VINC_CHICK - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: VINC_CHICK
• UniProt AC: P12003
• Protein Name: Vinculin
• Gene Name: VCL
• Organism: Gallus gallus (Chicken).
• Sequence Length: 1135
• Subcellular Localization: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side . Cell junction, adherens junction . Cell junction, focal adhesion . Cytoplasm, cytoskeleton . Cell membrane, sarcolemma ; Peripheral membrane protein ; Cytoplasmic side . Recruitment to
• Protein Description: Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion..
• Protein Sequence: MPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVSAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVRAAQMLQADPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNTKSQGIEEALKNRNFTVEKMSAEINEIIRVLQLTSWDEDAWASKDTEAMKRALALIDSKMNQAKGWLRDPNAPPGDAGEQAIRQILDEAGKAGELCAGKERREILGTCKTLGQMTDQLADLRARGQGATPMAMQKAQQVSQGLDLLTAKVENAARKLEAMTNSKQAIAKKIDAAQNWLADPNGGSEGEEHIRGIMSEARKVAELCEEPKERDDILRSLGEISALTAKLSDLRRHGKGDSPEARALAKQIATSLQNLQSKTNRAVANTRPVKAAVHLEGKIEQAQRWIDNPTVDDRGVGQAAIRGLVAEGRRLANVMMGPYRQDLLAKCDRVDQLAAQLADLAARGEGESPQARAIAAQLQDSLKDLKARMQEAMTQEVSDVFSDTTTPIKLLAVAATAPSDTPNREEVFEERAANFENHAARLGATAEKAAAVGTANKTTVEGIQATVKSARELTPQVVSAARILLRNPGNQAAYEHFETMKNQWIDNVEKMTGLVDEAIDTKSLLDASEEAIKKDLDKCKVAMANMQPQMLVAGATSIARRANRILLVAKREVENSEDPKFREAVKAASDELSKTISPMVMDAKAVAGNISDPGLQKSFLDSGYRILGAVAKVREAFQPQEPDFPPPPPDLEHLHLTDELAPPKPPLPEGEVPPPRPPPPEEKDEEFPEQKAGEAINQPMMMAARQLHDEARKWSSKPVTVINEAAEAGVDIDEEDDADVEFSLPSDIEDDYEPELLLMPTNQPVNQPILAAAQSLHREATKWSSKGNDIIAAAKRMALLMAEMSRLVRGGSGNKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTVKATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVRKTPWYQ

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
100	Phosphorylation	QMLQADPYSVPARDY HHHHCCCCCCCHHHE	23.89	15229287
434	Phosphorylation	ERDDILRSLGEISAL HHHHHHHHHHHHHHH	36.96	23106611
439	Phosphorylation	LRSLGEISALTAKLS HHHHHHHHHHHHHHH	16.96	23106611
442	Phosphorylation	LGEISALTAKLSDLR HHHHHHHHHHHHHHH	22.82	23106611
468	Phosphorylation	ALAKQIATSLQNLQS HHHHHHHHHHHHHHH	31.44	23106611
469	Phosphorylation	LAKQIATSLQNLQSK HHHHHHHHHHHHHHH	20.95	23106611
537	Phosphorylation	ANVMMGPYRQDLLAK HHHHCCHHHHHHHHH	18.38	-
619	Phosphorylation	AATAPSDTPNREEVF HHCCCCCCCCHHHHH	27.14	23106611
719	Phosphorylation	LVDEAIDTKSLLDAS CCCHHHCHHHHHHHC	19.20	23106611
721	Phosphorylation	DEAIDTKSLLDASEE CHHHCHHHHHHHCHH	35.94	23106611
755	Phosphorylation	MLVAGATSIARRANR HHHHCHHHHHHHHHH	17.45	23106611
795	Phosphorylation	DELSKTISPMVMDAK HHHHHCCCHHHHCHH	16.51	23106611
809	Phosphorylation	KAVAGNISDPGLQKS HHHCCCCCCCHHHHH	41.58	23106611
816	Phosphorylation	SDPGLQKSFLDSGYR CCCHHHHHHHHHHHH	20.34	23106611
822	Phosphorylation	KSFLDSGYRILGAVA HHHHHHHHHHHHHHH	9.83	-
983	Phosphorylation	REATKWSSKGNDIIA HHHHHHHHCCHHHHH	43.39	23106611
1102	Phosphorylation	NAQNLMQSVKETVRE HHHHHHHHHHHHHHH	22.61	-
1114	Phosphorylation	VREAEAASIKIRTDA HHHHHHHCCEEEECC	31.31	-
1134	Phosphorylation	WVRKTPWYQ------ EHHCCCCCC------	12.92	15229287

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
100	Y	Phosphorylation	Kinase	SRC	P12931	PSP
1102	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
1114	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
1134	Y	Phosphorylation	Kinase	SRC	P12931	PSP
1134	Y	Phosphorylation	Kinase	SRC-FAMILY	-	GPS
1134	Y	Phosphorylation	Kinase	SRC-TYPE TYR-KINASES	-	Uniprot

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ACT_YEAST	ACT1	physical	19736312

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"The phosphorylation of vinculin on tyrosine residues 100 and 1065,mediated by SRC kinases, affects cell spreading.";
Zhang Z., Izaguirre G., Lin S.-Y., Lee H.Y., Schaefer E.,Haimovich B.;
Mol. Biol. Cell 15:4234-4247(2004).
Cited for: PHOSPHORYLATION AT TYR-100 AND TYR-1134, FUNCTION, AND MUTAGENESIS OFTYR-100; TYR-160; TYR-537; TYR-692; TYR-822 AND TYR-1134.
PubMed: 15229287