SIR2_SCHPO - dbPTM
SIR2_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SIR2_SCHPO
UniProt AC O94640
Protein Name NAD-dependent histone deacetylase sir2
Gene Name sir2
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 475
Subcellular Localization Nucleus . Chromosome, centromere . Chromosome, telomere . Nuclear throughout the cell cycle. Binds to centromeres, telomeric sites and sites between the silent mating-type loci.
Protein Description Involved in silencing within the mating-type region, at the telomeres, and according to PubMed:12867036 also within centromeric DNA regions. Required for the localization of swi6 to the telomeres, silent mating type region, and according to PubMed:12867036 to the centromeric DNA regions. According to PubMed:15545655 not required for the localization of swi6 to centromeric foci. Deacetylates histone H3 on 'Lys-9' and 'Lys-16' of histone H4. This has a direct role in heterochromatin assembly..
Protein Sequence MASNPLDNNMPTTPVEEKIPVASYSPSSSGSSSGASLLVDIMCGSKETEDEEVDSDEWDKPETENISDLDERSEMVRYLRASGYAKFLEKYLIEEELPVRSILKKLGINLPSALEEFEDIDLLPLLKEVLKREVARRIKLPHFNTFEDVVNLLKKAKNVVVLVGAGISTSLGILDFRSDNGFYARLARHGLSEPSEMFDIHTFRENPEIFYTFARDLLPETNHYSPSHAFIRLLEKKNKLSTLFTQNIDNLEKKTGLSDNKIIQCHGSFATATCIKCKHKVDGSELYEDIRNQRVSYCNECGKPPLKLRRVGQNKKEKHYFSDGDSESSEDDLAQPGIMKPDITFFGEALPDSFFNKVGSGELEETDLLICIGTSLKVAPVSELISVIPPTTPQIYISRTPVRHTQFDVNFLSPYCDWVIVEICKRAGWLNELQALCDLPECHSGSKTRAFETDLDIKFEEPSTYHITSTTNGSC
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
12PhosphorylationPLDNNMPTTPVEEKI
CCCCCCCCCCCHHCC
32.7224763107
13PhosphorylationLDNNMPTTPVEEKIP
CCCCCCCCCCHHCCC
21.3321712547
33PhosphorylationPSSSGSSSGASLLVD
CCCCCCCCCCHHEEE
39.8227738172
45PhosphorylationLVDIMCGSKETEDEE
EEEECCCCCCCCCCC
23.5324763107
48PhosphorylationIMCGSKETEDEEVDS
ECCCCCCCCCCCCCC
53.0929996109
55PhosphorylationTEDEEVDSDEWDKPE
CCCCCCCCCCCCCCC
42.4828889911

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 SIR2_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SIR2_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 SIR2_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SWI3_SCHPOswi3genetic
18818364
CLR3_SCHPOclr3genetic
18818364
CID12_SCHPOcid12genetic
18818364
YBPD_SCHPOSPBC16H5.13genetic
18818364
ASK1_SCHPOask1genetic
18818364
JHD1_SCHPOepe1genetic
18818364
YAC5_SCHPOcph1genetic
22681890
PAB2_SCHPOpab2genetic
22681890
NAA35_SCHPOmak10genetic
22681890
ATP14_SCHPOatp14genetic
22681890
FFT3_SCHPOfft3genetic
22681890
IWR1_SCHPOiwr1genetic
22681890
SHF1_SCHPOshf1genetic
22681890
MCL1_SCHPOmcl1genetic
22681890
CLR3_SCHPOclr3genetic
23572080
JHD1_SCHPOepe1genetic
24013502
YK82_SCHPObdf2genetic
24013502
YH7G_SCHPOSPBC16G5.16physical
26771498
SOL1_SCHPOsol1physical
26771498
TAS3_SCHPOtas3physical
26771498

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SIR2_SCHPO

loading...

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-55, AND MASSSPECTROMETRY.

TOP