EGLN1_HUMAN - dbPTM
EGLN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EGLN1_HUMAN
UniProt AC Q9GZT9
Protein Name Egl nine homolog 1
Gene Name EGLN1 {ECO:0000312|HGNC:HGNC:1232}
Organism Homo sapiens (Human).
Sequence Length 426
Subcellular Localization Cytoplasm . Nucleus . Mainly cytoplasmic. Shuttles between the nucleus and cytoplasm (PubMed:19631610). 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 MANDSGGPGGPSPSERDRQYCELCGKMENLLRCSRCRSSFYCCKEHQRQDWKKHKLVCQGSEGALGHGVGPHQHSGPAPPAAVPPPRAGAREPRKAAARRDNASGDAAKGKVKAKPPADPAAAASPCRAAAGGQGSAVAAEAEPGKEEPPARSSLFQEKANLYPPSNTPGDALSPGGGLRPNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELNKPSDSVGKDVF
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
2Acetylation------MANDSGGPG
------CCCCCCCCC		28.6522814378
5Phosphorylation---MANDSGGPGGPS
---CCCCCCCCCCCC		45.5229255136
12PhosphorylationSGGPGGPSPSERDRQ
CCCCCCCCHHHHHHH		44.3129255136
14PhosphorylationGPGGPSPSERDRQYC
CCCCCCHHHHHHHHH		49.9929255136
20PhosphorylationPSERDRQYCELCGKM
HHHHHHHHHHHHHHH		6.7029496907
38PhosphorylationLRCSRCRSSFYCCKE
HHHCCCHHCEEECHH		28.5528555341
39PhosphorylationRCSRCRSSFYCCKEH
HHCCCHHCEEECHHH		10.8228857561
61PhosphorylationHKLVCQGSEGALGHG
CCEEECCCCCCCCCC		13.6427080861
125PhosphorylationADPAAAASPCRAAAG
CCHHHHHCCCHHHCC		21.5829255136
136PhosphorylationAAAGGQGSAVAAEAE
HHCCCCCCCEEEECC		16.2221601212
146AcetylationAAEAEPGKEEPPARS
EEECCCCCCCCCCCH		70.4026051181
153PhosphorylationKEEPPARSSLFQEKA
CCCCCCCHHHHHHHH		33.2428555341
154PhosphorylationEEPPARSSLFQEKAN
CCCCCCHHHHHHHHC		27.8728555341
166PhosphorylationKANLYPPSNTPGDAL
HHCCCCCCCCCCCCC		49.1629978859
168PhosphorylationNLYPPSNTPGDALSP
CCCCCCCCCCCCCCC		32.7429978859
174PhosphorylationNTPGDALSPGGGLRP
CCCCCCCCCCCCCCC		24.1829978859
185PhosphorylationGLRPNGQTKPLPALK
CCCCCCCCCCCHHHH		35.7129978859
201S-nitrosylationALEYIVPCMNKHGIC
HHHHHHHHCHHCCEE		3.0421601578
201S-nitrosocysteineALEYIVPCMNKHGIC
HHHHHHHHCHHCCEE		3.04-
208GlutathionylationCMNKHGICVVDDFLG
HCHHCCEEEEECCCC		2.6322555962
208S-nitrosylationCMNKHGICVVDDFLG
HCHHCCEEEEECCCC		2.6321601578
208S-nitrosocysteineCMNKHGICVVDDFLG
HCHHCCEEEEECCCC		2.63-
216UbiquitinationVVDDFLGKETGQQIG
EEECCCCCCHHCCHH		55.00-
232PhosphorylationEVRALHDTGKFTDGQ
HHHHHHHCCCCCCCC		31.3721601212
234 (in isoform 1)Ubiquitination-47.3821890473
234 (in isoform 2)Ubiquitination-47.3821890473
234UbiquitinationRALHDTGKFTDGQLV
HHHHHCCCCCCCCEE		47.3821890473
236PhosphorylationLHDTGKFTDGQLVSQ
HHHCCCCCCCCEEEC		42.5821601212
244MethylationDGQLVSQKSDSSKDI
CCCEEECCCCCCCCC		49.04-
244UbiquitinationDGQLVSQKSDSSKDI
CCCEEECCCCCCCCC		49.04-
248PhosphorylationVSQKSDSSKDIRGDK
EECCCCCCCCCCCCE		39.0621601212
255UbiquitinationSKDIRGDKITWIEGK
CCCCCCCEEEEEECC		44.88-
274PhosphorylationETIGLLMSSMDDLIR
HHHHHHHHCHHHHHH		23.6028122231
275PhosphorylationTIGLLMSSMDDLIRH
HHHHHHHCHHHHHHH		16.5628122231
286UbiquitinationLIRHCNGKLGSYKIN
HHHHCCCCCEEEEEC		35.37-
296PhosphorylationSYKINGRTKAMVACY
EEEECCCEEEEEEEE		25.2622210691
302S-nitrosocysteineRTKAMVACYPGNGTG
CEEEEEEEECCCCCE		2.61-
302S-nitrosylationRTKAMVACYPGNGTG
CEEEEEEEECCCCCE		2.6121601578
308PhosphorylationACYPGNGTGYVRHVD
EEECCCCCEEEEECC		29.37-
323S-nitrosocysteineNPNGDGRCVTCIYYL
CCCCCCEEEEEEEEE		3.48-
323S-nitrosylationNPNGDGRCVTCIYYL
CCCCCCEEEEEEEEE		3.4821601578
325PhosphorylationNGDGRCVTCIYYLNK
CCCCEEEEEEEEECC		9.2326503514
326S-nitrosylationGDGRCVTCIYYLNKD
CCCEEEEEEEEECCC		0.6621601578
326S-nitrosocysteineGDGRCVTCIYYLNKD
CCCEEEEEEEEECCC		0.66-
328PhosphorylationGRCVTCIYYLNKDWD
CEEEEEEEEECCCCC		12.2126503514
329PhosphorylationRCVTCIYYLNKDWDA
EEEEEEEEECCCCCC		5.4927642862
337UbiquitinationLNKDWDAKVSGGILR
ECCCCCCCCCCCEEE		34.17-
350UbiquitinationLRIFPEGKAQFADIE
EEECCCCCCEECCCC		37.03-
402UbiquitinationERARAKVKYLTGEKG
HHHHHHHHHHHCCCC		33.56-
403PhosphorylationRARAKVKYLTGEKGV
HHHHHHHHHHCCCCE		16.6922468782
405PhosphorylationRAKVKYLTGEKGVRV
HHHHHHHHCCCCEEE		39.96-
408UbiquitinationVKYLTGEKGVRVELN
HHHHHCCCCEEEEEC		65.14-
408AcetylationVKYLTGEKGVRVELN
HHHHHCCCCEEEEEC		65.1423749302
416UbiquitinationGVRVELNKPSDSVGK
CEEEEECCCCCCCCC		59.53-
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
125SPhosphorylationKinaseP70S6KP23443
PSP
-KUbiquitinationE3 ubiquitin ligaseSIAH1Q8IUQ4
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseSIAH2O43255
PMID:19546213
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EGLN1_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 EGLN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ING4_HUMANING4physical
15897452
ING4_HUMANING4physical
17848618
H31_HUMANHIST1H3Aphysical
19624289
SIAH2_HUMANSIAH2physical
16958618
EGLN1_HUMANEGLN1physical
16958618
SPY2_HUMANSPRY2physical
22006925
SRC_HUMANSRCphysical
21335603
HIF1A_HUMANHIF1Aphysical
19604478
EPAS1_HUMANEPAS1physical
19208626
FKBP8_HUMANFKBP8physical
19546213
LIMD1_HUMANLIMD1physical
22286099
SIAH2_HUMANSIAH2physical
15210114
EPAS1_HUMANEPAS1physical
19147576
FKBP8_HUMANFKBP8physical
19147576
MAGAB_HUMANMAGEA11physical
19147576
MAGA9_HUMANMAGEA9physical
19147576
RASK_HUMANKRASphysical
21988832
ZN281_HUMANZNF281physical
21988832
PLD1_HUMANPLD1physical
25361009
HIF1A_HUMANHIF1Aphysical
25361009
PLD2_HUMANPLD2physical
26611735
HIF1A_HUMANHIF1Aphysical
26611735
PHLD_HUMANGPLD1physical
26680696
RHBT3_HUMANRHOBTB3physical
26215701
VHL_HUMANVHLphysical
26215701
FKBP8_HUMANFKBP8physical
17353276
FKBP8_HUMANFKBP8physical
23413029
TEBP_HUMANPTGES3physical
23413029
FKBP4_HUMANFKBP4physical
23413029
HS90A_HUMANHSP90AA1physical
23413029
HS90B_HUMANHSP90AB1physical
23413029
TEBP_HUMANPTGES3physical
24711448
HS90A_HUMANHSP90AA1physical
24711448
HS90B_HUMANHSP90AB1physical
24711448
AKT1_HUMANAKT1physical
27563096
AKT2_HUMANAKT2physical
27563096
HIF1A_HUMANHIF1Aphysical
27563096
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609820Erythrocytosis, familial, 3 (ECYT3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00126Vitamin C
Regulatory Network of EGLN1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
S-nitrosylation
ReferencePubMed
"Studies on the reaction of nitric oxide with the hypoxia-induciblefactor prolyl hydroxylase domain 2 (EGLN1).";
Chowdhury R., Flashman E., Mecinovic J., Kramer H.B., Kessler B.M.,Frapart Y.M., Boucher J.L., Clifton I.J., McDonough M.A.,Schofield C.J.;
J. Mol. Biol. 410:268-279(2011).
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 181-426 IN COMPLEX WITHNITRIC OXIDE OR A NITRIC OXIDE TRANSFER REAGENT, MASS SPECTROMETRY,S-NITROSYLATION AT CYS-201; CYS-208; CYS-302; CYS-323 AND CYS-326, ANDMUTAGENESIS OF CYS-201; CYS-208; CYS-266; CYS-283; CYS-302; CYS-323AND CYS-326.

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