UGGG2_HUMAN - dbPTM
UGGG2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UGGG2_HUMAN
UniProt AC Q9NYU1
Protein Name UDP-glucose:glycoprotein glucosyltransferase 2
Gene Name UGGT2
Organism Homo sapiens (Human).
Sequence Length 1516
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 MAPAKATNVVRLLLGSTALWLSQLGSGTVAASKSVTAHLAAKWPETPLLLEASEFMAEESNEKFWQFLETVQELAIYKQTESDYSYYNLILKKAGQFLDNLHINLLKFAFSIRAYSPAIQMFQQIAADEPPPDGCNAFVVIHKKHTCKINEIKKLLKKAASRTRPYLFKGDHKFPTNKENLPVVILYAEMGTRTFSAFHKVLSEKAQNEEILYVLRHYIQKPSSRKMYLSGYGVELAIKSTEYKALDDTQVKTVTNTTVEDETETNEVQGFLFGKLKEIYSDLRDNLTAFQKYLIESNKQMMPLKVWELQDLSFQAASQIMSAPVYDSIKLMKDISQNFPIKARSLTRIAVNQHMREEIKENQKDLQVRFKIQPGDARLFINGLRVDMDVYDAFSILDMLKLEGKMMNGLRNLGINGEDMSKFLKLNSHIWEYTYVLDIRHSSIMWINDLENDDLYITWPTSCQKLLKPVFPGSVPSIRRNFHNLVLFIDPAQEYTLDFIKLADVFYSHEVPLRIGFVFILNTDDEVDGANDAGVALWRAFNYIAEEFDISEAFISIVHMYQKVKKDQNILTVDNVKSVLQNTFPHANIWDILGIHSKYDEERKAGASFYKMTGLGPLPQALYNGEPFKHEEMNIKELKMAVLQRMMDASVYLQREVFLGTLNDRTNAIDFLMDRNNVVPRINTLILRTNQQYLNLISTSVTADVEDFSTFFFLDSQDKSAVIAKNMYYLTQDDESIISAVTLWIIADFDKPSGRKLLFNALKHMKTSVHSRLGIIYNPTSKINEENTAISRGILAAFLTQKNMFLRSFLGQLAKEEIATAIYSGDKIKTFLIEGMDKNAFEKKYNTVGVNIFRTHQLFCQDVLKLRPGEMGIVSNGRFLGPLDEDFYAEDFYLLEKITFSNLGEKIKGIVENMGINANNMSDFIMKVDALMSSVPKRASRYDVTFLRENHSVIKTNPQENDMFFNVIAIVDPLTREAQKMAQLLVVLGKIINMKIKLFMNCRGRLSEAPLESFYRFVLEPELMSGANDVSSLGPVAKFLDIPESPLLILNMITPEGWLVETVHSNCDLDNIHLKDTEKTVTAEYELEYLLLEGQCFDKVTEQPPRGLQFTLGTKNKPAVVDTIVMAHHGYFQLKANPGAWILRLHQGKSEDIYQIVGHEGTDSQADLEDIIVVLNSFKSKILKVKVKKETDKIKEDILTDEDEKTKGLWDSIKSFTVSLHKENKKEKDVLNIFSVASGHLYERFLRIMMLSVLRNTKTPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQYRWPRWLRQQTERQRIIWGYKILFLDVLFPLAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGYTPFCDSRREMDGYRFWKTGYWASHLLRRKYHISALYVVDLKKFRRIGAGDRLRSQYQALSQDPNSLSNLDQDLPNNMIYQVAIKSLPQDWLWCETWCDDESKQRAKTIDLCNNPKTKESKLKAAARIVPEWVEYDAEIRQLLDHLENKKQDTILTHDEL
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
148UbiquitinationIHKKHTCKINEIKKL
EECCCEECHHHHHHH		50.12-
161PhosphorylationKLLKKAASRTRPYLF
HHHHHHHHCCCCCCC		38.76-
203PhosphorylationSAFHKVLSEKAQNEE
HHHHHHHCHHHCCHH		39.79-
213PhosphorylationAQNEEILYVLRHYIQ
HCCHHHHHHHHHHHC		11.78-
228PhosphorylationKPSSRKMYLSGYGVE
CCCCCCEECCCCCEE		10.7625954137
230PhosphorylationSSRKMYLSGYGVELA
CCCCEECCCCCEEEE		16.6925954137
232PhosphorylationRKMYLSGYGVELAIK
CCEECCCCCEEEEEE		18.0225954137
240PhosphorylationGVELAIKSTEYKALD
CEEEEEECCCCCCCC		21.9925954137
241PhosphorylationVELAIKSTEYKALDD
EEEEEECCCCCCCCC		38.0325954137
243PhosphorylationLAIKSTEYKALDDTQ
EEEECCCCCCCCCCE		11.1425954137
253PhosphorylationLDDTQVKTVTNTTVE
CCCCEEEEEECCEEC		33.4320068231
255PhosphorylationDTQVKTVTNTTVEDE
CCEEEEEECCEECCC		31.8920068231
256N-linked_GlycosylationTQVKTVTNTTVEDET
CEEEEEECCEECCCC		29.44UniProtKB CARBOHYD
257PhosphorylationQVKTVTNTTVEDETE
EEEEEECCEECCCCC		23.8920068231
258PhosphorylationVKTVTNTTVEDETET
EEEEECCEECCCCCC		24.7820068231
263PhosphorylationNTTVEDETETNEVQG
CCEECCCCCCCHHHH		61.5020068231
265PhosphorylationTVEDETETNEVQGFL
EECCCCCCCHHHHHH		44.0620068231
275AcetylationVQGFLFGKLKEIYSD
HHHHHHHHHHHHHHH		49.3918528951
277AcetylationGFLFGKLKEIYSDLR
HHHHHHHHHHHHHHH		45.6218528963
277UbiquitinationGFLFGKLKEIYSDLR
HHHHHHHHHHHHHHH		45.62-
286N-linked_GlycosylationIYSDLRDNLTAFQKY
HHHHHHHHHHHHHHH		32.62UniProtKB CARBOHYD
342UbiquitinationISQNFPIKARSLTRI
HHHCCCCCHHHHHHH		37.68-
422UbiquitinationINGEDMSKFLKLNSH
CCHHHHHHHHHHHHH		48.34-
474PhosphorylationLKPVFPGSVPSIRRN
HCCCCCCCCHHHHHC		30.9721406692
477PhosphorylationVFPGSVPSIRRNFHN
CCCCCCHHHHHCCCC		26.9421406692
495PhosphorylationFIDPAQEYTLDFIKL
EECHHHHCCCCHHHH		10.6720068231
496PhosphorylationIDPAQEYTLDFIKLA
ECHHHHCCCCHHHHH		21.0620068231
604UbiquitinationSKYDEERKAGASFYK
CCCCHHHHCCCCCCC		55.22-
623PhosphorylationGPLPQALYNGEPFKH
CCCCHHHHCCCCCCC		24.9222817900
756AcetylationFDKPSGRKLLFNALK
CCCCCHHHHHHHHHH		53.7320167786
782UbiquitinationIIYNPTSKINEENTA
EECCCCCCCCCCCHH		52.62-
823PhosphorylationEEIATAIYSGDKIKT
HHHHHHHHCCCHHHE		12.25-
827UbiquitinationTAIYSGDKIKTFLIE
HHHHCCCHHHEEEEE		50.02-
906UbiquitinationTFSNLGEKIKGIVEN
ECCCHHHHHHHHHHH		48.17-
920N-linked_GlycosylationNMGINANNMSDFIMK
HCCCCCCCHHHHHHH		28.99UniProtKB CARBOHYD
933PhosphorylationMKVDALMSSVPKRAS
HHHHHHHHCCCCCHH		29.0925690035
934PhosphorylationKVDALMSSVPKRASR
HHHHHHHCCCCCHHC		28.5925690035
942PhosphorylationVPKRASRYDVTFLRE
CCCCHHCCCEEEEEC		16.57-
950N-linked_GlycosylationDVTFLRENHSVIKTN
CEEEEECCCCEECCC		26.71UniProtKB CARBOHYD
952PhosphorylationTFLRENHSVIKTNPQ
EEEECCCCEECCCCC		36.8020068231
1200PhosphorylationKIKEDILTDEDEKTK
HHHHHHCCCCHHHCC		37.3630622161
1206PhosphorylationLTDEDEKTKGLWDSI
CCCCHHHCCCHHHHH		28.4429396449
1252PhosphorylationFLRIMMLSVLRNTKT
HHHHHHHHHHHCCCC		10.9524719451
1257PhosphorylationMLSVLRNTKTPVKFW
HHHHHHCCCCCHHHH		29.84-
1269PhosphorylationKFWLLKNYLSPTFKE
HHHHHHHCCCHHHHH		13.6320068231
1271PhosphorylationWLLKNYLSPTFKEVI
HHHHHCCCHHHHHHH		16.1320068231
1273PhosphorylationLKNYLSPTFKEVIPH
HHHCCCHHHHHHHHH		43.9220068231
1289PhosphorylationAKEYGFRYELVQYRW
HHHHCCCEEEECCCC		16.0210694380
1343MethylationQIVRHDLKELRDFDL
HHHHCCHHHHHCCCC		61.84-
1387PhosphorylationSHLLRRKYHISALYV
HHHHHHHHCEEEEEE		11.5429083192
1390PhosphorylationLRRKYHISALYVVDL
HHHHHCEEEEEEEEH		10.0229083192
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 UGGG2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UGGG2_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 UGGG2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
BIRC6_HUMANBIRC6physical
28514442
ITIH2_HUMANITIH2physical
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 UGGG2_HUMAN

loading...

Related Literatures of Post-Translational Modification
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 TYR-1289, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory