EGLN1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EGLN1_MOUSE
• UniProt AC: Q91YE3
• Protein Name: Egl nine homolog 1
• Gene Name: Egln1
• Organism: Mus musculus (Mouse).
• Sequence Length: 400
• Subcellular Localization: Cytoplasm . Nucleus . Mainly cytoplasmic. Shuttles between the nucleus and cytoplasm. Nuclear export requires functional XPO1.
• Protein Description: Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif..
• Protein Sequence: MASDSGGPGVLSASERDRQYCELCGKMENLLRCGRCRSSFYCCKEHQRQDWKKHKLVCQGGEAPRAQPAPAQPRVAPPPGGAPGAARAGGAARRGDSAAASRVPGPEDAAQARSGPGPAEPGSEDPPLSRSPGPERASLCPAGGGPGEALSPGGGLRPNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGRETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDQITWIEGKEPGCETIGLLMSSMDDLIRHCSGKLGNYRINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELKPNSVSKDV

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
2	Acetylation	------MASDSGGPG ------CCCCCCCCC	23.26	-
3	Phosphorylation	-----MASDSGGPGV -----CCCCCCCCCC	30.89	25338131
12	Phosphorylation	SGGPGVLSASERDRQ CCCCCCCCHHHHHHH	27.61	-
58	S-nitrosylation	WKKHKLVCQGGEAPR HHHCCEEECCCCCCC	4.51	21278135
58	S-nitrosocysteine	WKKHKLVCQGGEAPR HHHCCEEECCCCCCC	4.51	-
97	Phosphorylation	GAARRGDSAAASRVP CCCCCCCCCHHHCCC	23.72	29514104
114	Phosphorylation	EDAAQARSGPGPAEP HHHHHHHCCCCCCCC	52.97	23527152
123	Phosphorylation	PGPAEPGSEDPPLSR CCCCCCCCCCCCCCC	49.93	25266776
129	Phosphorylation	GSEDPPLSRSPGPER CCCCCCCCCCCCCCC	36.16	27149854
131	Phosphorylation	EDPPLSRSPGPERAS CCCCCCCCCCCCCCC	30.72	23527152
178	S-nitrosylation	ALEYIVPCMNKHGIC HHHHHHHHCHHCCEE	3.04	-
178	S-nitrosocysteine	ALEYIVPCMNKHGIC HHHHHHHHCHHCCEE	3.04	-
185	S-nitrosocysteine	CMNKHGICVVDDFLG HCHHCCEEEEECCCC	2.63	-
185	S-nitrosylation	CMNKHGICVVDDFLG HCHHCCEEEEECCCC	2.63	-
234	Phosphorylation	DIRGDQITWIEGKEP CCCCCCEEEEECCCC	18.11	26824392
279	S-nitrosocysteine	RTKAMVACYPGNGTG CEEEEEEEECCCCCE	2.61	-
279	S-nitrosylation	RTKAMVACYPGNGTG CEEEEEEEECCCCCE	2.61	-
300	S-nitrosocysteine	NPNGDGRCVTCIYYL CCCCCCEEEEEEEEE	3.48	-
300	S-nitrosylation	NPNGDGRCVTCIYYL CCCCCCEEEEEEEEE	3.48	-
303	S-nitrosocysteine	GDGRCVTCIYYLNKD CCCEEEEEEEEECCC	0.66	-
303	S-nitrosylation	GDGRCVTCIYYLNKD CCCEEEEEEEEECCC	0.66	-
385	Acetylation	VKYLTGEKGVRVELK HEEHHCCCCEEEEEC	65.14	23806337

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
-	K	Ubiquitination	E3 ubiquitin ligase	Siah1a	P61092	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	Siah2	Q06986	PMID:22199232

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EGLN1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of EGLN1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of EGLN1_MOUSE !!

Drug and Disease Associations

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