MYO1C_MOUSE - dbPTM
MYO1C_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYO1C_MOUSE
UniProt AC Q9WTI7
Protein Name Unconventional myosin-Ic
Gene Name Myo1c
Organism Mus musculus (Mouse).
Sequence Length 1063
Subcellular Localization Cytoplasm. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Cell projection, stereocilium membrane. Cytoplasmic vesicle. Cell projection, ruffle. Colocalizes with CABP1 and CIB1 at cell margin, membrane ruffles and punctate regions on th
Protein Description Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which then are moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes.; Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation..
Protein Sequence MALQVELIPTGEIIRVVHPHRPCKLALGSDGVRVTMESALTARDRVGVQDFVLLENFTSEAAFIENLRRRFRENLIYTYIGPVLVSVNPYRDLQIYSRQHMERYRGVSFYEVPPHLFAVADTVYRALRTERRDQAVMISGESGAGKTEATKRLLQFYAETCPAPERGGAVRDRLLQSNPVLEAFGNAKTLRNDNSSRFGKYMDVQFDFKGAPVGGHILSYLLEKSRVVHQNHGERNFHVFYQLLEGGEEETLRRLGLERNPQSYLYLVKGQCAKVSSINDKSDWKVMRKALSVIDFTEDEVEDLLSIVASVLHLGNIHFAADEDSNAQVTTENQLKYLTRLLGVEGTTLREALTHRKIIAKGEELLSPLNLEQAAYARDALAKAVYSRTFTWLVRKINRSLASKDAESPSWRSTTVLGLLDIYGFEVFQHNSFEQFCINYCNEKLQQLFIELTLKSEQEEYEAEGIAWEPVQYFNNKIICDLVEEKFKGIISILDEECLRPGEATDLTFLEKLEDTVKPHPHFLTHKLADQKTRKSLDRGEFRLLHYAGEVTYSVTGFLDKNNDLLFRNLKETMCSSMNPIMAQCFDKSELSDKKRPETVATQFKMSLLQLVEILRSKEPAYIRCIKPNDAKQPGRFDEVLIRHQVKYLGLMENLRVRRAGFAYRRKYEAFLQRYKSLCPETWPMWAGRPQDGVAVLVRHLGYKPEEYKMGRTKIFIRFPKTLFATEDSLEVRRQSLATKIQAAWRGFHWRQKFLRVKRSAICIQSWWRGTLGRRKAAKRKWAAQTIRRLIRGFILRHSPRCPENAFFLDHVRASFLLNLRRQLPRNVLDTSWPTPPPALREASELLRELCMKNMVWKYCRSISPEWKQQLQQKAVASEIFKGKKDNYPQSVPRLFISTRLGTEEISPRVLQSLGSEPIQYAVPVVKYDRKGYKPRPRQLLLTPSAVVIVEDAKVKQRIDYANLTGISVSSLSDSLFVLHVQREDNKQKGDVVLQSDHVIETLTKTALSADRVNNININQGSITFAGGPGRDGIIDFTSGSELLITKAKNGHLAVVAPRLNSR
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
1 (in isoform 2)Acetylation-38.07-
3 (in isoform 3)Phosphorylation-9.98-
6 (in isoform 3)Phosphorylation-28.2026239621
10 (in isoform 3)Phosphorylation-40.2230635358
188UbiquitinationLEAFGNAKTLRNDNS
HHHHCCCCCCCCCCC
52.6822790023
196PhosphorylationTLRNDNSSRFGKYMD
CCCCCCCCCCEEEEE
37.5726824392
269AcetylationQSYLYLVKGQCAKVS
CCEEEEEECCEEECC
40.4422826441
281UbiquitinationKVSSINDKSDWKVMR
ECCCCCCHHHHHHHH
45.9122790023
281AcetylationKVSSINDKSDWKVMR
ECCCCCCHHHHHHHH
45.9122826441
361UbiquitinationTHRKIIAKGEELLSP
HCCCHHHCCCHHCCC
57.3522790023
373PhosphorylationLSPLNLEQAAYARDA
CCCCCHHHHHHHHHH
34.1619144319
376PhosphorylationLNLEQAAYARDALAK
CCHHHHHHHHHHHHH
12.7526060331
383MethylationYARDALAKAVYSRTF
HHHHHHHHHHHHHHH
38.95-
383UbiquitinationYARDALAKAVYSRTF
HHHHHHHHHHHHHHH
38.9522790023
404UbiquitinationINRSLASKDAESPSW
HHHHHHCCCCCCCCH
56.1822790023
404AcetylationINRSLASKDAESPSW
HHHHHHCCCCCCCCH
56.1823806337
408PhosphorylationLASKDAESPSWRSTT
HHCCCCCCCCHHHHH
26.4227087446
410PhosphorylationSKDAESPSWRSTTVL
CCCCCCCCHHHHHHH
44.3822324799
480GlutathionylationYFNNKIICDLVEEKF
HHCCEEHHHHHHHHH
3.6424333276
486UbiquitinationICDLVEEKFKGIISI
HHHHHHHHHCCHHHH
38.5822790023
486AcetylationICDLVEEKFKGIISI
HHHHHHHHHCCHHHH
38.5823806337
498GlutathionylationISILDEECLRPGEAT
HHHCCHHHCCCCCCC
3.5324333276
536PhosphorylationADQKTRKSLDRGEFR
CCHHHHHCCCCCCEE
32.0125263469
594AcetylationDKSELSDKKRPETVA
CHHHHCCCCCHHHHH
47.5119849379
595UbiquitinationKSELSDKKRPETVAT
HHHHCCCCCHHHHHH
77.5022790023
595AcetylationKSELSDKKRPETVAT
HHHHCCCCCHHHHHH
77.5019849387
617PhosphorylationQLVEILRSKEPAYIR
HHHHHHHCCCCCEEE
37.6219144319
618UbiquitinationLVEILRSKEPAYIRC
HHHHHHCCCCCEEEE
62.3722790023
647AcetylationVLIRHQVKYLGLMEN
HHHHHHHHHHHHHHH
28.3422826441
729PhosphorylationTLFATEDSLEVRRQS
CCEECCCCHHHHHHH
21.8729514104
736PhosphorylationSLEVRRQSLATKIQA
CHHHHHHHHHHHHHH
20.4027149854
739PhosphorylationVRRQSLATKIQAAWR
HHHHHHHHHHHHHHC
33.6928066266
740UbiquitinationRRQSLATKIQAAWRG
HHHHHHHHHHHHHCC
27.4922790023
763S-nitrosylationRVKRSAICIQSWWRG
HHCHHHHHHHHHHCC
2.0120925432
763S-nitrosocysteineRVKRSAICIQSWWRG
HHCHHHHHHHHHHCC
2.01-
799PhosphorylationRGFILRHSPRCPENA
HHHHHHCCCCCCCCC
13.9627717184
802S-nitrosylationILRHSPRCPENAFFL
HHHCCCCCCCCCCHH
5.8720925432
802S-nitrosocysteineILRHSPRCPENAFFL
HHHCCCCCCCCCCHH
5.87-
815PhosphorylationFLDHVRASFLLNLRR
HHHHHHHHHHHHHHH
13.0824899341
862PhosphorylationMVWKYCRSISPEWKQ
HHHHHHHHCCHHHHH
24.6926643407
864PhosphorylationWKYCRSISPEWKQQL
HHHHHHCCHHHHHHH
20.2926824392
868UbiquitinationRSISPEWKQQLQQKA
HHCCHHHHHHHHHHH
26.8922790023
916PhosphorylationRVLQSLGSEPIQYAV
HHHHHCCCCCCEEEE
45.5529514104
1039PhosphorylationDGIIDFTSGSELLIT
CCEEECCCCCEEEEE
40.0723737553
1041PhosphorylationIIDFTSGSELLITKA
EEECCCCCEEEEEEC
25.4926824392
1046PhosphorylationSGSELLITKAKNGHL
CCCEEEEEECCCCCE
25.5623737553
1062PhosphorylationVVAPRLNSR------
EEECCCCCC------
43.9122324799

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
1020SPhosphorylationKinaseGSK3BQ9WV60
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYO1C_MOUSE !!

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 MYO1C_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PKHB1_MOUSEPlekhb1physical
15976448
ACTS_HUMANACTA1physical
26496610
ACTB_HUMANACTBphysical
26496610
ACTG_HUMANACTG1physical
26496610
ACTN4_HUMANACTN4physical
26496610
ACTN1_HUMANACTN1physical
26496610
ADDA_HUMANADD1physical
26496610
AP2A1_HUMANAP2A1physical
26496610
DYST_HUMANDSTphysical
26496610
KCC2G_HUMANCAMK2Gphysical
26496610
CAZA1_HUMANCAPZA1physical
26496610
CAZA2_HUMANCAPZA2physical
26496610
CAPZB_HUMANCAPZBphysical
26496610
COF1_HUMANCFL1physical
26496610
COF2_HUMANCFL2physical
26496610
AP2M1_HUMANAP2M1physical
26496610
CLCA_HUMANCLTAphysical
26496610
CLCB_HUMANCLTBphysical
26496610
CLH1_HUMANCLTCphysical
26496610
DAB2_HUMANDAB2physical
26496610
DAPK3_HUMANDAPK3physical
26496610
DREB_HUMANDBN1physical
26496610
DCTN1_HUMANDCTN1physical
26496610
SRC8_HUMANCTTNphysical
26496610
EPS15_HUMANEPS15physical
26496610
FLII_HUMANFLIIphysical
26496610
FLNA_HUMANFLNAphysical
26496610
FLNB_HUMANFLNBphysical
26496610
GELS_HUMANGSNphysical
26496610
HS90A_HUMANHSP90AA1physical
26496610
ITPR1_HUMANITPR1physical
26496610
ITPR2_HUMANITPR2physical
26496610
ITPR3_HUMANITPR3physical
26496610
ABLM1_HUMANABLIM1physical
26496610
LMO7_HUMANLMO7physical
26496610
MYO1B_HUMANMYO1Bphysical
26496610
MYH9_HUMANMYH9physical
26496610
MYL6_HUMANMYL6physical
26496610
MYLK_HUMANMYLKphysical
26496610
MYO1E_HUMANMYO1Ephysical
26496610
MYO5A_HUMANMYO5Aphysical
26496610
MYO5B_HUMANMYO5Bphysical
26496610
MYO6_HUMANMYO6physical
26496610
MYPT1_HUMANPPP1R12Aphysical
26496610
MYPT2_HUMANPPP1R12Bphysical
26496610
NP1L1_HUMANNAP1L1physical
26496610
P3C2A_HUMANPIK3C2Aphysical
26496610
PP1A_HUMANPPP1CAphysical
26496610
PP1B_HUMANPPP1CBphysical
26496610
PP1G_HUMANPPP1CCphysical
26496610
TWF1_HUMANTWF1physical
26496610
S10AA_HUMANS100A10physical
26496610
SPTN1_HUMANSPTAN1physical
26496610
SPTB2_HUMANSPTBN1physical
26496610
SPTN2_HUMANSPTBN2physical
26496610
SSFA2_HUMANSSFA2physical
26496610
ST5_HUMANST5physical
26496610
SVIL_HUMANSVILphysical
26496610
TMOD1_HUMANTMOD1physical
26496610
TPM1_HUMANTPM1physical
26496610
TPM2_HUMANTPM2physical
26496610
TPM4_HUMANTPM4physical
26496610
TRPS1_HUMANTRPS1physical
26496610
COR2A_HUMANCORO2Aphysical
26496610
LUZP1_HUMANLUZP1physical
26496610
KAT6A_HUMANKAT6Aphysical
26496610
CLH2_HUMANCLTCL1physical
26496610
PICAL_HUMANPICALMphysical
26496610
SRBS2_HUMANSORBS2physical
26496610
LIPB1_HUMANPPFIBP1physical
26496610
HIP1R_HUMANHIP1Rphysical
26496610
LRRF2_HUMANLRRFIP2physical
26496610
EPN4_HUMANCLINT1physical
26496610
RHGBA_HUMANARHGAP11Aphysical
26496610
SC16A_HUMANSEC16Aphysical
26496610
WDR1_HUMANWDR1physical
26496610
TOM1_HUMANTOM1physical
26496610
ARPC4_HUMANARPC4physical
26496610
ARPC3_HUMANARPC3physical
26496610
ARC1B_HUMANARPC1Bphysical
26496610
ARP3_HUMANACTR3physical
26496610
ARP2_HUMANACTR2physical
26496610
ARPC2_HUMANARPC2physical
26496610
DCTN2_HUMANDCTN2physical
26496610
ML12A_HUMANMYL12Aphysical
26496610
GA2L1_HUMANGAS2L1physical
26496610
SYNPO_HUMANSYNPOphysical
26496610
RRAS2_HUMANRRAS2physical
26496610
AAK1_HUMANAAK1physical
26496610
LIMC1_HUMANLIMCH1physical
26496610
MPRIP_HUMANMPRIPphysical
26496610
COBL_HUMANCOBLphysical
26496610
CYTSA_HUMANSPECC1Lphysical
26496610
FBX46_HUMANFBXO46physical
26496610
COR1C_HUMANCORO1Cphysical
26496610
ZDHC5_HUMANZDHHC5physical
26496610
PKHG3_HUMANPLEKHG3physical
26496610
SI1L1_HUMANSIPA1L1physical
26496610
RAI14_HUMANRAI14physical
26496610
TIM13_HUMANTIMM13physical
26496610
TMOD3_HUMANTMOD3physical
26496610
CAR10_HUMANCARD10physical
26496610
LIMA1_HUMANLIMA1physical
26496610
GTSE1_HUMANGTSE1physical
26496610
SPN90_HUMANNCKIPSDphysical
26496610
BMP2K_HUMANBMP2Kphysical
26496610
UN45A_HUMANUNC45Aphysical
26496610
MYO5C_HUMANMYO5Cphysical
26496610
JPH1_HUMANJPH1physical
26496610
COR1B_HUMANCORO1Bphysical
26496610
K1211_HUMANKIAA1211physical
26496610
MTUS1_HUMANMTUS1physical
26496610
RHG21_HUMANARHGAP21physical
26496610
DEN1A_HUMANDENND1Aphysical
26496610
AFAP1_HUMANAFAP1physical
26496610
INF2_HUMANINF2physical
26496610
MYO19_HUMANMYO19physical
26496610
ARP5L_HUMANARPC5Lphysical
26496610
LZTS2_HUMANLZTS2physical
26496610
DCTN5_HUMANDCTN5physical
26496610
NEB2_HUMANPPP1R9Bphysical
26496610
LRCH3_HUMANLRCH3physical
26496610
STON2_HUMANSTON2physical
26496610
DOCK7_HUMANDOCK7physical
26496610
SSH2_HUMANSSH2physical
26496610
NEXN_HUMANNEXNphysical
26496610
CYTSB_HUMANSPECC1physical
26496610
FCHO2_HUMANFCHO2physical
26496610
MISP_HUMANMISPphysical
26496610
CD109_HUMANCD109physical
26496610
MYL6B_HUMANMYL6Bphysical
26496610
GA2L3_HUMANGAS2L3physical
26496610
TPRN_HUMANTPRNphysical
26496610
MY18A_HUMANMYO18Aphysical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MYO1C_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-408, AND MASSSPECTROMETRY.

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