dbPTM

PARVA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PARVA_HUMAN
UniProt AC	Q9NVD7
Protein Name	Alpha-parvin
Gene Name	PARVA
Organism	Homo sapiens (Human).
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. Associates with the actin cytoskeleton.
Protein Description	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 (By similarity). 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..
Protein Sequence	MATSPQKSPSVPKSPTPKSPPSRKKDDSFLGKLGGTLARRKKAKEVSELQEEGMNAINLPLSPIPFELDPEDTMLEENEVRTMVDPNSRSDPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLESEKLNVAEVTQSEIAQKQKLQTVLEKINETLKLPPRSIKWNVDSVHAKSLVAILHLLVALSQYFRAPIRLPDHVSIQVVVVQKREGILQSRQIQEEITGNTEALSGRHERDAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTPDSFEQKVLNVSFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYRNVE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATSPQKSP ------CCCCCCCCC	19.45	-
3	Phosphorylation	-----MATSPQKSPS -----CCCCCCCCCC	39.37	29255136
4	Phosphorylation	----MATSPQKSPSV ----CCCCCCCCCCC	18.78	29255136
8	Phosphorylation	MATSPQKSPSVPKSP CCCCCCCCCCCCCCC	19.70	29255136
10	Phosphorylation	TSPQKSPSVPKSPTP CCCCCCCCCCCCCCC	59.13	29255136
14	Phosphorylation	KSPSVPKSPTPKSPP CCCCCCCCCCCCCCC	28.12	29255136
16	Phosphorylation	PSVPKSPTPKSPPSR CCCCCCCCCCCCCCC	50.90	29255136
19	Phosphorylation	PKSPTPKSPPSRKKD CCCCCCCCCCCCCCC	43.15	22167270
22	Phosphorylation	PTPKSPPSRKKDDSF CCCCCCCCCCCCCCH	61.18	22167270
28	Phosphorylation	PSRKKDDSFLGKLGG CCCCCCCCHHHHHHH	32.29	29255136
32	Acetylation	KDDSFLGKLGGTLAR CCCCHHHHHHHHHHH	46.21	23954790
36	Phosphorylation	FLGKLGGTLARRKKA HHHHHHHHHHHHHHH	18.55	29255136
43	Phosphorylation	TLARRKKAKEVSELQ HHHHHHHHHHHHHHH	19.10	-
44	Phosphorylation	LARRKKAKEVSELQE HHHHHHHHHHHHHHH	68.48	-
47	Phosphorylation	RKKAKEVSELQEEGM HHHHHHHHHHHHCCC	33.41	22210691
48	Phosphorylation	KKAKEVSELQEEGMN HHHHHHHHHHHCCCC	60.70	15353548
50	Phosphorylation	AKEVSELQEEGMNAI HHHHHHHHHCCCCCC	42.52	17081983
54	Phosphorylation	SELQEEGMNAINLPL HHHHHCCCCCCCCCC	3.28	20166139
56	Phosphorylation	LQEEGMNAINLPLSP HHHCCCCCCCCCCCC	5.33	19651622
59	Phosphorylation	EGMNAINLPLSPIPF CCCCCCCCCCCCCCC	3.54	19664995
62	Phosphorylation	NAINLPLSPIPFELD CCCCCCCCCCCCCCC	20.88	25159151
68	Phosphorylation	LSPIPFELDPEDTML CCCCCCCCCCCCCCC	15.85	20166139
72	Ubiquitination	PFELDPEDTMLEENE CCCCCCCCCCCCCCC	42.69	23000965
72	Acetylation	PFELDPEDTMLEENE CCCCCCCCCCCCCCC	42.69	-
73	Phosphorylation	FELDPEDTMLEENEV CCCCCCCCCCCCCCC	23.22	29523821
76	Phosphorylation	DPEDTMLEENEVRTM CCCCCCCCCCCCHHC	48.21	24719451
82	Phosphorylation	LEENEVRTMVDPNSR CCCCCCHHCCCCCCC	27.07	22210691
88	Phosphorylation	RTMVDPNSRSDPKLQ HHCCCCCCCCCHHHH	38.25	22210691
102	Phosphorylation	QELMKVLIDWINDVL HHHHHHHHHHHHHHH	4.64	18691976
124	Phosphorylation	KDLAEDLYDGQVLQK CCHHHHCCCHHHHHH	30.28	27259358
133	Ubiquitination	GQVLQKLFEKLESEK HHHHHHHHHHHHHCC	11.37	-
135	Acetylation	VLQKLFEKLESEKLN HHHHHHHHHHHCCCC	50.66	27178108
147	Phosphorylation	KLNVAEVTQSEIAQK CCCHHHHHHHHHHHH	20.20	28555341
167	Phosphorylation	VLEKINETLKLPPRS HHHHHHHHCCCCCCC	25.38	-
171	Ubiquitination	INETLKLPPRSIKWN HHHHCCCCCCCCCCC	22.22	-
172 (in isoform 2)	Phosphorylation	-	53.76	20068231
174	Phosphorylation	TLKLPPRSIKWNVDS HCCCCCCCCCCCCCH	34.00	-
175	Ubiquitination	LKLPPRSIKWNVDSV CCCCCCCCCCCCCHH	6.73	-
180	Ubiquitination	RSIKWNVDSVHAKSL CCCCCCCCHHHHHHH	41.55	-
194	Ubiquitination	LVAILHLLVALSQYF HHHHHHHHHHHHHHH	1.15	-
196	Ubiquitination	AILHLLVALSQYFRA HHHHHHHHHHHHHCC	11.06	-
235	Phosphorylation	RQIQEEITGNTEALS HHHHHHHHCCHHHHC	27.88	25072903
238	Phosphorylation	QEEITGNTEALSGRH HHHHHCCHHHHCCCC	24.79	25072903
242	Phosphorylation	TGNTEALSGRHERDA HCCHHHHCCCCHHHH	40.61	25072903
252	Phosphorylation	HERDAFDTLFDHAPD CHHHHHHHHHHHCCH	23.91	23403867
260	Ubiquitination	LFDHAPDKLNVVKKT HHHHCCHHHHHHHHH	40.68	33845483
267	Phosphorylation	KLNVVKKTLITFVNK HHHHHHHHHHHHHHH	20.06	28555341
270	Phosphorylation	VVKKTLITFVNKHLN HHHHHHHHHHHHHHH	25.33	28555341
282	Phosphorylation	HLNKLNLEVTELETQ HHHHCCCEEEHHHHH	46.44	27251275
284	Phosphorylation	NKLNLEVTELETQFA HHCCCEEEHHHHHHC	26.02	-
292	Phosphorylation	ELETQFADGVYLVLL HHHHHHCHHHHHHHH	48.67	27251275
300	Ubiquitination	GVYLVLLMGLLEGYF HHHHHHHHHHHHCCE	2.88	-
362	Phosphorylation	KSTLRVLYNLFTKYR HHHHHHHHHHHHHHC	13.63	27762562
383	Ubiquitination	------------------ ------------------		-

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
4	S	Phosphorylation	Kinase	ERK2	P28482	PSP
8	S	Phosphorylation	Kinase	ERK2	P28482	PSP

Functions of PTM Sites

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

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DHX36_HUMAN	DHX36	physical	17353931
A4_HUMAN	APP	physical	21832049
HS105_HUMAN	HSPH1	physical	22863883
ILK_HUMAN	ILK	physical	22863883
RSU1_HUMAN	RSU1	physical	22863883
SC24C_HUMAN	SEC24C	physical	22863883
MOCOS_HUMAN	MOCOS	physical	26186194
PARVB_HUMAN	PARVB	physical	26186194
IQGA1_HUMAN	IQGAP1	physical	26186194
VPS11_HUMAN	VPS11	physical	26186194
GRAN_HUMAN	GCA	physical	26186194
ILK_HUMAN	ILK	physical	26186194
DDX47_HUMAN	DDX47	physical	26186194
ILK_HUMAN	ILK	physical	28514442
PARVB_HUMAN	PARVB	physical	28514442
MOCOS_HUMAN	MOCOS	physical	28514442
IQGA1_HUMAN	IQGAP1	physical	28514442
GRAN_HUMAN	GCA	physical	28514442
DDX47_HUMAN	DDX47	physical	28514442
VPS11_HUMAN	VPS11	physical	28514442
CCNB1_HUMAN	CCNB1	physical	28514442

Drug and Disease Associations

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

Regulatory Network of PARVA_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND MASSSPECTROMETRY.	19369195 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-19 AND THR-36,AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-8; SER-28; THR-36AND SER-62, AND MASS SPECTROMETRY.	18691976 [Abstract]