UGGG1_MOUSE - dbPTM
UGGG1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UGGG1_MOUSE
UniProt AC Q6P5E4
Protein Name UDP-glucose:glycoprotein glucosyltransferase 1
Gene Name Uggt1
Organism Mus musculus (Mouse).
Sequence Length 1551
Subcellular Localization Endoplasmic reticulum lumen . Endoplasmic reticulum-Golgi intermediate compartment .
Protein Description Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation (By similarity)..
Protein Sequence MCSRGDANTADAAAARRVTGLRYNMRLLIALALPCLFSLAEANSKAITTSLTTKWFSAPLLLEASEFLAEDSQEKFWSFVEATQNIGSSDHHDTDHSYYDAVLEAAFRFLSPLQQNLLKFCLSLRSYSASIQAFQQIAVDEPPPEGCKSFLSVHGKQTCDLDTLESLLLTAADRPKPLLFKGDHRYPSSNPESPVVILYSEIGHEEFSNIHHQLISKSNEGKINYVFRHYISNPSKEPVYLSGYGVELAIKSTEYKAKDDTQVKGTEVNATVIGESDPIDEVQGFLFGKLRELYPALEGQLKEFRKHLVESTNEMAPLKVWQLQDLSFQTAARILAASGALSLVVMKDISQNFPTKARAITKTAVSAQLRAEVEENQKYFKGTIGLQPGDSALFINGLHIDLDTQDIFSLFDTLRNEARVMEGLHRLGIEGLSLHNILKLNIQPSETDYAVDIRSPAISWVNNLEVDSRYNSWPSSLQELLRPTFPGVIRQIRKNLHNMVFIIDPVHETTAELISIAEMFLSNHIPLRIGFIFVVNDSEDVDGMQDAGVAVLRAYNYVAQEVDGYHAFQTLTQIYNKVRTGETVKVEHVVSVLEKKYPYVEVNSILGIDSAYDQNRKEARGYYEQTGVGPLPVVLFNGMPFEKEQLDPDELETITMHKILETTTFFQRAVYLGELSHDQDVVEYIMNQPNVVPRINSRILTAKREYLDLTASNNFYVDDFARFSALDSRGKTAAIANSMNYLTKKGMSSKEIYDDSFIRPVTFWIVGDFDSPSGRQLLYDAIKHQKTSNNVRISMINNPSQEISDSSTPIFRAIWAALQTQASSSAKNFITKMAKEETAEALAAGVDIAEFSVGGMDVSLFKEVFESSRMDFILSHALYCRDVLKLKKGQRVVISNGRIIGPLEDNELFNQDDFHLLENIILKTSGQKIKSHIQQLRVEEDVASDLVMKVDALLSAQPKGEARIEYQFFEDKHSAIKLKPKEGETYYDVVAVVDPVTREAQRLAPLLLVLTQLINMNLRVFMNCQSKLSDMPLKSFYRYVLEPEISFTADSSFAKGPIAKFLDMPQSPLFTLNLNTPESWMVESVRTPYDLDNIYLEEVDSIVAAEYELEYLLLEGHCYDITTGQPPRGLQFTLGTSANPTIVDTIVMANLGYFQLKANPGAWILRLRKGRSDDIYRIYSHDGTDSPPDANDVVVILNNFKSKIIKVKVQKKADMANEDLLSDGTNENESGFWDSFKWGFSGQKAEEVKQDKDDIINIFSVASGHLYERFLRIMMLSVLKNTKTPVKFWFLKNYLSPTFKEFIPYMAKKYNFQYELVQYKWPRWLHQQTEKQRIIWGYKILFLDVLFPLVVDKFLFVDADQIVRTDLKELRDFNLDGAPYGYTPFCDSRREMDGYRFWKSGYWASHLAGRKYHISALYVVDLKKFRKIAAGDRLRGQYQGLSQDPNSLSNLDQDLPNNMIHQVPIKSLPQEWLWCETWCDDASKKRAKTIDLCNNPMTKEPKLEAAVRIVPEWQDYDQEIKQLQTLFQEEKELGTLHTEETQEGSQKHEEL
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
48PhosphorylationEANSKAITTSLTTKW
HHCCCCCCCCCCCCC		18.3922006019
49PhosphorylationANSKAITTSLTTKWF
HCCCCCCCCCCCCCC		18.6722006019
53PhosphorylationAITTSLTTKWFSAPL
CCCCCCCCCCCCCCH		31.4122006019
181AcetylationRPKPLLFKGDHRYPS
CCCCCCEECCCCCCC		64.5022826441
269N-linked_GlycosylationQVKGTEVNATVIGES
CCCCCEEEEEEECCC		24.54-
289AcetylationVQGFLFGKLRELYPA
HHHHHHHHHHHHHHH		36.7219865917
350PhosphorylationLVVMKDISQNFPTKA
EEEEECHHHCCCCCH		29.2521454597
355PhosphorylationDISQNFPTKARAITK
CHHHCCCCCHHHHHH		32.9521454597
362SuccinylationTKARAITKTAVSAQL
CCHHHHHHHHHHHHH		28.5123806337
362AcetylationTKARAITKTAVSAQL
CCHHHHHHHHHHHHH		28.5123806337
378AcetylationAEVEENQKYFKGTIG
HHHHHHHHHCCCCCC		65.3222826441
536N-linked_GlycosylationIGFIFVVNDSEDVDG
EEEEEEECCCCCCCC		41.61-
538PhosphorylationFIFVVNDSEDVDGMQ
EEEEECCCCCCCCCC		30.41-
744SuccinylationNSMNYLTKKGMSSKE
HHHHHHHHCCCCCCC		44.7423954790
779PhosphorylationPSGRQLLYDAIKHQK
CCHHHHHHHHHHCCC		16.36-
931O-linked_GlycosylationTSGQKIKSHIQQLRV
CCCHHHHHHHHHHHC		29.3330059200
955PhosphorylationMKVDALLSAQPKGEA
HHHHHHHCCCCCCCE		26.2120531401
972UbiquitinationEYQFFEDKHSAIKLK
EEEEECCCCCCEEEC		32.0622790023
974PhosphorylationQFFEDKHSAIKLKPK
EEECCCCCCEEECCC		37.11-
1034AcetylationKLSDMPLKSFYRYVL
HHCCCCHHHHHHHHH		32.4222826441
1035PhosphorylationLSDMPLKSFYRYVLE
HCCCCHHHHHHHHHC		34.88-
1037PhosphorylationDMPLKSFYRYVLEPE
CCCHHHHHHHHHCCC		14.23-
1137PhosphorylationLQFTLGTSANPTIVD
EEEECCCCCCCCHHE		25.0119655815
1222PhosphorylationMANEDLLSDGTNENE
CCCCCCCCCCCCCCC		41.0926525534
1228N-linked_GlycosylationLSDGTNENESGFWDS
CCCCCCCCCCCCCCC		51.29-
1244AcetylationKWGFSGQKAEEVKQD
CCCCCCCCHHHHHCC		62.386571511
1252AcetylationAEEVKQDKDDIINIF
HHHHHCCCCHHHHHH		55.606571601
1260PhosphorylationDDIINIFSVASGHLY
CHHHHHHHHHHHHHH		16.9930482847
1263PhosphorylationINIFSVASGHLYERF
HHHHHHHHHHHHHHH		25.2930482847
1277PhosphorylationFLRIMMLSVLKNTKT
HHHHHHHHHHHCCCC		13.91-
1292AcetylationPVKFWFLKNYLSPTF
CHHHHHHHHCCCHHH		33.7922826441
1308SuccinylationEFIPYMAKKYNFQYE
HHHHHHHHHCCCCEE		38.9823954790
1309AcetylationFIPYMAKKYNFQYEL
HHHHHHHHCCCCEEE		35.5722826441
1412PhosphorylationSHLAGRKYHISALYV
HHHCCCCEEEEEEEE		11.7420139300
1493GlutathionylationRAKTIDLCNNPMTKE
HHHHHHCCCCCCCCC		4.0324333276
1499AcetylationLCNNPMTKEPKLEAA
CCCCCCCCCCCHHHH		66.8122826441
1541PhosphorylationGTLHTEETQEGSQKH
CCCCCCCCCCHHHHH		26.2030635358
1545PhosphorylationTEETQEGSQKHEEL-
CCCCCCHHHHHCCC-		34.9927742792
1547AcetylationETQEGSQKHEEL---
CCCCHHHHHCCC---		55.4723806337
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 UGGG1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UGGG1_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 UGGG1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of UGGG1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UGGG1_MOUSE

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Related Literatures of Post-Translational Modification

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