SDE2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SDE2_HUMAN
• UniProt AC: Q6IQ49
• Protein Name: Replication stress response regulator SDE2 {ECO:0000305}
• Gene Name: SDE2
• Organism: Homo sapiens (Human).
• Sequence Length: 451
• Subcellular Localization: Nucleus .
• Protein Description: Involved in both DNA replication and cell cycle control. [PubMed: 27906959 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]
• Protein Sequence: MAEAAALVWIRGPGFGCKAVRCASGRCTVRDFIHRHCQDQNVPVENFFVKCNGALINTSDTVQHGAVYSLEPRLCGGKGGFGSMLRALGAQIEKTTNREACRDLSGRRLRDVNHEKAMAEWVKQQAEREAEKEQKRLERLQRKLVEPKHCFTSPDYQQQCHEMAERLEDSVLKGMQAASSKMVSAEISENRKRQWPTKSQTDRGASAGKRRCFWLGMEGLETAEGSNSESSDDDSEEAPSTSGMGFHAPKIGSNGVEMAAKFPSGSQRARVVNTDHGSPEQLQIPVTDSGRHILEDSCAELGESKEHMESRMVTETEETQEKKAESKEPIEEEPTGAGLNKDKETEERTDGERVAEVAPEERENVAVAKLQESQPGNAVIDKETIDLLAFTSVAELELLGLEKLKCELMALGLKCGGTLQERAARLFSVRGLAKEQIDPALFAKPLKGKKK

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
18	Ubiquitination	RGPGFGCKAVRCASG CCCCCCCCEEECCCC		-
58	Phosphorylation	CNGALINTSDTVQHG ECCEEEECCCCCCCC		24667141
59	Phosphorylation	NGALINTSDTVQHGA CCEEEECCCCCCCCC		24667141
61	O-linked_Glycosylation	ALINTSDTVQHGAVY EEEECCCCCCCCCEE		23301498
61	Phosphorylation	ALINTSDTVQHGAVY EEEECCCCCCCCCEE		24667141
94	Ubiquitination	ALGAQIEKTTNREAC HHHCHHHHHCCHHHH		29967540
116	Acetylation	LRDVNHEKAMAEWVK CCCCCHHHHHHHHHH		25953088
116	Ubiquitination	LRDVNHEKAMAEWVK CCCCCHHHHHHHHHH		29967540
123	Ubiquitination	KAMAEWVKQQAEREA HHHHHHHHHHHHHHH		29967540
148	Ubiquitination	QRKLVEPKHCFTSPD HHHHHCCHHHCCCHH		29967540
152	Phosphorylation	VEPKHCFTSPDYQQQ HCCHHHCCCHHHHHH		25159151
153	Phosphorylation	EPKHCFTSPDYQQQC CCHHHCCCHHHHHHH		25159151
156	Phosphorylation	HCFTSPDYQQQCHEM HHCCCHHHHHHHHHH		28985074
170	Phosphorylation	MAERLEDSVLKGMQA HHHHHHHHHHHHHHH		21815630
173	Ubiquitination	RLEDSVLKGMQAASS HHHHHHHHHHHHHHH		29967540
173	Methylation	RLEDSVLKGMQAASS HHHHHHHHHHHHHHH		115977609
181	Ubiquitination	GMQAASSKMVSAEIS HHHHHHHHHHCHHHH		-
188	Phosphorylation	KMVSAEISENRKRQW HHHCHHHHHHHCCCC		25159151
198	Ubiquitination	RKRQWPTKSQTDRGA HCCCCCCCCCCCCCC		29967540
199	Phosphorylation	KRQWPTKSQTDRGAS CCCCCCCCCCCCCCC		-
203	Methylation	PTKSQTDRGASAGKR CCCCCCCCCCCCCHH		54554875
222	Phosphorylation	LGMEGLETAEGSNSE EECCCCCCCCCCCCC		27251275
226	Phosphorylation	GLETAEGSNSESSDD CCCCCCCCCCCCCCC		27251275
228	Phosphorylation	ETAEGSNSESSDDDS CCCCCCCCCCCCCCC		27251275
230	Phosphorylation	AEGSNSESSDDDSEE CCCCCCCCCCCCCCC		27251275
231	Phosphorylation	EGSNSESSDDDSEEA CCCCCCCCCCCCCCC		27251275
253	Phosphorylation	FHAPKIGSNGVEMAA CCCCCCCCCCEEEHH		-
258	Sulfoxidation	IGSNGVEMAAKFPSG CCCCCEEEHHCCCCC		21406390
261	Acetylation	NGVEMAAKFPSGSQR CCEEEHHCCCCCCCE		25953088
264	Phosphorylation	EMAAKFPSGSQRARV EEHHCCCCCCCEEEE		26074081
266	Phosphorylation	AAKFPSGSQRARVVN HHCCCCCCCEEEEEE		26074081
274 (in isoform 3)	Ubiquitination	-		21906983
274	Phosphorylation	QRARVVNTDHGSPEQ CEEEEEECCCCCHHH		29255136
278	Phosphorylation	VVNTDHGSPEQLQIP EEECCCCCHHHCCEE		29255136
287	Phosphorylation	EQLQIPVTDSGRHIL HHCCEEECCCCCHHH		23927012
289	Phosphorylation	LQIPVTDSGRHILED CCEEECCCCCHHHHH		23927012
297	Phosphorylation	GRHILEDSCAELGES CCHHHHHHHHHHCCC		25849741
304	Phosphorylation	SCAELGESKEHMESR HHHHHCCCHHHHHHH		25159151
319	Phosphorylation	MVTETEETQEKKAES CCCCCHHHHHHHHHC		17525332
326	Phosphorylation	TQEKKAESKEPIEEE HHHHHHHCCCCCCCC		-
357 (in isoform 2)	Ubiquitination	-		21906983
369	Ubiquitination	RENVAVAKLQESQPG HHCEEEEECCCCCCC		22817900
369 (in isoform 1)	Ubiquitination	-		21906983
373	Phosphorylation	AVAKLQESQPGNAVI EEEECCCCCCCCEEE		28464451
434	Ubiquitination	FSVRGLAKEQIDPAL HCHHCHHHHHCCHHH		29967540

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
-	K	Ubiquitination	E3 ubiquitin ligase	DTL	Q9NZJ0	PMID:27906959

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
77	G	ubiquitylation	The protein is cleaved at Gly-77 by a deubiquitinating enzyme to form the active SDE2.	27906959

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SDE2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of SDE2_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.