dbPTM

CLUS_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CLUS_MOUSE
UniProt AC	Q06890
Protein Name	Clusterin
Gene Name	Clu
Organism	Mus musculus (Mouse).
Sequence Length	448
Subcellular Localization	Secreted . Nucleus . Cytoplasm . Mitochondrion membrane Peripheral membrane protein Cytoplasmic side. Cytoplasm, cytosol . Microsome. Endoplasmic reticulum. Cytoplasmic vesicle, secretory vesicle, chromaffin granule. Can retrotranslocate from the s
Protein Description	Functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. Promotes apoptosis when in the nucleus. Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation (By similarity)..
Protein Sequence	MKILLLCVALLLIWDNGMVLGEQEVSDNELQELSTQGSRYINKEIQNAVQGVKHIKTLIEKTNAERKSLLNSLEEAKKKKEDALEDTRDSEMKLKAFPEVCNETMMALWEECKPCLKHTCMKFYARVCRSGSGLVGQQLEEFLNQSSPFYFWMNGDRIDSLLESDRQQSQVLDAMQDSFARASGIIDTLFQDRFFARELHDPHYFSPIGFPHKRPHFLYPKSRLVRSLMSPSHYGPPSFHNMFQPFFEMIHQAQQAMDVQLHSPAFQFPDVDFLREGEDDRTVCKEIRRNSTGCLKMKGQCEKCQEILSVDCSTNNPAQANLRQELNDSLQVAERLTEQYKELLQSFQSKMLNTSSLLEQLNDQFNWVSQLANLTQGEDKYYLRVSTVTTHSSDSEVPSRVTEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSRAE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
102	N-linked_Glycosylation	KAFPEVCNETMMALW HHHHHHHHHHHHHHH	53.61	-
132	Phosphorylation	ARVCRSGSGLVGQQL HHHHHCCCCHHHHHH	30.15	-
144	N-linked_Glycosylation	QQLEEFLNQSSPFYF HHHHHHHHCCCCEEE	45.04	-
160	Phosphorylation	MNGDRIDSLLESDRQ ECCHHHHHHHHHHHH	32.27	-
188	Phosphorylation	RASGIIDTLFQDRFF HHHCHHHHHHHCHHH	21.04	27180971
206	Phosphorylation	LHDPHYFSPIGFPHK CCCCCCCCCCCCCCC	14.40	24719451
290	N-linked_Glycosylation	VCKEIRRNSTGCLKM HHHHHHHCCCCCCEE	33.79	17330941
327	N-linked_Glycosylation	ANLRQELNDSLQVAE HHHHHHHHHHHHHHH	35.75	16944957
341	Ubiquitination	ERLTEQYKELLQSFQ HHHHHHHHHHHHHHH	41.39	22790023
353	N-linked_Glycosylation	SFQSKMLNTSSLLEQ HHHHCCCCHHHHHHH	34.12	-
373	N-linked_Glycosylation	NWVSQLANLTQGEDK CHHHHHHCCCCCCCC	52.81	-
386	Phosphorylation	DKYYLRVSTVTTHSS CCEEEEEEEEEECCC	15.66	29472430
387	Phosphorylation	KYYLRVSTVTTHSSD CEEEEEEEEEECCCC	21.00	29472430
389	Phosphorylation	YLRVSTVTTHSSDSE EEEEEEEEECCCCCC	20.91	29472430
390	Phosphorylation	LRVSTVTTHSSDSEV EEEEEEEECCCCCCC	18.54	29472430
392	Phosphorylation	VSTVTTHSSDSEVPS EEEEEECCCCCCCCC	33.48	24719451
393	Phosphorylation	STVTTHSSDSEVPSR EEEEECCCCCCCCCC	37.24	24719451
395	Phosphorylation	VTTHSSDSEVPSRVT EEECCCCCCCCCCCE	42.30	29472430
399	Phosphorylation	SSDSEVPSRVTEVVV CCCCCCCCCCEEEHH	44.55	29472430

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 CLUS_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CLUS_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 CLUS_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HYALP_MOUSE	Spam1	physical	19357365
LEP_MOUSE	Lep	physical	12824284
VLDLR_HUMAN	VLDLR	physical	12824284

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CLUS_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."; Bernhard O.K., Kapp E.A., Simpson R.J.; J. Proteome Res. 6:987-995(2007). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-290, AND MASSSPECTROMETRY.	17330941 [Abstract]
"Proteome-wide characterization of N-glycosylation events by diagonalchromatography."; Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,Gevaert K.; J. Proteome Res. 5:2438-2447(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-327, AND MASSSPECTROMETRY.	16944957 [Abstract]