UB2J1_HUMAN - dbPTM
UB2J1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UB2J1_HUMAN
UniProt AC Q9Y385
Protein Name Ubiquitin-conjugating enzyme E2 J1
Gene Name UBE2J1
Organism Homo sapiens (Human).
Sequence Length 318
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type IV membrane protein .
Protein Description Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD)..
Protein Sequence METRYNLKSPAVKRLMKEAAELKDPTDHYHAQPLEDNLFEWHFTVRGPPDSDFDGGVYHGRIVLPPEYPMKPPSIILLTANGRFEVGKKICLSISGHHPETWQPSWSIRTALLAIIGFMPTKGEGAIGSLDYTPEERRALAKKSQDFCCEGCGSAMKDVLLPLKSGSDSSQADQEAKELARQISFKAEVNSSGKTISESDLNHSFSLTDLQDDIPTTFQGATASTSYGLQNSSAASFHQPTQPVAKNTSMSPRQRRAQQQSQRRLSTSPDVIQGHQPRDNHTDHGGSAVLIVILTLALAALIFRRIYLANEYIFDFEL
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
5Phosphorylation---METRYNLKSPAV
---CCCCCCCCCHHH		32.0625884760
8AcetylationMETRYNLKSPAVKRL
CCCCCCCCCHHHHHH		51.2488497
8MalonylationMETRYNLKSPAVKRL
CCCCCCCCCHHHHHH		51.2426320211
8UbiquitinationMETRYNLKSPAVKRL
CCCCCCCCCHHHHHH		51.2432015554
9PhosphorylationETRYNLKSPAVKRLM
CCCCCCCCHHHHHHH		22.6628387310
17AcetylationPAVKRLMKEAAELKD
HHHHHHHHHHHHCCC		49.1288493
51PhosphorylationTVRGPPDSDFDGGVY
EECCCCCCCCCCCEE		46.05-
89UbiquitinationGRFEVGKKICLSISG
CCEECCCEEEEEECC		32.4933845483
129PhosphorylationKGEGAIGSLDYTPEE
CCCCCCCCCCCCHHH		16.3825307156
132PhosphorylationGAIGSLDYTPEERRA
CCCCCCCCCHHHHHH		29.5025307156
133PhosphorylationAIGSLDYTPEERRAL
CCCCCCCCHHHHHHH		24.7225307156
143UbiquitinationERRALAKKSQDFCCE
HHHHHHHHCCCCCCC		47.9833845483
156SulfoxidationCEGCGSAMKDVLLPL
CCCCCHHHHHHEEEC		4.0021406390
157UbiquitinationEGCGSAMKDVLLPLK
CCCCHHHHHHEEECC		44.3933845483
164UbiquitinationKDVLLPLKSGSDSSQ
HHHEEECCCCCCCHH		51.3233845483
165PhosphorylationDVLLPLKSGSDSSQA
HHEEECCCCCCCHHH		51.7323312004
167PhosphorylationLLPLKSGSDSSQADQ
EEECCCCCCCHHHHH		41.2223312004
169PhosphorylationPLKSGSDSSQADQEA
ECCCCCCCHHHHHHH		26.5023312004
170PhosphorylationLKSGSDSSQADQEAK
CCCCCCCHHHHHHHH		34.0829214152
177UbiquitinationSQADQEAKELARQIS
HHHHHHHHHHHHHHH		53.1321906983
184PhosphorylationKELARQISFKAEVNS
HHHHHHHHHEEEECC		16.6223401153
186UbiquitinationLARQISFKAEVNSSG
HHHHHHHEEEECCCC		36.5321890473
186UbiquitinationLARQISFKAEVNSSG
HHHHHHHEEEECCCC		36.5322817900
191PhosphorylationSFKAEVNSSGKTISE
HHEEEECCCCCCCCH		45.7229978859
192PhosphorylationFKAEVNSSGKTISES
HEEEECCCCCCCCHH		38.8229978859
194UbiquitinationAEVNSSGKTISESDL
EEECCCCCCCCHHHC		44.63-
208PhosphorylationLNHSFSLTDLQDDIP
CCCCEECCCCCCCCC		33.2028464451
249PhosphorylationQPVAKNTSMSPRQRR
CCCCCCCCCCHHHHH		27.0223927012
251O-linked_GlycosylationVAKNTSMSPRQRRAQ
CCCCCCCCHHHHHHH		19.3930620550
251PhosphorylationVAKNTSMSPRQRRAQ
CCCCCCCCHHHHHHH		19.3920363803
261PhosphorylationQRRAQQQSQRRLSTS
HHHHHHHHHHHHCCC		22.7124043423
266PhosphorylationQQSQRRLSTSPDVIQ
HHHHHHHCCCCCHHC		25.6529255136
267PhosphorylationQSQRRLSTSPDVIQG
HHHHHHCCCCCHHCC		49.2023927012
268PhosphorylationSQRRLSTSPDVIQGH
HHHHHCCCCCHHCCC		18.7425159151
282PhosphorylationHQPRDNHTDHGGSAV
CCCCCCCCCCCHHHH		35.63-
295PhosphorylationAVLIVILTLALAALI
HHHHHHHHHHHHHHH		10.00-
307PhosphorylationALIFRRIYLANEYIF
HHHHHHHHHHHHCEE		9.6527251275
312PhosphorylationRIYLANEYIFDFEL-
HHHHHHHCEECCCC-		13.4918083107
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 UB2J1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UB2J1_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 UB2J1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BIRC2_HUMANBIRC2physical
19690564
BRCA1_HUMANBRCA1physical
19690564
LRSM1_HUMANLRSAM1physical
19690564
PJA2_HUMANPJA2physical
19690564
RING2_HUMANRNF2physical
19690564
SYVN1_HUMANSYVN1physical
19690564
TOPRS_HUMANTOPORSphysical
19690564
TRI63_HUMANTRIM63physical
19690564
TRI27_HUMANTRIM27physical
19549727
OTU1_HUMANYOD1physical
20435896
TERA_HUMANVCPphysical
20435896
DERL1_HUMANDERL1physical
20435896
DERL2_HUMANDERL2physical
20435896
DERL3_HUMANDERL3physical
20435896
AUP1_HUMANAUP1physical
20435896
FAF2_HUMANFAF2physical
20435896
ASNA_HUMANASNA1physical
20435896
GHITM_HUMANGHITMphysical
26186194
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 UB2J1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-266 AND SER-268, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266 AND SER-268, ANDMASS SPECTROMETRY.

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