dbPTM

VIME_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VIME_HUMAN
UniProt AC	P08670
Protein Name	Vimentin
Gene Name	VIM
Organism	Homo sapiens (Human).
Sequence Length	466
Subcellular Localization	Cytoplasm . Cytoplasm, cytoskeleton . Nucleus matrix .
Protein Description	Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally.; Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2..
Protein Sequence	MSTRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGVYATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSTRSVSSS ------CCCCCCCCH	32.31	20068231
2	Phosphorylation	------MSTRSVSSS ------CCCCCCCCH	32.31	22199227
3	Phosphorylation	-----MSTRSVSSSS -----CCCCCCCCHH	26.18	22199227
4	Methylation	----MSTRSVSSSSY ----CCCCCCCCHHH	27.96	115367719
5	Phosphorylation	---MSTRSVSSSSYR ---CCCCCCCCHHHH	26.83	30266825
5	O-linked_Glycosylation	---MSTRSVSSSSYR ---CCCCCCCCHHHH	26.83	31492838
7	O-linked_Glycosylation	-MSTRSVSSSSYRRM -CCCCCCCCHHHHHH	26.25	31492838
7	Phosphorylation	-MSTRSVSSSSYRRM -CCCCCCCCHHHHHH	26.25	29255136
7	O-linked_Glycosylation	-MSTRSVSSSSYRRM -CCCCCCCCHHHHHH	26.25	19664995
8	Phosphorylation	MSTRSVSSSSYRRMF CCCCCCCCHHHHHHH	22.58	30266825
9	Phosphorylation	STRSVSSSSYRRMFG CCCCCCCHHHHHHHC	24.71	30266825
10	Phosphorylation	TRSVSSSSYRRMFGG CCCCCCHHHHHHHCC	25.30	28355574
11	Nitrated tyrosine	RSVSSSSYRRMFGGP CCCCCHHHHHHHCCC	12.27	-
11	Phosphorylation	RSVSSSSYRRMFGGP CCCCCHHHHHHHCCC	12.27	26329039
12	Methylation	SVSSSSYRRMFGGPG CCCCHHHHHHHCCCC	26.07	80701209
13	Methylation	VSSSSYRRMFGGPGT CCCHHHHHHHCCCCC	19.29	80701221
14	Sulfoxidation	SSSSYRRMFGGPGTA CCHHHHHHHCCCCCC	2.43	21406390
20	Phosphorylation	RMFGGPGTASRPSSS HHHCCCCCCCCCCCC	25.29	29255136
20	O-linked_Glycosylation	RMFGGPGTASRPSSS HHHCCCCCCCCCCCC	25.29	31492838
22	Phosphorylation	FGGPGTASRPSSSRS HCCCCCCCCCCCCCC	44.56	29255136
22	O-linked_Glycosylation	FGGPGTASRPSSSRS HCCCCCCCCCCCCCC	44.56	31492838
23	Methylation	GGPGTASRPSSSRSY CCCCCCCCCCCCCCE	32.43	80701233
25	Phosphorylation	PGTASRPSSSRSYVT CCCCCCCCCCCCEEE	39.57	29255136
25	O-linked_Glycosylation	PGTASRPSSSRSYVT CCCCCCCCCCCCEEE	39.57	31492838
26	Phosphorylation	GTASRPSSSRSYVTT CCCCCCCCCCCEEEE	32.24	29255136
26	O-linked_Glycosylation	GTASRPSSSRSYVTT CCCCCCCCCCCEEEE	32.24	31492838
27	Phosphorylation	TASRPSSSRSYVTTS CCCCCCCCCCEEEEC	29.59	23401153
27	O-linked_Glycosylation	TASRPSSSRSYVTTS CCCCCCCCCCEEEEC	29.59	31492838
28	Methylation	ASRPSSSRSYVTTST CCCCCCCCCEEEECC	33.67	80701245
29	Phosphorylation	SRPSSSRSYVTTSTR CCCCCCCCEEEECCC	26.38	23401153
29	O-linked_Glycosylation	SRPSSSRSYVTTSTR CCCCCCCCEEEECCC	26.38	31492838
30	Phosphorylation	RPSSSRSYVTTSTRT CCCCCCCEEEECCCE	10.74	23911959
30	Nitration	RPSSSRSYVTTSTRT CCCCCCCEEEECCCE	10.74	-
32	Phosphorylation	SSSRSYVTTSTRTYS CCCCCEEEECCCEEE	13.54	21955146
32	O-linked_Glycosylation	SSSRSYVTTSTRTYS CCCCCEEEECCCEEE	13.54	31492838
33	O-linked_Glycosylation	SSRSYVTTSTRTYSL CCCCEEEECCCEEEC	20.32	31492838
33	Phosphorylation	SSRSYVTTSTRTYSL CCCCEEEECCCEEEC	20.32	21955146
33	O-linked_Glycosylation	SSRSYVTTSTRTYSL CCCCEEEECCCEEEC	20.32	17081983
34	O-linked_Glycosylation	SRSYVTTSTRTYSLG CCCEEEECCCEEECC	13.41	31492838
34	Phosphorylation	SRSYVTTSTRTYSLG CCCEEEECCCEEECC	13.41	23401153
34	O-linked_Glycosylation	SRSYVTTSTRTYSLG CCCEEEECCCEEECC	13.41	2500966
35	Phosphorylation	RSYVTTSTRTYSLGS CCEEEECCCEEECCC	25.57	21955146
35	O-linked_Glycosylation	RSYVTTSTRTYSLGS CCEEEECCCEEECCC	25.57	31492838
36	Methylation	SYVTTSTRTYSLGSA CEEEECCCEEECCCC	31.28	30761517
37	Phosphorylation	YVTTSTRTYSLGSAL EEEECCCEEECCCCC	19.97	30266825
37	O-linked_Glycosylation	YVTTSTRTYSLGSAL EEEECCCEEECCCCC	19.97	31492838
38	Phosphorylation	VTTSTRTYSLGSALR EEECCCEEECCCCCC	9.90	23927012
39	Phosphorylation	TTSTRTYSLGSALRP EECCCEEECCCCCCC	26.16	25159151
39	O-linked_Glycosylation	TTSTRTYSLGSALRP EECCCEEECCCCCCC	26.16	31492838
42	Phosphorylation	TRTYSLGSALRPSTS CCEEECCCCCCCCCC	29.44	23927012
45	Methylation	YSLGSALRPSTSRSL EECCCCCCCCCCCCC	23.88	80701293
47	Phosphorylation	LGSALRPSTSRSLYA CCCCCCCCCCCCCCC	32.36	23927012
47	O-linked_Glycosylation	LGSALRPSTSRSLYA CCCCCCCCCCCCCCC	32.36	31492838
48	Phosphorylation	GSALRPSTSRSLYAS CCCCCCCCCCCCCCC	30.73	23927012
49	Phosphorylation	SALRPSTSRSLYASS CCCCCCCCCCCCCCC	24.98	23927012
49	O-linked_Glycosylation	SALRPSTSRSLYASS CCCCCCCCCCCCCCC	24.98	31492838
50	Methylation	ALRPSTSRSLYASSP CCCCCCCCCCCCCCC	30.67	80701281
51	Phosphorylation	LRPSTSRSLYASSPG CCCCCCCCCCCCCCC	26.04	23927012
53	Phosphorylation	PSTSRSLYASSPGGV CCCCCCCCCCCCCCE	12.99	23927012
55	O-linked_Glycosylation	TSRSLYASSPGGVYA CCCCCCCCCCCCEEE	24.41	31492838
55	Phosphorylation	TSRSLYASSPGGVYA CCCCCCCCCCCCEEE	24.41	22167270
56	Phosphorylation	SRSLYASSPGGVYAT CCCCCCCCCCCEEEE	21.28	22167270
56	O-linked_Glycosylation	SRSLYASSPGGVYAT CCCCCCCCCCCEEEE	21.28	31492838
61	Phosphorylation	ASSPGGVYATRSSAV CCCCCCEEEECCCCC	12.91	23927012
63	Phosphorylation	SPGGVYATRSSAVRL CCCCEEEECCCCCCC	17.25	21945579
63	O-linked_Glycosylation	SPGGVYATRSSAVRL CCCCEEEECCCCCCC	17.25	31492838
64	Methylation	PGGVYATRSSAVRLR CCCEEEECCCCCCCC	22.05	24390813
65	Phosphorylation	GGVYATRSSAVRLRS CCEEEECCCCCCCCC	20.49	22617229
66	Phosphorylation	GVYATRSSAVRLRSS CEEEECCCCCCCCCC	27.74	22617229
69	Methylation	ATRSSAVRLRSSVPG EECCCCCCCCCCCCC	24.89	80701269
71	Methylation	RSSAVRLRSSVPGVR CCCCCCCCCCCCCHH	19.13	80701257
72	Phosphorylation	SSAVRLRSSVPGVRL CCCCCCCCCCCCHHH	40.03	29255136
73	Phosphorylation	SAVRLRSSVPGVRLL CCCCCCCCCCCHHHC	26.37	29255136
83	Phosphorylation	GVRLLQDSVDFSLAD CHHHCCCCCCHHHHH	15.60	26846344
87	Phosphorylation	LQDSVDFSLADAINT CCCCCCHHHHHHHCC	20.41	26846344
94	Phosphorylation	SLADAINTEFKNTRT HHHHHHCCCCCCCCC	36.36	23403867
97	Ubiquitination	DAINTEFKNTRTNEK HHHCCCCCCCCCCCC	51.70	21890473
97	Acetylation	DAINTEFKNTRTNEK HHHCCCCCCCCCCCC	51.70	26051181
99	Phosphorylation	INTEFKNTRTNEKVE HCCCCCCCCCCCCEE	39.19	23403867
101	Phosphorylation	TEFKNTRTNEKVELQ CCCCCCCCCCCEEHH	45.77	23403867
104	Acetylation	KNTRTNEKVELQELN CCCCCCCCEEHHHHH	42.98	21466224
104	Ubiquitination	KNTRTNEKVELQELN CCCCCCCCEEHHHHH	42.98	21890473
104	Malonylation	KNTRTNEKVELQELN CCCCCCCCEEHHHHH	42.98	26320211
104	Sumoylation	KNTRTNEKVELQELN CCCCCCCCEEHHHHH	42.98	28112733
113	Methylation	ELQELNDRFANYIDK EHHHHHHHHHHHHHH	31.35	115919809
117	Phosphorylation	LNDRFANYIDKVRFL HHHHHHHHHHHHHHH	13.68	22617229
120	Methylation	RFANYIDKVRFLEQQ HHHHHHHHHHHHHHH	26.25	-
120	Acetylation	RFANYIDKVRFLEQQ HHHHHHHHHHHHHHH	26.25	19608861
120	Succinylation	RFANYIDKVRFLEQQ HHHHHHHHHHHHHHH	26.25	-
120	Ubiquitination	RFANYIDKVRFLEQQ HHHHHHHHHHHHHHH	26.25	21890473
120	Malonylation	RFANYIDKVRFLEQQ HHHHHHHHHHHHHHH	26.25	26320211
120	Succinylation	RFANYIDKVRFLEQQ HHHHHHHHHHHHHHH	26.25	-
120	Sumoylation	RFANYIDKVRFLEQQ HHHHHHHHHHHHHHH	26.25	28112733
129	Acetylation	RFLEQQNKILLAELE HHHHHHCHHHHHHHH	30.32	25825284
129	Succinylation	RFLEQQNKILLAELE HHHHHHCHHHHHHHH	30.32	-
129	Ubiquitination	RFLEQQNKILLAELE HHHHHHCHHHHHHHH	30.32	21890473
129	Succinylation	RFLEQQNKILLAELE HHHHHHCHHHHHHHH	30.32	21906983
129	Sumoylation	RFLEQQNKILLAELE HHHHHHCHHHHHHHH	30.32	28112733
139	Acetylation	LAELEQLKGQGKSRL HHHHHHHCCCCCCCH	49.21	19608861
139	Ubiquitination	LAELEQLKGQGKSRL HHHHHHHCCCCCCCH	49.21	21890473
139	Glycation	LAELEQLKGQGKSRL HHHHHHHCCCCCCCH	49.21	-
139	Malonylation	LAELEQLKGQGKSRL HHHHHHHCCCCCCCH	49.21	26320211
139	Sumoylation	LAELEQLKGQGKSRL HHHHHHHCCCCCCCH	49.21	28112733
143	Ubiquitination	EQLKGQGKSRLGDLY HHHCCCCCCCHHHHH	25.23	21890473
143	Glycation	EQLKGQGKSRLGDLY HHHCCCCCCCHHHHH	25.23	-
143	Malonylation	EQLKGQGKSRLGDLY HHHCCCCCCCHHHHH	25.23	26320211
144	Phosphorylation	QLKGQGKSRLGDLYE HHCCCCCCCHHHHHH	39.29	30266825
150	Phosphorylation	KSRLGDLYEEEMREL CCCHHHHHHHHHHHH	26.49	23403867
154	Sulfoxidation	GDLYEEEMRELRRQV HHHHHHHHHHHHHHH	4.57	21406390
158	Methylation	EEEMRELRRQVDQLT HHHHHHHHHHHHHHH	23.41	115919813
168	Acetylation	VDQLTNDKARVEVER HHHHHCCHHHHHHCC	39.91	23749302
168	Ubiquitination	VDQLTNDKARVEVER HHHHHCCHHHHHHCC	39.91	21890473
168	Glycation	VDQLTNDKARVEVER HHHHHCCHHHHHHCC	39.91	-
168	Malonylation	VDQLTNDKARVEVER HHHHHCCHHHHHHCC	39.91	26320211
183	Sulfoxidation	DNLAEDIMRLREKLQ CCHHHHHHHHHHHHH	5.23	21406390
184	Methylation	NLAEDIMRLREKLQE CHHHHHHHHHHHHHH	30.81	115919817
188	Acetylation	DIMRLREKLQEEMLQ HHHHHHHHHHHHHHH	49.38	25953088
188	Succinylation	DIMRLREKLQEEMLQ HHHHHHHHHHHHHHH	49.38	-
188	Ubiquitination	DIMRLREKLQEEMLQ HHHHHHHHHHHHHHH	49.38	21890473
188	Malonylation	DIMRLREKLQEEMLQ HHHHHHHHHHHHHHH	49.38	26320211
188	Succinylation	DIMRLREKLQEEMLQ HHHHHHHHHHHHHHH	49.38	-
193	Sulfoxidation	REKLQEEMLQREEAE HHHHHHHHHHHHHHH	3.67	21406390
202	Phosphorylation	QREEAENTLQSFRQD HHHHHHHHHHHHHHH	20.06	30266825
205	Phosphorylation	EAENTLQSFRQDVDN HHHHHHHHHHHHHCH	26.05	23401153
214	Phosphorylation	RQDVDNASLARLDLE HHHHCHHHHHHHHHH	28.90	29255136
223	Acetylation	ARLDLERKVESLQEE HHHHHHHHHHHHHHH	40.76	21466224
223	Ubiquitination	ARLDLERKVESLQEE HHHHHHHHHHHHHHH	40.76	-
223	Malonylation	ARLDLERKVESLQEE HHHHHHHHHHHHHHH	40.76	26320211
223	Sumoylation	ARLDLERKVESLQEE HHHHHHHHHHHHHHH	40.76	28112733
226	Phosphorylation	DLERKVESLQEEIAF HHHHHHHHHHHHHHH	38.04	30266825
235	Acetylation	QEEIAFLKKLHEEEI HHHHHHHHHHCHHHH	47.00	25825284
235	Ubiquitination	QEEIAFLKKLHEEEI HHHHHHHHHHCHHHH	47.00	21906983
235	Malonylation	QEEIAFLKKLHEEEI HHHHHHHHHHCHHHH	47.00	26320211
236	Acetylation	EEIAFLKKLHEEEIQ HHHHHHHHHCHHHHH	58.17	30583443
236	Ubiquitination	EEIAFLKKLHEEEIQ HHHHHHHHHCHHHHH	58.17	-
261	Phosphorylation	VQIDVDVSKPDLTAA CEEEECCCCHHHHHH	33.73	20068231
262	Ubiquitination	QIDVDVSKPDLTAAL EEEECCCCHHHHHHH	42.26	-
262	Glycation	QIDVDVSKPDLTAAL EEEECCCCHHHHHHH	42.26	-
262	Sumoylation	QIDVDVSKPDLTAAL EEEECCCCHHHHHHH	42.26	28112733
266	Phosphorylation	DVSKPDLTAALRDVR CCCCHHHHHHHHHHH	19.77	20068231
276	Phosphorylation	LRDVRQQYESVAAKN HHHHHHHHHHHHHHC	11.22	21945579
276	Nitration	LRDVRQQYESVAAKN HHHHHHHHHHHHHHC	11.22	-
278	Phosphorylation	DVRQQYESVAAKNLQ HHHHHHHHHHHHCHH	16.48	25159151
282	Acetylation	QYESVAAKNLQEAEE HHHHHHHHCHHHHHH	48.75	25953088
282	Ubiquitination	QYESVAAKNLQEAEE HHHHHHHHCHHHHHH	48.75	21890473
282	Malonylation	QYESVAAKNLQEAEE HHHHHHHHCHHHHHH	48.75	26320211
291	Phosphorylation	LQEAEEWYKSKFADL HHHHHHHHHHHHHHH	14.52	25884760
292	Acetylation	QEAEEWYKSKFADLS HHHHHHHHHHHHHHH	48.52	25825284
292	Ubiquitination	QEAEEWYKSKFADLS HHHHHHHHHHHHHHH	48.52	21890473
292	Malonylation	QEAEEWYKSKFADLS HHHHHHHHHHHHHHH	48.52	26320211
293	Phosphorylation	EAEEWYKSKFADLSE HHHHHHHHHHHHHHH	19.80	28857561
294	Acetylation	AEEWYKSKFADLSEA HHHHHHHHHHHHHHH	40.18	25825284
294	Succinylation	AEEWYKSKFADLSEA HHHHHHHHHHHHHHH	40.18	-
294	Ubiquitination	AEEWYKSKFADLSEA HHHHHHHHHHHHHHH	40.18	21890473
294	Malonylation	AEEWYKSKFADLSEA HHHHHHHHHHHHHHH	40.18	26320211
294	Succinylation	AEEWYKSKFADLSEA HHHHHHHHHHHHHHH	40.18	-
294	Sumoylation	AEEWYKSKFADLSEA HHHHHHHHHHHHHHH	40.18	28112733
299	Phosphorylation	KSKFADLSEAANRNN HHHHHHHHHHHHHCH	26.24	30266825
310	Methylation	NRNNDALRQAKQEST HHCHHHHHHHHHHCH	35.81	-
313	Sumoylation	NDALRQAKQESTEYR HHHHHHHHHHCHHHH	46.38	-
313	Ubiquitination	NDALRQAKQESTEYR HHHHHHHHHHCHHHH	46.38	21890473
313	Sumoylation	NDALRQAKQESTEYR HHHHHHHHHHCHHHH	46.38	28112733
313	Acetylation	NDALRQAKQESTEYR HHHHHHHHHHCHHHH	46.38	26051181
313	Glycation	NDALRQAKQESTEYR HHHHHHHHHHCHHHH	46.38	-
313	Succinylation	NDALRQAKQESTEYR HHHHHHHHHHCHHHH	46.38	23954790
316	Phosphorylation	LRQAKQESTEYRRQV HHHHHHHCHHHHHHH	24.84	29514088
317	Phosphorylation	RQAKQESTEYRRQVQ HHHHHHCHHHHHHHH	35.96	29514088
319	Phosphorylation	AKQESTEYRRQVQSL HHHHCHHHHHHHHHH	15.93	21406692
325	Phosphorylation	EYRRQVQSLTCEVDA HHHHHHHHHHHHHHH	27.13	29255136
327	Phosphorylation	RRQVQSLTCEVDALK HHHHHHHHHHHHHHH	16.33	30266825
327	O-linked_Glycosylation	RRQVQSLTCEVDALK HHHHHHHHHHHHHHH	16.33	31492838
328	S-nitrosocysteine	RQVQSLTCEVDALKG HHHHHHHHHHHHHHC	6.10	-
328	Glutathionylation	RQVQSLTCEVDALKG HHHHHHHHHHHHHHC	6.10	22555962
328	S-nitrosylation	RQVQSLTCEVDALKG HHHHHHHHHHHHHHC	6.10	22178444
328	S-palmitoylation	RQVQSLTCEVDALKG HHHHHHHHHHHHHHC	6.10	29575903
334	Acetylation	TCEVDALKGTNESLE HHHHHHHHCCCHHHH	66.46	23749302
334	Ubiquitination	TCEVDALKGTNESLE HHHHHHHHCCCHHHH	66.46	21906983
334	Malonylation	TCEVDALKGTNESLE HHHHHHHHCCCHHHH	66.46	26320211
336	Phosphorylation	EVDALKGTNESLERQ HHHHHHCCCHHHHHH	33.94	23401153
339	Phosphorylation	ALKGTNESLERQMRE HHHCCCHHHHHHHHH	37.29	30266825
344	Sulfoxidation	NESLERQMREMEENF CHHHHHHHHHHHHHH	4.99	30846556
347	Sulfoxidation	LERQMREMEENFAVE HHHHHHHHHHHHHHH	5.74	30846556
358	Phosphorylation	FAVEAANYQDTIGRL HHHHHHCHHHHHHHH	11.75	25884760
361	Phosphorylation	EAANYQDTIGRLQDE HHHCHHHHHHHHHHH	15.14	26670566
372	Sulfoxidation	LQDEIQNMKEEMARH HHHHHHHHHHHHHHH	3.11	21406390
373	Acetylation	QDEIQNMKEEMARHL HHHHHHHHHHHHHHH	59.06	19608861
373	Ubiquitination	QDEIQNMKEEMARHL HHHHHHHHHHHHHHH	59.06	21890473
373	Malonylation	QDEIQNMKEEMARHL HHHHHHHHHHHHHHH	59.06	26320211
373	Sumoylation	QDEIQNMKEEMARHL HHHHHHHHHHHHHHH	59.06	28112733
381	Methylation	EEMARHLREYQDLLN HHHHHHHHHHHHHHC	34.16	-
383	Nitrated tyrosine	MARHLREYQDLLNVK HHHHHHHHHHHHCHH	10.82	-
383	Phosphorylation	MARHLREYQDLLNVK HHHHHHHHHHHHCHH	10.82	29496907
391	Sulfoxidation	QDLLNVKMALDIEIA HHHHCHHHHHHHHHH	3.79	28183972
400	Phosphorylation	LDIEIATYRKLLEGE HHHHHHHHHHHHCCC	9.20	18083107
401	Methylation	DIEIATYRKLLEGEE HHHHHHHHHHHCCCC	20.84	115384113
402	Acetylation	IEIATYRKLLEGEES HHHHHHHHHHCCCCC	47.19	22631371
402	Sumoylation	IEIATYRKLLEGEES HHHHHHHHHHCCCCC	47.19	-
402	Ubiquitination	IEIATYRKLLEGEES HHHHHHHHHHCCCCC	47.19	21906983
402	Sumoylation	IEIATYRKLLEGEES HHHHHHHHHHCCCCC	47.19	-
409	Phosphorylation	KLLEGEESRISLPLP HHHCCCCCCCCCCCC	30.52	30266825
410	Methylation	LLEGEESRISLPLPN HHCCCCCCCCCCCCC	26.29	115384127
412	Phosphorylation	EGEESRISLPLPNFS CCCCCCCCCCCCCCC	23.87	29255136
419	Phosphorylation	SLPLPNFSSLNLRET CCCCCCCCCCCCCCC	40.32	29255136
420	Phosphorylation	LPLPNFSSLNLRETN CCCCCCCCCCCCCCC	19.69	29255136
426	Phosphorylation	SSLNLRETNLDSLPL CCCCCCCCCCCCCCC	34.35	29255136
430	Phosphorylation	LRETNLDSLPLVDTH CCCCCCCCCCCCCCC	34.74	29255136
436	Phosphorylation	DSLPLVDTHSKRTLL CCCCCCCCCCCCEEE	22.14	29255136
438	Phosphorylation	LPLVDTHSKRTLLIK CCCCCCCCCCEEEEE	26.40	29255136
439	Acetylation	PLVDTHSKRTLLIKT CCCCCCCCCEEEEEE	41.62	25953088
439	Ubiquitination	PLVDTHSKRTLLIKT CCCCCCCCCEEEEEE	41.62	21890473
439	Malonylation	PLVDTHSKRTLLIKT CCCCCCCCCEEEEEE	41.62	26320211
439	Sumoylation	PLVDTHSKRTLLIKT CCCCCCCCCEEEEEE	41.62	28112733
441	Phosphorylation	VDTHSKRTLLIKTVE CCCCCCCEEEEEEEE	29.65	23403867
445	Methylation	SKRTLLIKTVETRDG CCCEEEEEEEECCCC	46.62	22631395
445	Acetylation	SKRTLLIKTVETRDG CCCEEEEEEEECCCC	46.62	19608861
445	Succinylation	SKRTLLIKTVETRDG CCCEEEEEEEECCCC	46.62	-
445	Ubiquitination	SKRTLLIKTVETRDG CCCEEEEEEEECCCC	46.62	21890473
445	Sumoylation	SKRTLLIKTVETRDG CCCEEEEEEEECCCC	46.62	19608861
445	Glycation	SKRTLLIKTVETRDG CCCEEEEEEEECCCC	46.62	-
445	Malonylation	SKRTLLIKTVETRDG CCCEEEEEEEECCCC	46.62	26320211
445	Succinylation	SKRTLLIKTVETRDG CCCEEEEEEEECCCC	46.62	-
446	Phosphorylation	KRTLLIKTVETRDGQ CCEEEEEEEECCCCC	19.31	21712546
449	Phosphorylation	LLIKTVETRDGQVIN EEEEEEECCCCCEEC	29.71	24732914
458	Phosphorylation	DGQVINETSQHHDDL CCCEECCCCCCCCCC	29.24	22167270
459	Phosphorylation	GQVINETSQHHDDLE CCEECCCCCCCCCCC	22.72	22167270

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
5	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
5	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
7	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
7	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
7	S	Phosphorylation	Kinase	PKA	-	Uniprot
7	S	Phosphorylation	Kinase	PKC	-	Uniprot
8	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
8	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
9	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
9	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
9	S	Phosphorylation	Kinase	PKC	-	Uniprot
10	S	Phosphorylation	Kinase	PKC	-	Uniprot
10	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
10	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
26	S	Phosphorylation	Kinase	PAK_GROUP	-	PhosphoELM
26	S	Phosphorylation	Kinase	PAK-SUBFAMILY	-	GPS
26	S	Phosphorylation	Kinase	PAK1	O88643	PSP
34	S	Phosphorylation	Kinase	PKC	-	Uniprot
39	S	Phosphorylation	Kinase	PAK1	O88643	PSP
39	S	Phosphorylation	Kinase	AKT1	P31749	PSP
39	S	Phosphorylation	Kinase	PKA	-	Uniprot
39	S	Phosphorylation	Kinase	CAMK2	-	Uniprot
39	S	Phosphorylation	Kinase	ROCK2	O75116	Uniprot
39	S	Phosphorylation	Kinase	PAK-SUBFAMILY	-	GPS
39	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
39	S	Phosphorylation	Kinase	PKC	-	Uniprot
39	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
39	S	Phosphorylation	Kinase	MAPKAPK2	P49137	GPS
39	S	Phosphorylation	Kinase	PAK_GROUP	-	PhosphoELM
42	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
42	S	Phosphorylation	Kinase	PKC	-	Uniprot
51	S	Phosphorylation	Kinase	PAK1	O88643	PSP
51	S	Phosphorylation	Kinase	PAK-SUBFAMILY	-	GPS
51	S	Phosphorylation	Kinase	PAK_GROUP	-	PhosphoELM
51	S	Phosphorylation	Kinase	MAPKAPK2	P49137	GPS
55	S	Phosphorylation	Kinase	CDK1	P06493	PSP
56	S	Phosphorylation	Kinase	MAPKAPK2	P49137	GPS
56	S	Phosphorylation	Kinase	PRKDC	P78527	GPS
56	S	Phosphorylation	Kinase	PLK1	P53350	PSP
56	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
56	S	Phosphorylation	Kinase	PAK_GROUP	-	PhosphoELM
56	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
56	S	Phosphorylation	Kinase	PAK-SUBFAMILY	-	GPS
56	S	Phosphorylation	Kinase	CDK5	Q00535	Uniprot
56	S	Phosphorylation	Kinase	CDK1	P11440	PSP
66	S	Phosphorylation	Kinase	PAK_GROUP	-	PhosphoELM
66	S	Phosphorylation	Kinase	PAK1	O88643	PSP
66	S	Phosphorylation	Kinase	PAK-SUBFAMILY	-	GPS
72	S	Phosphorylation	Kinase	ROCK_GROUP	-	PhosphoELM
72	S	Phosphorylation	Kinase	ROCK-SUBFAMILY	-	GPS
72	S	Phosphorylation	Kinase	AURKA	O14965	GPS
72	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
72	S	Phosphorylation	Kinase	AURKB	Q96GD4	Uniprot
72	S	Phosphorylation	Kinase	ROCK2	O75116	Uniprot
72	S	Phosphorylation	Kinase	ROCK1	Q13464	PSP
72	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
73	S	Phosphorylation	Kinase	AURKB	Q96GD4	PhosphoELM
73	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
73	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
73	S	Phosphorylation	Kinase	PAK-SUBFAMILY	-	GPS
73	S	Phosphorylation	Kinase	PAK_GROUP	-	PhosphoELM
73	S	Phosphorylation	Kinase	PAK1	O88643	PSP
83	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
83	S	Phosphorylation	Kinase	PLK1	P53350	PSP
83	S	Phosphorylation	Kinase	KCC2A	Q9UQM7	PhosphoELM
83	S	Phosphorylation	Kinase	MAPKAPK2	P49137	GPS
419	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
430	S	Phosphorylation	Kinase	PRKDC	P78527	GPS
430	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
458	T	Phosphorylation	Kinase	MOS	P00540	PSP
458	T	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
459	S	Phosphorylation	Kinase	MOS	P00540	PSP
459	S	Phosphorylation	Kinase	PRKDC	P78527	GPS
459	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
55	S	Phosphorylation	29496907
Filament disassembly during mitosis is promoted by phosphorylation at Ser-55 as well as by nestin (By similarity).
56	S	Phosphorylation
Phosphorylated at Ser-56 by CDK5 during neutrophil secretion in the cytoplasm.

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 VIME_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
C2CD6_HUMAN	ALS2CR11	physical	16189514
KAT7_HUMAN	KAT7	physical	16189514
TCHP_HUMAN	TCHP	physical	16189514
NIF3L_HUMAN	NIF3L1	physical	16189514
NOC4L_HUMAN	NOC4L	physical	16189514
F107A_HUMAN	FAM107A	physical	16189514
K1C20_HUMAN	KRT20	physical	16189514
K0408_HUMAN	KIAA0408	physical	16189514
MTNB_HUMAN	APIP	physical	16189514
GCP4_HUMAN	TUBGCP4	physical	16189514
PDLI1_HUMAN	PDLIM1	physical	16189514
GOPC_HUMAN	GOPC	physical	16189514
RIBC2_HUMAN	RIBC2	physical	16189514
VIME_HUMAN	VIM	physical	16169070
KAT7_HUMAN	KAT7	physical	16169070
LRIF1_HUMAN	LRIF1	physical	16169070
1433Z_HUMAN	YWHAZ	physical	10887173
OSBP2_HUMAN	OSBP2	physical	11802775
BFSP1_HUMAN	BFSP1	physical	1918147
MICA1_HUMAN	MICAL1	physical	11827972
VIME_HUMAN	VIM	physical	11889032
VIME_HUMAN	VIM	physical	11243787
NDKB_HUMAN	NME2	physical	11082283
PLEC_HUMAN	PLEC	physical	11441066
ACTS_HUMAN	ACTA1	physical	11441066
SPTN1_HUMAN	SPTAN1	physical	11441066
LMNB1_HUMAN	LMNB1	physical	11441066
ANR35_HUMAN	ANKRD35	physical	21900206
APLP1_HUMAN	APLP1	physical	21900206
SYK_HUMAN	KARS	physical	21900206
KAT7_HUMAN	KAT7	physical	21900206
VIME_HUMAN	VIM	physical	21900206
DGC14_HUMAN	DGCR14	physical	21900206
DPYL1_HUMAN	CRMP1	physical	21900206
SH3G1_HUMAN	SH3GL1	physical	21900206
PERI_HUMAN	PRPH	physical	21900206
TRI16_HUMAN	TRIM16	physical	20729920
UT14A_HUMAN	UTP14A	physical	15383276
VIME_HUMAN	VIM	physical	15383276
SETB1_HUMAN	SETDB1	physical	15383276
PSMD7_HUMAN	PSMD7	physical	15383276
KAT7_HUMAN	KAT7	physical	15383276
ZHX1_HUMAN	ZHX1	physical	15383276
PPHLN_HUMAN	PPHLN1	physical	15383276
PIAS4_HUMAN	PIAS4	physical	15383276
HAP1_HUMAN	HAP1	physical	15383276
RBM48_HUMAN	RBM48	physical	15383276
ING5_HUMAN	ING5	physical	15383276
ARMX2_HUMAN	ARMCX2	physical	15383276
AKT2_HUMAN	AKT2	physical	20856200
AKT1_HUMAN	AKT1	physical	20856200
A4_HUMAN	APP	physical	21832049
YETS4_HUMAN	YEATS4	physical	22939629
VP33A_HUMAN	VPS33A	physical	22939629
ZYX_HUMAN	ZYX	physical	22939629
TSG10_HUMAN	TSGA10	physical	20797700
PEPL_HUMAN	PPL	physical	12244133
EF1D_HUMAN	EEF1D	physical	22863883
FOXK1_HUMAN	FOXK1	physical	22863883
K1C20_HUMAN	KRT20	physical	25416956
PNMA5_HUMAN	PNMA5	physical	25416956
C19L2_HUMAN	CWF19L2	physical	25416956
TXLNB_HUMAN	TXLNB	physical	25416956
BASP1_HUMAN	BASP1	physical	26344197
OST48_HUMAN	DDOST	physical	26496610
NMT1_HUMAN	NMT1	physical	26496610
RL12_HUMAN	RPL12	physical	26496610
RS7_HUMAN	RPS7	physical	26496610
UBF1_HUMAN	UBTF	physical	26496610
MTA1_HUMAN	MTA1	physical	26496610
FLOT1_HUMAN	FLOT1	physical	26496610
PSIP1_HUMAN	PSIP1	physical	26496610
NELFD_HUMAN	NELFCD	physical	26496610
NAT10_HUMAN	NAT10	physical	26496610
NU133_HUMAN	NUP133	physical	26496610
XPP3_HUMAN	XPNPEP3	physical	26496610
RIOX1_HUMAN	C14orf169	physical	26496610
SYNCI_HUMAN	SYNC	physical	26496610
GAN_HUMAN	GAN	physical	26460568
AHR_HUMAN	AHR	physical	27752740
UBP14_HUMAN	USP14	physical	27448976
NFM_HUMAN	NEFM	physical	28514442
DESM_HUMAN	DES	physical	28514442
NEST_HUMAN	NES	physical	28514442
AINX_HUMAN	INA	physical	28514442
NFL_HUMAN	NEFL	physical	28514442
GFAP_HUMAN	GFAP	physical	28514442
GAN_HUMAN	GAN	physical	28514442
RSPRY_HUMAN	RSPRY1	physical	28514442
UBR1_HUMAN	UBR1	physical	28514442
EPIPL_HUMAN	EPPK1	physical	28514442
IDE_HUMAN	IDE	physical	28514442
NFM_HUMAN	NEFM	physical	27173435
NFL_HUMAN	NEFL	physical	27173435
ZY11B_HUMAN	ZYG11B	physical	27173435
TC1D2_HUMAN	TCTEX1D2	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
116300	Cataract 30 (CTRCT30)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of VIME_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-104; LYS-120; LYS-139;LYS-292; LYS-373; LYS-402 AND LYS-445, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Cdk5 mediates vimentin Ser56 phosphorylation during GTP-inducedsecretion by neutrophils."; Lee K.Y., Liu L., Jin Y., Fu S.B., Rosales J.L.; J. Cell. Physiol. 227:739-750(2012). Cited for: PHOSPHORYLATION AT SER-56, AND SUBCELLULAR LOCATION.	21465480 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-56; TYR-61 ANDSER-83, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-56 AND SER-459, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-459, AND MASSSPECTROMETRY.	19413330 [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-5; SER-25; SER-34;SER-39; SER-42; SER-51; SER-56; TYR-61; SER-72; SER-73; SER-83;SER-144; SER-226; SER-299; SER-409; SER-412 AND SER-459, AND MASSSPECTROMETRY.	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-56; SER-412 AND SER-459,AND MASS SPECTROMETRY.	18691976 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-412, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-29; THR-33;SER-39; SER-42; SER-51; SER-56; SER-72; SER-73; SER-214; SER-261;THR-266; SER-299 AND SER-459, AND MASS SPECTROMETRY.	19007248 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-47; SER-55;SER-56; TYR-61; SER-430; THR-458 AND SER-459, AND MASS SPECTROMETRY.	17287340 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-412; THR-446 ANDSER-459, AND MASS SPECTROMETRY.	17924679 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND MASSSPECTROMETRY.	16565220 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND MASSSPECTROMETRY.	16964243 [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-27; SER-56; SER-73;SER-214 AND SER-412, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Specific in vivo phosphorylation sites determine the assemblydynamics of vimentin intermediate filaments."; Eriksson J.E., He T., Trejo-Skalli A.V., Harmala-Brasken A.-S.,Hellman J., Chou Y.-H., Goldman R.D.; J. Cell Sci. 117:919-932(2004). Cited for: PHOSPHORYLATION AT SER-5; SER-7; SER-8; SER-9; SER-10; SER-39; SER-42;SER-72; SER-73; SER-420; SER-430; THR-458 AND SER-459, AND MASSSPECTROMETRY.	14762106 [Abstract]
"Aurora-B regulates the cleavage furrow-specific vimentinphosphorylation in the cytokinetic process."; Goto H., Yasui Y., Kawajiri A., Nigg E.A., Terada Y., Tatsuka M.,Nagata K., Inagaki M.; J. Biol. Chem. 278:8526-8530(2003). Cited for: PHOSPHORYLATION AT SER-72.	12458200 [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-38; TYR-53; TYR-61 ANDTYR-117, AND MASS SPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-117, AND MASSSPECTROMETRY.	15592455 [Abstract]

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