MY18A_MOUSE - dbPTM
MY18A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MY18A_MOUSE
UniProt AC Q9JMH9
Protein Name Unconventional myosin-XVIIIa
Gene Name Myo18a
Organism Mus musculus (Mouse).
Sequence Length 2050
Subcellular Localization Isoform 1: Endoplasmic reticulum-Golgi intermediate compartment. Cytoplasm, cytoskeleton. Colocalizes with actin.
Isoform 2: Cytoplasm. Lacks the PDZ domain. Diffusely localized in the cytoplasm.
Golgi apparatus. Golgi apparatus, trans-Golgi n
Protein Description May link Golgi membranes to the cytoskeleton and participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. [PubMed: 19837035 Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (By similarity May be involved in the maintenance of the stromal cell architectures required for cell to cell contact]
Protein Sequence MFNLMKKDKDKDGGRKEKKEKKEKKERMSAAELRSLEEMSMRRGFFNLNRSSKRESKTRLEISNPIPIKVASGSDLHLTDIDSDSNRGSIILDSGHLSTASSSDDLKGEEGSFRGSVLQRAAKFGSLAKQNSQMIVKRFSFSQRSRDESASETSTPSEHSAAPSPQVEVRTLEGQLMQHPGLGIPRPGPRSRVPELVTKRFPADLRLPALVPPPPPALRELELQRRPTGDFGFSLRRTTMLDRAPEGQAYRRVVHFAEPGAGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQPIPELSELSRSWLRTGEGHRREPADAKTEEQIAAEEAWYETEKVWLVHRDGFSLASQLKSEELSLPEGKARVKLDHDGAILDVDEDDIEKANAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRSTSFRQGPEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGGSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEARGLLWLLEEEALVPGATEDALLDRLFSYYGPQEGDKKGQSPLLRSSKPRHFLLGHSHGTNWVEYNVAGWLNYTKQNPATQNAPRLLQDSQKKIISNLFLGRAGSATVLSGSIAGLEGGSQLALRRATSMRKTFTTGMAAVKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGEPRSASSRRVSSSSELDLPPGDPCEAGLLQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGRNYIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFRAGTLARLEEQRDEQTSRHLTLFQAACRGYLARQHFKKRKIQDLAIRCVQKNIKKNKGVKDWPWWKLFTTVRPLIQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSLQDMVTKYQKKKNKLEGDSDVDSELEDRVDGVKSWLSKNKGPSKAPSDDGSLKSSSPTSHWKPLAPDPSDDEHDPVDSISRPRFSHSYLSDSDTEAKLTETSA
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
29PhosphorylationKEKKERMSAAELRSL
HHHHHHHCHHHHHHH
30.4622324799
35PhosphorylationMSAAELRSLEEMSMR
HCHHHHHHHHHHHHH
53.4021743459
40PhosphorylationLRSLEEMSMRRGFFN
HHHHHHHHHHHCCCC
16.6529514104
51PhosphorylationGFFNLNRSSKRESKT
CCCCCCCCCCCCCCC
38.8521743459
52PhosphorylationFFNLNRSSKRESKTR
CCCCCCCCCCCCCCC
32.2827087446
72PhosphorylationPIPIKVASGSDLHLT
CEEEEECCCCCCEEE
41.6427087446
74PhosphorylationPIKVASGSDLHLTDI
EEEECCCCCCEEEEC
34.2127087446
79PhosphorylationSGSDLHLTDIDSDSN
CCCCCEEEECCCCCC
21.8427087446
83PhosphorylationLHLTDIDSDSNRGSI
CEEEECCCCCCCCCE
43.1827087446
85PhosphorylationLTDIDSDSNRGSIIL
EEECCCCCCCCCEEE
32.1727742792
89PhosphorylationDSDSNRGSIILDSGH
CCCCCCCCEEEECCC
11.8326239621
94PhosphorylationRGSIILDSGHLSTAS
CCCEEEECCCCCCCC
25.3526239621
98PhosphorylationILDSGHLSTASSSDD
EEECCCCCCCCCCCC
19.0927087446
99PhosphorylationLDSGHLSTASSSDDL
EECCCCCCCCCCCCC
36.6027087446
101PhosphorylationSGHLSTASSSDDLKG
CCCCCCCCCCCCCCC
30.3925521595
102PhosphorylationGHLSTASSSDDLKGE
CCCCCCCCCCCCCCC
35.0127087446
103PhosphorylationHLSTASSSDDLKGEE
CCCCCCCCCCCCCCC
32.4221082442
112PhosphorylationDLKGEEGSFRGSVLQ
CCCCCCCCCHHHHHH
18.3030352176
116PhosphorylationEEGSFRGSVLQRAAK
CCCCCHHHHHHHHHH
18.5229514104
126PhosphorylationQRAAKFGSLAKQNSQ
HHHHHHHHHHHHHHH
28.4329899451
132PhosphorylationGSLAKQNSQMIVKRF
HHHHHHHHHHHHHHC
20.7322324799
132 (in isoform 6)Phosphorylation-20.7316452087
140PhosphorylationQMIVKRFSFSQRSRD
HHHHHHCCCCHHCCC
28.2027087446
142PhosphorylationIVKRFSFSQRSRDES
HHHHCCCCHHCCCCC
24.4022324799
145PhosphorylationRFSFSQRSRDESASE
HCCCCHHCCCCCCCC
36.1227087446
149PhosphorylationSQRSRDESASETSTP
CHHCCCCCCCCCCCC
41.1925619855
151PhosphorylationRSRDESASETSTPSE
HCCCCCCCCCCCCCC
51.1625619855
153PhosphorylationRDESASETSTPSEHS
CCCCCCCCCCCCCCC
35.0925619855
154PhosphorylationDESASETSTPSEHSA
CCCCCCCCCCCCCCC
33.9825619855
155PhosphorylationESASETSTPSEHSAA
CCCCCCCCCCCCCCC
37.9525619855
157PhosphorylationASETSTPSEHSAAPS
CCCCCCCCCCCCCCC
48.2927087446
160PhosphorylationTSTPSEHSAAPSPQV
CCCCCCCCCCCCCCE
23.2927087446
164PhosphorylationSEHSAAPSPQVEVRT
CCCCCCCCCCEEEEE
24.2027087446
228PhosphorylationLELQRRPTGDFGFSL
HHHCCCCCCCCCCCC
47.79-
234PhosphorylationPTGDFGFSLRRTTML
CCCCCCCCCEEECCH
22.7321183079
340 (in isoform 6)Phosphorylation-4.4225521595
372PhosphorylationQLKSEELSLPEGKAR
HHCCCCCCCCCCCCC
45.2029472430
429PhosphorylationLHTLRQRYGASLLHT
HHHHHHHHCCCHHCC
14.5425266776
432PhosphorylationLRQRYGASLLHTYAG
HHHHHCCCHHCCCCC
27.4025266776
436PhosphorylationYGASLLHTYAGPSLL
HCCCHHCCCCCCCEE
18.2925266776
437PhosphorylationGASLLHTYAGPSLLV
CCCHHCCCCCCCEEE
9.9825266776
446PhosphorylationGPSLLVLSTRGAPAV
CCCEEEEECCCCCCC
14.4725266776
447PhosphorylationPSLLVLSTRGAPAVY
CCEEEEECCCCCCCC
29.0325266776
457UbiquitinationAPAVYSEKVMHMFKG
CCCCCCHHHHHHHCC
38.63-
493PhosphorylationLMSRQDQSIVLLGSS
HHCCCCCEEEEECCC
23.9722802335
499PhosphorylationQSIVLLGSSGSGKTT
CEEEEECCCCCCCCC
31.3422802335
500PhosphorylationSIVLLGSSGSGKTTS
EEEEECCCCCCCCCC
34.8722802335
502PhosphorylationVLLGSSGSGKTTSFQ
EEECCCCCCCCCCHH
38.7822802335
514PhosphorylationSFQHLVQYLATIAGT
CHHHHHHHHHHHHCC
7.2722802335
517PhosphorylationHLVQYLATIAGTSGT
HHHHHHHHHHCCCCC
14.5722802335
521PhosphorylationYLATIAGTSGTKVFS
HHHHHHCCCCCEEEE
18.2422802335
522PhosphorylationLATIAGTSGTKVFSV
HHHHHCCCCCEEEEH
43.4722802335
524PhosphorylationTIAGTSGTKVFSVEK
HHHCCCCCEEEEHHH
24.6522802335
722PhosphorylationKHQLKGGTLQRSTSF
HHHHCCCCCCCCCCC
28.5226643407
726PhosphorylationKGGTLQRSTSFRQGP
CCCCCCCCCCCCCCC
18.5525521595
727PhosphorylationGGTLQRSTSFRQGPE
CCCCCCCCCCCCCCC
33.7925521595
728PhosphorylationGTLQRSTSFRQGPEE
CCCCCCCCCCCCCCC
21.4825521595
736PhosphorylationFRQGPEESGLGEGTK
CCCCCCCCCCCCCCC
37.3426643407
742PhosphorylationESGLGEGTKLSALEC
CCCCCCCCCHHHHHH
25.2220469934
865PhosphorylationQASHLVRSLAHADEA
HHHHHHHHHHCHHHH
23.5625521595
912PhosphorylationEGDKKGQSPLLRSSK
CCCCCCCCCCCCCCC
26.6129472430
951PhosphorylationYTKQNPATQNAPRLL
CCCCCCHHCCCCHHC
24.5022802335
964UbiquitinationLLQDSQKKIISNLFL
HCHHHHHHHHHHHHC
37.32-
976PhosphorylationLFLGRAGSATVLSGS
HHCCCCCCEEEECCC
21.5627180971
978PhosphorylationLGRAGSATVLSGSIA
CCCCCCEEEECCCCC
24.5526239621
981PhosphorylationAGSATVLSGSIAGLE
CCCEEEECCCCCCCC
26.5927087446
983PhosphorylationSATVLSGSIAGLEGG
CEEEECCCCCCCCCH
13.0925521595
991PhosphorylationIAGLEGGSQLALRRA
CCCCCCHHHHHHHHH
32.6423140645
1000PhosphorylationLALRRATSMRKTFTT
HHHHHHHHCCCCCCC
18.6623140645
1004PhosphorylationRATSMRKTFTTGMAA
HHHHCCCCCCCCCHH
18.8229899451
1031PhosphorylationQVDALIDTIKRSKMH
HHHHHHHHHHHHHCE
22.7722871156
1033AcetylationDALIDTIKRSKMHFV
HHHHHHHHHHHCEEE
53.3523576753
1063PhosphorylationSASSRRVSSSSELDL
CCCCCCCCCCCCCCC
23.7726239621
1064PhosphorylationASSRRVSSSSELDLP
CCCCCCCCCCCCCCC
34.7226239621
1065PhosphorylationSSRRVSSSSELDLPP
CCCCCCCCCCCCCCC
21.9626239621
1066PhosphorylationSRRVSSSSELDLPPG
CCCCCCCCCCCCCCC
44.0926239621
1136PhosphorylationTKKHGRNYIVVDEKR
HCCCCCCEEEECHHH
8.1729514104
1279PhosphorylationERNELRLSSDRLETR
HHHHHHCCHHHHHHH
24.6125338131
1514PhosphorylationGFTQKVVSLEAELQD
HHHHHHHHHHHHHHH
24.3929899451
1524PhosphorylationAELQDISSQESKDEA
HHHHHCCCCCCCCHH
38.0029514104
1560 (in isoform 4)Phosphorylation-16.80-
1607 (in isoform 5)Phosphorylation-5.3520531401
1616 (in isoform 5)Phosphorylation-63.1125195567
1619 (in isoform 7)Phosphorylation-48.8820531401
1620 (in isoform 5)Phosphorylation-55.9425195567
1624 (in isoform 5)Phosphorylation-58.2620531401
1628 (in isoform 7)Phosphorylation-11.9125195567
1632 (in isoform 7)Phosphorylation-7.0525195567
1633PhosphorylationRELESKLSTLSDQVN
HHHHHHHHHHHHHHH
30.9129472430
1634PhosphorylationELESKLSTLSDQVNQ
HHHHHHHHHHHHHHH
40.4929472430
1636PhosphorylationESKLSTLSDQVNQRD
HHHHHHHHHHHHHHH
26.5329472430
1636 (in isoform 7)Phosphorylation-26.5320531401
1646PhosphorylationVNQRDFESEKRLRKD
HHHHHHHHHHHHHHH
48.7028285833
1691PhosphorylationLKNQLEESEFTCAAA
HHHHHHHCCCHHHHH
28.7422807455
1694PhosphorylationQLEESEFTCAAAVKA
HHHHCCCHHHHHHHH
9.3622807455
1703AcetylationAAAVKARKAMEVEME
HHHHHHHHHCEEEHH
57.877385631
1831AcetylationETRLEFEKTQVKRLE
HHHHHHHHHHHHHHH
49.9723236377
1901 (in isoform 4)Phosphorylation-27.8920531401
1910 (in isoform 4)Phosphorylation-12.7625195567
1914 (in isoform 4)Phosphorylation-3.3325195567
1918 (in isoform 4)Phosphorylation-5.7020531401
1919AcetylationQSLQADLKLAFKRIG
HHHHHHHHHHHHHHH
38.017970537
1938PhosphorylationAIEDEMESDENEDLI
HHHHHHCCCCCHHHH
49.2527087446
1938 (in isoform 1)Phosphorylation-49.2520531401
1947PhosphorylationENEDLINSLQDMVTK
CCHHHHHHHHHHHHH
22.0326239621
1947 (in isoform 1)Phosphorylation-22.0325195567
1951 (in isoform 1)Phosphorylation-2.3825195567
1955 (in isoform 1)Phosphorylation-19.0520531401
1966PhosphorylationKNKLEGDSDVDSELE
HHCCCCCCCCCHHHH
50.8427087446
1970PhosphorylationEGDSDVDSELEDRVD
CCCCCCCHHHHHHHH
43.8825521595
1987UbiquitinationKSWLSKNKGPSKAPS
HHHHHCCCCCCCCCC
75.76-
1990PhosphorylationLSKNKGPSKAPSDDG
HHCCCCCCCCCCCCC
50.5525777480
1994PhosphorylationKGPSKAPSDDGSLKS
CCCCCCCCCCCCCCC
53.8725521595
1998PhosphorylationKAPSDDGSLKSSSPT
CCCCCCCCCCCCCCC
39.3525521595
2001PhosphorylationSDDGSLKSSSPTSHW
CCCCCCCCCCCCCCC
41.1423375375
2002PhosphorylationDDGSLKSSSPTSHWK
CCCCCCCCCCCCCCC
38.4623375375
2003PhosphorylationDGSLKSSSPTSHWKP
CCCCCCCCCCCCCCC
39.0123684622
2005PhosphorylationSLKSSSPTSHWKPLA
CCCCCCCCCCCCCCC
34.8623684622
2006PhosphorylationLKSSSPTSHWKPLAP
CCCCCCCCCCCCCCC
30.6321082442
2016PhosphorylationKPLAPDPSDDEHDPV
CCCCCCCCCCCCCCC
66.1426824392
2025PhosphorylationDEHDPVDSISRPRFS
CCCCCCCCCCCCCCC
23.7727742792
2027PhosphorylationHDPVDSISRPRFSHS
CCCCCCCCCCCCCCC
39.9427742792
2032PhosphorylationSISRPRFSHSYLSDS
CCCCCCCCCCCCCCC
16.8925521595
2034PhosphorylationSRPRFSHSYLSDSDT
CCCCCCCCCCCCCHH
26.9424925903
2035PhosphorylationRPRFSHSYLSDSDTE
CCCCCCCCCCCCHHC
12.5624925903
2037PhosphorylationRFSHSYLSDSDTEAK
CCCCCCCCCCHHCCH
27.1727087446
2039PhosphorylationSHSYLSDSDTEAKLT
CCCCCCCCHHCCHHC
42.9527087446
2041PhosphorylationSYLSDSDTEAKLTET
CCCCCCHHCCHHCCC
41.6225521595
2046PhosphorylationSDTEAKLTETSA---
CHHCCHHCCCCC---
36.1922345495
2048PhosphorylationTEAKLTETSA-----
HCCHHCCCCC-----
25.3922345495
2049PhosphorylationEAKLTETSA------
CCHHCCCCC------
26.2522345495

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

Oops, there are no upstream regulatory protein records of MY18A_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
340SPhosphorylation

16452087

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 MY18A_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MY18A_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MY18A_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1966 AND SER-1970, ANDMASS SPECTROMETRY.
"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-83; SER-1966; SER-1970;SER-2016; SER-2037 AND SER-2039, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-74; SER-83;SER-102; SER-164; SER-1966; SER-2032; SER-2037 AND SER-2039, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1966 AND SER-1970, ANDMASS SPECTROMETRY.

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