MYH10_HUMAN - dbPTM
MYH10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYH10_HUMAN
UniProt AC P35580
Protein Name Myosin-10
Gene Name MYH10
Organism Homo sapiens (Human).
Sequence Length 1976
Subcellular Localization Cell projection, lamellipodium . Colocalizes with MCC at the leading edge of migrating cells.
Protein Description Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the central part but not the margins of spreading cells), and lamellipodial extension; this function is mechanically antagonized by MYH9..
Protein Sequence MAQRTGLEDPERYLFVDRAVIYNPATQADWTAKKLVWIPSERHGFEAASIKEERGDEVMVELAENGKKAMVNKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERDLKITDIIIFFQAVCRGYLARKAFAKKQQQLSALKVLQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIDELKLQLAKKEEELQGALARGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEEETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKASKLQNELDNVSTLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDAEALSQRLEEKALAYDKLEKTKNRLQQELDDLTVDLDHQRQVASNLEKKQKKFDQLLAEEKSISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEITNSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRRGGPISFSSSRSGRRQLHLEGASLELSDDDTESKTSDVNETQPPQSE
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 Orthologous
Protein Cluster
2Acetylation------MAQRTGLED
------CCCCCCCCC
20.90-
13PhosphorylationGLEDPERYLFVDRAV
CCCCHHHEEEEEEEE
11.6621945579
13 (in isoform 4)Phosphorylation-11.6627642862
18MethylationERYLFVDRAVIYNPA
HHEEEEEEEEEECCC
26.0058858611
22PhosphorylationFVDRAVIYNPATQAD
EEEEEEEECCCCCCC
14.4321945579
22 (in isoform 4)Phosphorylation-14.4327642862
26PhosphorylationAVIYNPATQADWTAK
EEEECCCCCCCCCCC
26.0821712546
31PhosphorylationPATQADWTAKKLVWI
CCCCCCCCCCCEEEC
29.1921712546
34UbiquitinationQADWTAKKLVWIPSE
CCCCCCCCEEECCCC
45.89-
40PhosphorylationKKLVWIPSERHGFEA
CCEEECCCCCCCCEE
37.8221406692
51AcetylationGFEAASIKEERGDEV
CCEECCCHHHHCCHH
51.5326051181
51UbiquitinationGFEAASIKEERGDEV
CCEECCCHHHHCCHH
51.53-
68UbiquitinationELAENGKKAMVNKDD
HHHHCCCEEECCHHH
43.01-
73AcetylationGKKAMVNKDDIQKMN
CCEEECCHHHHHHCC
45.4226051181
73UbiquitinationGKKAMVNKDDIQKMN
CCEEECCHHHHHHCC
45.42-
78AcetylationVNKDDIQKMNPPKFS
CCHHHHHHCCCCCCC
40.7625953088
83UbiquitinationIQKMNPPKFSKVEDM
HHHCCCCCCCCHHHH
64.62-
83 (in isoform 3)Ubiquitination-64.62-
85PhosphorylationKMNPPKFSKVEDMAE
HCCCCCCCCHHHHHH
41.7529514088
86UbiquitinationMNPPKFSKVEDMAEL
CCCCCCCCHHHHHHH
53.42-
94PhosphorylationVEDMAELTCLNEASV
HHHHHHHHHCCHHHH
13.37-
106AcetylationASVLHNLKDRYYSGL
HHHHHHCCCCCCCCE
45.5425953088
117PhosphorylationYSGLIYTYSGLFCVV
CCCEEEEECCEEEEE
5.46-
155PhosphorylationHEMPPHIYAISESAY
CCCCCCEEEEEHHHH
8.54-
162PhosphorylationYAISESAYRCMLQDR
EEEEHHHHHHHCCCC
17.3922210691
163MethylationAISESAYRCMLQDRE
EEEHHHHHHHCCCCC
10.09115385341
173PhosphorylationLQDREDQSILCTGES
CCCCCCCCEEEECCC
29.8321712546
176S-palmitoylationREDQSILCTGESGAG
CCCCCEEEECCCCCC
4.3529575903
177PhosphorylationEDQSILCTGESGAGK
CCCCEEEECCCCCCC
40.30-
184UbiquitinationTGESGAGKTENTKKV
ECCCCCCCCCCHHHH
52.73-
194PhosphorylationNTKKVIQYLAHVASS
CHHHHHHHHHHHHHH
8.50-
201PhosphorylationYLAHVASSHKGRKDH
HHHHHHHHCCCCCCC
21.34-
206UbiquitinationASSHKGRKDHNIPGE
HHHCCCCCCCCCCHH
72.51-
213 (in isoform 1)Phosphorylation-41.9427251275
213 (in isoform 5)Phosphorylation-41.9427251275
214 (in isoform 2)Phosphorylation-9.0130266825
214 (in isoform 4)Phosphorylation-9.0130266825
222 (in isoform 2)Phosphorylation-15.9330622161
224 (in isoform 2)Phosphorylation-7.1830622161
227PhosphorylationQANPILESFGNAKTV
HHCHHHHHHCCCCCC
34.7020068231
227 (in isoform 2)Phosphorylation-34.7030622161
232UbiquitinationLESFGNAKTVKNDNS
HHHHCCCCCCCCCCC
58.8321906983
232 (in isoform 1)Ubiquitination-58.8321890473
232 (in isoform 3)Ubiquitination-58.8321890473
233PhosphorylationESFGNAKTVKNDNSS
HHHCCCCCCCCCCCC
34.0120068231
235UbiquitinationFGNAKTVKNDNSSRF
HCCCCCCCCCCCCCC
64.91-
239PhosphorylationKTVKNDNSSRFGKFI
CCCCCCCCCCCCEEE
26.2529514088
240PhosphorylationTVKNDNSSRFGKFIR
CCCCCCCCCCCEEEE
37.5729514088
244UbiquitinationDNSSRFGKFIRINFD
CCCCCCCEEEEEEEE
34.60-
248 (in isoform 2)Ubiquitination-5.2821890473
255PhosphorylationINFDVTGYIVGANIE
EEEECCEEEECCCHH
5.3118767875
268UbiquitinationIETYLLEKSRAVRQA
HHHHHHHHHHHHHHH
45.25-
269PhosphorylationETYLLEKSRAVRQAK
HHHHHHHHHHHHHHC
18.9818767875
285PhosphorylationERTFHIFYQLLSGAG
CCHHHHHHHHHHCCC
9.54-
307PhosphorylationLLEGFNNYRFLSNGY
HHCCCCCCEECCCCE
12.12-
360PhosphorylationVLQFGNISFKKERNT
HHHHCCCEEECCCCC
34.7124719451
362AcetylationQFGNISFKKERNTDQ
HHCCCEEECCCCCCC
47.1125953088
367PhosphorylationSFKKERNTDQASMPE
EEECCCCCCCCCCCH
35.3921406692
371PhosphorylationERNTDQASMPENTVA
CCCCCCCCCCHHHHH
29.2721406692
372SulfoxidationRNTDQASMPENTVAQ
CCCCCCCCCHHHHHH
5.6021406390
376PhosphorylationQASMPENTVAQKLCH
CCCCCHHHHHHHHHH
18.6321406692
407PhosphorylationRIKVGRDYVQKAQTK
CCCCCHHHHHHHCCH
11.9228152594
410AcetylationVGRDYVQKAQTKEQA
CCHHHHHHHCCHHHH
32.2030786423
410UbiquitinationVGRDYVQKAQTKEQA
CCHHHHHHHCCHHHH
32.2021906983
410 (in isoform 1)Ubiquitination-32.2021890473
410 (in isoform 3)Ubiquitination-32.2021890473
426 (in isoform 2)Ubiquitination-41.9521890473
442AcetylationWLVHRINKALDRTKR
HHHHHHHHHHHHHHH
48.2119608861
442MalonylationWLVHRINKALDRTKR
HHHHHHHHHHHHHHH
48.2126320211
451AcetylationLDRTKRQGASFIGIL
HHHHHHCCCCEEEEE
27.5019608861
491SulfoxidationQQLFNHTMFILEQEE
HHHHHHCHHHCCHHH
1.2128183972
547AcetylationWFPKATDKTFVEKLV
CCCCCCCHHHHHHHH
39.2425953088
552AcetylationTDKTFVEKLVQEQGS
CCHHHHHHHHHHCCC
48.9719608861
559PhosphorylationKLVQEQGSHSKFQKP
HHHHHCCCCCCCCCC
25.0429514088
561AcetylationVQEQGSHSKFQKPRQ
HHHCCCCCCCCCCCC
36.5419608861
561PhosphorylationVQEQGSHSKFQKPRQ
HHHCCCCCCCCCCCC
36.5429514088
562UbiquitinationQEQGSHSKFQKPRQL
HHCCCCCCCCCCCCC
46.52-
572AcetylationKPRQLKDKADFCIIH
CCCCCCCCCCEEEEE
48.5523749302
572UbiquitinationKPRQLKDKADFCIIH
CCCCCCCCCCEEEEE
48.55-
572 (in isoform 3)Ubiquitination-48.55-
576GlutathionylationLKDKADFCIIHYAGK
CCCCCCEEEEECCCC
2.6922555962
580PhosphorylationADFCIIHYAGKVDYK
CCEEEEECCCCCCCC
13.4728152594
587UbiquitinationYAGKVDYKADEWLMK
CCCCCCCCCCHHHHH
44.92-
587 (in isoform 3)Ubiquitination-44.92-
594MethylationKADEWLMKNMDPLND
CCCHHHHHCCCCCCH
47.12-
613MethylationLLHQSSDRFVAELWK
HHHHCHHHHHHHHHH
29.86115484131
620AcetylationRFVAELWKDVDRIVG
HHHHHHHHCHHHHCC
61.5725953088
620UbiquitinationRFVAELWKDVDRIVG
HHHHHHHHCHHHHCC
61.57-
634SulfoxidationGLDQVTGMTETAFGS
CCHHHCCCCHHHCCC
1.9230846556
637PhosphorylationQVTGMTETAFGSAYK
HHCCCCHHHCCCCHH
20.3729255136
641PhosphorylationMTETAFGSAYKTKKG
CCHHHCCCCHHCCCC
23.2129255136
643PhosphorylationETAFGSAYKTKKGMF
HHHCCCCHHCCCCCC
22.3824173317
644UbiquitinationTAFGSAYKTKKGMFR
HHCCCCHHCCCCCCC
54.29-
652PhosphorylationTKKGMFRTVGQLYKE
CCCCCCCCHHHHHHH
20.0920068231
657PhosphorylationFRTVGQLYKESLTKL
CCCHHHHHHHHHHHH
12.5720068231
658AcetylationRTVGQLYKESLTKLM
CCHHHHHHHHHHHHH
49.7926051181
658MethylationRTVGQLYKESLTKLM
CCHHHHHHHHHHHHH
49.7966722909
663AcetylationLYKESLTKLMATLRN
HHHHHHHHHHHHHHH
41.3725953088
667PhosphorylationSLTKLMATLRNTNPN
HHHHHHHHHHHCCCC
16.5730622161
668 (in isoform 4)Phosphorylation-2.6327251275
671PhosphorylationLMATLRNTNPNFVRC
HHHHHHHCCCCCEEE
45.6930622161
678GlutathionylationTNPNFVRCIIPNHEK
CCCCCEEEECCCCHH
2.5122555962
678S-palmitoylationTNPNFVRCIIPNHEK
CCCCCEEEECCCCHH
2.5129575903
689AcetylationNHEKRAGKLDPHLVL
CCHHHCCCCCHHHHH
49.0523749302
689UbiquitinationNHEKRAGKLDPHLVL
CCHHHCCCCCHHHHH
49.0521890473
689 (in isoform 1)Ubiquitination-49.0521890473
705 (in isoform 2)Ubiquitination-5.4521890473
710 (in isoform 3)Ubiquitination-1.8321890473
718MethylationCRQGFPNRIVFQEFR
HHCCCCCCCCHHHHH
27.04-
732PhosphorylationRQRYEILTPNAIPKG
HHHHCCCCCCCCCCC
21.8426471730
738 (in isoform 1)Ubiquitination-59.6821890473
738UbiquitinationLTPNAIPKGFMDGKQ
CCCCCCCCCCCCHHH
59.6821890473
738UbiquitinationLTPNAIPKGFMDGKQ
CCCCCCCCCCCCHHH
59.6821890473
744AcetylationPKGFMDGKQACERMI
CCCCCCHHHHHHHHH
30.3826051181
744UbiquitinationPKGFMDGKQACERMI
CCCCCCHHHHHHHHH
30.38-
754 (in isoform 2)Ubiquitination-4.8921890473
754UbiquitinationCERMIRALELDPNLY
HHHHHHHHCCCCCHH
4.8921890473
759UbiquitinationRALELDPNLYRIGQS
HHHCCCCCHHHCCCC
49.7421890473
759 (in isoform 3)Ubiquitination-49.7421890473
759UbiquitinationRALELDPNLYRIGQS
HHHCCCCCHHHCCCC
49.7421890473
761PhosphorylationLELDPNLYRIGQSKI
HCCCCCHHHCCCCCH
13.5623917254
766PhosphorylationNLYRIGQSKIFFRAG
CHHHCCCCCHHHHHH
23.62-
767AcetylationLYRIGQSKIFFRAGV
HHHCCCCCHHHHHHH
35.3325825284
767UbiquitinationLYRIGQSKIFFRAGV
HHHCCCCCHHHHHHH
35.33-
788 (in isoform 3)Ubiquitination-33.30-
809UbiquitinationARKAFAKKQQQLSAL
HHHHHHHHHHHHHHH
50.32-
814PhosphorylationAKKQQQLSALKVLQR
HHHHHHHHHHHHHHH
27.5026074081
817UbiquitinationQQQLSALKVLQRNCA
HHHHHHHHHHHHHHH
40.3921890473
823S-nitrosylationLKVLQRNCAAYLKLR
HHHHHHHHHHHHHHH
2.202212679
826PhosphorylationLQRNCAAYLKLRHWQ
HHHHHHHHHHHHCHH
5.9528152594
828AcetylationRNCAAYLKLRHWQWW
HHHHHHHHHHCHHHH
30.6924502331
828UbiquitinationRNCAAYLKLRHWQWW
HHHHHHHHHHCHHHH
30.6921906983
828 (in isoform 1)Ubiquitination-30.6921890473
838 (in isoform 3)Ubiquitination-4.03-
840UbiquitinationQWWRVFTKVKPLLQV
HHHHHHHCHHHHHHC
36.4821890473
842UbiquitinationWRVFTKVKPLLQVTR
HHHHHCHHHHHHCHH
31.35-
844 (in isoform 2)Ubiquitination-4.2921890473
849 (in isoform 3)Ubiquitination-42.9521890473
857AcetylationQEEELQAKDEELLKV
CHHHHHHCCHHHHHH
53.3526051181
857UbiquitinationQEEELQAKDEELLKV
CHHHHHHCCHHHHHH
53.35-
878SulfoxidationVEGELEEMERKHQQL
HHHHHHHHHHHHHHH
4.3921406390
881UbiquitinationELEEMERKHQQLLEE
HHHHHHHHHHHHHHH
32.24-
929PhosphorylationEILHDLESRVEEEEE
HHHHHHHHHHHHHHH
49.2630301811
948SulfoxidationLQNEKKKMQAHIQDL
HHHHHHHHHHHHHHH
6.1330846556
968UbiquitinationEEEGARQKLQLEKVT
HHHHHHHHHHHHHHH
32.42-
995PhosphorylationLLLEDQNSKFIKEKK
HHHCCCCCHHHHHHH
24.26-
1007MethylationEKKLMEDRIAECSSQ
HHHHHHHHHHHHHHH
19.40115484123
1011GlutathionylationMEDRIAECSSQLAEE
HHHHHHHHHHHHHHH
3.3322555962
1012PhosphorylationEDRIAECSSQLAEEE
HHHHHHHHHHHHHHH
16.7821406692
1013PhosphorylationDRIAECSSQLAEEEE
HHHHHHHHHHHHHHH
40.6517525332
1021AcetylationQLAEEEEKAKNLAKI
HHHHHHHHHHHHHHH
68.8623749302
1021MalonylationQLAEEEEKAKNLAKI
HHHHHHHHHHHHHHH
68.8626320211
1031UbiquitinationNLAKIRNKQEVMISD
HHHHHHCCHHHHHHH
37.68-
1035SulfoxidationIRNKQEVMISDLEER
HHCCHHHHHHHHHHH
2.0921406390
1037PhosphorylationNKQEVMISDLEERLK
CCHHHHHHHHHHHHH
20.3221406692
1044 (in isoform 4)Phosphorylation-65.4427251275
1059UbiquitinationELEKAKRKLDGETTD
HHHHHHHHCCCCCCC
50.66-
1129PhosphorylationELQEDFESEKASRNK
HHHHHHHHHHHHHHH
44.3727499020
1145O-linked_GlycosylationEKQKRDLSEELEALK
HHHHHHHHHHHHHHH
33.0623301498
1145PhosphorylationEKQKRDLSEELEALK
HHHHHHHHHHHHHHH
33.0622617229
1153PhosphorylationEELEALKTELEDTLD
HHHHHHHHHHHHHHC
46.8021406692
1158PhosphorylationLKTELEDTLDTTAAQ
HHHHHHHHHCHHHHH
19.7021406692
1160 (in isoform 4)Phosphorylation-44.0727251275
1161PhosphorylationELEDTLDTTAAQQEL
HHHHHHCHHHHHHHH
22.8021406692
1162PhosphorylationLEDTLDTTAAQQELR
HHHHHCHHHHHHHHH
21.4721406692
1170PhosphorylationAAQQELRTKREQEVA
HHHHHHHHHHHHHHH
47.2621406692
1176 (in isoform 4)Phosphorylation-5.1127251275
1187PhosphorylationKKALEEETKNHEAQI
HHHHHHHHHHHHHHH
40.19-
1188AcetylationKALEEETKNHEAQIQ
HHHHHHHHHHHHHHH
60.6326051181
1198MethylationEAQIQDMRQRHATAL
HHHHHHHHHHHHHHH
38.38115385333
1203PhosphorylationDMRQRHATALEELSE
HHHHHHHHHHHHHHH
26.1729116813
1216AcetylationSEQLEQAKRFKANLE
HHHHHHHHHHHHHHH
59.0525953088
1219MalonylationLEQAKRFKANLEKNK
HHHHHHHHHHHHHHH
40.1626320211
1224AcetylationRFKANLEKNKQGLET
HHHHHHHHHHCCCCC
73.0269725
1231PhosphorylationKNKQGLETDNKELAC
HHHCCCCCCCHHHHH
50.3321406692
1234AcetylationQGLETDNKELACEVK
CCCCCCCHHHHHHHH
57.8426051181
1234 (in isoform 4)Phosphorylation-57.8427251275
1238GlutathionylationTDNKELACEVKVLQQ
CCCHHHHHHHHHHHH
10.9122555962
1241AcetylationKELACEVKVLQQVKA
HHHHHHHHHHHHHHC
18.2223236377
1241MalonylationKELACEVKVLQQVKA
HHHHHHHHHHHHHHC
18.2226320211
1247AcetylationVKVLQQVKAESEHKR
HHHHHHHHCCCHHHH
41.9419608861
1255AcetylationAESEHKRKKLDAQVQ
CCCHHHHHHHHHHHH
63.5925953088
1256AcetylationESEHKRKKLDAQVQE
CCHHHHHHHHHHHHH
56.4826051181
1256MalonylationESEHKRKKLDAQVQE
CCHHHHHHHHHHHHH
56.4826320211
1267AcetylationQVQELHAKVSEGDRL
HHHHHHHHCCCCHHH
35.2325953088
1267UbiquitinationQVQELHAKVSEGDRL
HHHHHHHHCCCCHHH
35.23-
1281AcetylationLRVELAEKASKLQNE
HHHHHHHHHHHHHHH
52.9625953088
1301AcetylationTLLEEAEKKGIKFAK
HHHHHHHHHCCCHHH
64.4526051181
1312PhosphorylationKFAKDAASLESQLQD
CHHHHHHHHHHHHHH
34.1028348404
1315PhosphorylationKDAASLESQLQDTQE
HHHHHHHHHHHHHHH
41.2928348404
1335PhosphorylationTRQKLNLSSRIRQLE
HHHHCCHHHHHHHHH
19.2524719451
1343 (in isoform 4)Phosphorylation-80.8427251275
1345AcetylationIRQLEEEKNSLQEQQ
HHHHHHHHHHHHHHH
55.9388535
1347PhosphorylationQLEEEKNSLQEQQEE
HHHHHHHHHHHHHHH
42.3626471730
1376PhosphorylationLQSQLADTKKKVDDD
HHHHHHHHHHHHCCC
38.8719060867
1379AcetylationQLADTKKKVDDDLGT
HHHHHHHHHCCCCHH
53.0711791257
1386PhosphorylationKVDDDLGTIESLEEA
HHCCCCHHHHHHHHH
28.9521406692
1389PhosphorylationDDLGTIESLEEAKKK
CCCHHHHHHHHHHHH
36.9121406692
1396AcetylationSLEEAKKKLLKDAEA
HHHHHHHHHHHHHHH
59.3411791269
1399UbiquitinationEAKKKLLKDAEALSQ
HHHHHHHHHHHHHHH
66.39-
1411AcetylationLSQRLEEKALAYDKL
HHHHHHHHHHHHHHH
39.0525953088
1415PhosphorylationLEEKALAYDKLEKTK
HHHHHHHHHHHHHHH
17.9221082442
1417AcetylationEKALAYDKLEKTKNR
HHHHHHHHHHHHHHH
45.9625953088
1421PhosphorylationAYDKLEKTKNRLQQE
HHHHHHHHHHHHHHH
24.95-
1444PhosphorylationDHQRQVASNLEKKQK
HHHHHHHHHHHHHHH
42.99-
1446 (in isoform 4)Phosphorylation-10.6627251275
1448AcetylationQVASNLEKKQKKFDQ
HHHHHHHHHHHHHHH
64.7723749302
1451AcetylationSNLEKKQKKFDQLLA
HHHHHHHHHHHHHHH
65.377666121
1452AcetylationNLEKKQKKFDQLLAE
HHHHHHHHHHHHHHH
52.247666133
1452MethylationNLEKKQKKFDQLLAE
HHHHHHHHHHHHHHH
52.247666133
1452UbiquitinationNLEKKQKKFDQLLAE
HHHHHHHHHHHHHHH
52.24-
1461AcetylationDQLLAEEKSISARYA
HHHHHHHHCHHHHHH
44.5925953088
1462PhosphorylationQLLAEEKSISARYAE
HHHHHHHCHHHHHHH
25.6723403867
1464PhosphorylationLAEEKSISARYAEER
HHHHHCHHHHHHHHH
17.4923403867
1467PhosphorylationEKSISARYAEERDRA
HHCHHHHHHHHHHHH
20.3423403867
1473 (in isoform 3)Ubiquitination-40.32-
1484AcetylationEAREKETKALSLARA
HHHHHHHHHHHHHHH
48.7111922547
1484UbiquitinationEAREKETKALSLARA
HHHHHHHHHHHHHHH
48.71-
1487PhosphorylationEKETKALSLARALEE
HHHHHHHHHHHHHHH
25.5028060719
1499AcetylationLEEALEAKEEFERQN
HHHHHHHHHHHHHHH
48.6926051181
1505 (in isoform 3)Ubiquitination-55.03-
1513SulfoxidationNKQLRADMEDLMSSK
HHHHHHHHHHHHCCC
4.1630846556
1517SulfoxidationRADMEDLMSSKDDVG
HHHHHHHHCCCCHHH
7.0430846556
1532AcetylationKNVHELEKSKRALEQ
HHHHHHHHHHHHHHH
74.1125953088
1544SulfoxidationLEQQVEEMRTQLEEL
HHHHHHHHHHHHHHH
3.3930846556
1545MethylationEQQVEEMRTQLEELE
HHHHHHHHHHHHHHH
23.70115484147
1546PhosphorylationQQVEEMRTQLEELED
HHHHHHHHHHHHHHH
35.8721082442
1558PhosphorylationLEDELQATEDAKLRL
HHHHHHCCHHHHHHH
22.80-
1562UbiquitinationLQATEDAKLRLEVNM
HHCCHHHHHHHHHHH
46.60-
1582PhosphorylationQFERDLQTRDEQNEE
HHHHHHHCHHHCCHH
47.5927251275
1596AcetylationEKKRLLIKQVRELEA
HHHHHHHHHHHHHHH
42.5925953088
1609MethylationEAELEDERKQRALAV
HHHCHHHHHHHHHHH
53.37115484115
1613 (in isoform 4)Phosphorylation-9.4427251275
1619AcetylationRALAVASKKKMEIDL
HHHHHHCCCCCCCCH
46.8325953088
1645AcetylationKARDEVIKQLRKLQA
HHHHHHHHHHHHHHH
48.7519608861
1645MalonylationKARDEVIKQLRKLQA
HHHHHHHHHHHHHHH
48.7526320211
1649UbiquitinationEVIKQLRKLQAQMKD
HHHHHHHHHHHHHHH
54.25-
1654AcetylationLRKLQAQMKDYQREL
HHHHHHHHHHHHHHH
3.9019608861
1667PhosphorylationELEEARASRDEIFAQ
HHHHHHHCHHHHHHC
34.4126437602
1684PhosphorylationESEKKLKSLEAEILQ
HHHHHHHHHHHHHHH
41.7125693802
1698PhosphorylationQLQEELASSERARRH
HHHHHHHCHHHHHHH
45.4125693802
1699PhosphorylationLQEELASSERARRHA
HHHHHHCHHHHHHHH
26.0425693802
1720PhosphorylationLADEITNSASGKSAL
HHHHHHHCCCCHHHH
18.3728674419
1750O-linked_GlycosylationEELEEEQSNMELLND
HHHHHHHHHHHHHHH
41.2323301498
1750PhosphorylationEELEEEQSNMELLND
HHHHHHHHHHHHHHH
41.2327732954
1752SulfoxidationLEEEQSNMELLNDRF
HHHHHHHHHHHHHHH
4.6830846556
1762PhosphorylationLNDRFRKTTLQVDTL
HHHHHHHCCCCHHHH
28.6021406692
1763PhosphorylationNDRFRKTTLQVDTLN
HHHHHHCCCCHHHHH
20.4421406692
1768PhosphorylationKTTLQVDTLNAELAA
HCCCCHHHHHHHHHH
24.0521406692
1783PhosphorylationERSAAQKSDNARQQL
HHHHHHHCHHHHHHH
24.8227470641
1800AcetylationQNKELKAKLQELEGA
HHHHHHHHHHHHHHH
49.4623749302
1800MalonylationQNKELKAKLQELEGA
HHHHHHHHHHHHHHH
49.4626320211
1800UbiquitinationQNKELKAKLQELEGA
HHHHHHHHHHHHHHH
49.46-
1809AcetylationQELEGAVKSKFKATI
HHHHHHHHHHHHHHH
47.6025953088
1809MalonylationQELEGAVKSKFKATI
HHHHHHHHHHHHHHH
47.6026320211
1842AcetylationKERAAANKLVRRTEK
HHHHHHHHHHHHHHH
43.5725953088
1842MalonylationKERAAANKLVRRTEK
HHHHHHHHHHHHHHH
43.5726320211
1856SulfoxidationKKLKEIFMQVEDERR
HHHHHHHHHHHHHHH
5.5421406390
1872SulfoxidationADQYKEQMEKANARM
HHHHHHHHHHHHHHH
6.3030846556
1874AcetylationQYKEQMEKANARMKQ
HHHHHHHHHHHHHHH
41.4112437743
1894PhosphorylationEEAEEEATRANASRR
HHHHHHHHHHHHHHH
33.3323403867
1899PhosphorylationEATRANASRRKLQRE
HHHHHHHHHHHHHHH
32.21-
1922PhosphorylationEGLSREVSTLKNRLR
HHHHHHHHHHHHHHH
24.22-
1923PhosphorylationGLSREVSTLKNRLRR
HHHHHHHHHHHHHHC
47.10-
1930MethylationTLKNRLRRGGPISFS
HHHHHHHCCCCCCCC
60.0416187485
1935PhosphorylationLRRGGPISFSSSRSG
HHCCCCCCCCCCCCC
23.3930266825
1937PhosphorylationRGGPISFSSSRSGRR
CCCCCCCCCCCCCCC
22.1829255136
1938PhosphorylationGGPISFSSSRSGRRQ
CCCCCCCCCCCCCCE
27.9730266825
1939PhosphorylationGPISFSSSRSGRRQL
CCCCCCCCCCCCCEE
29.3029255136
1940MethylationPISFSSSRSGRRQLH
CCCCCCCCCCCCEEE
45.1158858623
1941PhosphorylationISFSSSRSGRRQLHL
CCCCCCCCCCCEEEE
38.3021406692
1952PhosphorylationQLHLEGASLELSDDD
EEEEECCEEECCCCC
32.9829255136
1956PhosphorylationEGASLELSDDDTESK
ECCEEECCCCCCCCC
29.6229255136
1960PhosphorylationLELSDDDTESKTSDV
EECCCCCCCCCCCCC
49.5029255136
1962PhosphorylationLSDDDTESKTSDVNE
CCCCCCCCCCCCCCC
43.2429255136
1964PhosphorylationDDDTESKTSDVNETQ
CCCCCCCCCCCCCCC
39.1623927012
1965PhosphorylationDDTESKTSDVNETQP
CCCCCCCCCCCCCCC
43.2123927012
1966 (in isoform 4)Phosphorylation-53.1227251275
1968 (in isoform 4)Phosphorylation-52.1427251275
1969 (in isoform 4)Phosphorylation-48.9827251275
1970PhosphorylationKTSDVNETQPPQSE-
CCCCCCCCCCCCCC-
40.9723927012
1975PhosphorylationNETQPPQSE------
CCCCCCCCC------
100.0023927012
1983 (in isoform 4)Phosphorylation-27251275
1987 (in isoform 4)Phosphorylation-27251275
1991 (in isoform 4)Phosphorylation-27251275
1995 (in isoform 4)Phosphorylation-27251275
2001 (in isoform 4)Phosphorylation-27251275
2006 (in isoform 4)Phosphorylation-27251275

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
1937SPhosphorylationKinasePRKCZQ05513
GPS
1952SPhosphorylationKinaseCSNK2A1P68400
GPS
1956SPhosphorylationKinaseCSNK2A1P68400
GPS
1960TPhosphorylationKinaseCSNK2A1P68400
GPS
1965SPhosphorylationKinaseCSNK2A1P68400
GPS
1975SPhosphorylationKinaseCSNK2A1P68400
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYH10_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 MYH10_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PBX1_HUMANPBX1physical
12724421
MYH9_HUMANMYH9physical
22939629
RB11A_HUMANRAB11Aphysical
22939629
MYO1C_HUMANMYO1Cphysical
22939629
RALA_HUMANRALAphysical
22939629
SEPT7_HUMANSEPT7physical
22939629

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.
Regulatory Network of MYH10_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-1964; SER-1965 AND SER-1975, AND MASSSPECTROMETRY.
"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-442; LYS-552; LYS-1247 ANDLYS-1645, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-1939; SER-1952 ANDSER-1956, AND MASS SPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-1964; SER-1965 AND SER-1975, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1956, AND MASSSPECTROMETRY.
"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-1939; SER-1952 ANDSER-1956, AND MASS SPECTROMETRY.
"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 SER-1956 AND SER-1975, ANDMASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1013, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1376, AND MASSSPECTROMETRY.
"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 THR-1960, AND MASSSPECTROMETRY.
"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-1415, AND MASSSPECTROMETRY.

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