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Protein Page:
OS9 (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
OS9 Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4. Belongs to the OS-9 family. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Endoplasmic reticulum
Cellular Component: endoplasmic reticulum lumen
Molecular Function: protein binding; protease binding; glycoprotein binding
Biological Process: ER-associated protein catabolic process; protein ubiquitination during ubiquitin-dependent protein catabolic process; protein ubiquitination; protein retention in ER; protein targeting
Reference #:  Q13438 (UniProtKB)
Alt. Names/Synonyms: Amplified in osteosarcoma 9; endoplasmic reticulum lectin 2; ERLEC2; erlectin 2; OS-9; OS9; osteosarcoma amplified 9, endoplasmic reticulum associated protein; osteosarcoma amplified 9, endoplasmic reticulum lectin; Protein OS-9
Gene Symbols: OS9
Molecular weight: 75,562 Da
Basal Isoelectric point: 4.8  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

OS9

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 5 K113-ub RDAPCLLkTkDWWTY
0 1 K115-ub APCLLkTkDWWTYEF
0 3 K271-ub DSKQYGDkIIEELQD
0 2 K288-ub PQVWSETkSGVAPQK
0 1 M296 SGVAPQKMAGASPTK
0 1 K380-ub KGGTKKGkPNIGQEQ
0 1 K438-ub QLLGEFEkELEGILL
0 1 K457 DRLRSEVKAGMEREL
0 1 K473 NIIQETEKELDPDGL
0 3 K499-ub ALTSTLNkLIKRLEE
0 2 K507-ub LIKRLEEkQsPELVK
0 1 S509-p KRLEEkQsPELVKKH
0 1 K515 QsPELVKKHKKKRVV
0 1 S529-ga VPKKPPPsPQPtEED
0 1 T533-ga PPPsPQPtEEDPEHR
0 1 K563-ub DLTVLEMkRENPQLK
0 2 K594-ub AAGKIEIkIVRPWAE
0 13 K619-ub DEDTRNLkEIFFNIL
0 1 K641-ub QKERQRQkELESNYR
  mouse

 
K113-ub RDAPCLLkTKDWWTY
K115 APCLLkTKDWWTYEF
K271 ESKQHEEKTTEEVQD
K288 RQVWSGSKAAGAPPK
K296-ac AAGAPPKkEDVSPAK
K378 LKAAEKGKPSVRREQ
K443 QLLGEFEKELEGMLL
K462-ub ERLRSEVkAGMEREL
K478-ub NIIQETEkELDPEGL
K504 ALTSTLDKLIKRLQE
N512 LIKRLQENQSPELVQ
S514 KRLQENQSPELVQkY
K520-ub QSPELVQkYKKRRVV
S534 VPQKPPPSPHPTEEE
T538 PPPSPHPTEEEPEHR
N568 DLTVLEMNRENPQLK
K599 AEGKIEIKIVRPGAE
K624 DEDTRNLKEIFFNIL
S646 NKERQRQSELESNYR
  rat

 
K113 RDAPCLLKTKDWWTY
K115 APCLLKTKDWWTYEF
K271 ESKQHEEKVTEEVQD
K288 HQVWSGSKAAGAPPK
K296 AAGAPPKKEDVSPTK
K379 LKGAEKGKPSVRQEQ
K437 QLLGEFEKELEGMLL
K456 ERLRSEVKAGMEREL
K472 NIIQETEKELDPEGL
K498 ALTSTLDKLIKRLQE
S506 LIKRLQESQSPELVQ
S508 KRLQESQSPELVQKY
K514 QSPELVQKYKKRRVV
S528 VPQKPPPSPHPTEEE
T532 PPPSPHPTEEEPEHR
N562 DLTVLEMNRENPQLK
K593 AEGKIEIKIVRPGAE
K618 DEDTRNLKEIFFNIL
S640 NKERQRQSELESNYR
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