EDEM1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EDEM1_HUMAN
• UniProt AC: Q92611
• Protein Name: ER degradation-enhancing alpha-mannosidase-like protein 1
• Gene Name: EDEM1
• Organism: Homo sapiens (Human).
• Sequence Length: 657
• Subcellular Localization: Endoplasmic reticulum membrane ; Single-pass type II membrane protein .
• Protein Description: Extracts misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle. It is directly involved in endoplasmic reticulum-associated degradation (ERAD) and targets misfolded glycoproteins for degradation in an N-glycan-independent manner, probably by forming a complex with SEL1L. It has low mannosidase activity, catalyzing mannose trimming from Man8GlcNAc2 to Man7GlcNAc2..
• Protein Sequence: MQWRALVLGLVLLRLGLHGVLWLVFGLGPSMGFYQRFPLSFGFQRLRSPDGPASPTSGPVGRPGGVSGPSWLQPPGTGAAQSPRKAPRRPGPGMCGPANWGYVLGGRGRGPDEYEKRYSGAFPPQLRAQMRDLARGMFVFGYDNYMAHAFPQDELNPIHCRGRGPDRGDPSNLNINDVLGNYSLTLVDALDTLAIMGNSSEFQKAVKLVINTVSFDKDSTVQVFEATIRVLGSLLSAHRIITDSKQPFGDMTIKDYDNELLYMAHDLAVRLLPAFENTKTGIPYPRVNLKTGVPPDTNNETCTAGAGSLLVEFGILSRLLGDSTFEWVARRAVKALWNLRSNDTGLLGNVVNIQTGHWVGKQSGLGAGLDSFYEYLLKSYILFGEKEDLEMFNAAYQSIQNYLRRGREACNEGEGDPPLYVNVNMFSGQLMNTWIDSLQAFFPGLQVLIGDVEDAICLHAFYYAIWKRYGALPERYNWQLQAPDVLFYPLRPELVESTYLLYQATKNPFYLHVGMDILQSLEKYTKVKCGYATLHHVIDKSTEDRMESFFLSETCKYLYLLFDEDNPVHKSGTRYMFTTEGHIVSVDEHLRELPWKEFFSEEGGQDQGGKSVHRPKPHELKVINSSSNCNRVPDERRYSLPLKSIYMRQIDQMVGLI

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
84	Ubiquitination	TGAAQSPRKAPRRPG CCCCCCCCCCCCCCC	53.68	-
116	Ubiquitination	RGPDEYEKRYSGAFP CCHHHHHHHHCCCCC	56.59	-
139	Ubiquitination	DLARGMFVFGYDNYM HHHHCCEEECCCCCC	2.43	-
181	N-linked_Glycosylation	NINDVLGNYSLTLVD CHHHHCCCCCEEHHH	21.04	UniProtKB CARBOHYD
198	N-linked_Glycosylation	DTLAIMGNSSEFQKA HHHHHCCCCHHHHHH	25.61	UniProtKB CARBOHYD
279	Ubiquitination	LPAFENTKTGIPYPR HHHHCCCCCCCCCCC	57.23	-
299	N-linked_Glycosylation	GVPPDTNNETCTAGA CCCCCCCCCCCCCCH	48.31	UniProtKB CARBOHYD
333	Ubiquitination	EWVARRAVKALWNLR HHHHHHHHHHHHHCC	3.37	-
334	Ubiquitination	WVARRAVKALWNLRS HHHHHHHHHHHHCCC	36.46	-
342	N-linked_Glycosylation	ALWNLRSNDTGLLGN HHHHCCCCCCCCCCC	44.42	UniProtKB CARBOHYD
520	Phosphorylation	VGMDILQSLEKYTKV CCHHHHHHHHHHHCC	34.74	23312004
528	Ubiquitination	LEKYTKVKCGYATLH HHHHHCCCCCEEEHH	24.41	-
570	Ubiquitination	DEDNPVHKSGTRYMF CCCCCCCCCCCEEEE	51.30	-
575	Phosphorylation	VHKSGTRYMFTTEGH CCCCCCEEEEEECCE	9.09	-
596	Ubiquitination	HLRELPWKEFFSEEG HHHHCCHHHHCCCCC	42.58	-
621	Ubiquitination	RPKPHELKVINSSSN CCCCCCCEEEECCCC	37.78	-
624	N-linked_Glycosylation	PHELKVINSSSNCNR CCCCEEEECCCCCCC	38.53	UniProtKB CARBOHYD
638	Phosphorylation	RVPDERRYSLPLKSI CCCCCHHCCCCHHHH	22.30	28270605
639	Phosphorylation	VPDERRYSLPLKSIY CCCCHHCCCCHHHHH	23.00	28270605
643	Ubiquitination	RRYSLPLKSIYMRQI HHCCCCHHHHHHHHH	32.63	-
644	Phosphorylation	RYSLPLKSIYMRQID HCCCCHHHHHHHHHH	27.00	28270605
646	Phosphorylation	SLPLKSIYMRQIDQM CCCHHHHHHHHHHHH	8.04	28270605

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of EDEM1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EDEM1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of EDEM1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SE1L1_HUMAN	SEL1L	physical	19524542
OPSD_HUMAN	RHO	physical	19934218
SE1L1_HUMAN	SEL1L	physical	21632540
DJC10_HUMAN	DNAJC10	physical	21632540
CALX_HUMAN	CANX	physical	21632540
SC61B_HUMAN	SEC61B	physical	17360537
DERL1_HUMAN	DERL1	physical	17360537
DERL2_HUMAN	DERL2	physical	17360537
CALX_HUMAN	CANX	physical	17360537
ASGR1_HUMAN	ASGR1	physical	23233672
SQSTM_HUMAN	SQSTM1	physical	24664425
1B07_HUMAN	HLA-B	physical	25132672
1B18_HUMAN	HLA-B	physical	25132672
UBQL2_HUMAN	UBQLN2	physical	22119785
CALX_HUMAN	CANX	physical	22119785
ESYT1_HUMAN	ESYT1	physical	22119785
MTCH1_HUMAN	MTCH1	physical	22119785
RICI_RICCO	RCOM_2159910	physical	24200403
PDIA1_HUMAN	P4HB	physical	26496610
PNISR_HUMAN	PNISR	physical	26496610
SUFU_HUMAN	SUFU	physical	26496610
CHD9_HUMAN	CHD9	physical	26496610
PHF6_HUMAN	PHF6	physical	26496610
SE1L1_HUMAN	SEL1L	physical	24910992
CALX_HUMAN	CANX	physical	24910992

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.