dbPTM

STT3A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STT3A_MOUSE
UniProt AC	P46978
Protein Name	Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
Gene Name	Stt3a
Organism	Mus musculus (Mouse).
Sequence Length	705
Subcellular Localization	Endoplasmic reticulum . Endoplasmic reticulum membrane Multi-pass membrane protein .
Protein Description	Catalytic 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. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). SST3A seems to be involved in complex substrate specificity. STT3A is present in the majority of OST complexes and mediates cotranslational N-glycosylation of most sites on target proteins, while STT3B-containing complexes are required for efficient post-translational glycosylation and mediate glycosylation of sites that have been skipped by STT3A (By similarity)..
Protein Sequence	MTKLGFLRLSYEKQDTLLKLLILSMAAVLSFSTRLFAVLRFESVIHEFDPYFNYRTTRFLAEEGFYKFHNWFDDRAWYPLGRIIGGTIYPGLMITSAAIYHVLHFFHITIDIRNVCVFLAPLFSSFTTIVTYHLTKELKDAGAGLLAAAMIAVVPGYISRSVAGSYDNEGIAIFCMLLTYYMWIKAVKTGSIYWAAKCALAYFYMVSSWGGYVFLINLIPLHVLVLMLTGRFSHRIYVAYCTVYCLGTILSMQISFVGFQPVLSSEHMAAFGVFGLCQIHAFVDYLRSKLNPQQFEVLFRSVISLVGFVLLTVGALLMLTGKISPWTGRFYSLLDPSYAKNNIPIIASVSEHQPTTWSSYYFDLQLLVFMFPVGLYYCFSNLSDARIFIIMYGVTSMYFSAVMVRLMLVLAPVMCILSGIGVSQVLSTYMKNLDISRPDKKSKKQQDSTYPIKNEVASGMILVMAFFLITYTFHSTWVTSEAYSSPSIVLSARGGDGSRIIFDDFREAYYWLRHNTPEDAKVMSWWDYGYQITAMANRTILVDNNTWNNTHISRVGQAMASTEEKAYEIMRELDVSYVLVIFGGLTGYSSDDINKFLWMVRIGGSTETGRHIKENDYYTPTGEFRVDREGSPVLLNCLMYKMCYYRFGQVYTEAKRPPGFDRVRNAEIGNKDFELDVLEEAYTTEHWLVRIYKVKDLDNRGLSRT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Ubiquitination	FLRLSYEKQDTLLKL CEECCHHCHHHHHHH	45.28	-
67	Ubiquitination	LAEEGFYKFHNWFDD HHHCCCHHCCCCCCC	37.57	-
340	Ubiquitination	LLDPSYAKNNIPIIA HCCHHHHCCCCCEEE	42.15	-
392	Phosphorylation	ARIFIIMYGVTSMYF CEEEEEHHCHHHHHH	9.68	25293948
395	Phosphorylation	FIIMYGVTSMYFSAV EEEHHCHHHHHHHHH	11.92	25293948
396	Phosphorylation	IIMYGVTSMYFSAVM EEHHCHHHHHHHHHH	14.74	25293948
398	Phosphorylation	MYGVTSMYFSAVMVR HHCHHHHHHHHHHHH	8.31	25293948
400	Phosphorylation	GVTSMYFSAVMVRLM CHHHHHHHHHHHHHH	11.49	25293948
436	Phosphorylation	YMKNLDISRPDKKSK HHHCCCCCCCCCCCC	37.11	27180971
537	N-linked_Glycosylation	YQITAMANRTILVDN HHEEEEECCEEEEEC	28.66	-
544	N-linked_Glycosylation	NRTILVDNNTWNNTH CCEEEEECCCCCCCC	40.11	-
548	N-linked_Glycosylation	LVDNNTWNNTHISRV EEECCCCCCCCHHHH	41.29	19349973
565	Ubiquitination	AMASTEEKAYEIMRE HHCCCHHHHHHHHHH	50.46	-
605	Phosphorylation	WMVRIGGSTETGRHI EEEEECCCCCCCCCC	20.18	-
613	Ubiquitination	TETGRHIKENDYYTP CCCCCCCCCCCEECC	44.32	-
613	Acetylation	TETGRHIKENDYYTP CCCCCCCCCCCEECC	44.32	23954790
613	Succinylation	TETGRHIKENDYYTP CCCCCCCCCCCEECC	44.32	23954790
619	Phosphorylation	IKENDYYTPTGEFRV CCCCCEECCCCCEEE	14.24	-
621	Phosphorylation	ENDYYTPTGEFRVDR CCCEECCCCCEEECC	41.36	-
637	S-palmitoylation	GSPVLLNCLMYKMCY CCHHHHHHHHHHHHH	2.03	28526873
671	Ubiquitination	RNAEIGNKDFELDVL CCCCCCCCCEECHHH	59.59	-

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 STT3A_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of STT3A_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 STT3A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of STT3A_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of STT3A_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-548, AND MASSSPECTROMETRY.	19349973 [Abstract]