LIMA1_MOUSE - dbPTM
LIMA1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LIMA1_MOUSE
UniProt AC Q9ERG0
Protein Name LIM domain and actin-binding protein 1
Gene Name Lima1
Organism Mus musculus (Mouse).
Sequence Length 753
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. This cytoskeletal protein colocalizes with actin stress fibers.
Protein Description Binds to actin monomers and filaments. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments (By similarity)..
Protein Sequence MESTPFNRRQWTSLSLRVTAKELSLVNKNKSSAIVEIFSKYQKAAEEANMERKKNNPESLPQHFRRGTLSVLKKKWENPVAGAEFHTDSLPNSSSEGGHTADYPPAEVTDKPAPGVRADREEHTQPKPRFGSRPEAVIQSRYPRSENSHDFKAQATESQKMENCLGDSRHEAEKPETSENTETSGKIEKYNVPLNRLKMMFEKGEHNQTKSLWTQSRNAGGRRLSENNCSLDDWEIGAGHLSSSAFNSEKNESKRNLELPRLSETSIKDRMAKYQAAVSKQSSPASYTNELKTSESKTHKWEQKENVPPGPEACSVHQEGSKVSTTENSLVALSVPAEDDTCNSQVKSEAQQPMHPKPLSPDARTSSLPESSPSKTAKKFQAPAKESCVECQKTVYPMERLLANQQVFHISCFRCSYCNNKLSLGTYASLHGRIYCKPHFNQLFKSKGNYDEGFGHKQHKDLWASKSDNEETLGRPAQPPNAGESPHSPGVEDAPIAKVGVLAASMEAKASSQREREDKPAETKKLRIAWPPPAELGGSGSALEEGIKVSKPKWPPEDDVCKTEAPEDVDLDLKKLRRSSSLKERSRPFTVAASFRTSSIKSPKASSPSLRKGWSESEQSEEFGGGIATMERKQTENARPSGEKENVGKSRWQGEEVPRSKDRSSFELESENFMENGANIAEDDNHVHAQQSPLEPEAPGWSGFVDTTAAKEFTTQNQKSQDVGFWEGEVVRELSVEEQIKRNRYYDEDEDEE
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
1Acetylation-------MESTPFNR
-------CCCCCCCH
9.18-
12PhosphorylationPFNRRQWTSLSLRVT
CCCHHHCHHEEEEEE
16.0826745281
13PhosphorylationFNRRQWTSLSLRVTA
CCHHHCHHEEEEEEH
17.0129895711
15PhosphorylationRRQWTSLSLRVTAKE
HHHCHHEEEEEEHHH
17.5627087446
21MalonylationLSLRVTAKELSLVNK
EEEEEEHHHHHHHCC
50.2326320211
59PhosphorylationRKKNNPESLPQHFRR
HHHCCHHHHCHHHHH
46.7522324799
65 (in isoform 2)Phosphorylation-33.7119144319
68PhosphorylationPQHFRRGTLSVLKKK
CHHHHHCHHHHHHHH
17.6622324799
70PhosphorylationHFRRGTLSVLKKKWE
HHHHCHHHHHHHHHC
25.8230352176
132PhosphorylationQPKPRFGSRPEAVIQ
CCCCCCCCCCHHHHH
41.7826643407
140PhosphorylationRPEAVIQSRYPRSEN
CCHHHHHCCCCCCCC
23.7429472430
148PhosphorylationRYPRSENSHDFKAQA
CCCCCCCCCCHHHHH
22.0027841257
181PhosphorylationKPETSENTETSGKIE
CCCCCCCCCCCCEEE
36.2725195567
189AcetylationETSGKIEKYNVPLNR
CCCCEEEECCCCHHH
45.6723806337
190PhosphorylationTSGKIEKYNVPLNRL
CCCEEEECCCCHHHH
14.4929514104
225PhosphorylationNAGGRRLSENNCSLD
CCCCCCCCCCCCCCC
36.1425521595
230PhosphorylationRLSENNCSLDDWEIG
CCCCCCCCCCCCCCC
36.6427087446
242PhosphorylationEIGAGHLSSSAFNSE
CCCCCCCCCHHHCCC
19.3025619855
243PhosphorylationIGAGHLSSSAFNSEK
CCCCCCCCHHHCCCC
31.8525619855
244PhosphorylationGAGHLSSSAFNSEKN
CCCCCCCHHHCCCCC
33.2425619855
248PhosphorylationLSSSAFNSEKNESKR
CCCHHHCCCCCHHHC
43.4225619855
253PhosphorylationFNSEKNESKRNLELP
HCCCCCHHHCCCCCC
46.4329514104
263PhosphorylationNLELPRLSETSIKDR
CCCCCCCCHHCHHHH
39.8626824392
265PhosphorylationELPRLSETSIKDRMA
CCCCCCHHCHHHHHH
32.1729176673
266PhosphorylationLPRLSETSIKDRMAK
CCCCCHHCHHHHHHH
24.4829514104
268UbiquitinationRLSETSIKDRMAKYQ
CCCHHCHHHHHHHHH
38.76-
273MalonylationSIKDRMAKYQAAVSK
CHHHHHHHHHHHHHC
28.6626320211
282PhosphorylationQAAVSKQSSPASYTN
HHHHHCCCCCCHHHH
41.8625619855
283PhosphorylationAAVSKQSSPASYTNE
HHHHCCCCCCHHHHC
23.2225619855
286PhosphorylationSKQSSPASYTNELKT
HCCCCCCHHHHCCCC
35.5525619855
287PhosphorylationKQSSPASYTNELKTS
CCCCCCHHHHCCCCC
18.7229514104
326O-linked_GlycosylationEGSKVSTTENSLVAL
CCCCEECCCCCEEEE
26.1828528544
328 (in isoform 2)Phosphorylation-38.2519144319
348PhosphorylationTCNSQVKSEAQQPMH
CCCHHHCHHCCCCCC
39.0325619855
360PhosphorylationPMHPKPLSPDARTSS
CCCCCCCCCCCCCCC
29.3025521595
365PhosphorylationPLSPDARTSSLPESS
CCCCCCCCCCCCCCC
25.1230635358
366PhosphorylationLSPDARTSSLPESSP
CCCCCCCCCCCCCCC
25.0730635358
367PhosphorylationSPDARTSSLPESSPS
CCCCCCCCCCCCCCC
47.5326824392
371PhosphorylationRTSSLPESSPSKTAK
CCCCCCCCCCCHHHH
45.6827087446
372PhosphorylationTSSLPESSPSKTAKK
CCCCCCCCCCHHHHH
31.3725521595
374PhosphorylationSLPESSPSKTAKKFQ
CCCCCCCCHHHHHHC
44.5822942356
376PhosphorylationPESSPSKTAKKFQAP
CCCCCCHHHHHHCCC
48.3124068923
396PhosphorylationVECQKTVYPMERLLA
HHHHCHHCCHHHHHC
11.33-
412S-palmitoylationQQVFHISCFRCSYCN
CCEEEEEEEECCCCC
2.1726165157
427PhosphorylationNKLSLGTYASLHGRI
CEEEECCCHHHCCEE
7.7529514104
437AcetylationLHGRIYCKPHFNQLF
HCCEEEECHHHHHHH
25.2623806337
437SuccinylationLHGRIYCKPHFNQLF
HCCEEEECHHHHHHH
25.2623806337
437SuccinylationLHGRIYCKPHFNQLF
HCCEEEECHHHHHHH
25.26-
450PhosphorylationLFKSKGNYDEGFGHK
HHHCCCCCCCCCCCC
24.8429514104
465PhosphorylationQHKDLWASKSDNEET
CHHHHHCCCCCCCCC
22.5527087446
467PhosphorylationKDLWASKSDNEETLG
HHHHCCCCCCCCCCC
43.0827087446
472PhosphorylationSKSDNEETLGRPAQP
CCCCCCCCCCCCCCC
28.4720469934
485PhosphorylationQPPNAGESPHSPGVE
CCCCCCCCCCCCCCC
27.3125521595
488PhosphorylationNAGESPHSPGVEDAP
CCCCCCCCCCCCCCC
27.0827087446
505PhosphorylationKVGVLAASMEAKASS
HHHHHHHHHHHHHHH
16.1426643407
539PhosphorylationPPAELGGSGSALEEG
CCHHHCCCCHHHHCC
27.9830352176
541PhosphorylationAELGGSGSALEEGIK
HHHCCCCHHHHCCCC
31.2323140645
579PhosphorylationDLKKLRRSSSLKERS
CHHHHHCCCCHHHCC
20.1820688971
580PhosphorylationLKKLRRSSSLKERSR
HHHHHCCCCHHHCCC
37.5722324799
581PhosphorylationKKLRRSSSLKERSRP
HHHHCCCCHHHCCCC
44.7130635358
590PhosphorylationKERSRPFTVAASFRT
HHCCCCCEEEEEEEC
16.3623140645
594PhosphorylationRPFTVAASFRTSSIK
CCCEEEEEEECCCCC
12.9118779572
597PhosphorylationTVAASFRTSSIKSPK
EEEEEEECCCCCCCC
25.4724453211
598PhosphorylationVAASFRTSSIKSPKA
EEEEEECCCCCCCCC
26.3023140645
599PhosphorylationAASFRTSSIKSPKAS
EEEEECCCCCCCCCC
33.1630352176
602PhosphorylationFRTSSIKSPKASSPS
EECCCCCCCCCCCCC
29.9326824392
604MalonylationTSSIKSPKASSPSLR
CCCCCCCCCCCCCHH
68.9126320211
606PhosphorylationSIKSPKASSPSLRKG
CCCCCCCCCCCHHCC
49.2422324799
607PhosphorylationIKSPKASSPSLRKGW
CCCCCCCCCCHHCCC
24.3026824392
609PhosphorylationSPKASSPSLRKGWSE
CCCCCCCCHHCCCCH
42.6321183079
615PhosphorylationPSLRKGWSESEQSEE
CCHHCCCCHHHHHHH
39.6625521595
617PhosphorylationLRKGWSESEQSEEFG
HHCCCCHHHHHHHHC
35.1123684622
620PhosphorylationGWSESEQSEEFGGGI
CCCHHHHHHHHCCCC
34.7325521595
629PhosphorylationEFGGGIATMERKQTE
HHCCCCCCCCHHHCC
20.0425777480
641PhosphorylationQTENARPSGEKENVG
HCCCCCCCCCCCCCC
54.7726824392
660PhosphorylationQGEEVPRSKDRSSFE
CCCCCCCCCCCCCHH
32.6029514104
664PhosphorylationVPRSKDRSSFELESE
CCCCCCCCCHHCCCC
49.8925338131
692PhosphorylationNHVHAQQSPLEPEAP
CCCCCCCCCCCCCCC
21.2624453211
714PhosphorylationTTAAKEFTTQNQKSQ
HHHHHHHCCCCCCCC
28.6726643407
715PhosphorylationTAAKEFTTQNQKSQD
HHHHHHCCCCCCCCC
30.7326643407
719UbiquitinationEFTTQNQKSQDVGFW
HHCCCCCCCCCCCCC
58.60-
720PhosphorylationFTTQNQKSQDVGFWE
HCCCCCCCCCCCCCC
23.1125521595
735PhosphorylationGEVVRELSVEEQIKR
CEEEEEECHHHHHHH
23.8025521595
745PhosphorylationEQIKRNRYYDEDEDE
HHHHHCCCCCCCCCC
20.8622817900
746PhosphorylationQIKRNRYYDEDEDEE
HHHHCCCCCCCCCCC
15.0422817900

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
360SPhosphorylationKinaseERK1P27361
PSP
602SPhosphorylationKinaseERK1P27361
PSP
692SPhosphorylationKinaseERK1P27361
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LIMA1_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 LIMA1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTS_HUMANACTA1physical
26496610
ACTG_HUMANACTG1physical
26496610
ACTN4_HUMANACTN4physical
26496610
ACTN1_HUMANACTN1physical
26496610
ADDA_HUMANADD1physical
26496610
ADDG_HUMANADD3physical
26496610
AP2A1_HUMANAP2A1physical
26496610
CAZA1_HUMANCAPZA1physical
26496610
CAZA2_HUMANCAPZA2physical
26496610
CAPZB_HUMANCAPZBphysical
26496610
CAV1_HUMANCAV1physical
26496610
CDC42_HUMANCDC42physical
26496610
COF1_HUMANCFL1physical
26496610
COF2_HUMANCFL2physical
26496610
AP2M1_HUMANAP2M1physical
26496610
CLCA_HUMANCLTAphysical
26496610
CLCB_HUMANCLTBphysical
26496610
CLH1_HUMANCLTCphysical
26496610
COX6C_HUMANCOX6Cphysical
26496610
CBPM_HUMANCPMphysical
26496610
DAB2_HUMANDAB2physical
26496610
DREB_HUMANDBN1physical
26496610
EPS15_HUMANEPS15physical
26496610
ADX_HUMANFDX1physical
26496610
FLII_HUMANFLIIphysical
26496610
FLNA_HUMANFLNAphysical
26496610
FLNB_HUMANFLNBphysical
26496610
GNAI1_HUMANGNAI1physical
26496610
GNAS3_HUMANGNASphysical
26496610
GNAS2_HUMANGNASphysical
26496610
ALEX_HUMANGNASphysical
26496610
GNAS1_HUMANGNASphysical
26496610
GELS_HUMANGSNphysical
26496610
GTF2I_HUMANGTF2Iphysical
26496610
ITPR1_HUMANITPR1physical
26496610
ITPR2_HUMANITPR2physical
26496610
ABLM1_HUMANABLIM1physical
26496610
LMO7_HUMANLMO7physical
26496610
MYO1B_HUMANMYO1Bphysical
26496610
MYO1C_HUMANMYO1Cphysical
26496610
MYO1E_HUMANMYO1Ephysical
26496610
MYO5A_HUMANMYO5Aphysical
26496610
MYO5B_HUMANMYO5Bphysical
26496610
MYPT1_HUMANPPP1R12Aphysical
26496610
NP1L1_HUMANNAP1L1physical
26496610
NP1L4_HUMANNAP1L4physical
26496610
PHB_HUMANPHBphysical
26496610
PLEC_HUMANPLECphysical
26496610
PP1A_HUMANPPP1CAphysical
26496610
PSMD4_HUMANPSMD4physical
26496610
TWF1_HUMANTWF1physical
26496610
RAP1B_HUMANRAP1Bphysical
26496610
S10AA_HUMANS100A10physical
26496610
SDC4_HUMANSDC4physical
26496610
SOAT1_HUMANSOAT1physical
26496610
SPTN1_HUMANSPTAN1physical
26496610
SPTB2_HUMANSPTBN1physical
26496610
SSFA2_HUMANSSFA2physical
26496610
SVIL_HUMANSVILphysical
26496610
TMOD1_HUMANTMOD1physical
26496610
BACD2_HUMANTNFAIP1physical
26496610
TPM1_HUMANTPM1physical
26496610
TPM2_HUMANTPM2physical
26496610
ENPL_HUMANHSP90B1physical
26496610
COR2A_HUMANCORO2Aphysical
26496610
LUZP1_HUMANLUZP1physical
26496610
CLH2_HUMANCLTCL1physical
26496610
PICAL_HUMANPICALMphysical
26496610
IQGA1_HUMANIQGAP1physical
26496610
HIP1R_HUMANHIP1Rphysical
26496610
RAI3_HUMANGPRC5Aphysical
26496610
LRRF2_HUMANLRRFIP2physical
26496610
NOLC1_HUMANNOLC1physical
26496610
SC16A_HUMANSEC16Aphysical
26496610
WDR1_HUMANWDR1physical
26496610
ARPC5_HUMANARPC5physical
26496610
ARPC4_HUMANARPC4physical
26496610
ARPC3_HUMANARPC3physical
26496610
ARC1B_HUMANARPC1Bphysical
26496610
ARP2_HUMANACTR2physical
26496610
ARPC2_HUMANARPC2physical
26496610
BASP1_HUMANBASP1physical
26496610
IPO7_HUMANIPO7physical
26496610
DCTN2_HUMANDCTN2physical
26496610
SMC2_HUMANSMC2physical
26496610
AKAP2_HUMANAKAP2physical
26496610
PHB2_HUMANPHB2physical
26496610
SYNPO_HUMANSYNPOphysical
26496610
RRAS2_HUMANRRAS2physical
26496610
CE162_HUMANCEP162physical
26496610
AAK1_HUMANAAK1physical
26496610
SI1L3_HUMANSIPA1L3physical
26496610
MPRIP_HUMANMPRIPphysical
26496610
COBL_HUMANCOBLphysical
26496610
CYTSA_HUMANSPECC1Lphysical
26496610
SIR1_HUMANSIRT1physical
26496610
ZN346_HUMANZNF346physical
26496610
COR1C_HUMANCORO1Cphysical
26496610
ZDHC5_HUMANZDHHC5physical
26496610
PKHG3_HUMANPLEKHG3physical
26496610
RAI14_HUMANRAI14physical
26496610
ZBT20_HUMANZBTB20physical
26496610
TMOD3_HUMANTMOD3physical
26496610
DCTN4_HUMANDCTN4physical
26496610
EURL_HUMANC21orf91physical
26496610
NDE1_HUMANNDE1physical
26496610
LIN7C_HUMANLIN7Cphysical
26496610
MYO5C_HUMANMYO5Cphysical
26496610
CCD47_HUMANCCDC47physical
26496610
COR1B_HUMANCORO1Bphysical
26496610
AFAP1_HUMANAFAP1physical
26496610
INF2_HUMANINF2physical
26496610
AHNK_HUMANAHNAKphysical
26496610
MYO19_HUMANMYO19physical
26496610
ARP5L_HUMANARPC5Lphysical
26496610
BACD3_HUMANKCTD10physical
26496610
GLYR1_HUMANGLYR1physical
26496610
STON2_HUMANSTON2physical
26496610
DIXC1_HUMANDIXDC1physical
26496610
SSH2_HUMANSSH2physical
26496610
NEXN_HUMANNEXNphysical
26496610
CYTSB_HUMANSPECC1physical
26496610
FCHO2_HUMANFCHO2physical
26496610
MISP_HUMANMISPphysical
26496610
UBX2A_HUMANUBXN2Aphysical
26496610
PPR18_HUMANPPP1R18physical
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 LIMA1_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-488, AND MASSSPECTROMETRY.
"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-735, 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-225; SER-230; SER-467AND SER-488, AND MASS SPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND MASSSPECTROMETRY.
"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-225; SER-230; SER-367;SER-485; SER-488 AND SER-615, AND MASS SPECTROMETRY.
"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-539, AND MASSSPECTROMETRY.

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