dbPTM

VINC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VINC_HUMAN
UniProt AC	P18206
Protein Name	Vinculin
Gene Name	VCL
Organism	Homo sapiens (Human).
Sequence Length	1134
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	MPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVEKMSAEINEIIRVLQLTSWDEDAWASKDTEAMKRALASIDSKLNQAKGWLRDPSASPGDAGEQAIRQILDEAGKVGELCAGKERREILGTCKMLGQMTDQVADLRARGQGSSPVAMQKAQQVSQGLDVLTAKVENAARKLEAMTNSKQSIAKKIDAAQNWLADPNGGPEGEEQIRGALAEARKIAELCDDPKERDDILRSLGEISALTSKLADLRRQGKGDSPEARALAKQVATALQNLQTKTNRAVANSRPAKAAVHLEGKIEQAQRWIDNPTVDDRGVGQAAIRGLVAEGHRLANVMMGPYRQDLLAKCDRVDQLTAQLADLAARGEGESPQARALASQLQDSLKDLKARMQEAMTQEVSDVFSDTTTPIKLLAVAATAPPDAPNREEVFDERAANFENHSGKLGATAEKAAAVGTANKSTVEGIQASVKTARELTPQVVSAARILLRNPGNQAAYEHFETMKNQWIDNVEKMTGLVDEAIDTKSLLDASEEAIKKDLDKCKVAMANIQPQMLVAGATSIARRANRILLVAKREVENSEDPKFREAVKAASDELSKTISPMVMDAKAVAGNISDPGLQKSFLDSGYRILGAVAKVREAFQPQEPDFPPPPPDLEQLRLTDELAPPKPPLPEGEVPPPRPPPPEEKDEEFPEQKAGEVINQPMMMAARQLHDEARKWSSKPGIPAAEVGIGVVAEADAADAAGFPVPPDMEDDYEPELLLMPSNQPVNQPILAAAQSLHREATKWSSKGNDIIAAAKRMALLMAEMSRLVRGGSGTKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTVKATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVRKTPWYQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MPVFHTRTIESILEP CCCCCCCCHHHHHHH	30.19	27251275
26	Sulfoxidation	QISHLVIMHEEGEVD HCCCEEEECCCCCCC	2.25	30846556
52	Phosphorylation	AAVQAAVSNLVRVGK HHHHHHHHHHHHCCC	21.51	22673903
59	Malonylation	SNLVRVGKETVQTTE HHHHHCCCCCCCCCH	47.56	26320211
59	Ubiquitination	SNLVRVGKETVQTTE HHHHHCCCCCCCCCH	47.56	-
71	2-Hydroxyisobutyrylation	TTEDQILKRDMPPAF CCHHHHHHCCCCHHH	48.24	-
71	Acetylation	TTEDQILKRDMPPAF CCHHHHHHCCCCHHH	48.24	7668235
71	Succinylation	TTEDQILKRDMPPAF CCHHHHHHCCCCHHH	48.24	23954790
71	Ubiquitination	TTEDQILKRDMPPAF CCHHHHHHCCCCHHH	48.24	-
74	Sulfoxidation	DQILKRDMPPAFIKV HHHHHCCCCHHHHHH	5.07	30846556
85	S-nitrosocysteine	FIKVENACTKLVQAA HHHHHHHHHHHHHHH	5.34	-
85	S-nitrosylation	FIKVENACTKLVQAA HHHHHHHHHHHHHHH	5.34	22178444
87	Acetylation	KVENACTKLVQAAQM HHHHHHHHHHHHHHH	46.69	26051181
94	Sulfoxidation	KLVQAAQMLQSDPYS HHHHHHHHHHCCCCC	2.93	30846556
97	Phosphorylation	QAAQMLQSDPYSVPA HHHHHHHCCCCCCCH	36.27	26356563
100	Phosphorylation	QMLQSDPYSVPARDY HHHHCCCCCCCHHHE	27.56	26356563
101	Phosphorylation	MLQSDPYSVPARDYL HHHCCCCCCCHHHEE	27.32	26356563
107	Phosphorylation	YSVPARDYLIDGSRG CCCCHHHEEEECCCC	10.45	29457462
112	Phosphorylation	RDYLIDGSRGILSGT HHEEEECCCCCCCCC	24.48	21712546
117	Phosphorylation	DGSRGILSGTSDLLL ECCCCCCCCCCCEEE	37.80	26657352
144	Phosphorylation	VCKGILEYLTVAEVV HHHHHHHHHCHHHHH	12.29	24275569
146 (in isoform 3)	Ubiquitination	-	19.44	21890473
154	Sulfoxidation	VAEVVETMEDLVTYT HHHHHHHHHHHHHHH	2.09	30846556
170	Malonylation	NLGPGMTKMAKMIDE CCCCCHHHHHHHHHH	28.15	26320211
173	2-Hydroxyisobutyrylation	PGMTKMAKMIDERQQ CCHHHHHHHHHHHHH	32.65	-
173	Acetylation	PGMTKMAKMIDERQQ CCHHHHHHHHHHHHH	32.65	19608861
173	Malonylation	PGMTKMAKMIDERQQ CCHHHHHHHHHHHHH	32.65	26320211
190	Sulfoxidation	THQEHRVMLVNSMNT CCCHHHHHHHHCHHH	3.31	21406390
195	Sulfoxidation	RVMLVNSMNTVKELL HHHHHHCHHHHHHHH	4.04	30846556
199	Ubiquitination	VNSMNTVKELLPVLI HHCHHHHHHHHHHHH	40.37	-
207	Phosphorylation	ELLPVLISAMKIFVT HHHHHHHHHHHHEEE	20.39	21712546
209	Sulfoxidation	LPVLISAMKIFVTTK HHHHHHHHHHEEECC	2.46	30846556
216	2-Hydroxyisobutyrylation	MKIFVTTKNSKNQGI HHHEEECCCCCCCCH	50.27	-
216	Ubiquitination	MKIFVTTKNSKNQGI HHHEEECCCCCCCCH	50.27	-
219	2-Hydroxyisobutyrylation	FVTTKNSKNQGIEEA EEECCCCCCCCHHHH	63.78	-
219	Ubiquitination	FVTTKNSKNQGIEEA EEECCCCCCCCHHHH	63.78	21890473
219 (in isoform 1)	Ubiquitination	-	63.78	21890473
219 (in isoform 2)	Ubiquitination	-	63.78	21890473
228	Malonylation	QGIEEALKNRNFTVE CCHHHHHHCCCCCHH	61.99	26320211
228	Ubiquitination	QGIEEALKNRNFTVE CCHHHHHHCCCCCHH	61.99	-
237	Sulfoxidation	RNFTVEKMSAEINEI CCCCHHHHHHHHHHH	2.65	30846556
252	Phosphorylation	IRVLQLTSWDEDAWA HHHHHCCCCCCCHHH	40.91	21712546
260	Phosphorylation	WDEDAWASKDTEAMK CCCCHHHCCCHHHHH	21.99	28192239
263	Phosphorylation	DAWASKDTEAMKRAL CHHHCCCHHHHHHHH	29.40	28857561
272	Phosphorylation	AMKRALASIDSKLNQ HHHHHHHHHHHHHHH	27.98	22617229
275	Phosphorylation	RALASIDSKLNQAKG HHHHHHHHHHHHCCC	37.05	30266825
276	2-Hydroxyisobutyrylation	ALASIDSKLNQAKGW HHHHHHHHHHHCCCC	47.94	-
276	Acetylation	ALASIDSKLNQAKGW HHHHHHHHHHHCCCC	47.94	23236377
288	Phosphorylation	KGWLRDPSASPGDAG CCCCCCCCCCCCHHH	45.74	19664994
290	Phosphorylation	WLRDPSASPGDAGEQ CCCCCCCCCCHHHHH	33.48	19664994
308	Ubiquitination	QILDEAGKVGELCAG HHHHHHCCHHHHHCC	54.86	-
316	2-Hydroxyisobutyrylation	VGELCAGKERREILG HHHHHCCHHHHHHHH	29.53	-
316	Acetylation	VGELCAGKERREILG HHHHHCCHHHHHHHH	29.53	26051181
316	Malonylation	VGELCAGKERREILG HHHHHCCHHHHHHHH	29.53	26320211
316	Ubiquitination	VGELCAGKERREILG HHHHHCCHHHHHHHH	29.53	-
324	Phosphorylation	ERREILGTCKMLGQM HHHHHHHHHHHHHCC	12.90	29970186
326	2-Hydroxyisobutyrylation	REILGTCKMLGQMTD HHHHHHHHHHHCCHH	36.68	-
326	Acetylation	REILGTCKMLGQMTD HHHHHHHHHHHCCHH	36.68	23236377
327	Sulfoxidation	EILGTCKMLGQMTDQ HHHHHHHHHHCCHHH	5.74	30846556
331	Sulfoxidation	TCKMLGQMTDQVADL HHHHHHCCHHHHHHH	4.18	30846556
332	Phosphorylation	CKMLGQMTDQVADLR HHHHHCCHHHHHHHH	18.52	20068231
345	Phosphorylation	LRARGQGSSPVAMQK HHHCCCCCCHHHHHH	24.47	29255136
346	Phosphorylation	RARGQGSSPVAMQKA HHCCCCCCHHHHHHH	30.16	29255136
350	Sulfoxidation	QGSSPVAMQKAQQVS CCCCHHHHHHHHHHH	4.23	30846556
352	Malonylation	SSPVAMQKAQQVSQG CCHHHHHHHHHHHHC	34.77	26320211
357	Phosphorylation	MQKAQQVSQGLDVLT HHHHHHHHHCHHHHH	17.75	26657352
364	Phosphorylation	SQGLDVLTAKVENAA HHCHHHHHHHHHHHH	25.04	26852163
366	2-Hydroxyisobutyrylation	GLDVLTAKVENAARK CHHHHHHHHHHHHHH	44.86	-
366	Acetylation	GLDVLTAKVENAARK CHHHHHHHHHHHHHH	44.86	26051181
366	Ubiquitination	GLDVLTAKVENAARK CHHHHHHHHHHHHHH	44.86	-
366 (in isoform 2)	Ubiquitination	-	44.86	-
377	Sulfoxidation	AARKLEAMTNSKQSI HHHHHHHHHCCHHHH	2.38	30846556
378	Phosphorylation	ARKLEAMTNSKQSIA HHHHHHHHCCHHHHH	43.31	23403867
380	Phosphorylation	KLEAMTNSKQSIAKK HHHHHHCCHHHHHHH	23.94	23403867
383	Phosphorylation	AMTNSKQSIAKKIDA HHHCCHHHHHHHHHH	28.40	23403867
386	Ubiquitination	NSKQSIAKKIDAAQN CCHHHHHHHHHHHHH	48.90	17370265
387	Malonylation	SKQSIAKKIDAAQNW CHHHHHHHHHHHHHH	36.48	26320211
387	Ubiquitination	SKQSIAKKIDAAQNW CHHHHHHHHHHHHHH	36.48	-
409	Methylation	PEGEEQIRGALAEAR HHHHHHHHHHHHHHH	24.83	115919829
426	2-Hydroxyisobutyrylation	AELCDDPKERDDILR HHHCCCHHHHHHHHH	72.82	-
426	Acetylation	AELCDDPKERDDILR HHHCCCHHHHHHHHH	72.82	27452117
426	Malonylation	AELCDDPKERDDILR HHHCCCHHHHHHHHH	72.82	26320211
426	Ubiquitination	AELCDDPKERDDILR HHHCCCHHHHHHHHH	72.82	-
434	Phosphorylation	ERDDILRSLGEISAL HHHHHHHHHHHHHHH	36.96	19664994
439	Phosphorylation	LRSLGEISALTSKLA HHHHHHHHHHHHHHH	16.96	30266825
442	Phosphorylation	LGEISALTSKLADLR HHHHHHHHHHHHHHH	24.43	28355574
443	Phosphorylation	GEISALTSKLADLRR HHHHHHHHHHHHHHH	26.90	22617229
444	Acetylation	EISALTSKLADLRRQ HHHHHHHHHHHHHHC	42.32	23236377
444	Ubiquitination	EISALTSKLADLRRQ HHHHHHHHHHHHHHC	42.32	21890473
444 (in isoform 1)	Ubiquitination	-	42.32	21890473
444 (in isoform 2)	Ubiquitination	-	42.32	21890473
456	Phosphorylation	RRQGKGDSPEARALA HHCCCCCCHHHHHHH	33.05	29514088
464	2-Hydroxyisobutyrylation	PEARALAKQVATALQ HHHHHHHHHHHHHHH	46.27	-
464	Ubiquitination	PEARALAKQVATALQ HHHHHHHHHHHHHHH	46.27	21890473
464 (in isoform 1)	Ubiquitination	-	46.27	21890473
464 (in isoform 2)	Ubiquitination	-	46.27	21890473
476	Ubiquitination	ALQNLQTKTNRAVAN HHHHHHHHHHHHHHH	30.73	21890473
476 (in isoform 1)	Ubiquitination	-	30.73	21890473
476 (in isoform 2)	Ubiquitination	-	30.73	21890473
484	Phosphorylation	TNRAVANSRPAKAAV HHHHHHHCCCCHHHH	29.88	20068231
496	2-Hydroxyisobutyrylation	AAVHLEGKIEQAQRW HHHHHCHHHHHHHHH	33.42	-
496	Acetylation	AAVHLEGKIEQAQRW HHHHHCHHHHHHHHH	33.42	19608861
508	Phosphorylation	QRWIDNPTVDDRGVG HHHHHCCCCCCCCHH	42.70	16097034
512	Methylation	DNPTVDDRGVGQAAI HCCCCCCCCHHHHHH	36.91	115919833
533	Sulfoxidation	GHRLANVMMGPYRQD CHHHHCHHCCHHHHH	2.29	30846556
534	Sulfoxidation	HRLANVMMGPYRQDL HHHHCHHCCHHHHHH	4.21	30846556
537	Phosphorylation	ANVMMGPYRQDLLAK HCHHCCHHHHHHHHH	18.38	27259358
544	2-Hydroxyisobutyrylation	YRQDLLAKCDRVDQL HHHHHHHHCCHHHHH	36.32	-
544	Ubiquitination	YRQDLLAKCDRVDQL HHHHHHHHCCHHHHH	36.32	-
545	Glutathionylation	RQDLLAKCDRVDQLT HHHHHHHCCHHHHHH	3.16	22555962
545	S-nitrosylation	RQDLLAKCDRVDQLT HHHHHHHCCHHHHHH	3.16	25040305
552	Phosphorylation	CDRVDQLTAQLADLA CCHHHHHHHHHHHHH	13.51	21406692
566	Phosphorylation	AARGEGESPQARALA HHCCCCCCHHHHHHH	32.92	27422710
574	Phosphorylation	PQARALASQLQDSLK HHHHHHHHHHHHHHH	32.07	22617229
579	Phosphorylation	LASQLQDSLKDLKAR HHHHHHHHHHHHHHH	25.10	19664994
581	2-Hydroxyisobutyrylation	SQLQDSLKDLKARMQ HHHHHHHHHHHHHHH	66.04	-
581	Ubiquitination	SQLQDSLKDLKARMQ HHHHHHHHHHHHHHH	66.04	21890473
581 (in isoform 1)	Ubiquitination	-	66.04	21890473
581 (in isoform 2)	Ubiquitination	-	66.04	21890473
584	Ubiquitination	QDSLKDLKARMQEAM HHHHHHHHHHHHHHH	44.04	-
587	Sulfoxidation	LKDLKARMQEAMTQE HHHHHHHHHHHHHHH	5.15	30846556
591	Sulfoxidation	KARMQEAMTQEVSDV HHHHHHHHHHHHHHH	3.80	30846556
596	Phosphorylation	EAMTQEVSDVFSDTT HHHHHHHHHHHCCCC	27.57	23403867
600	Phosphorylation	QEVSDVFSDTTTPIK HHHHHHHCCCCCCCH	33.62	21955146
602	Phosphorylation	VSDVFSDTTTPIKLL HHHHHCCCCCCCHHE	31.22	30278072
603	Phosphorylation	SDVFSDTTTPIKLLA HHHHCCCCCCCHHEH	35.25	30278072
604	Phosphorylation	DVFSDTTTPIKLLAV HHHCCCCCCCHHEHH	25.71	30278072
614	Phosphorylation	KLLAVAATAPPDAPN HHEHHHHCCCCCCCC	29.93	29523821
622	Methylation	APPDAPNREEVFDER CCCCCCCHHHHHCHH	40.15	115919837
637	Phosphorylation	AANFENHSGKLGATA HHHCCCCCCCCCHHH	49.56	27251275
639	Ubiquitination	NFENHSGKLGATAEK HCCCCCCCCCHHHHH	46.92	-
643	Phosphorylation	HSGKLGATAEKAAAV CCCCCCHHHHHHHHH	33.28	23312004
646	2-Hydroxyisobutyrylation	KLGATAEKAAAVGTA CCCHHHHHHHHHCCC	40.64	-
652	Phosphorylation	EKAAAVGTANKSTVE HHHHHHCCCCHHHHH	22.06	26307563
655	Ubiquitination	AAVGTANKSTVEGIQ HHHCCCCHHHHHHHH	45.07	21906983
655 (in isoform 1)	Ubiquitination	-	45.07	21890473
655 (in isoform 2)	Ubiquitination	-	45.07	21890473
656	Phosphorylation	AVGTANKSTVEGIQA HHCCCCHHHHHHHHH	37.18	28857561
657	Phosphorylation	VGTANKSTVEGIQAS HCCCCHHHHHHHHHH	24.96	21406692
664	Phosphorylation	TVEGIQASVKTAREL HHHHHHHHHHHHHHH	14.05	21406692
666	2-Hydroxyisobutyrylation	EGIQASVKTARELTP HHHHHHHHHHHHHCH	33.69	-
666	Ubiquitination	EGIQASVKTARELTP HHHHHHHHHHHHHCH	33.69	-
672	Phosphorylation	VKTARELTPQVVSAA HHHHHHHCHHHHHHH	13.61	28985074
677	Phosphorylation	ELTPQVVSAARILLR HHCHHHHHHHHHHHH	19.84	28060719
692	Phosphorylation	NPGNQAAYEHFETMK CCCCHHHHHHHHHHH	16.98	21082442
697	Phosphorylation	AAYEHFETMKNQWID HHHHHHHHHHHHHHH	32.28	28152594
698	Sulfoxidation	AYEHFETMKNQWIDN HHHHHHHHHHHHHHH	2.78	30846556
699	Acetylation	YEHFETMKNQWIDNV HHHHHHHHHHHHHHH	54.10	23236377
699	Ubiquitination	YEHFETMKNQWIDNV HHHHHHHHHHHHHHH	54.10	21890473
699 (in isoform 1)	Ubiquitination	-	54.10	21890473
699 (in isoform 2)	Ubiquitination	-	54.10	21890473
708	Ubiquitination	QWIDNVEKMTGLVDE HHHHHHHHHHCCCCH	37.16	-
710	Phosphorylation	IDNVEKMTGLVDEAI HHHHHHHHCCCCHHH	38.13	28857561
719	Phosphorylation	LVDEAIDTKSLLDAS CCCHHHCHHHHHHHC	19.20	22617229
720	2-Hydroxyisobutyrylation	VDEAIDTKSLLDASE CCHHHCHHHHHHHCH	35.04	-
720	Ubiquitination	VDEAIDTKSLLDASE CCHHHCHHHHHHHCH	35.04	-
721	Phosphorylation	DEAIDTKSLLDASEE CHHHCHHHHHHHCHH	35.94	19664994
726	Phosphorylation	TKSLLDASEEAIKKD HHHHHHHCHHHHHHH	35.32	23927012
731	2-Hydroxyisobutyrylation	DASEEAIKKDLDKCK HHCHHHHHHHHHHHC	47.48	-
731	Acetylation	DASEEAIKKDLDKCK HHCHHHHHHHHHHHC	47.48	26051181
731	Ubiquitination	DASEEAIKKDLDKCK HHCHHHHHHHHHHHC	47.48	-
741	Sulfoxidation	LDKCKVAMANIQPQM HHHHCHHHHCCCHHH	3.08	30846556
748	Sulfoxidation	MANIQPQMLVAGATS HHCCCHHHHHHCHHH	4.07	30846556
754	Phosphorylation	QMLVAGATSIARRAN HHHHHCHHHHHHHHH	21.54	26846344
755	Phosphorylation	MLVAGATSIARRANR HHHHCHHHHHHHHHH	17.45	26846344
768	2-Hydroxyisobutyrylation	NRILLVAKREVENSE HHHEEEEEHHHCCCC	41.43	-
768	Acetylation	NRILLVAKREVENSE HHHEEEEEHHHCCCC	41.43	7681199
768	Malonylation	NRILLVAKREVENSE HHHEEEEEHHHCCCC	41.43	26320211
768	Ubiquitination	NRILLVAKREVENSE HHHEEEEEHHHCCCC	41.43	-
774	Phosphorylation	AKREVENSEDPKFRE EEHHHCCCCCHHHHH	29.85	21082442
778	Ubiquitination	VENSEDPKFREAVKA HCCCCCHHHHHHHHH	70.18	-
784	Malonylation	PKFREAVKAASDELS HHHHHHHHHHHHHHH	45.33	26320211
784	Ubiquitination	PKFREAVKAASDELS HHHHHHHHHHHHHHH	45.33	-
784 (in isoform 2)	Ubiquitination	-	45.33	-
787	Phosphorylation	REAVKAASDELSKTI HHHHHHHHHHHHHCC	36.16	26657352
791	Phosphorylation	KAASDELSKTISPMV HHHHHHHHHCCCHHH	26.21	30242111
792	Ubiquitination	AASDELSKTISPMVM HHHHHHHHCCCHHHH	63.60	21906983
792 (in isoform 1)	Ubiquitination	-	63.60	21890473
792 (in isoform 2)	Ubiquitination	-	63.60	21890473
793	Phosphorylation	ASDELSKTISPMVMD HHHHHHHCCCHHHHC	24.26	23403867
795	Phosphorylation	DELSKTISPMVMDAK HHHHHCCCHHHHCHH	16.51	23927012
802	Acetylation	SPMVMDAKAVAGNIS CHHHHCHHHHCCCCC	38.85	26051181
802	Ubiquitination	SPMVMDAKAVAGNIS CHHHHCHHHHCCCCC	38.85	-
802 (in isoform 2)	Ubiquitination	-	38.85	-
809	Phosphorylation	KAVAGNISDPGLQKS HHHCCCCCCCHHHHH	41.58	19664994
815	2-Hydroxyisobutyrylation	ISDPGLQKSFLDSGY CCCCHHHHHHHHHHH	48.49	-
815	Acetylation	ISDPGLQKSFLDSGY CCCCHHHHHHHHHHH	48.49	26051181
815	Ubiquitination	ISDPGLQKSFLDSGY CCCCHHHHHHHHHHH	48.49	21890473
815 (in isoform 1)	Ubiquitination	-	48.49	21890473
815 (in isoform 2)	Ubiquitination	-	48.49	21890473
816	Phosphorylation	SDPGLQKSFLDSGYR CCCHHHHHHHHHHHH	20.34	22617229
820	Phosphorylation	LQKSFLDSGYRILGA HHHHHHHHHHHHHHH	39.61	27273156
822	Phosphorylation	KSFLDSGYRILGAVA HHHHHHHHHHHHHHH	9.83	19664994
830	2-Hydroxyisobutyrylation	RILGAVAKVREAFQP HHHHHHHHHHHHHCC	34.91	-
830	Malonylation	RILGAVAKVREAFQP HHHHHHHHHHHHHCC	34.91	26320211
855	Phosphorylation	DLEQLRLTDELAPPK CHHHHCCCCCCCCCC	22.46	29255136
862	Ubiquitination	TDELAPPKPPLPEGE CCCCCCCCCCCCCCC	59.20	-
881	Acetylation	RPPPPEEKDEEFPEQ CCCCCHHCCCCCCHH	69.63	26051181
898	Sulfoxidation	GEVINQPMMMAARQL HHHHCHHHHHHHHHH	1.75	21406390
972	Phosphorylation	PILAAAQSLHREATK HHHHHHHHHHHHHHH	22.78	24275569
981	Phosphorylation	HREATKWSSKGNDII HHHHHHHHHCCHHHH	24.59	24719451
982	Phosphorylation	REATKWSSKGNDIIA HHHHHHHHCCHHHHH	43.39	28857561
983	2-Hydroxyisobutyrylation	EATKWSSKGNDIIAA HHHHHHHCCHHHHHH	57.10	-
983	Malonylation	EATKWSSKGNDIIAA HHHHHHHCCHHHHHH	57.10	26320211
983	Ubiquitination	EATKWSSKGNDIIAA HHHHHHHCCHHHHHH	57.10	21890473
983 (in isoform 1)	Ubiquitination	-	57.10	21890473
992	2-Hydroxyisobutyrylation	NDIIAAAKRMALLMA HHHHHHHHHHHHHHH	37.67	-
992	Acetylation	NDIIAAAKRMALLMA HHHHHHHHHHHHHHH	37.67	7617863
992	Succinylation	NDIIAAAKRMALLMA HHHHHHHHHHHHHHH	37.67	23954790
993	Methylation	DIIAAAKRMALLMAE HHHHHHHHHHHHHHH	15.75	30761523
994	Sulfoxidation	IIAAAKRMALLMAEM HHHHHHHHHHHHHHH	2.80	30846556
996 (in isoform 2)	Ubiquitination	-	2.16	-
998	Sulfoxidation	AKRMALLMAEMSRLV HHHHHHHHHHHHHHH	2.86	30846556
1001	Sulfoxidation	MALLMAEMSRLVRGG HHHHHHHHHHHHCCC	1.73	30846556
1002	Phosphorylation	ALLMAEMSRLVRGGS HHHHHHHHHHHCCCC	17.61	25599653
1002 (in isoform 2)	Ubiquitination	-	17.61	21890473
1003	Methylation	LLMAEMSRLVRGGSG HHHHHHHHHHCCCCC	35.57	30761529
1009	Phosphorylation	SRLVRGGSGTKRALI HHHHCCCCCHHHHHH	46.22	29514088
1011	Phosphorylation	LVRGGSGTKRALIQC HHCCCCCHHHHHHHH	21.03	29514088
1020	2-Hydroxyisobutyrylation	RALIQCAKDIAKASD HHHHHHHHHHHHCCH	58.24	-
1020	Acetylation	RALIQCAKDIAKASD HHHHHHHHHHHHCCH	58.24	26051181
1020	Malonylation	RALIQCAKDIAKASD HHHHHHHHHHHHCCH	58.24	26320211
1020	Succinylation	RALIQCAKDIAKASD HHHHHHHHHHHHCCH	58.24	23954790
1020	Ubiquitination	RALIQCAKDIAKASD HHHHHHHHHHHHCCH	58.24	-
1024	2-Hydroxyisobutyrylation	QCAKDIAKASDEVTR HHHHHHHHCCHHHHH	49.08	-
1024	Acetylation	QCAKDIAKASDEVTR HHHHHHHHCCHHHHH	49.08	26051181
1024	Malonylation	QCAKDIAKASDEVTR HHHHHHHHCCHHHHH	49.08	26320211
1034	2-Hydroxyisobutyrylation	DEVTRLAKEVAKQCT HHHHHHHHHHHHHCC	58.26	-
1053	S-nitrosylation	RTNLLQVCERIPTIS HHHHHHHHHHCCCHH	1.55	25040305
1053	S-palmitoylation	RTNLLQVCERIPTIS HHHHHHHHHHCCCHH	1.55	29575903
1058	Phosphorylation	QVCERIPTISTQLKI HHHHHCCCHHHHHHH	25.78	21712546
1060	Phosphorylation	CERIPTISTQLKILS HHHCCCHHHHHHHHH	16.75	21712546
1061	Phosphorylation	ERIPTISTQLKILST HHCCCHHHHHHHHHH	33.79	20068231
1064	Ubiquitination	PTISTQLKILSTVKA CCHHHHHHHHHHHHH	31.61	-
1070	2-Hydroxyisobutyrylation	LKILSTVKATMLGRT HHHHHHHHHHHCCCC	37.92	-
1070	Acetylation	LKILSTVKATMLGRT HHHHHHHHHHHCCCC	37.92	87849
1070	Ubiquitination	LKILSTVKATMLGRT HHHHHHHHHHHCCCC	37.92	2190698
1070 (in isoform 1)	Ubiquitination	-	37.92	21890473
1077	Phosphorylation	KATMLGRTNISDEES HHHHCCCCCCCHHHH	34.80	21406692
1080	Phosphorylation	MLGRTNISDEESEQA HCCCCCCCHHHHHHH	40.83	22199227
1084	Phosphorylation	TNISDEESEQATEML CCCCHHHHHHHHHHH	32.72	21406692
1088	Phosphorylation	DEESEQATEMLVHNA HHHHHHHHHHHHHHH	22.94	27251275
1090	Sulfoxidation	ESEQATEMLVHNAQN HHHHHHHHHHHHHHH	4.04	28465586
1099	Sulfoxidation	VHNAQNLMQSVKETV HHHHHHHHHHHHHHH	3.51	30846556
1101	Phosphorylation	NAQNLMQSVKETVRE HHHHHHHHHHHHHHH	22.61	21406692
1113	Phosphorylation	VREAEAASIKIRTDA HHHHHHHCCEEEECC	31.31	28258704
1115	2-Hydroxyisobutyrylation	EAEAASIKIRTDAGF HHHHHCCEEEECCCC	24.52	-
1118	Phosphorylation	AASIKIRTDAGFTLR HHCCEEEECCCCEEE	33.40	23403867
1123	Phosphorylation	IRTDAGFTLRWVRKT EEECCCCEEEEHHCC	17.94	19664994
1130	Phosphorylation	TLRWVRKTPWYQ--- EEEEHHCCCCCC---	14.43	24719451
1133	Phosphorylation	WVRKTPWYQ------ EHHCCCCCC------	12.92	16712796

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	GPS
1065	Y	Phosphorylation	Kinase	SRC	P12931	GPS
1101	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
1113	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
1133	Y	Phosphorylation	Kinase	SRC-FAMILY	-	GPS
1133	Y	Phosphorylation	Kinase	SRC-TYPE TYR-KINASES	-	Uniprot

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ABI2_HUMAN	ABI2	physical	16189514
CS057_HUMAN	C19orf57	physical	16189514
COR2B_HUMAN	CORO2B	physical	10224093
RAVR1_MOUSE	Raver1	physical	11724819
SRBS1_HUMAN	SORBS1	physical	10085297
CLH1_HUMAN	CLTC	physical	8276759
DAG1_HUMAN	DAG1	physical	18341635
TBA1A_HUMAN	TUBA1A	physical	18341635
ZCCHL_HUMAN	ZC3HAV1L	physical	22939629
ASNS_HUMAN	ASNS	physical	22863883
PYRG1_HUMAN	CTPS1	physical	22863883
ECHM_HUMAN	ECHS1	physical	22863883
IF5_HUMAN	EIF5	physical	22863883
FERM2_HUMAN	FERMT2	physical	22863883
PSF3_HUMAN	GINS3	physical	22863883
GSHB_HUMAN	GSS	physical	22863883
GRP78_HUMAN	HSPA5	physical	22863883
GRP75_HUMAN	HSPA9	physical	22863883
MOES_HUMAN	MSN	physical	22863883
PDC10_HUMAN	PDCD10	physical	22863883
ODPA_HUMAN	PDHA1	physical	22863883
PDIA4_HUMAN	PDIA4	physical	22863883
IPP2_HUMAN	PPP1R2	physical	22863883
PPP5_HUMAN	PPP5C	physical	22863883
GDS1_HUMAN	RAP1GDS1	physical	22863883
1433S_HUMAN	SFN	physical	22863883
RUXF_HUMAN	SNRPF	physical	22863883
STK24_HUMAN	STK24	physical	22863883
TBB3_HUMAN	TUBB3	physical	22863883
UBFD1_HUMAN	UBFD1	physical	22863883
1433F_HUMAN	YWHAH	physical	22863883
VINC_HUMAN	VCL	physical	25416956
TEKT1_HUMAN	TEKT1	physical	25416956
FERM2_HUMAN	FERMT2	physical	26344197
PICAL_HUMAN	PICALM	physical	26344197
PAXI_HUMAN	PXN	physical	26344197
LPXN_HUMAN	LPXN	physical	21516116
ACTG_HUMAN	ACTG1	physical	26496610
CAPZB_HUMAN	CAPZB	physical	26496610
CTNA1_HUMAN	CTNNA1	physical	26496610
MYO1C_HUMAN	MYO1C	physical	26496610
RS27A_HUMAN	RPS27A	physical	26496610
SPTN1_HUMAN	SPTAN1	physical	26496610
TLN1_HUMAN	TLN1	physical	26496610
MPDZ_HUMAN	MPDZ	physical	26496610
AP3M1_HUMAN	AP3M1	physical	26496610
LIMA1_HUMAN	LIMA1	physical	26496610
PPHLN_HUMAN	PPHLN1	physical	26496610
RBM26_HUMAN	RBM26	physical	26496610
GKAP1_HUMAN	GKAP1	physical	26496610
ASCC2_HUMAN	ASCC2	physical	26496610
TT21B_HUMAN	TTC21B	physical	27173435
UBE2N_HUMAN	UBE2N	physical	27173435

Drug and Disease Associations

Kegg Disease
H00292	Hypertrophic cardiomyopathy (HCM)
H00294	Dilated cardiomyopathy (DCM)
OMIM Disease
611407	Cardiomyopathy, dilated 1W (CMD1W)
613255	Cardiomyopathy, familial hypertrophic 15 (CMH15)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of VINC_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173 AND LYS-496, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-290; SER-721 ANDTYR-822, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; THR-604 ANDSER-721, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC."; Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.; Proteomics 5:3589-3599(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-508, AND MASSSPECTROMETRY.	16097034 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-822, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-822, AND MASSSPECTROMETRY.	17389395 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-692 AND TYR-822, ANDMASS SPECTROMETRY.	18083107 [Abstract]
"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-1133, AND MASS SPECTROMETRY.	15229287 [Abstract]