RPN2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RPN2_MOUSE
• UniProt AC: Q9DBG6
• Protein Name: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
• Gene Name: Rpn2
• Organism: Mus musculus (Mouse).
• Sequence Length: 631
• Subcellular Localization: Endoplasmic reticulum . Endoplasmic reticulum membrane; Multi-pass membrane protein .
• Protein Description: Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains..
• Protein Sequence: MAPPGSSAVFLLALTITASVQALTPTHYLTKQDVERLKASLDRPFTDLESAFYSIVGLSSLGVQVPDVKKACTFIKSNLDPSNVDSLFYAAQSSQVLSGCEISVSNETKELLLAAVSEDSPIAQIYHAVAALSGFGLPLASNEALGALTARLGKEETVLATVQALQTASHLSQQADLRNIVEEIEDLVARLDELGGVYLQFEEGLELTALFVAATYKLMDHVGTEPSMKEDQVIQLMNTIFSKKNFESLSEAFSVASAAAALSQNRYHVPVVVVPEGSTSDTQEQAILRLQVSNVLSQPLAQAAVKLEHAKSAATRATVLQKTPFSLVGNVFELNFKNVKLSSGYYDFSVRVEGDSRYIANTVELRVKISTEVGITNVDLSTVDKDQSIAPKTTRVTYPAKAKGTFIADSHQNFALFFQLVDVNTGAELTPHQTFVRLHNQKTGQEVVFVAEPDNKNVYKFELDTSERKIEFDSASGTYTLYLIIGDATLKNPILWNVADVVIKFPEEEAPSTVLSQSLFTPKQEIQHLFREPEKRPPTVVSNTFTALILSPLLLLFALWIRIGANVSNFTFAPSTVIFHLGHAAMLGLMYIYWTQLNMFQTLKYLAVLGTVTFLAGNRMLAQHAVKRTAH

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
15	Phosphorylation	AVFLLALTITASVQA HHHHHHHHHHHHHHH	15.63	-
17	Phosphorylation	FLLALTITASVQALT HHHHHHHHHHHHHHC	13.98	-
72	Glutathionylation	VPDVKKACTFIKSNL CCCHHHHHHHHHHCC	4.36	24333276
106	N-linked_Glycosylation	GCEISVSNETKELLL CCEEEECHHHHHHHH	59.82	-
224	Phosphorylation	KLMDHVGTEPSMKED HHHHCCCCCCCCCHH	43.57	-
242	Phosphorylation	QLMNTIFSKKNFESL HHHHHHHCCCCHHHH	38.58	26160508
244	Acetylation	MNTIFSKKNFESLSE HHHHHCCCCHHHHHH	66.72	22826441
254	Phosphorylation	ESLSEAFSVASAAAA HHHHHHHHHHHHHHH	24.66	25177544
263	Phosphorylation	ASAAAALSQNRYHVP HHHHHHHHCCCCCCC	22.23	25177544
306	Acetylation	PLAQAAVKLEHAKSA HHHHHHHHHHHHHHH	43.35	23201123
311	Ubiquitination	AVKLEHAKSAATRAT HHHHHHHHHHHHHHH	42.40	-
322	Acetylation	TRATVLQKTPFSLVG HHHHHHHCCCCCCCC	54.74	23954790
337	Ubiquitination	NVFELNFKNVKLSSG CEEEEEEEEEEECCC	60.81	-
394	Phosphorylation	QSIAPKTTRVTYPAK CCCCCCCCEEEEECC	29.30	28576409
439	Ubiquitination	HQTFVRLHNQKTGQE CCEEEEEECCCCCCE	24.90	27667366
442	Ubiquitination	FVRLHNQKTGQEVVF EEEEECCCCCCEEEE	61.00	27667366
459	Ubiquitination	EPDNKNVYKFELDTS CCCCCCEEEEEEECC	21.25	27667366
460	Succinylation	PDNKNVYKFELDTSE CCCCCEEEEEEECCC	28.25	23954790
464	Ubiquitination	NVYKFELDTSERKIE CEEEEEEECCCCEEE	40.77	27667366
539	Phosphorylation	EPEKRPPTVVSNTFT CCCCCCCCCCCCHHH	35.90	-
627	Acetylation	MLAQHAVKRTAH--- HHHHHHHHHCCC---	44.83	7622803

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RPN2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RPN2_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RPN2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of RPN2_MOUSE !!

Drug and Disease Associations

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