UniProt ID | VIME_MOUSE | |
---|---|---|
UniProt AC | P20152 | |
Protein Name | Vimentin | |
Gene Name | Vim | |
Organism | Mus musculus (Mouse). | |
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 | MSTRSVSSSSYRRMFGGSGTSSRPSSNRSYVTTSTRTYSLGSALRPSTSRSLYSSSPGGAYVTRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFALEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPTFSSLNLRETNLESLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MSTRSVSSS ------CCCCCCCCH | 32.31 | - | |
2 | Phosphorylation | ------MSTRSVSSS ------CCCCCCCCH | 32.31 | 26745281 | |
3 | Phosphorylation | -----MSTRSVSSSS -----CCCCCCCCHH | 26.18 | 26745281 | |
5 | Phosphorylation | ---MSTRSVSSSSYR ---CCCCCCCCHHCH | 26.83 | 27087446 | |
7 | Phosphorylation | -MSTRSVSSSSYRRM -CCCCCCCCHHCHHH | 26.25 | 27087446 | |
7 | O-linked_Glycosylation | -MSTRSVSSSSYRRM -CCCCCCCCHHCHHH | 26.25 | - | |
8 | Phosphorylation | MSTRSVSSSSYRRMF CCCCCCCCHHCHHHC | 22.58 | 23684622 | |
9 | Phosphorylation | STRSVSSSSYRRMFG CCCCCCCHHCHHHCC | 24.71 | 23684622 | |
10 | Phosphorylation | TRSVSSSSYRRMFGG CCCCCCHHCHHHCCC | 25.30 | 27149854 | |
11 | Nitrated tyrosine | RSVSSSSYRRMFGGS CCCCCHHCHHHCCCC | 12.27 | - | |
11 | Phosphorylation | RSVSSSSYRRMFGGS CCCCCHHCHHHCCCC | 12.27 | 24899341 | |
18 | Phosphorylation | YRRMFGGSGTSSRPS CHHHCCCCCCCCCCC | 39.00 | 26824392 | |
20 | Phosphorylation | RMFGGSGTSSRPSSN HHCCCCCCCCCCCCC | 25.81 | 23684622 | |
21 | Phosphorylation | MFGGSGTSSRPSSNR HCCCCCCCCCCCCCC | 28.07 | 23684622 | |
21 | O-linked_Glycosylation | MFGGSGTSSRPSSNR HCCCCCCCCCCCCCC | 28.07 | 21540332 | |
22 | Phosphorylation | FGGSGTSSRPSSNRS CCCCCCCCCCCCCCC | 48.31 | 24899341 | |
25 | Phosphorylation | SGTSSRPSSNRSYVT CCCCCCCCCCCCEEE | 38.85 | 22942356 | |
26 | Phosphorylation | GTSSRPSSNRSYVTT CCCCCCCCCCCEEEE | 38.66 | 7530295 | |
29 | Phosphorylation | SRPSSNRSYVTTSTR CCCCCCCCEEEEECC | 28.36 | 25263469 | |
30 | Phosphorylation | RPSSNRSYVTTSTRT CCCCCCCEEEEECCE | 9.89 | 26160508 | |
32 | O-linked_Glycosylation | SSNRSYVTTSTRTYS CCCCCEEEEECCEEE | 13.54 | 21540332 | |
32 | Phosphorylation | SSNRSYVTTSTRTYS CCCCCEEEEECCEEE | 13.54 | 24453211 | |
33 | Phosphorylation | SNRSYVTTSTRTYSL CCCCEEEEECCEEEC | 20.32 | 26160508 | |
33 | O-linked_Glycosylation | SNRSYVTTSTRTYSL CCCCEEEEECCEEEC | 20.32 | - | |
34 | Phosphorylation | NRSYVTTSTRTYSLG CCCEEEEECCEEECC | 13.41 | 27149854 | |
34 | O-linked_Glycosylation | NRSYVTTSTRTYSLG CCCEEEEECCEEECC | 13.41 | 21540332 | |
35 | Phosphorylation | RSYVTTSTRTYSLGS CCEEEEECCEEECCC | 25.57 | 26160508 | |
37 | Phosphorylation | YVTTSTRTYSLGSAL EEEEECCEEECCCCC | 19.97 | 27087446 | |
38 | Phosphorylation | VTTSTRTYSLGSALR EEEECCEEECCCCCC | 9.90 | 26060331 | |
39 | Phosphorylation | TTSTRTYSLGSALRP EEECCEEECCCCCCC | 26.16 | 27087446 | |
39 | O-linked_Glycosylation | TTSTRTYSLGSALRP EEECCEEECCCCCCC | 26.16 | 21540332 | |
42 | Phosphorylation | TRTYSLGSALRPSTS CCEEECCCCCCCCCC | 29.44 | 28725479 | |
47 | Phosphorylation | LGSALRPSTSRSLYS CCCCCCCCCCCCCCC | 32.36 | 22942356 | |
48 | Phosphorylation | GSALRPSTSRSLYSS CCCCCCCCCCCCCCC | 30.73 | 22942356 | |
48 | O-linked_Glycosylation | GSALRPSTSRSLYSS CCCCCCCCCCCCCCC | 30.73 | 21540332 | |
49 | Phosphorylation | SALRPSTSRSLYSSS CCCCCCCCCCCCCCC | 24.98 | 22942356 | |
49 | O-linked_Glycosylation | SALRPSTSRSLYSSS CCCCCCCCCCCCCCC | 24.98 | 21540332 | |
51 | Phosphorylation | LRPSTSRSLYSSSPG CCCCCCCCCCCCCCC | 31.27 | 27087446 | |
53 | Phosphorylation | PSTSRSLYSSSPGGA CCCCCCCCCCCCCCE | 14.04 | 28725479 | |
54 | Phosphorylation | STSRSLYSSSPGGAY CCCCCCCCCCCCCEE | 29.63 | 23527152 | |
54 | O-linked_Glycosylation | STSRSLYSSSPGGAY CCCCCCCCCCCCCEE | 29.63 | 21540332 | |
55 | Phosphorylation | TSRSLYSSSPGGAYV CCCCCCCCCCCCEEE | 27.31 | 27087446 | |
55 | O-linked_Glycosylation | TSRSLYSSSPGGAYV CCCCCCCCCCCCEEE | 27.31 | 21540332 | |
56 | Phosphorylation | SRSLYSSSPGGAYVT CCCCCCCCCCCEEEE | 22.94 | 27087446 | |
61 | Phosphorylation | SSSPGGAYVTRSSAV CCCCCCEEEECCCCC | 12.96 | 27149854 | |
63 | Phosphorylation | SPGGAYVTRSSAVRL CCCCEEEECCCCCCC | 16.50 | 27742792 | |
65 | Phosphorylation | GGAYVTRSSAVRLRS CCEEEECCCCCCCCC | 17.18 | 21454597 | |
66 | Phosphorylation | GAYVTRSSAVRLRSS CEEEECCCCCCCCCC | 27.74 | 7530295 | |
72 | Phosphorylation | SSAVRLRSSVPGVRL CCCCCCCCCCCCCHH | 40.03 | 7530295 | |
73 | Phosphorylation | SAVRLRSSVPGVRLL CCCCCCCCCCCCHHC | 26.37 | 26824392 | |
83 | Phosphorylation | GVRLLQDSVDFSLAD CCHHCCCCCCHHHHH | 15.60 | 15140879 | |
87 | Phosphorylation | LQDSVDFSLADAINT CCCCCCHHHHHHHCC | 20.41 | 26824392 | |
94 | Phosphorylation | SLADAINTEFKNTRT HHHHHHCCCCCCCCC | 36.36 | 29119230 | |
97 | Ubiquitination | DAINTEFKNTRTNEK HHHCCCCCCCCCCCC | 51.70 | - | |
104 | Ubiquitination | KNTRTNEKVELQELN CCCCCCCCEEHHHHH | 42.98 | - | |
104 | Acetylation | KNTRTNEKVELQELN CCCCCCCCEEHHHHH | 42.98 | 23806337 | |
104 | Succinylation | KNTRTNEKVELQELN CCCCCCCCEEHHHHH | 42.98 | 23806337 | |
117 | Phosphorylation | LNDRFANYIDKVRFL HHHHHHHHHHHHHHH | 13.68 | 26824392 | |
120 | Methylation | RFANYIDKVRFLEQQ HHHHHHHHHHHHHHH | 26.25 | - | |
120 | Acetylation | RFANYIDKVRFLEQQ HHHHHHHHHHHHHHH | 26.25 | 23806337 | |
120 | Succinylation | RFANYIDKVRFLEQQ HHHHHHHHHHHHHHH | 26.25 | - | |
120 | Ubiquitination | RFANYIDKVRFLEQQ HHHHHHHHHHHHHHH | 26.25 | - | |
120 | Succinylation | RFANYIDKVRFLEQQ HHHHHHHHHHHHHHH | 26.25 | 23806337 | |
129 | Acetylation | RFLEQQNKILLAELE HHHHHHCHHHHHHHH | 30.32 | 23806337 | |
129 | Succinylation | RFLEQQNKILLAELE HHHHHHCHHHHHHHH | 30.32 | - | |
129 | Succinylation | RFLEQQNKILLAELE HHHHHHCHHHHHHHH | 30.32 | 23806337 | |
139 | Acetylation | LAELEQLKGQGKSRL HHHHHHHCCCCCCCH | 49.21 | 23806337 | |
139 | Ubiquitination | LAELEQLKGQGKSRL HHHHHHHCCCCCCCH | 49.21 | - | |
139 | Succinylation | LAELEQLKGQGKSRL HHHHHHHCCCCCCCH | 49.21 | 23806337 | |
143 | Ubiquitination | EQLKGQGKSRLGDLY HHHCCCCCCCHHHHH | 25.23 | 22790023 | |
144 | Phosphorylation | QLKGQGKSRLGDLYE HHCCCCCCCHHHHHH | 39.29 | 26824392 | |
150 | Phosphorylation | KSRLGDLYEEEMREL CCCHHHHHHHHHHHH | 26.49 | 19854140 | |
168 | Acetylation | VDQLTNDKARVEVER HHHHHCCHHHHHHCC | 39.91 | 23806337 | |
168 | Ubiquitination | VDQLTNDKARVEVER HHHHHCCHHHHHHCC | 39.91 | - | |
168 | Succinylation | VDQLTNDKARVEVER HHHHHCCHHHHHHCC | 39.91 | 23806337 | |
188 | Acetylation | DIMRLREKLQEEMLQ HHHHHHHHHHHHHHH | 49.38 | 23806337 | |
188 | Succinylation | DIMRLREKLQEEMLQ HHHHHHHHHHHHHHH | 49.38 | - | |
188 | Ubiquitination | DIMRLREKLQEEMLQ HHHHHHHHHHHHHHH | 49.38 | - | |
188 | Succinylation | DIMRLREKLQEEMLQ HHHHHHHHHHHHHHH | 49.38 | 23806337 | |
201 | Phosphorylation | LQREEAESTLQSFRQ HHHHHHHHHHHHHHH | 41.27 | 26824392 | |
202 | Phosphorylation | QREEAESTLQSFRQD HHHHHHHHHHHHHHH | 21.96 | 26824392 | |
205 | Phosphorylation | EAESTLQSFRQDVDN HHHHHHHHHHHHHCH | 26.05 | 26824392 | |
214 | Phosphorylation | RQDVDNASLARLDLE HHHHCHHHHHHHHHH | 28.90 | 27087446 | |
223 | Acetylation | ARLDLERKVESLQEE HHHHHHHHHHHHHHH | 40.76 | 23806337 | |
223 | Ubiquitination | ARLDLERKVESLQEE HHHHHHHHHHHHHHH | 40.76 | - | |
223 | Succinylation | ARLDLERKVESLQEE HHHHHHHHHHHHHHH | 40.76 | 23806337 | |
226 | Phosphorylation | DLERKVESLQEEIAF HHHHHHHHHHHHHHH | 38.04 | 27180971 | |
235 | Acetylation | QEEIAFLKKLHDEEI HHHHHHHHHHCHHHH | 47.00 | 23806337 | |
235 | Ubiquitination | QEEIAFLKKLHDEEI HHHHHHHHHHCHHHH | 47.00 | - | |
235 | Succinylation | QEEIAFLKKLHDEEI HHHHHHHHHHCHHHH | 47.00 | 23806337 | |
236 | Ubiquitination | EEIAFLKKLHDEEIQ HHHHHHHHHCHHHHH | 53.88 | - | |
261 | Phosphorylation | VQIDVDVSKPDLTAA CEEEECCCCHHHHHH | 33.73 | 26824392 | |
276 | Phosphorylation | LRDVRQQYESVAAKN HHHHHHHHHHHHHHC | 11.22 | 22817900 | |
278 | Phosphorylation | DVRQQYESVAAKNLQ HHHHHHHHHHHHCHH | 16.48 | 24899341 | |
282 | Ubiquitination | QYESVAAKNLQEAEE HHHHHHHHCHHHHHH | 48.75 | 22790023 | |
291 | Phosphorylation | LQEAEEWYKSKFADL HHHHHHHHHHHHHHH | 14.52 | 25367039 | |
292 | Acetylation | QEAEEWYKSKFADLS HHHHHHHHHHHHHHH | 48.52 | 134195 | |
292 | Ubiquitination | QEAEEWYKSKFADLS HHHHHHHHHHHHHHH | 48.52 | 22790023 | |
293 | Phosphorylation | EAEEWYKSKFADLSE HHHHHHHHHHHHHHH | 19.80 | 25367039 | |
294 | Acetylation | AEEWYKSKFADLSEA HHHHHHHHHHHHHHH | 40.18 | 23806337 | |
294 | Succinylation | AEEWYKSKFADLSEA HHHHHHHHHHHHHHH | 40.18 | - | |
294 | Ubiquitination | AEEWYKSKFADLSEA HHHHHHHHHHHHHHH | 40.18 | - | |
294 | Succinylation | AEEWYKSKFADLSEA HHHHHHHHHHHHHHH | 40.18 | 23806337 | |
299 | Phosphorylation | KSKFADLSEAANRNN HHHHHHHHHHHHHCH | 26.24 | 26824392 | |
325 | Phosphorylation | EYRRQVQSLTCEVDA HHHHHHHHHHHHHHH | 27.13 | 25521595 | |
327 | Phosphorylation | RRQVQSLTCEVDALK HHHHHHHHHHHHHHH | 16.33 | 27742792 | |
328 | S-nitrosocysteine | RQVQSLTCEVDALKG HHHHHHHHHHHHHHC | 6.10 | - | |
328 | Glutathionylation | RQVQSLTCEVDALKG HHHHHHHHHHHHHHC | 6.10 | 24333276 | |
328 | S-nitrosylation | RQVQSLTCEVDALKG HHHHHHHHHHHHHHC | 6.10 | 20925432 | |
328 | S-palmitoylation | RQVQSLTCEVDALKG HHHHHHHHHHHHHHC | 6.10 | 28526873 | |
334 | Ubiquitination | TCEVDALKGTNESLE HHHHHHHHCCCHHHH | 66.46 | 22790023 | |
334 | Acetylation | TCEVDALKGTNESLE HHHHHHHHCCCHHHH | 66.46 | 22826441 | |
336 | Phosphorylation | EVDALKGTNESLERQ HHHHHHCCCHHHHHH | 33.94 | 25619855 | |
339 | Phosphorylation | ALKGTNESLERQMRE HHHCCCHHHHHHHHH | 37.29 | 27087446 | |
358 | Phosphorylation | FALEAANYQDTIGRL HHHHHHHHHHHHHHH | 11.75 | 30635358 | |
361 | Phosphorylation | EAANYQDTIGRLQDE HHHHHHHHHHHHHHH | 15.14 | 30635358 | |
373 | Acetylation | QDEIQNMKEEMARHL HHHHHHHHHHHHHHH | 59.06 | 23806337 | |
373 | Ubiquitination | QDEIQNMKEEMARHL HHHHHHHHHHHHHHH | 59.06 | - | |
373 | Succinylation | QDEIQNMKEEMARHL HHHHHHHHHHHHHHH | 59.06 | 23806337 | |
383 | Nitrated tyrosine | MARHLREYQDLLNVK HHHHHHHHHHHHCHH | 10.82 | - | |
383 | Phosphorylation | MARHLREYQDLLNVK HHHHHHHHHHHHCHH | 10.82 | 25367039 | |
402 | Ubiquitination | IEIATYRKLLEGEES HHHHHHHHHHCCCCC | 47.19 | 22790023 | |
409 | Phosphorylation | KLLEGEESRISLPLP HHHCCCCCCCCCCCC | 30.52 | 24899341 | |
412 | Phosphorylation | EGEESRISLPLPTFS CCCCCCCCCCCCCCC | 23.87 | 7530295 | |
417 | Phosphorylation | RISLPLPTFSSLNLR CCCCCCCCCCCCCCC | 43.78 | 26824392 | |
419 | Phosphorylation | SLPLPTFSSLNLRET CCCCCCCCCCCCCCC | 36.07 | 27087446 | |
420 | Phosphorylation | LPLPTFSSLNLRETN CCCCCCCCCCCCCCC | 19.65 | 27087446 | |
426 | Phosphorylation | SSLNLRETNLESLPL CCCCCCCCCCHHCCC | 38.37 | 26824392 | |
430 | Phosphorylation | LRETNLESLPLVDTH CCCCCCHHCCCCCCC | 38.15 | 25521595 | |
436 | Phosphorylation | ESLPLVDTHSKRTLL HHCCCCCCCCCCEEE | 22.14 | 25521595 | |
438 | Phosphorylation | LPLVDTHSKRTLLIK CCCCCCCCCCEEEEE | 26.40 | 26824392 | |
439 | Acetylation | PLVDTHSKRTLLIKT CCCCCCCCCEEEEEE | 41.62 | 23806337 | |
439 | Ubiquitination | PLVDTHSKRTLLIKT CCCCCCCCCEEEEEE | 41.62 | - | |
439 | Succinylation | PLVDTHSKRTLLIKT CCCCCCCCCEEEEEE | 41.62 | 23806337 | |
441 | Phosphorylation | VDTHSKRTLLIKTVE CCCCCCCEEEEEEEE | 29.65 | 29514104 | |
445 | Acetylation | SKRTLLIKTVETRDG CCCEEEEEEEECCCC | 46.62 | 23806337 | |
445 | Succinylation | SKRTLLIKTVETRDG CCCEEEEEEEECCCC | 46.62 | - | |
445 | Ubiquitination | SKRTLLIKTVETRDG CCCEEEEEEEECCCC | 46.62 | - | |
445 | Succinylation | SKRTLLIKTVETRDG CCCEEEEEEEECCCC | 46.62 | 23806337 | |
446 | Phosphorylation | KRTLLIKTVETRDGQ CCEEEEEEEECCCCC | 19.31 | 26824392 | |
449 | Phosphorylation | LLIKTVETRDGQVIN EEEEEEECCCCCEEC | 29.71 | 29550500 | |
458 | Phosphorylation | DGQVINETSQHHDDL CCCEECCCCCCCCCC | 29.24 | 27087446 | |
459 | Phosphorylation | GQVINETSQHHDDLE CCEECCCCCCCCCCC | 22.72 | 25521595 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
5 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
5 | S | Phosphorylation | Kinase | PKC_GROUP | - | PhosphoELM |
5 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
5 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
7 | S | Phosphorylation | Kinase | PRKCA | P20444 | GPS |
7 | S | Phosphorylation | Kinase | PRKACA | P05132 | GPS |
7 | S | Phosphorylation | Kinase | AURKB | O70126 | GPS |
7 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
7 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
7 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
7 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
8 | S | Phosphorylation | Kinase | PKC_GROUP | - | PhosphoELM |
8 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
9 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
9 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
9 | S | Phosphorylation | Kinase | PRKCA | P20444 | GPS |
10 | S | Phosphorylation | Kinase | PRKCA | P20444 | GPS |
10 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
10 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
21 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
21 | S | Phosphorylation | Kinase | PKC_GROUP | - | PhosphoELM |
21 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
21 | S | Phosphorylation | Kinase | PRKCA | P20444 | GPS |
25 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
25 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
25 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
25 | S | Phosphorylation | Kinase | PRKCA | P20444 | GPS |
25 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
25 | S | Phosphorylation | Kinase | AURKB | O70126 | GPS |
25 | S | Phosphorylation | Kinase | PRKACA | P05132 | GPS |
26 | S | Phosphorylation | Kinase | PRKCA | P20444 | GPS |
26 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
26 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
34 | S | Phosphorylation | Kinase | PRKCA | P20444 | GPS |
34 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
34 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
34 | S | Phosphorylation | Kinase | PKC_GROUP | - | PhosphoELM |
39 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
39 | S | Phosphorylation | Kinase | AURKB | O70126 | GPS |
39 | S | Phosphorylation | Kinase | CAM-KII_GROUP | - | PhosphoELM |
39 | S | Phosphorylation | Kinase | PRKACA | P05132 | GPS |
39 | S | Phosphorylation | Kinase | PRKCA | P20444 | GPS |
39 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
39 | S | Phosphorylation | Kinase | CAMK2A | P11275 | PSP |
39 | S | Phosphorylation | Kinase | CAMK2B | P28652 | GPS |
39 | S | Phosphorylation | Kinase | ROCK2 | P70336 | Uniprot |
39 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
39 | S | Phosphorylation | Kinase | CAMK2-FAMILY | - | GPS |
39 | S | Phosphorylation | Kinase | CAMK2 | - | Uniprot |
39 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
42 | S | Phosphorylation | Kinase | PKC_GROUP | - | PhosphoELM |
42 | S | Phosphorylation | Kinase | PRKCA | P20444 | GPS |
42 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
42 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
47 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
47 | S | Phosphorylation | Kinase | AURKB | O70126 | GPS |
47 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
47 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
47 | S | Phosphorylation | Kinase | PRKACA | P05132 | GPS |
51 | S | Phosphorylation | Kinase | PRKACA | P05132 | GPS |
51 | S | Phosphorylation | Kinase | PKC_GROUP | - | PhosphoELM |
51 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
51 | S | Phosphorylation | Kinase | PKACA | P17612 | PSP |
51 | S | Phosphorylation | Kinase | PRKCA | P20444 | GPS |
51 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
51 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
51 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
51 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
56 | S | Phosphorylation | Kinase | CDK_GROUP | - | PhosphoELM |
56 | S | Phosphorylation | Kinase | CDK-FAMILY | - | GPS |
56 | S | Phosphorylation | Kinase | CDK1 | P11440 | PSP |
56 | S | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
65 | S | Phosphorylation | Kinase | AURKB | O70126 | GPS |
66 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
66 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
66 | S | Phosphorylation | Kinase | PRKCA | P20444 | GPS |
66 | S | Phosphorylation | Kinase | PRKACA | P05132 | GPS |
66 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
66 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
66 | S | Phosphorylation | Kinase | AURKB | O70126 | GPS |
72 | S | Phosphorylation | Kinase | ROCK2 | P70336 | Uniprot |
72 | S | Phosphorylation | Kinase | ROCK1 | P70335 | PSP |
72 | S | Phosphorylation | Kinase | ROCK1 | Q13464 | PSP |
72 | S | Phosphorylation | Kinase | AURKB | O70126 | Uniprot |
73 | S | Phosphorylation | Kinase | AURKB | O70126 | PhosphoELM |
83 | S | Phosphorylation | Kinase | CAMK2 | - | Uniprot |
83 | S | Phosphorylation | Kinase | CAMK2-FAMILY | - | GPS |
83 | S | Phosphorylation | Kinase | PLK1 | P53350 | PSP |
83 | S | Phosphorylation | Kinase | CAMK2B | P28652 | GPS |
83 | S | Phosphorylation | Kinase | CAMK2A | P11275 | PSP |
83 | S | Phosphorylation | Kinase | CAMK2A | P11798 | PSP |
83 | S | Phosphorylation | Kinase | CAM-KII_GROUP | - | PhosphoELM |
87 | S | Phosphorylation | Kinase | AURKB | O70126 | GPS |
459 | S | Phosphorylation | Kinase | PLK1 | P53350 | PSP |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
55 | S | Phosphorylation |
| - |
56 | S | Phosphorylation |
| 17242355 |
* 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_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
PPARG_MOUSE | Pparg | physical | 23297177 | |
RAB7A_HUMAN | RAB7A | physical | 26496610 | |
PHB2_HUMAN | PHB2 | physical | 26496610 | |
ZBT11_HUMAN | ZBTB11 | physical | 26496610 | |
CENPJ_HUMAN | CENPJ | physical | 26496610 | |
SYNCI_HUMAN | SYNC | physical | 26496610 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-49; SER-56;SER-66; SER-419; SER-420; SER-430 AND SER-459, AND MASS SPECTROMETRY. | |
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-214, AND MASSSPECTROMETRY. | |
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-72; SER-73;SER-144; SER-226; SER-430 AND SER-459, AND MASS SPECTROMETRY. | |
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line."; Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; Mol. Cell. Proteomics 3:279-286(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-73, AND MASSSPECTROMETRY. | |
"Phosphorylation of vimentin by Rho-associated kinase at a uniqueamino-terminal site that is specifically phosphorylated duringcytokinesis."; Goto H., Kosako H., Tanabe K., Yanagida M., Sakurai M., Amano M.,Kaibuchi K., Inagaki M.; J. Biol. Chem. 273:11728-11736(1998). Cited for: PHOSPHORYLATION AT SER-39 AND SER-72. | |
"Evidence that Ser-82 is a unique phosphorylation site on vimentin forCa2(+)-calmodulin-dependent protein kinase II."; Ando S., Tokui T., Yamauchi T., Sugiura H., Tanabe K., Inagaki M.; Biochem. Biophys. Res. Commun. 175:955-962(1991). Cited for: PHOSPHORYLATION AT SER-39 AND SER-83. | |
"Domain- and sequence-specific phosphorylation of vimentin inducesdisassembly of the filament structure."; Ando S., Tanabe K., Gonda Y., Sato C., Inagaki M.; Biochemistry 28:2974-2979(1989). Cited for: PROTEIN SEQUENCE OF 5-69, AND PHOSPHORYLATION AT SER-7; SER-9; SER-10;SER-21; SER-25; SER-26; SER-34; SER-39; SER-42; SER-47; SER-51 ANDSER-66. | |
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53 AND TYR-61, AND MASSSPECTROMETRY. |