RAD21_MOUSE - dbPTM
RAD21_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAD21_MOUSE
UniProt AC Q61550
Protein Name Double-strand-break repair protein rad21 homolog
Gene Name Rad21
Organism Mus musculus (Mouse).
Sequence Length 635
Subcellular Localization Nucleus . Chromosome . Chromosome, centromere . Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except
Protein Description Cleavable component of the cohesin complex, involved in chromosome cohesion during cell cycle, in DNA repair, and in apoptosis. Plays a role in apoptosis, via its cleavage by caspase-3/CASP3 or caspase-7/CASP7 during early steps of apoptosis: the C-terminal 64 kDa cleavage product may act as a nuclear signal to initiate cytoplasmic events involved in the apoptotic pathway (By similarity). 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 separase/ESPL1 and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis..
Protein Sequence MFYAHFVLSKRGPLAKIWLAAHWDKKLTKAHVFECNLESSVESIISPKVKMALRTSGHLLLGVVRIYHRKAKYLLADCNEAFIKIKMAFRPGVVDLPEENREAAYNAITLPEEFHDFDQPLPDLDDIDVAQQFSLNQSRVEEITMREEVGNISILQENDFGDFGMDDREIMREGSAFEDDDMLVSTSASNLLLEPEQSTSNLNEKMNHLEYEDQYKDDNFGEGNDGGILDDKLISNNDGGIFDDPPALSEAGVMLPEQPAHDDMDEDDNGSLGGPDSPDSVDPVEPMPTMTDQTTLVPNEEEAFALEPIDITVKETKAKRKRKLIVDSVKELDSKTIRAQLSDYSDIVTTLDLAPPTKKLMMWKETGGVEKLFFLPAQPLWNNRLLKLFTRCLTPLVPEDLRKRRKGGEADNLDEFLKEFENPEVPREEQQPQQQQPQPQRDVIDEPIIEEPSRLQDSVMEASRTTIEESAMPPPPPQGVKRKAGQIDPEPSIPPQQVEQMEIPPVELPPEEPPNICQLIPELELLPEKEKEKEKEKEEEEEEEDEDASGGDQDQEERRWNKRTQQMLHGLQRALAKTGAESISLLELCRNTNRKQAAAKFYSFLVLKKQQAIELTQEEPYSDIIATPGPRFHII
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
43PhosphorylationNLESSVESIISPKVK
CCCHHHHHHHCHHHH		24.0626745281
46PhosphorylationSSVESIISPKVKMAL
HHHHHHHCHHHHHHH		19.5926824392
153PhosphorylationREEVGNISILQENDF
CHHCCCEEEECCCCC		22.6525619855
175PhosphorylationREIMREGSAFEDDDM
HHHHHHCCCCCCCCC		25.6527087446
185PhosphorylationEDDDMLVSTSASNLL
CCCCCEEECCHHHHH		16.8125159016
186PhosphorylationDDDMLVSTSASNLLL
CCCCEEECCHHHHHC		22.3422668510
187PhosphorylationDDMLVSTSASNLLLE
CCCEEECCHHHHHCC		23.3825168779
189PhosphorylationMLVSTSASNLLLEPE
CEEECCHHHHHCCCC		27.9825159016
200PhosphorylationLEPEQSTSNLNEKMN
CCCCCCCCHHHHHHH		44.5625159016
211PhosphorylationEKMNHLEYEDQYKDD
HHHHHHHHHHHHCCC		31.0325159016
215PhosphorylationHLEYEDQYKDDNFGE
HHHHHHHHCCCCCCC		28.8025159016
249PhosphorylationFDDPPALSEAGVMLP
CCCCHHHHHCCCCCC		27.75-
328PhosphorylationKRKLIVDSVKELDSK
HHHEEEHHHHHHCCH		24.9729176673
358UbiquitinationLDLAPPTKKLMMWKE
HCCCCCCCCEEEEEC		50.08-
387AcetylationLWNNRLLKLFTRCLT
CCCHHHHHHHHHHHC		46.2622826441
387UbiquitinationLWNNRLLKLFTRCLT
CCCHHHHHHHHHHHC		46.26-
390PhosphorylationNRLLKLFTRCLTPLV
HHHHHHHHHHHCCCC		30.8026643407
394PhosphorylationKLFTRCLTPLVPEDL
HHHHHHHCCCCHHHH		20.4328833060
406UbiquitinationEDLRKRRKGGEADNL
HHHHHHCCCCCCCCH		75.26-
458PhosphorylationEPSRLQDSVMEASRT
CHHHHHHHHHHHHCC		15.4828066266
549PhosphorylationEEEDEDASGGDQDQE
HHHCCCCCCCCHHHH		56.4830635358
577UbiquitinationGLQRALAKTGAESIS
HHHHHHHHHCHHHHH		48.63-
627PhosphorylationPYSDIIATPGPRFHI
CCCCCCCCCCCCCCC		20.54-
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAD21_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMC1A_HUMANSMC1Aphysical
20360068
STAG2_HUMANSTAG2physical
20360068
SMC3_HUMANSMC3physical
20360068
WAPL_HUMANWAPALphysical
20360068
PDS5A_HUMANPDS5Aphysical
20360068
STAG1_HUMANSTAG1physical
20360068
RAD21_HUMANRAD21physical
20360068
PDS5B_HUMANPDS5Bphysical
20360068
NANOG_MOUSENanogphysical
21589869
SOX2_MOUSESox2physical
21589869
PO5F1_MOUSEPou5f1physical
21589869
KLF4_MOUSEKlf4physical
21589869
ERR2_MOUSEEsrrbphysical
21589869
SMC1A_HUMANSMC1Aphysical
26496610
SMC3_HUMANSMC3physical
26496610
STAG2_HUMANSTAG2physical
26496610
PDS5B_HUMANPDS5Bphysical
26496610
WAPL_HUMANWAPALphysical
26496610
PDS5A_HUMANPDS5Aphysical
26496610
AKIP_HUMANAURKAIP1physical
26496610
ZN768_HUMANZNF768physical
26496610
CDCA5_HUMANCDCA5physical
26496610
STAG1_HUMANSTAG1physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAD21_MOUSE

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Related Literatures of Post-Translational Modification

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