HSP72_SCHPO - dbPTM
HSP72_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSP72_SCHPO
UniProt AC O59855
Protein Name Probable heat shock protein ssa2
Gene Name ssa2
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 647
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MSKSIGIDLGTTYSCVGHFSNNRVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPHNTIFDAKRLIGRKFDDPEVQSDMKHWPFKVISKDGKPVLQVEYKGETKTFTPEEISSMVLMKMRETAEAYLGGKVTDAVVTVPAYFNDSQRQATKDAGLIAGLNVLRIINEPTAAAIAYGLDRSNQGESNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDSRLVNHFIQEFKRKNKKDITGNARAVRRLRTACERAKRTLSSSAQASIEIDSLFEGIDFYTSITRARFEELCADLFRKTMEPVERVLRDSKVDKASVNEIVLVGGSTRIPRVQKLVSDFFNGKEPCKSINPDEAVAYGAAVQAAVLTGDTSEKTQDLLLLDVAPLSMGIETAGGVMTPLIKRNTTIPTKKSEIFSTYSDNQPGVLIQVFEGERARTKDCNLLGKFELSGIPPAPRGVPQIEVTFDVDANGILNVSALEKGTGKTQKITITNDKGRLSKEEIDRMVAEAEKYKAEDEAESGRIQAKNHLESYAYSLRNSLDDPNLKDKVDASDKETVDKAVKETIEWLDSNTTAAKDEFEAKQKELESVANPIMAKIYQAGGAPGGMPGAAPGAAPGAAPGAAPGGDNGPEVEEVD
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
2Acetylation------MSKSIGIDL
------CCCCCCEEC
34.80-
35PhosphorylationANDQGNRTTPSYVAF
ECCCCCCCCCCEEEE
47.2425720772
36PhosphorylationNDQGNRTTPSYVAFT
CCCCCCCCCCEEEEE
13.6528889911
147PhosphorylationAVVTVPAYFNDSQRQ
EEEEEECCCCHHHCH
9.2424763107
151PhosphorylationVPAYFNDSQRQATKD
EECCCCHHHCHHHHH
28.5028889911
339PhosphorylationIVLVGGSTRIPRVQK
EEEECCCCCCHHHHH
35.5728889911
383PhosphorylationAVLTGDTSEKTQDLL
HHHCCCCCHHHHHEE
41.6627738172
416PhosphorylationTPLIKRNTTIPTKKS
CHHHCCCCCCCCCHH
30.0924763107
417PhosphorylationPLIKRNTTIPTKKSE
HHHCCCCCCCCCHHH
28.6328889911
420PhosphorylationKRNTTIPTKKSEIFS
CCCCCCCCCHHHHEE
47.4525720772
423PhosphorylationTTIPTKKSEIFSTYS
CCCCCCHHHHEEEEC
37.1629996109
427PhosphorylationTKKSEIFSTYSDNQP
CCHHHHEEEECCCCC
31.9029996109
428PhosphorylationKKSEIFSTYSDNQPG
CHHHHEEEECCCCCE
19.1229996109
429PhosphorylationKSEIFSTYSDNQPGV
HHHHEEEECCCCCEE
16.9021712547
430PhosphorylationSEIFSTYSDNQPGVL
HHHEEEECCCCCEEE
30.1225720772
502PhosphorylationKTQKITITNDKGRLS
CCEEEEEECCCCCCC
28.8129996109
509PhosphorylationTNDKGRLSKEEIDRM
ECCCCCCCHHHHHHH
36.3428889911
542PhosphorylationQAKNHLESYAYSLRN
CHHHHHHHHHHHHHH
22.7921712547
543PhosphorylationAKNHLESYAYSLRNS
HHHHHHHHHHHHHHC
10.5321712547
545PhosphorylationNHLESYAYSLRNSLD
HHHHHHHHHHHHCCC
10.4521712547
546PhosphorylationHLESYAYSLRNSLDD
HHHHHHHHHHHCCCC
16.8128889911
550PhosphorylationYAYSLRNSLDDPNLK
HHHHHHHCCCCCCHH
27.0924763107
563PhosphorylationLKDKVDASDKETVDK
HHHCCCCCCHHHHHH
44.7621712547
567PhosphorylationVDASDKETVDKAVKE
CCCCCHHHHHHHHHH
39.4821712547
581PhosphorylationETIEWLDSNTTAAKD
HHHHHHHHCCCHHHH
33.6329996109
583PhosphorylationIEWLDSNTTAAKDEF
HHHHHHCCCHHHHHH
23.0521712547
584PhosphorylationEWLDSNTTAAKDEFE
HHHHHCCCHHHHHHH
28.9429996109

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 HSP72_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSP72_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 HSP72_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of HSP72_SCHPO !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HSP72_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 THR-36; THR-339; THR-417 ANDSER-546, AND MASS SPECTROMETRY.

TOP