYVGEQTGVSGVVENVRGSVITMVSSDGLRLDVPSRGLRKRFRHGDYVKVIAGKYKDDTGMVVRISKDEVTFLSDTLMTELTVFSRDLGEASSAQAVNSAYELHDLVQLDVNTVACIFSVDRDTYKVIDQNGGVRTVLASQITMRHSNRRGVATDRNGAEIRIGDKVKEVGGEGKQGTILHIYRAFVFLHNRDIAENNGVFSARSRNVATIAAKGARISADLTKMNPALSNGPALPPVANLKRTIGRDKAIGATVRIRRGPMKGLLGVIKDTTDANARVELHTGNKMVTIPKENLLYTTKTGELISYTEFIERSRGIRPGSISTADGPNVPNWAQGARTPAVANGSRTPAWNTGSRTPAWNSGSKTPAWNSGSRTPAWNSGNKTPAWNAGSRTPAWNSGNKTPAWNVGNKTPAWNSGAKTPAWNAGNKTPSWNNGTKTPAWNANQTPMVANGTNTSWGQTPAYGGFSETNWDTEDNSKPYTAPTPGAWAAPTPGGWDDEEGDSPKYVPPSP
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
3Phosphorylation-----MDTNSPKSID
-----CCCCCCCCCC
35.9821712547
5Phosphorylation---MDTNSPKSIDKD
---CCCCCCCCCCCC
35.4824763107
8PhosphorylationMDTNSPKSIDKDANS
CCCCCCCCCCCCCCC
39.1328889911
27PhosphorylationAAEQDAASVKINSTR
HHHHHHHCCEEECCC
26.1824763107
32PhosphorylationAASVKINSTRASPNG
HHCCEEECCCCCCCH
23.8121712547
33PhosphorylationASVKINSTRASPNGS
HCCEEECCCCCCCHH
26.2628889911
36PhosphorylationKINSTRASPNGSDLL
EEECCCCCCCHHHHC
18.6628889911
40PhosphorylationTRASPNGSDLLNDDS
CCCCCCHHHHCCCCC
31.5529996109
47PhosphorylationSDLLNDDSEAAKITT
HHHCCCCCHHHHCCC
31.8129996109
53PhosphorylationDSEAAKITTNEKQSS
CCHHHHCCCCCCCCC
23.9021712547
54PhosphorylationSEAAKITTNEKQSSP
CHHHHCCCCCCCCCC
44.8721712547
59PhosphorylationITTNEKQSSPVDSHN
CCCCCCCCCCCCCCC
47.9121712547
60PhosphorylationTTNEKQSSPVDSHNE
CCCCCCCCCCCCCCC
26.8424763107
64PhosphorylationKQSSPVDSHNESPND
CCCCCCCCCCCCCCC
28.5721712547
68PhosphorylationPVDSHNESPNDTTIN
CCCCCCCCCCCCCCC
34.0321712547
218PhosphorylationYREKYGRSQTVVGDT
HHHHHCCCCCCCCCC
26.3225720772
818PhosphorylationNWAQGARTPAVANGS
CCCCCCCCCCCCCCC
18.3129996109
825PhosphorylationTPAVANGSRTPAWNT
CCCCCCCCCCCCCCC
32.5629996109
827PhosphorylationAVANGSRTPAWNTGS
CCCCCCCCCCCCCCC
21.0329996109
836PhosphorylationAWNTGSRTPAWNSGS
CCCCCCCCCCCCCCC
21.0329996109
845PhosphorylationAWNSGSKTPAWNSGS
CCCCCCCCCCCCCCC
21.6721712547
850PhosphorylationSKTPAWNSGSRTPAW
CCCCCCCCCCCCCCC
27.6921712547
852PhosphorylationTPAWNSGSRTPAWNS
CCCCCCCCCCCCCCC
32.5727738172
854PhosphorylationAWNSGSRTPAWNSGN
CCCCCCCCCCCCCCC
21.0324763107
863PhosphorylationAWNSGNKTPAWNAGS
CCCCCCCCCCCCCCC
23.4121712547
870PhosphorylationTPAWNAGSRTPAWNS
CCCCCCCCCCCCCCC
30.4821712547
872PhosphorylationAWNAGSRTPAWNSGN
CCCCCCCCCCCCCCC
21.0324763107
877PhosphorylationSRTPAWNSGNKTPAW
CCCCCCCCCCCCCCC
32.8021712547
881PhosphorylationAWNSGNKTPAWNVGN
CCCCCCCCCCCCCCC
23.4124763107
890PhosphorylationAWNVGNKTPAWNSGA
CCCCCCCCCCCCCCC
23.4124763107
899PhosphorylationAWNSGAKTPAWNAGN
CCCCCCCCCCCCCCC
20.0824763107
908PhosphorylationAWNAGNKTPSWNNGT
CCCCCCCCCCCCCCC
26.9321712547
910PhosphorylationNAGNKTPSWNNGTKT
CCCCCCCCCCCCCCC
47.9024763107
915PhosphorylationTPSWNNGTKTPAWNA
CCCCCCCCCCCCCCC
33.5924763107
963PhosphorylationSKPYTAPTPGAWAAP
CCCCCCCCCCCCCCC
31.7124763107
971PhosphorylationPGAWAAPTPGGWDDE
CCCCCCCCCCCCCCC
29.8224763107
982PhosphorylationWDDEEGDSPKYVPPS
CCCCCCCCCCCCCCC
33.8624763107
985PhosphorylationEEGDSPKYVPPSP--
CCCCCCCCCCCCC--
22.9027738172
989PhosphorylationSPKYVPPSP------
CCCCCCCCC------
0.0021712547

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 SPT5_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPT5_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 SPT5_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MCE1_SCHPOceg1physical
11893740
CET1_SCHPOpct1physical
11893740
CET1_SCHPOpct1genetic
20231361
MCE1_SCHPOceg1genetic
20231361
GEMI4_HUMANGEMIN4genetic
20231361
RPB1_SCHPOrpb1genetic
20231361
SET1_SCHPOset1genetic
22876190
RTF1_SCHPOprf1physical
24385927

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPT5_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-36, AND MASSSPECTROMETRY.

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