ERN1_HUMAN - dbPTM
ERN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERN1_HUMAN
UniProt AC O75460
Protein Name Serine/threonine-protein kinase/endoribonuclease IRE1 {ECO:0000305}
Gene Name ERN1 {ECO:0000312|HGNC:HGNC:3449}
Organism Homo sapiens (Human).
Sequence Length 977
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type I membrane protein .
Protein Description Serine/threonine-protein kinase and endoribonuclease that acts as a key sensor for the endoplasmic reticulum unfolded protein response (UPR). [PubMed: 11779464]
Protein Sequence MPARRLLLLLTLLLPGLGIFGSTSTVTLPETLLFVSTLDGSLHAVSKRTGSIKWTLKEDPVLQVPTHVEEPAFLPDPNDGSLYTLGSKNNEGLTKLPFTIPELVQASPCRSSDGILYMGKKQDIWYVIDLLTGEKQQTLSSAFADSLCPSTSLLYLGRTEYTITMYDTKTRELRWNATYFDYAASLPEDDVDYKMSHFVSNGDGLVVTVDSESGDVLWIQNYASPVVAFYVWQREGLRKVMHINVAVETLRYLTFMSGEVGRITKWKYPFPKETEAKSKLTPTLYVGKYSTSLYASPSMVHEGVAVVPRGSTLPLLEGPQTDGVTIGDKGECVITPSTDVKFDPGLKSKNKLNYLRNYWLLIGHHETPLSASTKMLERFPNNLPKHRENVIPADSEKKSFEEVINLVDQTSENAPTTVSRDVEEKPAHAPARPEAPVDSMLKDMATIILSTFLLIGWVAFIITYPLSMHQQQQLQHQQFQKELEKIQLLQQQQQQLPFHPPGDTAQDGELLDTSGPYSESSGTSSPSTSPRASNHSLCSGSSASKAGSSPSLEQDDGDEETSVVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFADREVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHLGLEPITLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMISDFGLCKKLAVGRHSFSRRSGVPGTEGWIAPEMLSEDCKENPTYTVDIFSAGCVFYYVISEGSHPFGKSLQRQANILLGACSLDCLHPEKHEDVIARELIEKMIAMDPQKRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKESLDGPIVKQLERGGRAVVKMDWRENITVPLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPAEVRETLGSLPDDFVCYFTSRFPHLLAHTYRAMELCSHERLFQPYYFHEPPEPQPPVTPDAL
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
32 (in isoform 2)O-linked_Glycosylation-3.13OGP
36PhosphorylationPETLLFVSTLDGSLH
CCEEEEEEECCCCEE		18.8726657352
49PhosphorylationLHAVSKRTGSIKWTL
EEEECCCCCCEEEEE		38.73-
88UbiquitinationSLYTLGSKNNEGLTK
CEEECCCCCCCCCCC		63.0929967540
95UbiquitinationKNNEGLTKLPFTIPE
CCCCCCCCCCCCHHH		60.24-
132PhosphorylationWYVIDLLTGEKQQTL
EEEEECCCCCCHHHH		51.06-
161PhosphorylationLYLGRTEYTITMYDT
EEEECCEEEEEEEEC		11.66-
166PhosphorylationTEYTITMYDTKTREL
CEEEEEEEECCCCEE		16.29-
176N-linked_GlycosylationKTRELRWNATYFDYA
CCCEEEEEEEECCHH		18.90UniProtKB CARBOHYD
179PhosphorylationELRWNATYFDYAASL
EEEEEEEECCHHHCC		7.64-
283PhosphorylationAKSKLTPTLYVGKYS
CCCCCCCEEEEEECC		26.03-
289PhosphorylationPTLYVGKYSTSLYAS
CEEEEEECCCEEEEC		15.97-
311PhosphorylationVAVVPRGSTLPLLEG
EEEECCCCCCCCCCC		28.2226074081
312PhosphorylationAVVPRGSTLPLLEGP
EEECCCCCCCCCCCC		34.9126074081
321PhosphorylationPLLEGPQTDGVTIGD
CCCCCCCCCCEEECC		37.5426074081
325PhosphorylationGPQTDGVTIGDKGEC
CCCCCCEEECCCCCE		25.4426074081
347UbiquitinationVKFDPGLKSKNKLNY
CCCCCCCCCHHHHHH		66.36-
349UbiquitinationFDPGLKSKNKLNYLR
CCCCCCCHHHHHHHH		57.42-
374AcetylationTPLSASTKMLERFPN
CCCCCCHHHHHHCCC		38.717960371
374UbiquitinationTPLSASTKMLERFPN
CCCCCCHHHHHHCCC		38.71-
417PhosphorylationTSENAPTTVSRDVEE
CCCCCCCCCCCCCCC		18.5422468782
419PhosphorylationENAPTTVSRDVEEKP
CCCCCCCCCCCCCCC		22.2222468782
485UbiquitinationQFQKELEKIQLLQQQ
HHHHHHHHHHHHHHH		48.6729967540
525PhosphorylationSESSGTSSPSTSPRA
CCCCCCCCCCCCCCC		23.7824275569
533PhosphorylationPSTSPRASNHSLCSG
CCCCCCCCCCCCCCC		36.0327251275
536PhosphorylationSPRASNHSLCSGSSA
CCCCCCCCCCCCCCC		35.0129449344
539PhosphorylationASNHSLCSGSSASKA
CCCCCCCCCCCCCCC		47.1823612710
541PhosphorylationNHSLCSGSSASKAGS
CCCCCCCCCCCCCCC		13.3627251275
542PhosphorylationHSLCSGSSASKAGSS
CCCCCCCCCCCCCCC		39.8427251275
544PhosphorylationLCSGSSASKAGSSPS
CCCCCCCCCCCCCCC		25.6127251275
548PhosphorylationSSASKAGSSPSLEQD
CCCCCCCCCCCCCCC		43.8926471730
549PhosphorylationSASKAGSSPSLEQDD
CCCCCCCCCCCCCCC		20.0026471730
551PhosphorylationSKAGSSPSLEQDDGD
CCCCCCCCCCCCCCC		46.6226471730
561PhosphorylationQDDGDEETSVVIVGK
CCCCCCCEEEEEEEE		25.4423612710
562PhosphorylationDDGDEETSVVIVGKI
CCCCCCEEEEEEEEE		20.0523612710
584PhosphorylationLGHGAEGTIVYRGMF
CCCCCCCEEEEECCC		9.9726074081
587PhosphorylationGAEGTIVYRGMFDNR
CCCCEEEEECCCCCH		9.5226074081
628PhosphorylationEHPNVIRYFCTEKDR
CCCCCEEEEECCCHH		7.59-
633UbiquitinationIRYFCTEKDRQFQYI
EEEEECCCHHHHHHH		39.80-
706UbiquitinationPNAHGKIKAMISDFG
CCCCHHHHHHHCCCC		35.07-
724PhosphorylationKLAVGRHSFSRRSGV
HHHCCCCCCCCCCCC		24.4522169477
726PhosphorylationAVGRHSFSRRSGVPG
HCCCCCCCCCCCCCC		29.7827251275
729PhosphorylationRHSFSRRSGVPGTEG
CCCCCCCCCCCCCCC		42.9327251275
851UbiquitinationDVSDRIEKESLDGPI
HHHHHHHHHHCCCHH		50.6729967540
860UbiquitinationSLDGPIVKQLERGGR
HCCCHHHHHHHHCCE		50.3029967540
879PhosphorylationMDWRENITVPLQTDL
ECHHHCEEEEECCCH		27.8728509920
884PhosphorylationNITVPLQTDLRKFRT
CEEEEECCCHHHCCC		44.6928509920
973PhosphorylationPEPQPPVTPDAL---
CCCCCCCCCCCC---		22.6411175748
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
628YPhosphorylationKinaseERN1O75460
GPS
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:25225294
-KUbiquitinationE3 ubiquitin ligaseSYVN1Q86TM6
PMID:18369366
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERN1_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 ERN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERN1_HUMANERN1physical
12637535
M3K5_HUMANMAP3K5physical
12050113
HS90A_HUMANHSP90AA1physical
12446770
TAOK3_HUMANTAOK3physical
11278723
PSN1_HUMANPSEN1physical
10587643
CSN5_HUMANCOPS5physical
17951406
UBP14_HUMANUSP14physical
19135427
SE1L1_HUMANSEL1Lphysical
19135427
SYVN1_HUMANSYVN1physical
19135427
CSN5_HUMANCOPS5physical
15234121
TRAF6_HUMANTRAF6physical
23942232
RNF13_HUMANRNF13physical
23378536
CHIP_HUMANSTUB1physical
25225294
OTUB1_HUMANOTUB1physical
25225294
UCHL1_HUMANUCHL1physical
25225294
FXL21_HUMANFBXL21physical
25225294
FBX11_HUMANFBXO11physical
25225294
TRAF2_HUMANTRAF2physical
25225294
TRAF2_HUMANTRAF2physical
25797626
M3K5_HUMANMAP3K5physical
25797626
SYVN1_HUMANSYVN1physical
26254280
RIPK1_HUMANRIPK1physical
25476903
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 ERN1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533; SER-548; SER-551;SER-726 AND THR-973, AND MASS SPECTROMETRY.

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