RPN2_HUMAN - dbPTM
RPN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPN2_HUMAN
UniProt AC P04844
Protein Name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
Gene Name RPN2
Organism Homo sapiens (Human).
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 MAPPGSSTVFLLALTIIASTWALTPTHYLTKHDVERLKASLDRPFTNLESAFYSIVGLSSLGAQVPDAKKACTYIRSNLDPSNVDSLFYAAQASQALSGCEISISNETKDLLLAAVSEDSSVTQIYHAVAALSGFGLPLASQEALSALTARLSKEETVLATVQALQTASHLSQQADLRSIVEEIEDLVARLDELGGVYLQFEEGLETTALFVAATYKLMDHVGTEPSIKEDQVIQLMNAIFSKKNFESLSEAFSVASAAAVLSHNRYHVPVVVVPEGSASDTHEQAILRLQVTNVLSQPLTQATVKLEHAKSVASRATVLQKTSFTPVGDVFELNFMNVKFSSGYYDFLVEVEGDNRYIANTVELRVKISTEVGITNVDLSTVDKDQSIAPKTTRVTYPAKAKGTFIADSHQNFALFFQLVDVNTGAELTPHQTFVRLHNQKTGQEVVFVAEPDNKNVYKFELDTSERKIEFDSASGTYTLYLIIGDATLKNPILWNVADVVIKFPEEEAPSTVLSQNLFTPKQEIQHLFREPEKRPPTVVSNTFTALILSPLLLLFALWIRIGANVSNFTFAPSTIIFHLGHAAMLGLMYVYWTQLNMFQTLKYLAILGSVTFLAGNRMLAQQAVKRTAH
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
38UbiquitinationKHDVERLKASLDRPF
HHHHHHHHHHCCCCC		41.9929967540
40PhosphorylationDVERLKASLDRPFTN
HHHHHHHHCCCCCCC		29.25-
40 (in isoform 2)Phosphorylation-29.2522210691
46PhosphorylationASLDRPFTNLESAFY
HHCCCCCCCHHHHHH		41.39-
46 (in isoform 2)Phosphorylation-41.3922210691
50PhosphorylationRPFTNLESAFYSIVG
CCCCCHHHHHHHHHH		27.18-
54O-linked_GlycosylationNLESAFYSIVGLSSL
CHHHHHHHHHHHHHC		12.3528510447
69UbiquitinationGAQVPDAKKACTYIR
CCCCCCHHHHHHHHH		48.5621906983
702-HydroxyisobutyrylationAQVPDAKKACTYIRS
CCCCCHHHHHHHHHH		50.87-
70UbiquitinationAQVPDAKKACTYIRS
CCCCCHHHHHHHHHH		50.8721906983
72UbiquitinationVPDAKKACTYIRSNL
CCCHHHHHHHHHHCC		3.9921963094
77UbiquitinationKACTYIRSNLDPSNV
HHHHHHHHCCCHHHH		31.9922817900
86UbiquitinationLDPSNVDSLFYAAQA
CCHHHHHHHHHHHHH		18.9821963094
87UbiquitinationDPSNVDSLFYAAQAS
CHHHHHHHHHHHHHH		3.0921963094
106N-linked_GlycosylationGCEISISNETKDLLL
CCEEECCHHCHHHHH		60.3219159218
109UbiquitinationISISNETKDLLLAAV
EECCHHCHHHHHHHH		39.9522817900
122UbiquitinationAVSEDSSVTQIYHAV
HHCCCCCHHHHHHHH		5.4523000965
122UbiquitinationAVSEDSSVTQIYHAV
HHCCCCCHHHHHHHH		5.4521890473
149UbiquitinationQEALSALTARLSKEE
HHHHHHHHHHCCHHH		14.9521963094
153PhosphorylationSALTARLSKEETVLA
HHHHHHCCHHHHHHH		32.2520068231
1542-HydroxyisobutyrylationALTARLSKEETVLAT
HHHHHCCHHHHHHHH		65.25-
154UbiquitinationALTARLSKEETVLAT
HHHHHCCHHHHHHHH		65.2523000965
157PhosphorylationARLSKEETVLATVQA
HHCCHHHHHHHHHHH		23.1620068231
161PhosphorylationKEETVLATVQALQTA
HHHHHHHHHHHHHHH		14.6920068231
165UbiquitinationVLATVQALQTASHLS
HHHHHHHHHHHHHHH		2.3121963094
167PhosphorylationATVQALQTASHLSQQ
HHHHHHHHHHHHHHH		30.8620068231
169PhosphorylationVQALQTASHLSQQAD
HHHHHHHHHHHHHHH		28.4820068231
172PhosphorylationLQTASHLSQQADLRS
HHHHHHHHHHHHHHH		18.1520068231
179PhosphorylationSQQADLRSIVEEIED
HHHHHHHHHHHHHHH		37.9821712546
197UbiquitinationRLDELGGVYLQFEEG
HHHHCCCEEEEECCC		4.0121963094
198PhosphorylationLDELGGVYLQFEEGL
HHHCCCEEEEECCCH		9.6920736484
211UbiquitinationGLETTALFVAATYKL
CHHHHHHHHHHHHHH		3.0521963094
212UbiquitinationLETTALFVAATYKLM
HHHHHHHHHHHHHHH		3.5421963094
216PhosphorylationALFVAATYKLMDHVG
HHHHHHHHHHHCCCC		9.4420736484
224PhosphorylationKLMDHVGTEPSIKED
HHHCCCCCCCCCCHH		43.5721406692
227PhosphorylationDHVGTEPSIKEDQVI
CCCCCCCCCCHHHHH		39.8121406692
228UbiquitinationHVGTEPSIKEDQVIQ
CCCCCCCCCHHHHHH		9.1829967540
229UbiquitinationVGTEPSIKEDQVIQL
CCCCCCCCHHHHHHH		60.6221963094
235UbiquitinationIKEDQVIQLMNAIFS
CCHHHHHHHHHHHHC		35.4829967540
242PhosphorylationQLMNAIFSKKNFESL
HHHHHHHCCCCHHHH		36.2924719451
243UbiquitinationLMNAIFSKKNFESLS
HHHHHHCCCCHHHHH		40.7721963094
244UbiquitinationMNAIFSKKNFESLSE
HHHHHCCCCHHHHHH		66.7227667366
245UbiquitinationNAIFSKKNFESLSEA
HHHHCCCCHHHHHHH		50.0521963094
246UbiquitinationAIFSKKNFESLSEAF
HHHCCCCHHHHHHHH		10.4122817900
257PhosphorylationSEAFSVASAAAVLSH
HHHHHHHHHHHHHCC		19.11-
259UbiquitinationAFSVASAAAVLSHNR
HHHHHHHHHHHCCCC		8.8021963094
260UbiquitinationFSVASAAAVLSHNRY
HHHHHHHHHHCCCCC		11.5121963094
267PhosphorylationAVLSHNRYHVPVVVV
HHHCCCCCCCCEEEE		16.7026437602
274UbiquitinationYHVPVVVVPEGSASD
CCCCEEEECCCCCCC		2.1121963094
278PhosphorylationVVVVPEGSASDTHEQ
EEEECCCCCCCCHHH		23.9626437602
279UbiquitinationVVVPEGSASDTHEQA
EEECCCCCCCCHHHH		23.4521963094
280PhosphorylationVVPEGSASDTHEQAI
EECCCCCCCCHHHHH		44.75-
282PhosphorylationPEGSASDTHEQAILR
CCCCCCCCHHHHHHH		25.4719060867
285UbiquitinationSASDTHEQAILRLQV
CCCCCHHHHHHHHHH		26.5421963094
290UbiquitinationHEQAILRLQVTNVLS
HHHHHHHHHHHHHHC		4.2721963094
299UbiquitinationVTNVLSQPLTQATVK
HHHHHCCCCCEEECC		33.7221963094
303UbiquitinationLSQPLTQATVKLEHA
HCCCCCEEECCHHHH		14.7721963094
306SumoylationPLTQATVKLEHAKSV
CCCEEECCHHHHHHH		43.75-
306AcetylationPLTQATVKLEHAKSV
CCCEEECCHHHHHHH		43.7526051181
306SumoylationPLTQATVKLEHAKSV
CCCEEECCHHHHHHH		43.75-
306UbiquitinationPLTQATVKLEHAKSV
CCCEEECCHHHHHHH		43.7521906983
3112-HydroxyisobutyrylationTVKLEHAKSVASRAT
ECCHHHHHHHHHHCE		47.58-
311AcetylationTVKLEHAKSVASRAT
ECCHHHHHHHHHHCE		47.5825953088
311UbiquitinationTVKLEHAKSVASRAT
ECCHHHHHHHHHHCE		47.5821906983
322UbiquitinationSRATVLQKTSFTPVG
HHCEEEECCCCCCCC		41.8121906983
324PhosphorylationATVLQKTSFTPVGDV
CEEEECCCCCCCCCE		33.87-
326PhosphorylationVLQKTSFTPVGDVFE
EEECCCCCCCCCEEE		19.48-
327UbiquitinationLQKTSFTPVGDVFEL
EECCCCCCCCCEEEE		26.5321963094
337SulfoxidationDVFELNFMNVKFSSG
CEEEEEEEEEEECCC		5.6921406390
338UbiquitinationVFELNFMNVKFSSGY
EEEEEEEEEEECCCE		29.6821963094
347UbiquitinationKFSSGYYDFLVEVEG
EECCCEEEEEEEEEC		23.1716196087
353UbiquitinationYDFLVEVEGDNRYIA
EEEEEEEECCCCEEE		47.5329967540
360UbiquitinationEGDNRYIANTVELRV
ECCCCEEECEEEEEE		9.1929967540
366UbiquitinationIANTVELRVKISTEV
EECEEEEEEEEECCC		17.7421963094
368UbiquitinationNTVELRVKISTEVGI
CEEEEEEEEECCCCC		25.22-
369UbiquitinationTVELRVKISTEVGIT
EEEEEEEEECCCCCC		5.8821963094
371UbiquitinationELRVKISTEVGITNV
EEEEEEECCCCCCEE		37.8622817900
3852-HydroxyisobutyrylationVDLSTVDKDQSIAPK
EECCCCCCCCCCCCC		54.02-
385UbiquitinationVDLSTVDKDQSIAPK
EECCCCCCCCCCCCC		54.0229967540
3922-HydroxyisobutyrylationKDQSIAPKTTRVTYP
CCCCCCCCCCEEEEE		54.21-
392UbiquitinationKDQSIAPKTTRVTYP
CCCCCCCCCCEEEEE		54.2129967540
397PhosphorylationAPKTTRVTYPAKAKG
CCCCCEEEEECCCCC		22.09-
398PhosphorylationPKTTRVTYPAKAKGT
CCCCEEEEECCCCCE		9.80-
401UbiquitinationTRVTYPAKAKGTFIA
CEEEEECCCCCEEEE		46.2427667366
403UbiquitinationVTYPAKAKGTFIADS
EEEECCCCCEEEECC		58.7522817900
405PhosphorylationYPAKAKGTFIADSHQ
EECCCCCEEEECCCC		15.91-
408UbiquitinationKAKGTFIADSHQNFA
CCCCEEEECCCCCEE		14.2029967540
410UbiquitinationKGTFIADSHQNFALF
CCEEEECCCCCEEEE		20.2521963094
417UbiquitinationSHQNFALFFQLVDVN
CCCCEEEEEEEEECC		3.0821963094
419UbiquitinationQNFALFFQLVDVNTG
CCEEEEEEEEECCCC		32.9922817900
424UbiquitinationFFQLVDVNTGAELTP
EEEEEECCCCCCCCC		28.4721963094
428UbiquitinationVDVNTGAELTPHQTF
EECCCCCCCCCCCEE		55.3021963094
4422-HydroxyisobutyrylationFVRLHNQKTGQEVVF
EEEEECCCCCCEEEE		61.00-
442UbiquitinationFVRLHNQKTGQEVVF
EEEEECCCCCCEEEE		61.0021906983
456UbiquitinationFVAEPDNKNVYKFEL
EEECCCCCCEEEEEE		55.9921906983
458UbiquitinationAEPDNKNVYKFELDT
ECCCCCCEEEEEEEC		6.1621963094
460AcetylationPDNKNVYKFELDTSE
CCCCCEEEEEEECCC		28.2588467
460UbiquitinationPDNKNVYKFELDTSE
CCCCCEEEEEEECCC		28.2521906983
470UbiquitinationLDTSERKIEFDSASG
EECCCCEEEEECCCC		8.8124816145
472UbiquitinationTSERKIEFDSASGTY
CCCCEEEEECCCCEE		11.6421963094
476UbiquitinationKIEFDSASGTYTLYL
EEEEECCCCEEEEEE		35.3021963094
491UbiquitinationIIGDATLKNPILWNV
EECCCCCCCCCEEEE		57.2221963094
504UbiquitinationNVADVVIKFPEEEAP
EEEEEEEECCHHHCC		43.1716196087
520UbiquitinationTVLSQNLFTPKQEIQ
CHHHCCCCCCHHHHH		16.8116196087
521PhosphorylationVLSQNLFTPKQEIQH
HHHCCCCCCHHHHHH		32.5125022875
523UbiquitinationSQNLFTPKQEIQHLF
HCCCCCCHHHHHHHH		58.4621963094
539UbiquitinationEPEKRPPTVVSNTFT
CCCCCCCCCCCCHHH		35.9021963094
546PhosphorylationTVVSNTFTALILSPL
CCCCCHHHHHHHHHH		20.65-
595UbiquitinationGLMYVYWTQLNMFQT
HHHHHHHHHCCHHHH		12.9023000965
610PhosphorylationLKYLAILGSVTFLAG
HHHHHHHCCCHHHHC		17.60-
610 (in isoform 2)Phosphorylation-17.60-
611UbiquitinationKYLAILGSVTFLAGN
HHHHHHCCCHHHHCC		17.9723000965
6272-HydroxyisobutyrylationMLAQQAVKRTAH---
HHHHHHHHHHCC---		47.23-
627UbiquitinationMLAQQAVKRTAH---
HHHHHHHHHHCC---		47.2323000965
643Ubiquitination-------------------
-------------------		23000965
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 RPN2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPN2_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 RPN2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBBP4_HUMANRBBP4physical
21900206
TNR16_HUMANNGFRphysical
21900206
FBN3_HUMANFBN3physical
21900206
STT3B_HUMANSTT3Bphysical
22939629
TM9S2_HUMANTM9SF2physical
22939629
OST48_HUMANDDOSTphysical
26344197
DX39B_HUMANDDX39Bphysical
26344197
ENPL_HUMANHSP90B1physical
26344197
IPO9_HUMANIPO9physical
26344197
KDSR_HUMANKDSRphysical
26344197
PYC_HUMANPCphysical
26344197
RPN1_HUMANRPN1physical
26344197
SPTN1_HUMANSPTAN1physical
26344197
QCR2_HUMANUQCRC2physical
26344197
TERA_HUMANVCPphysical
26344197
E2AK3_HUMANEIF2AK3physical
28514442
LIN54_HUMANLIN54physical
28514442
CD032_HUMANC4orf32physical
28514442
DSG4_HUMANDSG4physical
28514442
TM258_HUMANTMEM258physical
28514442
OST48_HUMANDDOSTphysical
28514442
HPHL1_HUMANHEPHL1physical
28514442
LYG2_HUMANLYG2physical
28514442
NEUR2_HUMANNEU2physical
28514442
LIN9_HUMANLIN9physical
28514442
APOB_HUMANAPOBphysical
28514442
NSMA_HUMANSMPD2physical
28514442
RPN1_HUMANRPN1physical
28514442
TACC1_HUMANTACC1physical
28514442
MLEC_HUMANMLECphysical
28514442
ALG8_HUMANALG8physical
28514442
ORML2_HUMANORMDL2physical
28514442
LRC15_HUMANLRRC15physical
28514442
DAD1_HUMANDAD1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RPN2_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-106, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-282, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry.";
Meierhofer D., Wang X., Huang L., Kaiser P.;
J. Proteome Res. 7:4566-4576(2008).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-154, AND MASSSPECTROMETRY.

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