EDEM3_HUMAN - dbPTM
EDEM3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EDEM3_HUMAN
UniProt AC Q9BZQ6
Protein Name ER degradation-enhancing alpha-mannosidase-like protein 3
Gene Name EDEM3
Organism Homo sapiens (Human).
Sequence Length 932
Subcellular Localization Endoplasmic reticulum lumen .
Protein Description Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes, by catalyzing mannose trimming from Man8GlcNAc2 to Man7GlcNAc2 in the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity)..
Protein Sequence MSEAGGRGCGSPVPQRARWRLVAATAAFCLVSATSVWTAGAEPMSREEKQKLGNQVLEMFDHAYGNYMEHAYPADELMPLTCRGRVRGQEPSRGDVDDALGKFSLTLIDSLDTLVVLNKTKEFEDAVRKVLRDVNLDNDVVVSVFETNIRVLGGLLGGHSLAIMLKEKGEYMQWYNDELLQMAKQLGYKLLPAFNTTSGLPYPRINLKFGIRKPEARTGTETDTCTACAGTLILEFAALSRFTGATIFEEYARKALDFLWEKRQRSSNLVGVTINIHTGDWVRKDSGVGAGIDSYYEYLLKAYVLLGDDSFLERFNTHYDAIMRYISQPPLLLDVHIHKPMLNARTWMDALLAFFPGLQVLKGDIRPAIETHEMLYQVIKKHNFLPEAFTTDFRVHWAQHPLRPEFAESTYFLYKATGDPYYLEVGKTLIENLNKYARVPCGFAAMKDVRTGSHEDRMDSFFLAEMFKYLYLLFADKEDIIFDIEDYIFTTEAHLLPLWLSTTNQSISKKNTTSEYTELDDSNFDWTCPNTQILFPNDPLYAQSIREPLKNVVDKSCPRGIIRVEESFRSGAKPPLRARDFMATNPEHLEILKKMGVSLIHLKDGRVQLVQHAIQAASSIDAEDGLRFMQEMIELSSQQQKEQQLPPRAVQIVSHPFFGRVVLTAGPAQFGLDLSKHKETRGFVASSKPSNGCSELTNPEAVMGKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEGSSSDTAPLFQMAGDGKDTDDIKIPMLFLFSKEGSIILDAIREYEEVEVLLSDKAKDRDPEMENEEQPSSENDSQNQSGEQISSSSQEVDLVDQESSEENSLNSHPESLSLADMDNAASISPSEQTSNPTENHETTNLNGECTDLDNQLQEQSETEEDSNPNVSWGKKVQPIDSILADWNEDIEAFEMMEKDEL
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
104PhosphorylationDDALGKFSLTLIDSL
HHHHHHHHEEHHHHC		24.7524114839
106PhosphorylationALGKFSLTLIDSLDT
HHHHHHEEHHHHCCE		22.0724114839
118N-linked_GlycosylationLDTLVVLNKTKEFED
CCEEEEECCCHHHHH		38.04UniProtKB CARBOHYD
146UbiquitinationDVVVSVFETNIRVLG
CEEEEEEECCCHHHH		38.50-
165UbiquitinationGHSLAIMLKEKGEYM
CCEEEEEHHHCCCHH		5.46-
189UbiquitinationMAKQLGYKLLPAFNT
HHHHHCCCHHHCCCC		41.57-
195N-linked_GlycosylationYKLLPAFNTTSGLPY
CCHHHCCCCCCCCCC		44.5519159218
208UbiquitinationPYPRINLKFGIRKPE
CCCEEEEEEEECCCC		36.74-
219UbiquitinationRKPEARTGTETDTCT
CCCCCCCCCCCCCCH		18.92-
262UbiquitinationALDFLWEKRQRSSNL
HHHHHHHHHHCCCCC		42.10-
266PhosphorylationLWEKRQRSSNLVGVT
HHHHHHCCCCCEEEE		18.4228348404
267PhosphorylationWEKRQRSSNLVGVTI
HHHHHCCCCCEEEEE		36.0528348404
273PhosphorylationSSNLVGVTINIHTGD
CCCCEEEEEEEECCC		11.4628348404
286PhosphorylationGDWVRKDSGVGAGID
CCEEECCCCCCCCCH		38.11-
295PhosphorylationVGAGIDSYYEYLLKA
CCCCCHHHHHHHHHH		9.14-
296PhosphorylationGAGIDSYYEYLLKAY
CCCCHHHHHHHHHHH		11.31-
303PhosphorylationYEYLLKAYVLLGDDS
HHHHHHHHHHHCCHH		7.0518785766
310PhosphorylationYVLLGDDSFLERFNT
HHHHCCHHHHHHHHH		36.1518785766
358UbiquitinationLLAFFPGLQVLKGDI
HHHHCCCCEEECCCC		3.0321890473
392UbiquitinationLPEAFTTDFRVHWAQ
CCCCCCCCCCEECCC		26.71-
392UbiquitinationLPEAFTTDFRVHWAQ
CCCCCCCCCCEECCC		26.7121890473
404UbiquitinationWAQHPLRPEFAESTY
CCCCCCCHHHHCCCE		49.06-
427UbiquitinationPYYLEVGKTLIENLN
CEEEEHHHHHHHHHH		45.38-
435UbiquitinationTLIENLNKYARVPCG
HHHHHHHHHCCCCCC		43.3721890473
435UbiquitinationTLIENLNKYARVPCG
HHHHHHHHHCCCCCC		43.3722817900
447UbiquitinationPCGFAAMKDVRTGSH
CCCEECCCCCCCCCC		48.63-
504N-linked_GlycosylationPLWLSTTNQSISKKN
HHHHHCCCCCCCCCC		33.42UniProtKB CARBOHYD
511N-linked_GlycosylationNQSISKKNTTSEYTE
CCCCCCCCCCCCCEE		52.94UniProtKB CARBOHYD
512UbiquitinationQSISKKNTTSEYTEL
CCCCCCCCCCCCEEC		40.35-
550UbiquitinationQSIREPLKNVVDKSC
HHHHHHHHHCCCCCC		59.4129967540
551UbiquitinationSIREPLKNVVDKSCP
HHHHHHHHCCCCCCC		46.88-
555UbiquitinationPLKNVVDKSCPRGII
HHHHCCCCCCCCCEE		42.2029967540
573UbiquitinationESFRSGAKPPLRARD
HHHHCCCCCCCCHHH		51.1729967540
594UbiquitinationEHLEILKKMGVSLIH
HHHHHHHHHCCEEEE		37.12-
662UbiquitinationHPFFGRVVLTAGPAQ
CCCCCEEEEEECCHH		3.66-
676UbiquitinationQFGLDLSKHKETRGF
HHCCCHHHCCCCCCE		67.03-
686PhosphorylationETRGFVASSKPSNGC
CCCCEECCCCCCCCC		33.3322210691
690PhosphorylationFVASSKPSNGCSELT
EECCCCCCCCCCCCC		49.9822210691
694PhosphorylationSKPSNGCSELTNPEA
CCCCCCCCCCCCHHH		36.7222210691
705UbiquitinationNPEAVMGKIALIQRG
CHHHHHHHHHHHHCC		13.50-
719UbiquitinationGQCMFAEKARNIQNA
CCCHHHHHHHCCCCC		49.5729967540
769PhosphorylationIPMLFLFSKEGSIIL
CCEEEEECCCCCCHH		31.7624719451
810N-linked_GlycosylationEEQPSSENDSQNQSG
CCCCCCCCCCCCCCC		57.07UniProtKB CARBOHYD
814N-linked_GlycosylationSSENDSQNQSGEQIS
CCCCCCCCCCCCCCC		41.77UniProtKB CARBOHYD
835PhosphorylationDLVDQESSEENSLNS
EECCCCCCHHHCCCC		48.4524275569
900N-linked_GlycosylationTEEDSNPNVSWGKKV
CCCCCCCCCCCCCCC		44.71UniProtKB CARBOHYD
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 EDEM3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EDEM3_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 EDEM3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SE1L1_HUMANSEL1Lphysical
24910992
HSPB1_HUMANHSPB1physical
28366632
STT3A_HUMANSTT3Aphysical
28366632
SAE1_HUMANSAE1physical
28366632
ECM29_HUMANKIAA0368physical
28366632
EDEM2_HUMANEDEM2physical
28366632
ERP29_HUMANERP29physical
28366632
MOGS_HUMANMOGSphysical
28366632
ERAP1_HUMANERAP1physical
28366632
ERLN2_HUMANERLIN2physical
28366632
HPBP1_HUMANHSPBP1physical
28366632
EMC1_HUMANEMC1physical
28366632
SEC13_HUMANSEC13physical
28366632
STT3B_HUMANSTT3Bphysical
28366632
ERP44_HUMANERP44physical
28366632
GLU2B_HUMANPRKCSHphysical
28366632
RPN1_HUMANRPN1physical
28366632
RPN2_HUMANRPN2physical
28366632
COPB2_HUMANCOPB2physical
28366632
COPB_HUMANCOPB1physical
28366632
OST48_HUMANDDOSTphysical
28366632
LMAN1_HUMANLMAN1physical
28366632
SAE2_HUMANUBA2physical
28366632
HS71L_HUMANHSPA1Lphysical
28366632
CDC37_HUMANCDC37physical
28366632
TRAP1_HUMANTRAP1physical
28366632
ERGI2_HUMANERGIC2physical
28366632
EMC2_HUMANEMC2physical
28366632
SSRA_HUMANSSR1physical
28366632
ERLEC_HUMANERLEC1physical
28366632
CH60_HUMANHSPD1physical
28366632
ERLN1_HUMANERLIN1physical
28366632
HS74L_HUMANHSPA4Lphysical
28366632
EMC3_HUMANEMC3physical
28366632
DJC10_HUMANDNAJC10physical
28366632
SE1L1_HUMANSEL1Lphysical
28366632
VCIP1_HUMANVCPIP1physical
28366632
TGON2_HUMANTGOLN2physical
28366632
MA2A1_HUMANMAN2A1physical
28366632
COPA_HUMANCOPAphysical
28366632
HS105_HUMANHSPH1physical
28366632
GANAB_HUMANGANABphysical
28366632
CALR_HUMANCALRphysical
28366632
UBA1_HUMANUBA1physical
28366632
CALX_HUMANCANXphysical
28366632
ENPL_HUMANHSP90B1physical
28366632
HSP7C_HUMANHSPA8physical
28366632
GRP78_HUMANHSPA5physical
28366632
HYOU1_HUMANHYOU1physical
28366632
NED4L_HUMANNEDD4Lphysical
28366632
PDIA3_HUMANPDIA3physical
28366632
PDIA4_HUMANPDIA4physical
28366632
PSMD5_HUMANPSMD5physical
28366632
PSMD1_HUMANPSMD1physical
28366632
SERPH_HUMANSERPINH1physical
28366632
SRPRA_HUMANSRPRphysical
28366632
OS9_HUMANOS9physical
28366632
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 EDEM3_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-195, AND MASSSPECTROMETRY.

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