SDE2_MOUSE - dbPTM
SDE2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SDE2_MOUSE
UniProt AC Q8K1J5
Protein Name Replication stress response regulator SDE2 {ECO:0000305}
Gene Name Sde2
Organism Mus musculus (Mouse).
Sequence Length 448
Subcellular Localization Nucleus .
Protein Description Involved in both DNA replication and cell cycle control. Unprocessed SDE2 interacts with PCNA via its PIP-box. The interaction with PCNA prevents monoubiquitination of the latter thereby inhibiting translesion DNA synthesis. The binding of SDE2 to PCNA also leads to processing of SDE2 by an unidentified deubiquinating enzyme, cleaving off the N-terminal ubiquitin-like domain. The resulting mature SDE2 is degraded by the DCX(DTL) complex in a cell cycle- and DNA damage dependent manner. Binding of SDE2 to PCNA is necessary to counteract damage due to ultraviolet light induced replication stress. The complete degradation of SDE2 is necessary to allow S-phase progression..
Protein Sequence MAEAAVVAWVRGPGTVWKALPCASVGCSVRDVIYRHCQEQEVPVECFFVTCNGVLVNAGDKVQHGAVYSLEPRLRGGKGGFGSMLRALGAQIEKTTNREACRDLSGRRLRDVNHEKAMAEWVKQQAEREAEKEQRRLERLQRKLAEPAHCFTSPDYQRQCHEMAERLEDSVLKGMQAASSKMVSAEITETRKRPNKSKTDQETSAKKRKRKCFWLGMDGLEAAEGSSTGSSEDSSEDDSEDAPGTSEQSCCAREDGIDAVEVAADRPGSPRSSASGTHSESPEKLQCPVTEPGQGILENTGTEPGETSDKECNERKTVTDPEETPARKETESHEATEKDQKTGMSGGDRAAMVLSGEDRKSVPAANLEGNNSGDTALGLEAVDLSAFSSAAELESLGLERLKCELMVLGLKCGGTLQERAARLFSVRGLTKELIDPALFAKPSKGKKK
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
83PhosphorylationGGKGGFGSMLRALGA
CCCCCHHHHHHHHHC
26239621
152PhosphorylationAEPAHCFTSPDYQRQ
HCCHHHCCCHHHHHH
28066266
153PhosphorylationEPAHCFTSPDYQRQC
CCHHHCCCHHHHHHH
26643407
156PhosphorylationHCFTSPDYQRQCHEM
HHCCCHHHHHHHHHH
26643407
269PhosphorylationVAADRPGSPRSSASG
EECCCCCCCCCCCCC
24925903
272PhosphorylationDRPGSPRSSASGTHS
CCCCCCCCCCCCCCC
25159016
273PhosphorylationRPGSPRSSASGTHSE
CCCCCCCCCCCCCCC
25777480
275PhosphorylationGSPRSSASGTHSESP
CCCCCCCCCCCCCCC
25777480
277PhosphorylationPRSSASGTHSESPEK
CCCCCCCCCCCCCCC
25159016
279PhosphorylationSSASGTHSESPEKLQ
CCCCCCCCCCCCCCC
25159016
281PhosphorylationASGTHSESPEKLQCP
CCCCCCCCCCCCCCC
27087446
290PhosphorylationEKLQCPVTEPGQGIL
CCCCCCCCCCCCCHH
25777480
300PhosphorylationGQGILENTGTEPGET
CCCHHHCCCCCCCCC
21149613
302PhosphorylationGILENTGTEPGETSD
CHHHCCCCCCCCCCC
21149613
307PhosphorylationTGTEPGETSDKECNE
CCCCCCCCCCCCHHC
21149613
308PhosphorylationGTEPGETSDKECNER
CCCCCCCCCCCHHCC
27087446
317PhosphorylationKECNERKTVTDPEET
CCHHCCCCCCCCCCC
27180971
324PhosphorylationTVTDPEETPARKETE
CCCCCCCCCCHHHCC
27180971
330PhosphorylationETPARKETESHEATE
CCCCHHHCCCCCCCH
30482847
332PhosphorylationPARKETESHEATEKD
CCHHHCCCCCCCHHH
29895711
355PhosphorylationDRAAMVLSGEDRKSV
CCEEEEECCCCCCCC
-
431UbiquitinationFSVRGLTKELIDPAL
HCHHCHHHHHCCHHH
22790023
441AcetylationIDPALFAKPSKGKKK
CCHHHHCCCCCCCCC
23806337

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 SDE2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
77Gubiquitylation

-

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 SDE2_MOUSE !!

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

Oops, there are no PPI records of SDE2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SDE2_MOUSE

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Related Literatures of Post-Translational Modification

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