EDEM2_HUMAN - dbPTM
EDEM2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EDEM2_HUMAN
UniProt AC Q9BV94
Protein Name ER degradation-enhancing alpha-mannosidase-like protein 2
Gene Name EDEM2
Organism Homo sapiens (Human).
Sequence Length 578
Subcellular Localization Endoplasmic reticulum lumen .
Protein Description Initiates the endoplasmic reticulum-associated degradation (ERAD) that targets misfolded glycoproteins for degradation in an N-glycan-dependent manner. Catalyzes the first mannose trimming step, from Man9GlcNAc2 to Man8GlcNAc2. [PubMed: 25092655 Extracts misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle.]
Protein Sequence MPFRLLIPLGLLCALLPQHHGAPGPDGSAPDPAHYRERVKAMFYHAYDSYLENAFPFDELRPLTCDGHDTWGSFSLTLIDALDTLLILGNVSEFQRVVEVLQDSVDFDIDVNASVFETNIRVVGGLLSAHLLSKKAGVEVEAGWPCSGPLLRMAEEAARKLLPAFQTPTGMPYGTVNLLHGVNPGETPVTCTAGIGTFIVEFATLSSLTGDPVFEDVARVALMRLWESRSDIGLVGNHIDVLTGKWVAQDAGIGAGVDSYFEYLVKGAILLQDKKLMAMFLEYNKAIRNYTRFDDWYLWVQMYKGTVSMPVFQSLEAYWPGLQSLIGDIDNAMRTFLNYYTVWKQFGGLPEFYNIPQGYTVEKREGYPLRPELIESAMYLYRATGDPTLLELGRDAVESIEKISKVECGFATIKDLRDHKLDNRMESFFLAETVKYLYLLFDPTNFIHNNGSTFDAVITPYGECILGAGGYIFNTEAHPIDPAALHCCQRLKEEQWEVEDLMREFYSLKRSRSKFQKNTVSSGPWEPPARPGTLFSPENHDQARERKPAKQKVPLLSCPSQPFTSKLALLGQVFLDSS
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
90N-linked_GlycosylationDTLLILGNVSEFQRV
HHHHHCCCHHHHHHH
30.60UniProtKB CARBOHYD
98UbiquitinationVSEFQRVVEVLQDSV
HHHHHHHHHHHHHCC
4.6029967540
112N-linked_GlycosylationVDFDIDVNASVFETN
CCEECCCCCCHHCCC
23.81UniProtKB CARBOHYD
135UbiquitinationSAHLLSKKAGVEVEA
HHHHHHCCCCCEEEC
47.1729967540
275UbiquitinationAILLQDKKLMAMFLE
HHHHCCHHHHHHHHH
52.35-
283PhosphorylationLMAMFLEYNKAIRNY
HHHHHHHHHHHHHHC
24.9027134283
289N-linked_GlycosylationEYNKAIRNYTRFDDW
HHHHHHHHCCCCCCE
36.09UniProtKB CARBOHYD
291PhosphorylationNKAIRNYTRFDDWYL
HHHHHHCCCCCCEEE
28.5422210691
365 (in isoform 2)Ubiquitination-74.3121906983
365UbiquitinationGYTVEKREGYPLRPE
CCEEEECCCCCCCHH
74.3122817900
368UbiquitinationVEKREGYPLRPELIE
EEECCCCCCCHHHHH
32.5222817900
377UbiquitinationRPELIESAMYLYRAT
CHHHHHHHHHHHHHH
4.2829967540
384PhosphorylationAMYLYRATGDPTLLE
HHHHHHHHCCCHHHH
32.8725690035
388PhosphorylationYRATGDPTLLELGRD
HHHHCCCHHHHHCHH
49.0325690035
402 (in isoform 1)Ubiquitination-51.0821906983
402UbiquitinationDAVESIEKISKVECG
HHHHHHHHHHCCCCC
51.0821906983
405UbiquitinationESIEKISKVECGFAT
HHHHHHHCCCCCEEE
45.5922817900
412PhosphorylationKVECGFATIKDLRDH
CCCCCEEEHHHHHHC
26.7128060719
414UbiquitinationECGFATIKDLRDHKL
CCCEEEHHHHHHCCC
46.4829967540
450N-linked_GlycosylationPTNFIHNNGSTFDAV
CCCCCCCCCCCCCEE
31.46UniProtKB CARBOHYD
455UbiquitinationHNNGSTFDAVITPYG
CCCCCCCCEEEECCC
39.7622817900
455 (in isoform 2)Ubiquitination-39.7621906983
480UbiquitinationFNTEAHPIDPAALHC
ECCCCCCCCHHHHHH
7.7129967540
492UbiquitinationLHCCQRLKEEQWEVE
HHHHHHHHHHCCCHH
62.4922817900
492 (in isoform 1)Ubiquitination-62.4921906983
507PhosphorylationDLMREFYSLKRSRSK
HHHHHHHHHHHHHHH
32.5124719451
517UbiquitinationRSRSKFQKNTVSSGP
HHHHHHCCCCCCCCC
58.6929967540

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 EDEM2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EDEM2_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 EDEM2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RICI_RICCORCOM_2159910physical
24200403
SE1L1_HUMANSEL1Lphysical
24910992
CALX_HUMANCANXphysical
24910992
UHMK1_HUMANUHMK1physical
28514442
HACD1_HUMANPTPLAphysical
28514442
CC033_HUMANC3orf33physical
28514442
TXD11_HUMANTXNDC11physical
28514442
B3GN2_HUMANB3GNT2physical
28514442
S35B2_HUMANSLC35B2physical
28514442
MCU_HUMANMCUphysical
28514442
MOT10_HUMANSLC16A10physical
28514442
OS9_HUMANOS9physical
28514442
SURF1_HUMANSURF1physical
28514442
BLK_HUMANBLKphysical
28514442
TIM29_HUMANC19orf52physical
28514442
GDC_HUMANSLC25A16physical
28514442
S38AA_HUMANSLC38A10physical
28514442
TMTC4_HUMANTMTC4physical
28514442
TV23C_HUMANTVP23Cphysical
28514442
MCL1_HUMANMCL1physical
28514442
SFXN3_HUMANSFXN3physical
28514442
OMA1_HUMANOMA1physical
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 EDEM2_HUMAN

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Related Literatures of Post-Translational Modification

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