dbPTM

COR1A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	COR1A_MOUSE
UniProt AC	O89053
Protein Name	Coronin-1A
Gene Name	Coro1a
Organism	Mus musculus (Mouse).
Sequence Length	461
Subcellular Localization	Cytoplasm, cytoskeleton . Cytoplasm, cell cortex . Cytoplasmic vesicle, phagosome membrane . In non-infected macrophages, associated with the cortical microtubule network. In mycobacteria-infected macrophages, becomes progressively relocalized and re
Protein Description	May be a crucial component of the cytoskeleton of highly motile cells, functioning both in the invagination of large pieces of plasma membrane, as well as in forming protrusions of the plasma membrane involved in cell locomotion. In mycobacteria-infected cells, its retention on the phagosomal membrane prevents fusion between phagosomes and lysosomes..
Protein Sequence	MSRQVVRSSKFRHVFGQPAKADQCYEDVRVSQTTWDSGFCAVNPKFMALICEASGGGAFLVLPLGKTGRVDKNVPLVCGHTAPVLDIAWCPHNDNVIASGSEDCTVMVWEIPDGGLVLPLREPVITLEGHTKRVGIVAWHPTAQNVLLSAGCDNVILVWDVGTGAAVLTLGPDVHPDTIYSVDWSRDGALICTSCRDKRVRVIEPRKGTVVAEKDRPHEGTRPVHAVFVSEGKILTTGFSRMSERQVALWDTKHLEEPLSLQELDTSSGVLLPFFDPDTNIVYLCGKGDSSIRYFEITSEAPFLHYLSMFSSKESQRGMGYMPKRGLEVNKCEIARFYKLHERKCEPIAMTVPRKSDLFQEDLYPPTAGPDPALTAEEWLGGRDAGPLLISLKDGYVPPKSRELRVNRGLDSARRRATPEPSGTPSSDTVSRLEEDVRNLNAIVQKLQERLDRLEETVQAK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSRQVVRSS ------CCCHHHHHH	31.27	21844203
2	Acetylation	------MSRQVVRSS ------CCCHHHHHH	31.27	-
24	Glutathionylation	QPAKADQCYEDVRVS CCCCCCHHCCCCCCC	4.06	24333276
25	Phosphorylation	PAKADQCYEDVRVSQ CCCCCHHCCCCCCCC	14.99	25367039
40	Glutathionylation	TTWDSGFCAVNPKFM CCCCCCCCCCCHHHE	4.76	24333276
180	Phosphorylation	DVHPDTIYSVDWSRD CCCCCCEEEEECCCC	12.53	-
195	Glutathionylation	GALICTSCRDKRVRV CCEEEECCCCCEEEE	3.34	24333276
221	Phosphorylation	KDRPHEGTRPVHAVF CCCCCCCCCCEEEEE	28.90	29899451
236	Phosphorylation	VSEGKILTTGFSRMS EECCCEEEECCCCCC	28.48	23737553
237	Phosphorylation	SEGKILTTGFSRMSE ECCCEEEECCCCCCC	32.55	23737553
240	Phosphorylation	KILTTGFSRMSERQV CEEEECCCCCCCCCE	28.55	23737553
285	Glutathionylation	DTNIVYLCGKGDSSI CCCEEEEECCCCCEE	2.64	24333276
332	Glutathionylation	RGLEVNKCEIARFYK CCCCCCHHHHHHHHH	3.74	24333276
345	Glutathionylation	YKLHERKCEPIAMTV HHHHCCCCEECEEEC	10.61	24333276
356	Phosphorylation	AMTVPRKSDLFQEDL EEECCCHHHCCCCCC	40.60	21082442
412	Phosphorylation	RVNRGLDSARRRATP HHHCCHHHHHHHCCC	28.81	28833060
418	Phosphorylation	DSARRRATPEPSGTP HHHHHHCCCCCCCCC	26.77	26824392
422	Phosphorylation	RRATPEPSGTPSSDT HHCCCCCCCCCCHHH	54.35	25521595
424	Phosphorylation	ATPEPSGTPSSDTVS CCCCCCCCCCHHHHH	25.08	27742792
426	Phosphorylation	PEPSGTPSSDTVSRL CCCCCCCCHHHHHHH	40.46	22942356
427	Phosphorylation	EPSGTPSSDTVSRLE CCCCCCCHHHHHHHH	38.20	25521595
429	Phosphorylation	SGTPSSDTVSRLEED CCCCCHHHHHHHHHH	23.48	28833060
431	Phosphorylation	TPSSDTVSRLEEDVR CCCHHHHHHHHHHHH	32.99	28833060

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
2	S	Phosphorylation	Kinase	PKC	-	Uniprot
412	S	Phosphorylation	Kinase	PKC	-	Uniprot
418	T	Phosphorylation	Kinase	CDK5	P49615	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
412	S	Phosphorylation		23100250
phosphorylation at Ser-412 by PKC strongly down-regulates the association with actin.

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 COR1A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CAPZB_MOUSE	Capzb	physical	15800061

Drug and Disease Associations

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

Regulatory Network of COR1A_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-418, AND MASSSPECTROMETRY.	19367708 [Abstract]

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