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Protein Page:
HYOU1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

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: Heat shock protein; Chaperone
Cellular Component: endoplasmic reticulum lumen; endoplasmic reticulum; extracellular region
Molecular Function: ATP binding
Biological Process: unfolded protein response, activation of signaling protein activity; cellular protein metabolic process; 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 S84 NERFFGDSAASMAIk
0 1 K91-u SAASMAIkNPKATLR
0 11 K198-a AARMAGLkVLQLIND
0 2 K198-u AARMAGLkVLQLIND
0 1 K398-u RVQEVLLkAVGKEEL
0 2 S567 FETLVEDSAEEESTL
0 1 T580-ga TLTKLGNtISSLFGG
0 1 T589-ga SSLFGGGttPDAKEN
0 1 T590-ga SLFGGGttPDAKENG
0 1 T727-p VQKLQDLtLRDLEKQ
  mouse

 
S84-p NERFLGDsAAGMAIK
K91 sAAGMAIKNPKATLR
K198 AARMAGLKVLQLIND
K198 AARMAGLKVLQLIND
K398 KVQEVLLKAVGKEEL
S567-p FETLVEDsPEEESTL
T580 TLTKLGNTISSLFGG
T589 SSLFGGGTSSDAKEN
S590 SLFGGGTSSDAKENG
T727 VQKLEELTLRDLEKQ
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