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Protein Page:
HYOU1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
HYOU1 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. Belongs to the heat shock protein 70 family. Note: This description may include information from UniProtKB.
Protein type: Chaperone; Heat shock protein
Cellular Component: endoplasmic reticulum lumen; endoplasmic reticulum; extracellular region
Molecular Function: ATP binding
Biological Process: cellular protein metabolic process; unfolded protein response, activation of signaling protein activity; unfolded protein response; response to stress
Reference #:  Q9Y4L1 (UniProtKB)
Alt. Names/Synonyms: 150 kDa oxygen-regulated protein; 170 kDa glucose-regulated protein; DKFZp686N08236; FLJ94899; FLJ97572; glucose-regulated protein 170; GRP-170; GRP170; HSP12A; HYOU1; hypoxia up-regulated 1; Hypoxia up-regulated protein 1; ORP-150; ORP150; oxygen regulated protein (150kD)
Gene Symbols: HYOU1
Molecular weight: 111,335 Da
Basal Isoelectric point: 5.16  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

HYOU1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T73 RKTPVIVTLKENERF
0 1 K75 TPVIVTLKENERFFG
0 1 K75 TPVIVTLKENERFFG
0 1 S84 NERFFGDSAASMAIk
0 1 K91-ub SAASMAIkNPKATLR
0 1 K170 DFAEQPIKDAVITVP
0 11 K198-ac AARMAGLkVLQLIND
0 2 K198-ub AARMAGLkVLQLIND
0 1 T269-p RGVGFDRtLGGLEME
0 1 K398-ub RVQEVLLkAVGKEEL
0 1 S427 VYQAAALSKAFKVKP
0 1 S527-p KLKGVGDsFKKYPDY
0 1 K529 KGVGDsFKKYPDYES
0 3 S567-p FETLVEDsAEEESTL
0 1 T580-ga TLTKLGNtISSLFGG
0 1 T589-ga SSLFGGGttPDAKEN
0 1 T590-ga SLFGGGttPDAKENG
0 1 T600-p AKENGTDtVQEEEES
0 1 T727-p VQKLQDLtLRDLEKQ
0 1 K883 AKLPATEKPVLLSKD
0 1 K889 EKPVLLSKDIEAKMM
0 1 K889 EKPVLLSKDIEAKMM
  mouse

 
T73-p RKTPVTVtLkENERF
K75-ac TPVTVtLkENERFLG
K75-sc TPVTVtLkENERFLG
S84-p NERFLGDsAAGMAIK
K91 sAAGMAIKNPKATLR
K170-sc DFAEQPIkDAVITVP
K198 AARMAGLKVLQLIND
K198 AARMAGLKVLQLIND
T269 RGVGFDRTLGGLEME
K398 KVQEVLLKAVGKEEL
S427-p VYQAAALsKAFKVKP
S527 KLKGVGESFkKYPDY
K529-ac KGVGESFkKYPDYES
S567-p FETLVEDsPEEESTL
T580 TLTKLGNTISSLFGG
T589 SSLFGGGTSSDAKEN
S590 SLFGGGTSSDAKENG
A600 AKENGTDAVQEEEES
T727 VQKLEELTLRDLEKQ
K883-ac AKLPATEkPVLLSkD
K889-ac EkPVLLSkDIEAKMM
K889-sc EkPVLLSkDIEAKMM
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