STT3B_HUMAN - dbPTM
STT3B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STT3B_HUMAN
UniProt AC Q8TCJ2
Protein Name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
Gene Name STT3B
Organism Homo sapiens (Human).
Sequence Length 826
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). STT3B is present in a small subset of OST complexes and mediates both cotranslational and post-translational N-glycosylation of target proteins: STT3B-containing complexes are required for efficient post-translational glycosylation and while they are less competent than STT3A-containing complexes for cotranslational glycosylation, they have the ability to mediate glycosylation of some nascent sites that are not accessible for STT3A. STT3B-containing complexes also act post-translationally and mediate modification of skipped glycosylation sites in unfolded proteins. Plays a role in ER-associated degradation (ERAD) pathway that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins by mediating N-glycosylation of unfolded proteins, which are then recognized by the ERAD pathway and targeted for degradation. Mediates glycosylation of the disease variant AMYL-TTR 'Asp-38' of TTR at 'Asn-118', leading to its degradation..
Protein Sequence MAEPSAPESKHKSSLNSSPWSGLMALGNSRHGHHGPGAQCAHKAAGGAAPPKPAPAGLSGGLSQPAGWQSLLSFTILFLAWLAGFSSRLFAVIRFESIIHEFDPWFNYRSTHHLASHGFYEFLNWFDERAWYPLGRIVGGTVYPGLMITAGLIHWILNTLNITVHIRDVCVFLAPTFSGLTSISTFLLTRELWNQGAGLLAACFIAIVPGYISRSVAGSFDNEGIAIFALQFTYYLWVKSVKTGSVFWTMCCCLSYFYMVSAWGGYVFIINLIPLHVFVLLLMQRYSKRVYIAYSTFYIVGLILSMQIPFVGFQPIRTSEHMAAAGVFALLQAYAFLQYLRDRLTKQEFQTLFFLGVSLAAGAVFLSVIYLTYTGYIAPWSGRFYSLWDTGYAKIHIPIIASVSEHQPTTWVSFFFDLHILVCTFPAGLWFCIKNINDERVFVALYAISAVYFAGVMVRLMLTLTPVVCMLSAIAFSNVFEHYLGDDMKRENPPVEDSSDEDDKRNQGNLYDKAGKVRKHATEQEKTEEGLGPNIKSIVTMLMLMLLMMFAVHCTWVTSNAYSSPSVVLASYNHDGTRNILDDFREAYFWLRQNTDEHARVMSWWDYGYQIAGMANRTTLVDNNTWNNSHIALVGKAMSSNETAAYKIMRTLDVDYVLVIFGGVIGYSGDDINKFLWMVRIAEGEHPKDIRESDYFTPQGEFRVDKAGSPTLLNCLMYKMSYYRFGEMQLDFRTPPGFDRTRNAEIGNKDIKFKHLEEAFTSEHWLVRIYKVKAPDNRETLDHKPRVTNIFPKQKYLSKKTTKRKRGYIKNKLVFKKGKKISKKTV
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
2Acetylation------MAEPSAPES
------CCCCCCCCC		37.0919413330
5Phosphorylation---MAEPSAPESKHK
---CCCCCCCCCCCC		48.2226074081
9PhosphorylationAEPSAPESKHKSSLN
CCCCCCCCCCCCCCC		38.7125159151
10AcetylationEPSAPESKHKSSLNS
CCCCCCCCCCCCCCC		54.0825953088
10UbiquitinationEPSAPESKHKSSLNS
CCCCCCCCCCCCCCC		54.0833845483
12UbiquitinationSAPESKHKSSLNSSP
CCCCCCCCCCCCCCC		45.54-
13PhosphorylationAPESKHKSSLNSSPW
CCCCCCCCCCCCCCC		39.5123401153
14PhosphorylationPESKHKSSLNSSPWS
CCCCCCCCCCCCCCC		36.0523927012
17PhosphorylationKHKSSLNSSPWSGLM
CCCCCCCCCCCCCCH		42.9725159151
18PhosphorylationHKSSLNSSPWSGLMA
CCCCCCCCCCCCCHH		29.3425159151
21PhosphorylationSLNSSPWSGLMALGN
CCCCCCCCCCHHCCC		25.9823927012
29PhosphorylationGLMALGNSRHGHHGP
CCHHCCCCCCCCCCC		24.6923401153
52UbiquitinationAGGAAPPKPAPAGLS
CCCCCCCCCCCCCCC		53.40-
161N-linked_GlycosylationHWILNTLNITVHIRD
HHHHHHCCCCEEHHH		26.33UniProtKB CARBOHYD
345PhosphorylationQYLRDRLTKQEFQTL
HHHHHHCCHHHHHHH		31.41-
358UbiquitinationTLFFLGVSLAAGAVF
HHHHHHHHHHHHHHH		15.5322817900
367UbiquitinationAAGAVFLSVIYLTYT
HHHHHHHHHHHHHHC		8.5922817900
370UbiquitinationAVFLSVIYLTYTGYI
HHHHHHHHHHHCCCC		7.2822817900
498PhosphorylationENPPVEDSSDEDDKR
CCCCCCCCCCCCHHC		26.6129255136
499PhosphorylationNPPVEDSSDEDDKRN
CCCCCCCCCCCHHCC		58.2929255136
501UbiquitinationPVEDSSDEDDKRNQG
CCCCCCCCCHHCCCC		70.7922505724
504UbiquitinationDSSDEDDKRNQGNLY
CCCCCCHHCCCCCHH		66.6221906983
511PhosphorylationKRNQGNLYDKAGKVR
HCCCCCHHHHHHHHH		21.2821955146
513UbiquitinationNQGNLYDKAGKVRKH
CCCCHHHHHHHHHHH		45.5427667366
5132-HydroxyisobutyrylationNQGNLYDKAGKVRKH
CCCCHHHHHHHHHHH		45.54-
513AcetylationNQGNLYDKAGKVRKH
CCCCHHHHHHHHHHH		45.5423236377
516UbiquitinationNLYDKAGKVRKHATE
CHHHHHHHHHHHHCH		43.6622817900
519UbiquitinationDKAGKVRKHATEQEK
HHHHHHHHHHCHHHH		40.3529967540
526UbiquitinationKHATEQEKTEEGLGP
HHHCHHHHHHCCCCC		62.0129901268
527PhosphorylationHATEQEKTEEGLGPN
HHCHHHHHHCCCCCH		38.22-
542UbiquitinationIKSIVTMLMLMLLMM
HHHHHHHHHHHHHHH		1.4224816145
560UbiquitinationHCTWVTSNAYSSPSV
HHHHHCCCCCCCCEE		33.2721963094
573UbiquitinationSVVLASYNHDGTRNI
EEEEEEECCCCCCCH		25.0321963094
603UbiquitinationDEHARVMSWWDYGYQ
HHHHHHHHHHHHHHH		23.3522817900
606UbiquitinationARVMSWWDYGYQIAG
HHHHHHHHHHHHHEE		22.2622817900
608UbiquitinationVMSWWDYGYQIAGMA
HHHHHHHHHHHEEEC		12.8521963094
616N-linked_GlycosylationYQIAGMANRTTLVDN
HHHEEECCCEEEECC		32.70UniProtKB CARBOHYD
623N-linked_GlycosylationNRTTLVDNNTWNNSH
CCEEEECCCCCCCCE		40.1119159218
625UbiquitinationTTLVDNNTWNNSHIA
EEEECCCCCCCCEEE		35.5124816145
625O-linked_GlycosylationTTLVDNNTWNNSHIA
EEEECCCCCCCCEEE		35.5130059200
627N-linked_GlycosylationLVDNNTWNNSHIALV
EECCCCCCCCEEEEE		37.7820068230
627N-linked_GlycosylationLVDNNTWNNSHIALV
EECCCCCCCCEEEEE		37.7819159218
638UbiquitinationIALVGKAMSSNETAA
EEEEEHHHCCCHHHH		5.2724816145
639PhosphorylationALVGKAMSSNETAAY
EEEEHHHCCCHHHHH		34.57-
640PhosphorylationLVGKAMSSNETAAYK
EEEHHHCCCHHHHHH		26.12-
641N-linked_GlycosylationVGKAMSSNETAAYKI
EEHHHCCCHHHHHHH		43.24UniProtKB CARBOHYD
643PhosphorylationKAMSSNETAAYKIMR
HHHCCCHHHHHHHHH		22.34-
646PhosphorylationSSNETAAYKIMRTLD
CCCHHHHHHHHHHCC		9.89-
647UbiquitinationSNETAAYKIMRTLDV
CCHHHHHHHHHHCCC		25.8722505724
657UbiquitinationRTLDVDYVLVIFGGV
HHCCCCEEEEEECCC		2.7324816145
688UbiquitinationIAEGEHPKDIRESDY
CCCCCCCCCCCCCCC		68.6324816145
693PhosphorylationHPKDIRESDYFTPQG
CCCCCCCCCCCCCCC		27.97-
695PhosphorylationKDIRESDYFTPQGEF
CCCCCCCCCCCCCCE		20.73-
706UbiquitinationQGEFRVDKAGSPTLL
CCCEEECCCCCHHHH		52.3621963094
709PhosphorylationFRVDKAGSPTLLNCL
EEECCCCCHHHHHHH		21.4128851738
711PhosphorylationVDKAGSPTLLNCLMY
ECCCCCHHHHHHHHH		45.6428851738
718PhosphorylationTLLNCLMYKMSYYRF
HHHHHHHHHHHHHEE		7.2128851738
719UbiquitinationLLNCLMYKMSYYRFG
HHHHHHHHHHHHEEC		13.8621963094
728SulfoxidationSYYRFGEMQLDFRTP
HHHEECCCEEECCCC		4.9921406390
749UbiquitinationRNAEIGNKDIKFKHL
CCCCCCCCCCCCHHH		56.4722817900
752UbiquitinationEIGNKDIKFKHLEEA
CCCCCCCCCHHHHHH		59.5022817900
754UbiquitinationGNKDIKFKHLEEAFT
CCCCCCCHHHHHHHC		42.1321963094
754AcetylationGNKDIKFKHLEEAFT
CCCCCCCHHHHHHHC		42.1325825284
771UbiquitinationHWLVRIYKVKAPDNR
CEEEEEEEEECCCCC		34.5824816145
784UbiquitinationNRETLDHKPRVTNIF
CCCCCCCCCCCCCCC		33.9024816145
793UbiquitinationRVTNIFPKQKYLSKK
CCCCCCCCHHHCCCC		48.9929967540
795UbiquitinationTNIFPKQKYLSKKTT
CCCCCCHHHCCCCCC		55.04-
803UbiquitinationYLSKKTTKRKRGYIK
HCCCCCCCCCCCCCC		62.2424816145
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 STT3B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STT3B_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 STT3B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OST48_HUMANDDOSTphysical
26344197
RPN1_HUMANRPN1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615597Congenital disorder of glycosylation 1X (CDG1X)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STT3B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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-623 AND ASN-627, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-29, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498 AND SER-499, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-29; SER-498 ANDSER-499, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498 AND SER-499, ANDMASS SPECTROMETRY.

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