PARVB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PARVB_HUMAN
• UniProt AC: Q9HBI1
• Protein Name: Beta-parvin
• Gene Name: PARVB
• Organism: Homo sapiens (Human).
• Sequence Length: 364
• Subcellular Localization: Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cytoplasm, myofibril, sarcomere. Cytoplasm, myofibril, sarcomere, Z line. Constituent of focal adhes
• Protein Description: Adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases CDC42 and RAC1 by guanine exchange factors, such as ARHGEF6. Is involved in the reorganization of the actin cytoskeleton and formation of lamellipodia. Plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration..
• Protein Sequence: MSSAPRSPTPRPRRMKKDESFLGKLGGTLARKRRAREVSDLQEEGKNAINSPMSPALVDVHPEDTQLEENEERTMIDPTSKEDPKFKELVKVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLRPRGWALRWSVDSIHGKNLVAILHLLVSLAMHFRAPIRLPEHVTVQVVVVRKREGLLHSSHISEELTTTTEMMMGRFERDAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHHFYLTPESFDQKVHNVSFAFELMLDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSAPRSPT ------CCCCCCCCC	34.90	30108239
3	Phosphorylation	-----MSSAPRSPTP -----CCCCCCCCCC	40.78	30108239
7	Phosphorylation	-MSSAPRSPTPRPRR -CCCCCCCCCCCCCC	31.87	28348404
9	Phosphorylation	SSAPRSPTPRPRRMK CCCCCCCCCCCCCCC	32.93	30108239
20	Phosphorylation	RRMKKDESFLGKLGG CCCCCCHHHHHHHHH	35.59	23401153
24	Acetylation	KDESFLGKLGGTLAR CCHHHHHHHHHHHHH	46.21	23236377
28	Phosphorylation	FLGKLGGTLARKRRA HHHHHHHHHHHHHHH	18.55	29255136
39	Phosphorylation	KRRAREVSDLQEEGK HHHHHHHHHHHHHHH	28.05	20071362
51	Phosphorylation	EGKNAINSPMSPALV HHHHHCCCCCCCHHC	18.83	28060719
54	Phosphorylation	NAINSPMSPALVDVH HHCCCCCCCHHCCCC	15.48	18691976
65	Phosphorylation	VDVHPEDTQLEENEE CCCCCCCCCCHHHHC	33.13	22468782
74	Phosphorylation	LEENEERTMIDPTSK CHHHHCCCCCCCCCC	23.04	20071362
79	Phosphorylation	ERTMIDPTSKEDPKF CCCCCCCCCCCCHHH	49.00	20071362
116	Phosphorylation	KQLEEDLYDGQVLQK HHHHHCCCCHHHHHH	30.28	28060719
123	Ubiquitination	YDGQVLQKLLEKLAG CCHHHHHHHHHHHCC	51.37	-
132	Ubiquitination	LEKLAGCKLNVAEVT HHHHCCCCCCHHHHH	42.02	-
139	Phosphorylation	KLNVAEVTQSEIGQK CCCHHHHHHHHHHHH	20.20	28555341
170	Phosphorylation	RGWALRWSVDSIHGK CCCEEEEEEECCCCH	15.04	28060719
173	Phosphorylation	ALRWSVDSIHGKNLV EEEEEEECCCCHHHH	17.83	28060719
227	Phosphorylation	SHISEELTTTTEMMM CCCCHHHCCHHHHHH	25.94	24532841
228	Phosphorylation	HISEELTTTTEMMMG CCCHHHCCHHHHHHH	44.33	24532841
229	Phosphorylation	ISEELTTTTEMMMGR CCHHHCCHHHHHHHH	18.61	24532841
230	Phosphorylation	SEELTTTTEMMMGRF CHHHCCHHHHHHHHH	21.57	24532841
244	Phosphorylation	FERDAFDTLFDHAPD HHHHHHHHHHHCCCC	23.91	23403867
252	Ubiquitination	LFDHAPDKLSVVKKS HHHCCCCHHHHHHHH	41.42	-
254	Phosphorylation	DHAPDKLSVVKKSLI HCCCCHHHHHHHHHH	30.52	28060719
276	Phosphorylation	NKLNLEVTELETQFA HHCCCEEEHHHHHHC	26.02	-
354	Phosphorylation	KSTLRVLYNLFTKYK HHHHHHHHHHHHHHC	13.63	-
360	Phosphorylation	LYNLFTKYKNVE--- HHHHHHHHCCCC---	12.53	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PARVB_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PARVB_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PARVB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSME1_HUMAN	PSME1	physical	22939629
F262_HUMAN	PFKFB2	physical	26344197

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-54, AND MASSSPECTROMETRY.
PubMed: 18691976