HYOU1_MOUSE - dbPTM
HYOU1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HYOU1_MOUSE
UniProt AC Q9JKR6
Protein Name Hypoxia up-regulated protein 1
Gene Name Hyou1
Organism Mus musculus (Mouse).
Sequence Length 999
Subcellular Localization Endoplasmic reticulum lumen .
Protein Description Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding (By similarity)..
Protein Sequence MAATVRRQRPRRLLCWALVAVLLADLLALSDTLAVMSVDLGSESMKVAIVKPGVPMEIVLNKESRRKTPVTVTLKENERFLGDSAAGMAIKNPKATLRYFQHLLGKQADNPHVALYRSRFPEHELIVDPQRQTVRFQISPQLQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPAFFNQAERRAVLQAARMAGLKVLQLINDNTATALSYGVFRRKDINSTAQNVMFYDMGSGSTVCTIVTYQTVKTKEAGMQPQLQIRGVGFDRTLGGLEMELRLREHLAKLFNEQRKGQKAKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLMDDVDFKAKVTRVEFEELCADLFDRVPGPVQQALQSAEMSLDQIEQVILVGGATRVPKVQEVLLKAVGKEELGKNINADEAAAMGAVYQAAALSKAFKVKPFVVRDAVIYPILVEFTREVEEEPGLRSLKHNKRVLFSRMGPYPQRKVITFNRYSHDFNFHINYGDLGFLGPEDLRVFGSQNLTTVKLKGVGESFKKYPDYESKGIKAHFNLDESGVLSLDRVESVFETLVEDSPEEESTLTKLGNTISSLFGGGTSSDAKENGTDAVQEEEESPAEGSKDEPAEQGELKEEAEPPAEETSQPPPSEPKGDAAREGEKPDEKESGDKPEAQKPNEKGQAGPEGAAPAPEEDKKPKPARKQKMVEEIGVELAVLDLPDLPEDELARSVQKLEELTLRDLEKQEREKAANSLEAFIFETQDKLYQPEYQEVSTEEQREEISGKLSATSTWLEDEGFGATTVMLKDKLAELRKLCQGLFFRVEERRKWPERLSALDNLLNHSSIFLKGARLIPEMDQVFTEVEMTTLEKVINDTWAWKNATLAEQAKLPATEKPVLLSKDIEAKMMALDREVQYLLNKAKFTKPRPRPKDKNGTRAEPPLNASAGDQEEKVIPPAGQTEEAKPILEPDKEETGTEPADSEPLELGGPGAGPEQEEQSAGQKRPSKNDEL
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
4Phosphorylation----MAATVRRQRPR
----CCCCHHHHCHH		22.93-
73PhosphorylationRKTPVTVTLKENERF
CCCCEEEEECCCCEE		23.81-
75AcetylationTPVTVTLKENERFLG
CCEEEEECCCCEECC		49.4823954790
75SuccinylationTPVTVTLKENERFLG
CCEEEEECCCCEECC		49.4823954790
84PhosphorylationNERFLGDSAAGMAIK
CCEECCCCCCCHHCC		20.4422817900
91AcetylationSAAGMAIKNPKATLR
CCCCHHCCCHHHHHH		58.6322826441
106AcetylationYFQHLLGKQADNPHV
HHHHHHCCCCCCCCE		42.1322826441
155N-linked_GlycosylationEVLGMVLNYSRSLAE
HHHHHHHHHCHHHHH		22.71-
170SuccinylationDFAEQPIKDAVITVP
HHHHCCCCCCEEEHH		46.4423954790
222N-linked_GlycosylationVFRRKDINSTAQNVM
EEECCCCCCCCCEEE		43.36-
352GlutathionylationRVEFEELCADLFDRV
EEHHHHHHHHHHHCC		2.9124333276
398AcetylationKVQEVLLKAVGKEEL
HHHHHHHHHHCHHHH		36.5422826441
427PhosphorylationVYQAAALSKAFKVKP
HHHHHHHHHHHCCCC		19.74-
515N-linked_GlycosylationLRVFGSQNLTTVKLK
HEEECCCCCEEEEEE		40.8419349973
529AcetylationKGVGESFKKYPDYES
EECHHHHHHCCCCCC		61.752374519
531PhosphorylationVGESFKKYPDYESKG
CHHHHHHCCCCCCCC		11.2628576409
534PhosphorylationSFKKYPDYESKGIKA
HHHHCCCCCCCCCCC		20.0028576409
558PhosphorylationLSLDRVESVFETLVE
CCHHHHHHHHHHHHC		29.2927180971
562PhosphorylationRVESVFETLVEDSPE
HHHHHHHHHHCCCHH		25.3329472430
567PhosphorylationFETLVEDSPEEESTL
HHHHHCCCHHHHHHH		22.2417203969
572PhosphorylationEDSPEEESTLTKLGN
CCCHHHHHHHHHHHH		31.8117203969
573PhosphorylationDSPEEESTLTKLGNT
CCHHHHHHHHHHHHH		41.5517203969
575PhosphorylationPEEESTLTKLGNTIS
HHHHHHHHHHHHHHH		25.0623140645
580PhosphorylationTLTKLGNTISSLFGG
HHHHHHHHHHHHHCC		22.0428066266
582PhosphorylationTKLGNTISSLFGGGT
HHHHHHHHHHHCCCC		20.9628066266
583PhosphorylationKLGNTISSLFGGGTS
HHHHHHHHHHCCCCC		24.7028066266
589PhosphorylationSSLFGGGTSSDAKEN
HHHHCCCCCHHHHHH		28.4728066266
590PhosphorylationSLFGGGTSSDAKENG
HHHCCCCCHHHHHHC		29.5129472430
591PhosphorylationLFGGGTSSDAKENGT
HHCCCCCHHHHHHCC		41.2325195567
596N-linked_GlycosylationTSSDAKENGTDAVQE
CCHHHHHHCCCHHHH		58.94-
651AcetylationDAAREGEKPDEKESG
CCCCCCCCCCCCCCC		69.4923201123
722AcetylationELARSVQKLEELTLR
HHHHHHHHHHHHCHH		56.5622826441
742PhosphorylationEREKAANSLEAFIFE
HHHHHHHHHHHHHHH		23.9029899451
803AcetylationDKLAELRKLCQGLFF
HHHHHHHHHHHHHHC		67.2622826441
805GlutathionylationLAELRKLCQGLFFRV
HHHHHHHHHHHHCCH		3.1924333276
830N-linked_GlycosylationSALDNLLNHSSIFLK
HHHHHHHCCCHHHHH		35.84-
862N-linked_GlycosylationTTLEKVINDTWAWKN
HHHHHHHCCCCHHHH		43.58-
869N-linked_GlycosylationNDTWAWKNATLAEQA
CCCCHHHHCHHHHHC		27.70-
883AcetylationAKLPATEKPVLLSKD
CCCCCCCCCEEECCH		35.7523806337
889AcetylationEKPVLLSKDIEAKMM
CCCEEECCHHHHHHH		63.8023954790
889SuccinylationEKPVLLSKDIEAKMM
CCCEEECCHHHHHHH		63.8023954790
894AcetylationLSKDIEAKMMALDRE
ECCHHHHHHHHHHHH		19.2022826441
922N-linked_GlycosylationRPRPKDKNGTRAEPP
CCCCCCCCCCCCCCC		68.17-
931N-linked_GlycosylationTRAEPPLNASAGDQE
CCCCCCCCCCCCCCC		37.31-
933PhosphorylationAEPPLNASAGDQEEK
CCCCCCCCCCCCCCC		31.5430635358
933O-linked_GlycosylationAEPPLNASAGDQEEK
CCCCCCCCCCCCCCC		31.5430059200
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 HYOU1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HYOU1_MOUSE !!
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 HYOU1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIL1_MOUSESil1genetic
19801575
S61A1_MOUSESec61a1physical
12065409
TMEDA_MOUSETmed10physical
12065409
S61A1_MOUSESec61a1physical
24218449
CHIP_MOUSEStub1physical
24218449
TERA_MOUSEVcpphysical
24218449
GRP78_MOUSEHspa5physical
24218449
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HYOU1_MOUSE

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory