dbPTM

PARVA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PARVA_MOUSE
UniProt AC	Q9EPC1
Protein Name	Alpha-parvin
Gene Name	Parva
Organism	Mus musculus (Mouse).
Sequence Length	372
Subcellular Localization	Cell junction, focal adhesion. Cell membrane Peripheral membrane protein Cytoplasmic side. Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line. Constituent of focal adhesions.
Protein Description	Plays a role in the reorganization of the actin cytoskeleton, formation of lamellipodia and ciliogenesis. Plays a role in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells to endothelial cells during blood vessel development..
Protein Sequence	MATSPQKSPLVPKSPTPKSPPSRKKDDSFLGKLGGTLARRKKAKEVSEFQEEGMNAINLPLSPISFELDPEDTLLEENEVRTMVDPNSRNDPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLESEKLNVAEVTQSEIAQKQKLQTVLEKINETLKLPPRSIKWNVDSVHAKNLVAILHLLVALSQYFRAPIRLPDHVSIQVVVVQKREGILQSRQIQEEITGNTEALSGRHERDAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTPDSFEQKVLNVSFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYRNVE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATSPQKSP ------CCCCCCCCC	19.45	19131326
3	Phosphorylation	-----MATSPQKSPL -----CCCCCCCCCC	39.37	26824392
4	Phosphorylation	----MATSPQKSPLV ----CCCCCCCCCCC	18.78	23527152
8	Phosphorylation	MATSPQKSPLVPKSP CCCCCCCCCCCCCCC	20.44	26824392
14	Phosphorylation	KSPLVPKSPTPKSPP CCCCCCCCCCCCCCC	28.12	25521595
16	Phosphorylation	PLVPKSPTPKSPPSR CCCCCCCCCCCCCCC	50.90	26824392
19	Phosphorylation	PKSPTPKSPPSRKKD CCCCCCCCCCCCCCC	43.15	25521595
22	Phosphorylation	PTPKSPPSRKKDDSF CCCCCCCCCCCCCCH	61.18	27149854
28	Phosphorylation	PSRKKDDSFLGKLGG CCCCCCCCHHHHHHH	32.29	25521595
32	Acetylation	KDDSFLGKLGGTLAR CCCCHHHHHHHHHHH	46.21	23236377
36	Phosphorylation	FLGKLGGTLARRKKA HHHHHHHHHHHHHHH	18.55	22942356
47	Phosphorylation	RKKAKEVSEFQEEGM HHHHHHHHHHHHHHC	33.51	26239621
62	Phosphorylation	NAINLPLSPISFELD CCCCCCCCCCEEECC	20.46	26239621
65	Phosphorylation	NLPLSPISFELDPED CCCCCCCEEECCCCC	18.95	23649490
88	Phosphorylation	RTMVDPNSRNDPKLQ CCCCCCCCCCCHHHH	37.54	21659604
140	Ubiquitination	FEKLESEKLNVAEVT HHHHHHCCCCHHHHH	55.42	-
169	Ubiquitination	EKINETLKLPPRSIK HHHHHHCCCCCCCCC	67.38	-
266	Ubiquitination	DKLNVVKKTLITFVN HHHHHHHHHHHHHHH	36.63	-
270	Phosphorylation	VVKKTLITFVNKHLN HHHHHHHHHHHHHHH	25.33	25195567

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 PARVA_MOUSE !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
ILK_MOUSE	Ilk	physical	12432066
LIMS1_MOUSE	Lims1	physical	12432066

Drug and Disease Associations

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

Regulatory Network of PARVA_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-14 AND SER-19,AND MASS SPECTROMETRY.	19131326 [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-28, AND MASSSPECTROMETRY.	19367708 [Abstract]