OS9 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0030968Biological processendoplasmic reticulum unfolded protein response
GO_1904153Biological processnegative regulation of retrograde protein transport, ER to cytosol
GO_0016567Biological processprotein ubiquitination
GO_0006511Biological processubiquitin-dependent protein catabolic process
GO_0030970Biological processretrograde protein transport, ER to cytosol
GO_0006621Biological processprotein retention in ER lumen
GO_0006605Biological processprotein targeting
GO_0036503Biological processERAD pathway
GO_0034976Biological processresponse to endoplasmic reticulum stress
GO_0005788Cellular componentendoplasmic reticulum lumen
GO_0005783Cellular componentendoplasmic reticulum
GO_0000836Cellular componentHrd1p ubiquitin ligase complex
GO_0005789Cellular componentendoplasmic reticulum membrane
GO_0002020Molecular functionprotease binding
GO_0030246Molecular functioncarbohydrate binding
GO_0005515Molecular functionprotein binding

IV. Literature review

[source]
Gene nameOS9
Protein nameEndoplasmic reticulum lectin (Protein OS-9)
Protein OS-9 (Amplified in osteosarcoma 9)
Endoplasmic reticulum lectin
OS9 endoplasmic reticulum lectin
Synonyms
DescriptionFUNCTION: 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. .

FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .

FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .

FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .

FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .

FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .

FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .

FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .

FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .

FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .

FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .

FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .

FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .

FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .

FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .

FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .

FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .

FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .

AccessionsA0A8V8TPZ9
ENST00000257966.13 [Q13438-7]
A0A8V8TQI4
ENST00000700664.1
A0A8V8TQ04
ENST00000315970.12 [Q13438-1]
A0A8V8TRE0
A0A8V8TR31
ENST00000389146.11 [Q13438-4]
ENST00000551035.5 [Q13438-5]
ENST00000700665.1
F8W1V2
ENST00000700661.1
A0A8V8TQI8
Q9BR60
ENST00000389142.10 [Q13438-3]
ENST00000550848.5
A0A8V8TQI9
A0A8V8TRD7
ENST00000700660.1
ENST00000700670.1
ENST00000700656.1
F8W1N0
F8VZI7
F8VWQ2
A0A8V8TQI2
ENST00000551285.5
ENST00000700667.1
ENST00000552787.5
ENST00000435406.6 [Q13438-6]
A0A8V8TR34
ENST00000700658.1
B4E321
ENST00000550372.5
A0A8V8TQI0
ENST00000547079.5
ENST00000700662.1
ENST00000700663.1
A0A8V8TPZ4
ENST00000700659.1
ENST00000700668.1
Q13438
ENST00000700657.1
A0A8V8TR37
ENST00000552285.6 [Q13438-2]
F8W0R2
ENST00000413095.6
ENST00000552423.2
ENST00000439210.6 [Q13438-8]