SPT7_SCHPO - dbPTM
SPT7_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPT7_SCHPO
UniProt AC P87152
Protein Name Transcriptional activator spt7
Gene Name spt7
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 992
Subcellular Localization Nucleus .
Protein Description Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation and deubiquitination. SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3 (By similarity)..
Protein Sequence METNFEDSKSLDEPVLHDIAIALLKNDYWSLYLSPEQKRKYISILNDTLLWNRFINVIEWDKLCDEKDSNGSNDDEEDDLDITTLFRCRCMIFDAKINPALFDLSSTSSGSIEHVDHQNISLEASLAEEEERKKGDAKKSEATGRQLFDDDDFDESDAEDSSKATITLDLQKDKSLRKSIIDLKSVDIDDMDTSGFAAIESNKALSNISFNYVYYTLENDSENINEVKKFEDEEDTSTPNTSSFQNNSSSLDLSDNLSLNSKFGSLTSSFKYLLQYLEGNRSKINATDADVKQLLSDVKKNKSKWANDQRIGQEELYEAAEKVVLELRSYTEHSLAFLTKVSKRDAPDYYTVIKEPMDLGTILRNLKNLHYNSKKEFVHDLMLIWSNCFLYNSHPDHPLRVHAQFMKDKSLELINLIPDIVIQSRKDYDDSLIEAELESDEESTAETSKHVTSKKTSSRGGQTQQAVEVHTDANSPEENNTPVTKKEVETSKPPAVSGSTPPVNEAAVIESSNTLEKEPLSDVATEYWKIKTKDIRESHILNNRRILKSLQFIETELPMIRKPTAMSAFIDREVAYGSIDCLPMDKGDFEPIMKLDTTPLLEYDVGSGVPMTAGSVLETESEEDLYFRDYSLFEINRNTPGVPSLMYKNIAKMQEIRKLCNKIQTVRQLQLPQPFYYEHHKSHVPFANNEPILLDIPQNYDNMSSFKPLAHDVLKKLCTIILFHAGFESFQMGALDALTEIAADYMAKMGAVMDQYLIYGKDKSQQEIVGQTLGELGVDDVNDLISYVYHDVERQSVKLLEIHQRLQRHFVELLRPALSERNDEEAIFNQNGESFVTGNFSYETGDDFFGLRELGLDRELGLDSLSVPLHLLQSRLRSNMSWQPEATIKGDQEYAPPPKYPPITAESISNEIGLIQGFLKKNLEEFGLDELLEDEDIRPRSKPPRPRLPPNGKITTGRKRIASSVFLNQSLRKKRCLKENEQGTEVTTLPEE
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
10PhosphorylationTNFEDSKSLDEPVLH
CCCCCCCCCCCCHHH		45.0321712547
69PhosphorylationKLCDEKDSNGSNDDE
HHCCCCCCCCCCCCH		54.9125720772
72PhosphorylationDEKDSNGSNDDEEDD
CCCCCCCCCCCHHHC		41.1425720772
140PhosphorylationKKGDAKKSEATGRQL
HHCCCCCCHHHCCCC		31.5821712547
156PhosphorylationDDDDFDESDAEDSSK
CCCCCCCCCCCCCCC		43.9224763107
161PhosphorylationDESDAEDSSKATITL
CCCCCCCCCCCEEEE		25.8321712547
162PhosphorylationESDAEDSSKATITLD
CCCCCCCCCCEEEEE		38.3321712547
165PhosphorylationAEDSSKATITLDLQK
CCCCCCCEEEEEHHC		20.4529996109
179PhosphorylationKDKSLRKSIIDLKSV
CCHHHHHHHHCCCCC		20.5225720772
439PhosphorylationLIEAELESDEESTAE
HHHHHHCCCCCCHHH		64.0529996109
471PhosphorylationQQAVEVHTDANSPEE
EEEEEEECCCCCCCC		41.8229996109
475PhosphorylationEVHTDANSPEENNTP
EEECCCCCCCCCCCC		35.0928889911
490PhosphorylationVTKKEVETSKPPAVS
CCHHHHCCCCCCCCC		47.4229996109
497PhosphorylationTSKPPAVSGSTPPVN
CCCCCCCCCCCCCCC		29.1829996109
499PhosphorylationKPPAVSGSTPPVNEA
CCCCCCCCCCCCCHH		30.1824763107
500PhosphorylationPPAVSGSTPPVNEAA
CCCCCCCCCCCCHHH		34.8329996109
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 SPT7_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPT7_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 SPT7_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAF9_SCHPOtaf9physical
19056896
UBP8_SCHPOubp8physical
19056896
TAF12_SCHPOtaf12physical
19056896
GCN5_SCHPOgcn5physical
19056896
SPT20_SCHPOspt20physical
19056896
SGF11_SCHPOsgf11physical
19056896
SPT8_SCHPOspt8physical
19056896
SGF29_SCHPOsgf29physical
19056896
TAF10_SCHPOtaf10physical
19056896
NGG1_SCHPOngg1physical
19056896
SUS1_SCHPOsus1physical
19056896
HFI1_SCHPOhfi1physical
19056896
TRA1_SCHPOtra1physical
19056896
SGF73_SCHPOsgf73physical
19056896
TAF6_SCHPOtaf6physical
19056896
ADA2_SCHPOada2physical
19056896
TAF5_SCHPOtaf5physical
19056896
SPT3_SCHPOspt3physical
19056896
SPT7_SCHPOspt7physical
26771498
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPT7_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-475, AND MASSSPECTROMETRY.

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