dbPTM

SLU7_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SLU7_MOUSE
UniProt AC	Q8BHJ9
Protein Name	Pre-mRNA-splicing factor SLU7
Gene Name	Slu7
Organism	Mus musculus (Mouse).
Sequence Length	585
Subcellular Localization	Nucleus. Cytoplasm. Predominantly nuclear. Shuttling between the nucleus and the cytoplasm is regulated by the CCHC-type zinc finger. Translocates from the nucleus to the cytoplasm after heat shock cell treatment. Accumulates in cytoplasmic vesicle-l
Protein Description	Participates in the second catalytic step of pre-mRNA splicing, when the free hydroxyl group of exon I attacks the 3'-splice site to generate spliced mRNA and the excised lariat intron. Required for holding exon 1 properly in the spliceosome and for correct AG identification when more than one possible AG exists in 3'-splicing site region. May be involved in the activation of proximal AG. Probably also involved in alternative splicing regulation (By similarity)..
Protein Sequence	MSAAAVDPVSATPMTGSKEMSLEEPKKMTREDWRKKKELEEQRKLGNAPAEVDEEGKDINPHIPQYISSVPWYIDPSKRPTLKHQRPQPEKQKQFSSSGEWYKRGVKENSITTKYRKGACENCGAMTHKRKDCFERPRRVGAKFTGTNIAPDEHVQPQLMFDYDGKRDRWNGYNPEEHMKIVEEYAKVDLAKRTLKAQKLQEELASGKLVEQANSPKHQWGEEEPNSQMEKDHNSEDEDEDKYADDIDMPGQNFDSKRRITVRNLRIREDIAKYLRNLDPNSAYYDPKTRAMRENPYANAGKNPDEVSYAGDNFVRYTGDTISMAQTQLFAWEAYDKGSEVHLQADPTKLELLYKSFKVKKEDFKEQQKESILEKYGGQEHLDAPPAELLLAQTEDYVEYSRHGTVIKGQERAVACSKYEEDVKINNHTHIWGSYWKEGRWGYKCCHSFFKYSYCTGEAGKESVNSEECIITGATAEESVKKPQALLELHQEKLKEEKKKKKKKKKHRKSSSDSDDEERKQEKLKKALNAEEARLLHVKEIMQIDERKRPYNSIYETREPTEEEMEAYRMKRQRPDDPMASFLGQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSAAAVDPV ------CCCCCCCCC	26.98	-
2	Phosphorylation	------MSAAAVDPV ------CCCCCCCCC	26.98	30482847
206	Phosphorylation	KLQEELASGKLVEQA HHHHHHHHCCHHHHC	49.43	29514104
215	Phosphorylation	KLVEQANSPKHQWGE CHHHHCCCCCCCCCC	38.04	27087446
227	Phosphorylation	WGEEEPNSQMEKDHN CCCCCCCCHHCCCCC	41.44	23984901
235	Phosphorylation	QMEKDHNSEDEDEDK HHCCCCCCCCCCHHH	42.90	27087446
243	Phosphorylation	EDEDEDKYADDIDMP CCCCHHHHHCCCCCC	27.82	25619855
256	Phosphorylation	MPGQNFDSKRRITVR CCCCCCCCCCCEEEE	24.75	25619855
302	Acetylation	NPYANAGKNPDEVSY CCCCCCCCCCHHCCC	64.00	23806337
302	Ubiquitination	NPYANAGKNPDEVSY CCCCCCCCCCHHCCC	64.00	22790023
463	Phosphorylation	TGEAGKESVNSEECI CCCCCCCCCCCCCEE	30.04	30635358
466	Phosphorylation	AGKESVNSEECIITG CCCCCCCCCCEEEEC	32.39	30635358
510	Phosphorylation	KKKKHRKSSSDSDDE HHHHHHCCCCCCCHH	34.72	27087446
511	Phosphorylation	KKKHRKSSSDSDDEE HHHHHCCCCCCCHHH	41.00	-
512	Phosphorylation	KKHRKSSSDSDDEER HHHHCCCCCCCHHHH	48.50	27087446
514	Phosphorylation	HRKSSSDSDDEERKQ HHCCCCCCCHHHHHH	49.24	27087446
539	Acetylation	EARLLHVKEIMQIDE HHHHHHHHHHHHHHC	30.67	22826441
561	Phosphorylation	IYETREPTEEEMEAY CCCCCCCCHHHHHHH	51.80	28576409
568	Phosphorylation	TEEEMEAYRMKRQRP CHHHHHHHHHHHHCC	9.64	28576409

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 SLU7_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SLU7_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 SLU7_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SLU7_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of SLU7_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND MASSSPECTROMETRY.	19144319 [Abstract]
"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 SER-235, AND MASSSPECTROMETRY.	19367708 [Abstract]