STT3A_HUMAN - dbPTM
STT3A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STT3A_HUMAN
UniProt AC P46977
Protein Name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
Gene Name STT3A
Organism Homo sapiens (Human).
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..
Protein Sequence MTKFGFLRLSYEKQDTLLKLLILSMAAVLSFSTRLFAVLRFESVIHEFDPYFNYRTTRFLAEEGFYKFHNWFDDRAWYPLGRIIGGTIYPGLMITSAAIYHVLHFFHITIDIRNVCVFLAPLFSSFTTIVTYHLTKELKDAGAGLLAAAMIAVVPGYISRSVAGSYDNEGIAIFCMLLTYYMWIKAVKTGSICWAAKCALAYFYMVSSWGGYVFLINLIPLHVLVLMLTGRFSHRIYVAYCTVYCLGTILSMQISFVGFQPVLSSEHMAAFGVFGLCQIHAFVDYLRSKLNPQQFEVLFRSVISLVGFVLLTVGALLMLTGKISPWTGRFYSLLDPSYAKNNIPIIASVSEHQPTTWSSYYFDLQLLVFMFPVGLYYCFSNLSDARIFIIMYGVTSMYFSAVMVRLMLVLAPVMCILSGIGVSQVLSTYMKNLDISRPDKKSKKQQDSTYPIKNEVASGMILVMAFFLITYTFHSTWVTSEAYSSPSIVLSARGGDGSRIIFDDFREAYYWLRHNTPEDAKVMSWWDYGYQITAMANRTILVDNNTWNNTHISRVGQAMASTEEKAYEIMRELDVSYVLVIFGGLTGYSSDDINKFLWMVRIGGSTDTGKHIKENDYYTPTGEFRVDREGSPVLLNCLMYKMCYYRFGQVYTEAKRPPGFDRVRNAEIGNKDFELDVLEEAYTTEHWLVRIYKVKDLDNRGLSRT
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
2Phosphorylation------MTKFGFLRL
------CCCCCCEEC		34.7729083192
3Ubiquitination-----MTKFGFLRLS
-----CCCCCCEECC		42.0421890473
3Ubiquitination-----MTKFGFLRLS
-----CCCCCCEECC		42.0421890473
8MethylationMTKFGFLRLSYEKQD
CCCCCCEECCHHCHH		21.23115480679
11PhosphorylationFGFLRLSYEKQDTLL
CCCEECCHHCHHHHH		31.5629083192
13UbiquitinationFLRLSYEKQDTLLKL
CEECCHHCHHHHHHH		45.2827667366
13UbiquitinationFLRLSYEKQDTLLKL
CEECCHHCHHHHHHH		45.2821890473
19UbiquitinationEKQDTLLKLLILSMA
HCHHHHHHHHHHHHH		44.3423503661
44UbiquitinationAVLRFESVIHEFDPY
HHHHHHHHHHHCCCC		4.0023503661
47UbiquitinationRFESVIHEFDPYFNY
HHHHHHHHCCCCCCH		40.39-
47UbiquitinationRFESVIHEFDPYFNY
HHHHHHHHCCCCCCH		40.3923503661
66PhosphorylationFLAEEGFYKFHNWFD
HHHHCCCHHCCCCCC		24.49-
67UbiquitinationLAEEGFYKFHNWFDD
HHHCCCHHCCCCCCC		37.5721963094
67SumoylationLAEEGFYKFHNWFDD
HHHCCCHHCCCCCCC		37.57-
67UbiquitinationLAEEGFYKFHNWFDD
HHHCCCHHCCCCCCC		37.5721890473
124O-linked_GlycosylationVFLAPLFSSFTTIVT
HHHHHHHHHCHHHHH		32.0230059200
136UbiquitinationIVTYHLTKELKDAGA
HHHHHHHHHHHHHCH		68.3723503661
139UbiquitinationYHLTKELKDAGAGLL
HHHHHHHHHHCHHHH		46.7723503661
188UbiquitinationYMWIKAVKTGSICWA
HHHHHHHHHCCHHHH		52.61-
197UbiquitinationGSICWAAKCALAYFY
CCHHHHHHHHHHHHH		16.58-
197UbiquitinationGSICWAAKCALAYFY
CCHHHHHHHHHHHHH		16.5821963094
289UbiquitinationFVDYLRSKLNPQQFE
HHHHHHHCCCHHHHH		45.9421906983
331PhosphorylationSPWTGRFYSLLDPSY
CCCCCCCHHHCCHHH		9.3128152594
332PhosphorylationPWTGRFYSLLDPSYA
CCCCCCHHHCCHHHH		21.5328152594
337PhosphorylationFYSLLDPSYAKNNIP
CHHHCCHHHHCCCCC		37.0728152594
338PhosphorylationYSLLDPSYAKNNIPI
HHHCCHHHHCCCCCE		27.3028152594
340UbiquitinationLLDPSYAKNNIPIIA
HCCHHHHCCCCCEEE		42.15-
348UbiquitinationNNIPIIASVSEHQPT
CCCCEEEEECCCCCC		18.7727667366
348UbiquitinationNNIPIIASVSEHQPT
CCCCEEEEECCCCCC		18.77-
349UbiquitinationNIPIIASVSEHQPTT
CCCEEEEECCCCCCC		6.0222817900
349UbiquitinationNIPIIASVSEHQPTT
CCCEEEEECCCCCCC		6.02-
351UbiquitinationPIIASVSEHQPTTWS
CEEEEECCCCCCCCH		44.3722817900
352UbiquitinationIIASVSEHQPTTWSS
EEEEECCCCCCCCHH		31.26-
352UbiquitinationIIASVSEHQPTTWSS
EEEEECCCCCCCCHH		31.2627667366
392PhosphorylationARIFIIMYGVTSMYF
CEEEEEHHCHHHHHH		9.6824043423
395PhosphorylationFIIMYGVTSMYFSAV
EEEHHCHHHHHHHHH		11.9224043423
396PhosphorylationIIMYGVTSMYFSAVM
EEHHCHHHHHHHHHH		14.7424043423
398PhosphorylationMYGVTSMYFSAVMVR
HHCHHHHHHHHHHHH		8.3124043423
400PhosphorylationGVTSMYFSAVMVRLM
CHHHHHHHHHHHHHH		11.4924043423
429UbiquitinationVSQVLSTYMKNLDIS
HHHHHHHHHHCCCCC		11.61-
429UbiquitinationVSQVLSTYMKNLDIS
HHHHHHHHHHCCCCC		11.6121963094
440UbiquitinationLDISRPDKKSKKQQD
CCCCCCCCCCCCCCC		62.7221906983
441UbiquitinationDISRPDKKSKKQQDS
CCCCCCCCCCCCCCC		74.9222817900
443UbiquitinationSRPDKKSKKQQDSTY
CCCCCCCCCCCCCCC		64.5822817900
444UbiquitinationRPDKKSKKQQDSTYP
CCCCCCCCCCCCCCC		61.3521906983
473UbiquitinationFFLITYTFHSTWVTS
HHHHHHHCCCCCCCC		2.7821963094
473UbiquitinationFFLITYTFHSTWVTS
HHHHHHHCCCCCCCC		2.78-
509PhosphorylationFDDFREAYYWLRHNT
ECCHHHHHHHHHCCC		7.16-
510PhosphorylationDDFREAYYWLRHNTP
CCHHHHHHHHHCCCH		12.67-
518UbiquitinationWLRHNTPEDAKVMSW
HHHCCCHHHCCCCCH		69.4427667366
518UbiquitinationWLRHNTPEDAKVMSW
HHHCCCHHHCCCCCH		69.44-
521UbiquitinationHNTPEDAKVMSWWDY
CCCHHHCCCCCHHHC		51.2821963094
521UbiquitinationHNTPEDAKVMSWWDY
CCCHHHCCCCCHHHC		51.28-
524PhosphorylationPEDAKVMSWWDYGYQ
HHHCCCCCHHHCCHH		28.1822210691
528PhosphorylationKVMSWWDYGYQITAM
CCCCHHHCCHHEEEE		12.1922210691
533PhosphorylationWDYGYQITAMANRTI
HHCCHHEEEEECCEE		8.5422210691
537N-linked_GlycosylationYQITAMANRTILVDN
HHEEEEECCEEEEEC		28.6619159218
544N-linked_GlycosylationNRTILVDNNTWNNTH
CCEEEEECCCCCCCC		40.1119159218
546O-linked_GlycosylationTILVDNNTWNNTHIS
EEEEECCCCCCCCHH		35.5130059200
548N-linked_GlycosylationLVDNNTWNNTHISRV
EEECCCCCCCCHHHH		41.2919159218
549UbiquitinationVDNNTWNNTHISRVG
EECCCCCCCCHHHHH		25.29-
549UbiquitinationVDNNTWNNTHISRVG
EECCCCCCCCHHHHH		25.2921963094
561PhosphorylationRVGQAMASTEEKAYE
HHHHHHCCCHHHHHH		24.2228122231
562PhosphorylationVGQAMASTEEKAYEI
HHHHHCCCHHHHHHH		38.3328122231
563UbiquitinationGQAMASTEEKAYEIM
HHHHCCCHHHHHHHH		55.8123000965
563UbiquitinationGQAMASTEEKAYEIM
HHHHCCCHHHHHHHH		55.81-
565UbiquitinationAMASTEEKAYEIMRE
HHCCCHHHHHHHHHH		50.4621906983
567PhosphorylationASTEEKAYEIMRELD
CCCHHHHHHHHHHCC		19.6328122231
579UbiquitinationELDVSYVLVIFGGLT
HCCCCEEEEEECCCC		1.53-
579UbiquitinationELDVSYVLVIFGGLT
HCCCCEEEEEECCCC		1.5322817900
603UbiquitinationFLWMVRIGGSTDTGK
HEEEEEECCCCCCCC		17.2721890473
605PhosphorylationWMVRIGGSTDTGKHI
EEEEECCCCCCCCCC		20.2122210691
606PhosphorylationMVRIGGSTDTGKHIK
EEEECCCCCCCCCCC		40.6322210691
610UbiquitinationGGSTDTGKHIKENDY
CCCCCCCCCCCCCCE		44.2221906983
613UbiquitinationTDTGKHIKENDYYTP
CCCCCCCCCCCEECC		50.6221890473
613UbiquitinationTDTGKHIKENDYYTP
CCCCCCCCCCCEECC		50.6221963094
617PhosphorylationKHIKENDYYTPTGEF
CCCCCCCEECCCCCE		22.3328152594
618PhosphorylationHIKENDYYTPTGEFR
CCCCCCEECCCCCEE		14.7628152594
619PhosphorylationIKENDYYTPTGEFRV
CCCCCEECCCCCEEE		14.2428152594
621PhosphorylationENDYYTPTGEFRVDR
CCCEECCCCCEEECC		41.3628152594
641UbiquitinationLLNCLMYKMCYYRFG
HHHHHHHHHHHHHHC		14.4521906983
651PhosphorylationYYRFGQVYTEAKRPP
HHHHCCHHHCCCCCC		7.32-
652PhosphorylationYRFGQVYTEAKRPPG
HHHCCHHHCCCCCCC		30.52-
655UbiquitinationGQVYTEAKRPPGFDR
CCHHHCCCCCCCCCC		60.2421890473
655UbiquitinationGQVYTEAKRPPGFDR
CCHHHCCCCCCCCCC		60.2423000965
671UbiquitinationRNAEIGNKDFELDVL
CCCCCCCCCEECHHH		59.5921906983
695UbiquitinationLVRIYKVKDLDNRGL
EEEEEECCCCCCCCC		48.7121890473
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STT3A_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of STT3A_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615596Congenital disorder of glycosylation 1W (CDG1W)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STT3A_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-537; ASN-544 AND ASN-548,AND MASS SPECTROMETRY.

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