RAD21_SCHPO - dbPTM
RAD21_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAD21_SCHPO
UniProt AC P30776
Protein Name Cohesin subunit rad21
Gene Name rad21
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 628
Subcellular Localization Nucleus . Chromosome, centromere . Associates with chromatin. Cohesin complex mainly associates with broad centromere region. Also associates with mating-type heterochromatic region.
Protein Description Cleavable component of the cohesin complex, involved in chromosome cohesion during cell cycle. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by cut1 and dissociates from chromatin, allowing sister chromatids to segregate. Also involved in the DNA double-strand-break (DSB) repair system..
Protein Sequence MFYSEAILSKKGPLAKVWLAAHWEKKLSKVQTLHTSIEQSVHAIVTEETAPMALRLSGQLMLGVVRIYSRKARYLLEDCTEALMRLKMSFQPGQVDMIEPATALQSLKGKDAVTQSANLTLPETITEFDLLVPDSTFDFQWSQLLRTPSRSSNTLELHSLPISSSPSFPSSQLSIEAGRNAQVESGFSLGESFAHVGNDMQFHLPISNSGAATPRSVHSDNQSQISIEVGRDAPAAAATDLSGIIGPQMTKSPASSVTHFSTPSMLPIGGTSLDDELLAPVDDLNLDLGLDDLLGDEQGANAPAIEADEQAETSSIHLPSDIMEDDSSRPAAAGVEEGQVVESATAPQQEKINPQKTVRRQRAIIDPVTELSSKQMKKQLADTSSITSPLCLNTSSIVFNATVNFTRNGKFNTSIFSSNLNPKVNELLQADFKQAILRKRKNESPEEVEPAKHQRTDTSTENQETAEVLDPEEIAAAELANITEAAIATLPQETVVQPEGEAPELGSPMGFPVTALESADDSLFDAPPVMLDEADLLGSERLDSSVSEALPSSQTAKDSLRNKWDPYTEGEKVSFQTLSAGCNREEAVQLFFDVLVLATKDVISVKQDVAIQNEITLTAKRGMLLSSL
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
164PhosphorylationLHSLPISSSPSFPSS
EEECCCCCCCCCCHH
47.1629996109
165PhosphorylationHSLPISSSPSFPSSQ
EECCCCCCCCCCHHH
20.1329996109
167PhosphorylationLPISSSPSFPSSQLS
CCCCCCCCCCHHHEE
52.3029996109
216PhosphorylationSGAATPRSVHSDNQS
CCCCCCCEECCCCCC
25.9425720772
219PhosphorylationATPRSVHSDNQSQIS
CCCCEECCCCCCCEE
35.7828889911
242PhosphorylationAAAATDLSGIIGPQM
CHHHHCCCCCCCCCC
30.6529996109
547PhosphorylationERLDSSVSEALPSSQ
CCCCCHHHHHCCCCH
21.0728889911
552PhosphorylationSVSEALPSSQTAKDS
HHHHHCCCCHHHHHH
35.6128889911
553PhosphorylationVSEALPSSQTAKDSL
HHHHCCCCHHHHHHH
29.6128889911
555PhosphorylationEALPSSQTAKDSLRN
HHCCCCHHHHHHHHH
37.3129996109

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 RAD21_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAD21_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 RAD21_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAD22_SCHPOrad52genetic
166019
SCC4_SCHPOssl3physical
16682348
SWI6_SCHPOswi6physical
11598266
SMC1_SCHPOpsm1physical
11069892
SMC3_SCHPOpsm3physical
11069892
WAPL_SCHPOwpl1physical
26687354
PDS5_SCHPOpds5physical
26687354

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAD21_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-219; SER-547 ANDSER-553, AND MASS SPECTROMETRY.

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