NGBR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NGBR_HUMAN
• UniProt AC: Q96E22
• Protein Name: Dehydrodolichyl diphosphate synthase complex subunit NUS1 {ECO:0000305}
• Gene Name: NUS1
• Organism: Homo sapiens (Human).
• Sequence Length: 293
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein . Colocalizes with Nogo-B during VEGF and wound healing angiogenesis.
• Protein Description: With DHDDS, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol. Acts as a specific receptor for the N-terminus of Nogo-B, a neural and cardiovascular regulator..
• Protein Sequence: MTGLYELVWRVLHALLCLHRTLTSWLRVRFGTWNWIWRRCCRAASAAVLAPLGFTLRKPPAVGRNRRHHRHPRGGSCLAAAHHRMRWRADGRSLEKLPVHMGLVITEVEQEPSFSDIASLVVWCMAVGISYISVYDHQGIFKRNNSRLMDEILKQQQELLGLDCSKYSPEFANSNDKDDQVLNCHLAVKVLSPEDGKADIVRAAQDFCQLVAQKQKRPTDLDVDTLASLLSSNGCPDPDLVLKFGPVDSTLGFLPWHIRLTEIVSLPSHLNISYEDFFSALRQYAACEQRLGK

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
45	Phosphorylation	RRCCRAASAAVLAPL HHHHHHHHHHHHHCC	18.77	30108239
55	Phosphorylation	VLAPLGFTLRKPPAV HHHCCCCCCCCCCCC	24.69	24719451
58	2-Hydroxyisobutyrylation	PLGFTLRKPPAVGRN CCCCCCCCCCCCCCC	59.47	-
58	Ubiquitination	PLGFTLRKPPAVGRN CCCCCCCCCCCCCCC	59.47	27667366
76	Phosphorylation	HRHPRGGSCLAAAHH CCCCCCCCHHHHHHH	14.58	23663014
144	N-linked_Glycosylation	HQGIFKRNNSRLMDE CCCHHHHCCHHHHHH	51.96	21572394
154	Ubiquitination	RLMDEILKQQQELLG HHHHHHHHHHHHHHC	52.28	29967540
166	Ubiquitination	LLGLDCSKYSPEFAN HHCCCHHHCCHHHHC	56.96	29967540
168	Phosphorylation	GLDCSKYSPEFANSN CCCHHHCCHHHHCCC	22.99	21815630
177	Ubiquitination	EFANSNDKDDQVLNC HHHCCCCCCCCEEEC	68.41	29967540
189	Ubiquitination	LNCHLAVKVLSPEDG EECEEEEEEECCCCC	31.67	29967540
197	Ubiquitination	VLSPEDGKADIVRAA EECCCCCCHHHHHHH	56.03	33845483
214	Ubiquitination	FCQLVAQKQKRPTDL HHHHHHHHCCCCCCC	48.31	29967540
216	Ubiquitination	QLVAQKQKRPTDLDV HHHHHHCCCCCCCCH	68.34	-
271	N-linked_Glycosylation	VSLPSHLNISYEDFF HHCCCCCCCCHHHHH	18.75	21572394

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
POTEI_HUMAN	POTEI	physical	28514442
HSP7C_HUMAN	HSPA8	physical	28514442
ACTB_HUMAN	ACTB	physical	28514442

Drug and Disease Associations

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