LMNA_MOUSE - dbPTM
LMNA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LMNA_MOUSE
UniProt AC P48678
Protein Name Prelamin-A/C
Gene Name Lmna
Organism Mus musculus (Mouse).
Sequence Length 665
Subcellular Localization Nucleus . Nucleus envelope. Nucleus lamina. Nucleus, nucleoplasm. Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleaveage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then b
Protein Description Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone. Required for cardiac homeostasis. [PubMed: 26436652 Isoform C2 may have a role in determining the organization of nuclear and chromosomal structures during spermatogenesis.; Prelamin-A/C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (By similarity]
Protein Sequence METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQSQGGGSVTKKRKLESSESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIRRQNGDDPLMTYRFPPKFTLKAGQVVTIWASGAGATHSPPTDLVWKAQNTWGCGSSLRTALINSTGEEVAMRKLVRSLTMVEDNEDDDEDGEELLHHHRGSHCSGSGDPAEYNLRSRTVLCGTCGQPADKAAGGAGAQVGGSISSGSSASSVTVTRSFRSVGGSGGGSFGDNLVTRSYLLGNSSPRSQSSQNCSIM
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-------METPSQRR
-------CCCHHHHH
13.44-
3Phosphorylation-----METPSQRRAT
-----CCCHHHHHHC
27.2627717184
5Phosphorylation---METPSQRRATRS
---CCCHHHHHHCCC
43.6828507225
10PhosphorylationTPSQRRATRSGAQAS
CHHHHHHCCCCCCCC
24.4526160508
12PhosphorylationSQRRATRSGAQASST
HHHHHCCCCCCCCCC
33.8427087446
17PhosphorylationTRSGAQASSTPLSPT
CCCCCCCCCCCCCCC
23.7527087446
18PhosphorylationRSGAQASSTPLSPTR
CCCCCCCCCCCCCCH
36.7427087446
19PhosphorylationSGAQASSTPLSPTRI
CCCCCCCCCCCCCHH
26.2527087446
22PhosphorylationQASSTPLSPTRITRL
CCCCCCCCCCHHHHC
25.9827087446
23UbiquitinationASSTPLSPTRITRLQ
CCCCCCCCCHHHHCH
33.1227667366
24PhosphorylationSSTPLSPTRITRLQE
CCCCCCCCHHHHCHH
31.1825521595
27PhosphorylationPLSPTRITRLQEKED
CCCCCHHHHCHHHHH
23.2624453211
32UbiquitinationRITRLQEKEDLQELN
HHHHCHHHHHHHHHH
43.5022790023
32AcetylationRITRLQEKEDLQELN
HHHHCHHHHHHHHHH
43.5023806337
32SuccinylationRITRLQEKEDLQELN
HHHHCHHHHHHHHHH
43.50-
32SuccinylationRITRLQEKEDLQELN
HHHHCHHHHHHHHHH
43.5023806337
32UbiquitinationRITRLQEKEDLQELN
HHHHCHHHHHHHHHH
43.50-
45PhosphorylationLNDRLAVYIDRVRSL
HHHHHHHHHHHHHHH
7.4725367039
51PhosphorylationVYIDRVRSLETENAG
HHHHHHHHHCCCCCC
27.9227180971
54PhosphorylationDRVRSLETENAGLRL
HHHHHHCCCCCCEEE
39.5728066266
59UbiquitinationLETENAGLRLRITES
HCCCCCCEEEEEECC
4.3027667366
66PhosphorylationLRLRITESEEVVSRE
EEEEEECCHHHHHHH
30.3327180971
68UbiquitinationLRITESEEVVSREVS
EEEECCHHHHHHHHH
58.4627667366
69UbiquitinationRITESEEVVSREVSG
EEECCHHHHHHHHHC
4.0927667366
71PhosphorylationTESEEVVSREVSGIK
ECCHHHHHHHHHCHH
28.0926824392
75PhosphorylationEVVSREVSGIKAAYE
HHHHHHHHCHHHHHH
30.0126060331
78UbiquitinationSREVSGIKAAYEAEL
HHHHHCHHHHHHHHH
30.4122790023
78UbiquitinationSREVSGIKAAYEAEL
HHHHHCHHHHHHHHH
30.41-
89UbiquitinationEAELGDARKTLDSVA
HHHHCCHHHHHHHHH
36.9127667366
90AcetylationAELGDARKTLDSVAK
HHHCCHHHHHHHHHH
55.9823806337
90MalonylationAELGDARKTLDSVAK
HHHCCHHHHHHHHHH
55.9832601280
90SuccinylationAELGDARKTLDSVAK
HHHCCHHHHHHHHHH
55.9823806337
94PhosphorylationDARKTLDSVAKERAR
CHHHHHHHHHHHHHH
27.38-
96UbiquitinationRKTLDSVAKERARLQ
HHHHHHHHHHHHHHH
16.3727667366
97UbiquitinationKTLDSVAKERARLQL
HHHHHHHHHHHHHHH
45.6522790023
97AcetylationKTLDSVAKERARLQL
HHHHHHHHHHHHHHH
45.6523954790
97MalonylationKTLDSVAKERARLQL
HHHHHHHHHHHHHHH
45.6526073543
97UbiquitinationKTLDSVAKERARLQL
HHHHHHHHHHHHHHH
45.6527667366
107PhosphorylationARLQLELSKVREEFK
HHHHHHHHHHHHHHH
21.5226824392
108UbiquitinationRLQLELSKVREEFKE
HHHHHHHHHHHHHHH
58.9222790023
108AcetylationRLQLELSKVREEFKE
HHHHHHHHHHHHHHH
58.9222826441
108MalonylationRLQLELSKVREEFKE
HHHHHHHHHHHHHHH
58.9226320211
108UbiquitinationRLQLELSKVREEFKE
HHHHHHHHHHHHHHH
58.92-
114UbiquitinationSKVREEFKELKARNT
HHHHHHHHHHHHHCC
66.4722790023
114AcetylationSKVREEFKELKARNT
HHHHHHHHHHHHHCC
66.4723236377
114MalonylationSKVREEFKELKARNT
HHHHHHHHHHHHHCC
66.4726320211
114UbiquitinationSKVREEFKELKARNT
HHHHHHHHHHHHHCC
66.4727667366
121UbiquitinationKELKARNTKKEGDLL
HHHHHHCCHHHHHHH
37.6327667366
123AcetylationLKARNTKKEGDLLAA
HHHHCCHHHHHHHHH
65.9623806337
123MalonylationLKARNTKKEGDLLAA
HHHHCCHHHHHHHHH
65.9626320211
135UbiquitinationLAAQARLKDLEALLN
HHHHHHHHHHHHHHC
55.5022790023
135AcetylationLAAQARLKDLEALLN
HHHHHHHHHHHHHHC
55.5023806337
135MalonylationLAAQARLKDLEALLN
HHHHHHHHHHHHHHC
55.5026320211
135UbiquitinationLAAQARLKDLEALLN
HHHHHHHHHHHHHHC
55.5027667366
143PhosphorylationDLEALLNSKEAALST
HHHHHHCCHHHHHHH
31.6629514104
144UbiquitinationLEALLNSKEAALSTA
HHHHHCCHHHHHHHH
50.7522790023
144AcetylationLEALLNSKEAALSTA
HHHHHCCHHHHHHHH
50.7523806337
144SuccinylationLEALLNSKEAALSTA
HHHHHCCHHHHHHHH
50.7523806337
144UbiquitinationLEALLNSKEAALSTA
HHHHHCCHHHHHHHH
50.75-
153PhosphorylationAALSTALSEKRTLEG
HHHHHHHHHCCHHHH
38.3128464351
155UbiquitinationLSTALSEKRTLEGEL
HHHHHHHCCHHHHHH
47.5122790023
155AcetylationLSTALSEKRTLEGEL
HHHHHHHCCHHHHHH
47.5123806337
155MalonylationLSTALSEKRTLEGEL
HHHHHHHCCHHHHHH
47.5126320211
155UbiquitinationLSTALSEKRTLEGEL
HHHHHHHCCHHHHHH
47.51-
158UbiquitinationALSEKRTLEGELHDL
HHHHCCHHHHHHHHH
10.3927667366
171UbiquitinationDLRGQVAKLEAALGE
HHHHHHHHHHHHHHH
48.2622790023
171AcetylationDLRGQVAKLEAALGE
HHHHHHHHHHHHHHH
48.2623806337
171SuccinylationDLRGQVAKLEAALGE
HHHHHHHHHHHHHHH
48.26-
171SuccinylationDLRGQVAKLEAALGE
HHHHHHHHHHHHHHH
48.2623806337
171UbiquitinationDLRGQVAKLEAALGE
HHHHHHHHHHHHHHH
48.2627667366
180UbiquitinationEAALGEAKKQLQDEM
HHHHHHHHHHHHHHH
36.4322790023
180AcetylationEAALGEAKKQLQDEM
HHHHHHHHHHHHHHH
36.437668129
180MalonylationEAALGEAKKQLQDEM
HHHHHHHHHHHHHHH
36.4326320211
180UbiquitinationEAALGEAKKQLQDEM
HHHHHHHHHHHHHHH
36.4327667366
181UbiquitinationAALGEAKKQLQDEML
HHHHHHHHHHHHHHH
64.3922790023
181MalonylationAALGEAKKQLQDEML
HHHHHHHHHHHHHHH
64.3926320211
181UbiquitinationAALGEAKKQLQDEML
HHHHHHHHHHHHHHH
64.3927667366
199PhosphorylationDAENRLQTLKEELDF
CHHHHHHHHHHHHHH
44.378477740
199UbiquitinationDAENRLQTLKEELDF
CHHHHHHHHHHHHHH
44.3727667366
201UbiquitinationENRLQTLKEELDFQK
HHHHHHHHHHHHHHH
53.1622790023
201AcetylationENRLQTLKEELDFQK
HHHHHHHHHHHHHHH
53.1623806337
201MalonylationENRLQTLKEELDFQK
HHHHHHHHHHHHHHH
53.1626320211
201SuccinylationENRLQTLKEELDFQK
HHHHHHHHHHHHHHH
53.1623806337
201SumoylationENRLQTLKEELDFQK
HHHHHHHHHHHHHHH
53.16-
201UbiquitinationENRLQTLKEELDFQK
HHHHHHHHHHHHHHH
53.1627667366
208UbiquitinationKEELDFQKNIYSEEL
HHHHHHHHHHCCHHH
45.3522790023
208AcetylationKEELDFQKNIYSEEL
HHHHHHHHHHCCHHH
45.3523954790
208UbiquitinationKEELDFQKNIYSEEL
HHHHHHHHHHCCHHH
45.3527667366
211PhosphorylationLDFQKNIYSEELRET
HHHHHHHCCHHHHHH
21.3023984901
212PhosphorylationDFQKNIYSEELRETK
HHHHHHCCHHHHHHH
22.3126824392
218PhosphorylationYSEELRETKRRHETR
CCHHHHHHHHHHCCE
24.3423984901
219UbiquitinationSEELRETKRRHETRL
CHHHHHHHHHHCCEE
42.5622790023
219UbiquitinationSEELRETKRRHETRL
CHHHHHHHHHHCCEE
42.56-
224PhosphorylationETKRRHETRLVEIDN
HHHHHHCCEEEEECC
24.15-
233UbiquitinationLVEIDNGKQREFESR
EEEECCCCHHHHHHH
53.0622790023
233AcetylationLVEIDNGKQREFESR
EEEECCCCHHHHHHH
53.0623236377
233UbiquitinationLVEIDNGKQREFESR
EEEECCCCHHHHHHH
53.0627667366
239PhosphorylationGKQREFESRLADALQ
CCHHHHHHHHHHHHH
37.6025338131
260AcetylationEDQVEQYKKELEKTY
HHHHHHHHHHHHHHH
39.1923806337
261AcetylationDQVEQYKKELEKTYS
HHHHHHHHHHHHHHH
63.70129605
265AcetylationQYKKELEKTYSAKLD
HHHHHHHHHHHHHHH
66.4423954790
265MalonylationQYKKELEKTYSAKLD
HHHHHHHHHHHHHHH
66.4426320211
266PhosphorylationYKKELEKTYSAKLDN
HHHHHHHHHHHHHHH
17.2120469934
267PhosphorylationKKELEKTYSAKLDNA
HHHHHHHHHHHHHHH
20.0720469934
268PhosphorylationKELEKTYSAKLDNAR
HHHHHHHHHHHHHHH
24.9420469934
270UbiquitinationLEKTYSAKLDNARQS
HHHHHHHHHHHHHHH
50.8922790023
270AcetylationLEKTYSAKLDNARQS
HHHHHHHHHHHHHHH
50.8923806337
270MalonylationLEKTYSAKLDNARQS
HHHHHHHHHHHHHHH
50.8926320211
270SuccinylationLEKTYSAKLDNARQS
HHHHHHHHHHHHHHH
50.8923806337
270UbiquitinationLEKTYSAKLDNARQS
HHHHHHHHHHHHHHH
50.8927667366
277PhosphorylationKLDNARQSAERNSNL
HHHHHHHHHHHHHCH
26.9226824392
282PhosphorylationRQSAERNSNLVGAAH
HHHHHHHHCHHHHHH
37.4524453211
301PhosphorylationQSRIRIDSLSAQLSQ
HHCHHHHHHHHHHHH
23.1125521595
303PhosphorylationRIRIDSLSAQLSQLQ
CHHHHHHHHHHHHHH
20.2327742792
307PhosphorylationDSLSAQLSQLQKQLA
HHHHHHHHHHHHHHH
19.4329472430
311UbiquitinationAQLSQLQKQLAAKEA
HHHHHHHHHHHHHHH
56.7422790023
311AcetylationAQLSQLQKQLAAKEA
HHHHHHHHHHHHHHH
56.7423806337
311UbiquitinationAQLSQLQKQLAAKEA
HHHHHHHHHHHHHHH
56.7427667366
316MalonylationLQKQLAAKEAKLRDL
HHHHHHHHHHHHHHH
53.2326320211
319UbiquitinationQLAAKEAKLRDLEDS
HHHHHHHHHHHHHHH
45.1822790023
319AcetylationQLAAKEAKLRDLEDS
HHHHHHHHHHHHHHH
45.1823236377
319UbiquitinationQLAAKEAKLRDLEDS
HHHHHHHHHHHHHHH
45.18-
326PhosphorylationKLRDLEDSLARERDT
HHHHHHHHHHHHHHH
17.9819367708
345UbiquitinationLAEKEREMAEMRARM
HHHHHHHHHHHHHHH
4.8527667366
378UbiquitinationMEIHAYRKLLEGEEE
HHHHHHHHHHCCHHH
44.7622790023
378AcetylationMEIHAYRKLLEGEEE
HHHHHHHHHHCCHHH
44.7622631205
378UbiquitinationMEIHAYRKLLEGEEE
HHHHHHHHHHCCHHH
44.76-
390PhosphorylationEEERLRLSPSPTSQR
HHHHHCCCCCCCCCC
19.5227087446
392PhosphorylationERLRLSPSPTSQRSR
HHHCCCCCCCCCCCC
37.1227087446
392 (in isoform 2)Phosphorylation-37.121959608
394PhosphorylationLRLSPSPTSQRSRGR
HCCCCCCCCCCCCCC
41.6627087446
395PhosphorylationRLSPSPTSQRSRGRA
CCCCCCCCCCCCCCC
27.2925521595
398PhosphorylationPSPTSQRSRGRASSH
CCCCCCCCCCCCCCC
31.3026824392
403PhosphorylationQRSRGRASSHSSQSQ
CCCCCCCCCCCCCCC
27.5027087446
404PhosphorylationRSRGRASSHSSQSQG
CCCCCCCCCCCCCCC
26.8027087446
406PhosphorylationRGRASSHSSQSQGGG
CCCCCCCCCCCCCCC
31.8327087446
407PhosphorylationGRASSHSSQSQGGGS
CCCCCCCCCCCCCCC
28.5527087446
407 (in isoform 2)Phosphorylation-28.551959608
409PhosphorylationASSHSSQSQGGGSVT
CCCCCCCCCCCCCCC
32.5127087446
409 (in isoform 2)Phosphorylation-32.511959608
414PhosphorylationSQSQGGGSVTKKRKL
CCCCCCCCCCCCHHC
29.8627087446
416PhosphorylationSQGGGSVTKKRKLES
CCCCCCCCCCHHCCC
32.3327087446
417AcetylationQGGGSVTKKRKLESS
CCCCCCCCCHHCCCC
48.72109369
418AcetylationGGGSVTKKRKLESSE
CCCCCCCCHHCCCCC
45.457338331
420AcetylationGSVTKKRKLESSESR
CCCCCCHHCCCCCCH
66.5423806337
423PhosphorylationTKKRKLESSESRSSF
CCCHHCCCCCCHHHH
50.2526824392
424PhosphorylationKKRKLESSESRSSFS
CCHHCCCCCCHHHHH
30.1626824392
426PhosphorylationRKLESSESRSSFSQH
HHCCCCCCHHHHHHH
39.1426824392
428PhosphorylationLESSESRSSFSQHAR
CCCCCCHHHHHHHHH
45.0423684622
429PhosphorylationESSESRSSFSQHART
CCCCCHHHHHHHHHH
28.0127087446
431PhosphorylationSESRSSFSQHARTSG
CCCHHHHHHHHHHHC
24.0124899341
450UbiquitinationEEVDEEGKFVRLRNK
EEECCCCCEEEEECC
43.9222790023
450AcetylationEEVDEEGKFVRLRNK
EEECCCCCEEEEECC
43.9223806337
450SuccinylationEEVDEEGKFVRLRNK
EEECCCCCEEEEECC
43.9223806337
450UbiquitinationEEVDEEGKFVRLRNK
EEECCCCCEEEEECC
43.92-
457AcetylationKFVRLRNKSNEDQSM
CEEEEECCCCCCCCC
48.5023806337
457MalonylationKFVRLRNKSNEDQSM
CEEEEECCCCCCCCC
48.5026320211
457UbiquitinationKFVRLRNKSNEDQSM
CEEEEECCCCCCCCC
48.5027667366
458PhosphorylationFVRLRNKSNEDQSMG
EEEEECCCCCCCCCC
49.3425521595
458 (in isoform 3)Phosphorylation-49.3428507225
460 (in isoform 3)Phosphorylation-65.6029514104
463PhosphorylationNKSNEDQSMGNWQIR
CCCCCCCCCCCCCHH
40.7627742792
480PhosphorylationNGDDPLMTYRFPPKF
CCCCCCEEEECCCCE
21.168477740
496PhosphorylationLKAGQVVTIWASGAG
EECCCEEEEEECCCC
16.3723984901
500PhosphorylationQVVTIWASGAGATHS
CEEEEEECCCCCCCC
17.7423984901
505PhosphorylationWASGAGATHSPPTDL
EECCCCCCCCCCCCC
23.2023984901
507PhosphorylationSGAGATHSPPTDLVW
CCCCCCCCCCCCCEE
28.3723984901
510PhosphorylationGATHSPPTDLVWKAQ
CCCCCCCCCCEEECC
45.4023984901
522GlutathionylationKAQNTWGCGSSLRTA
ECCCCCCCCHHHHHH
3.4424333276
522S-palmitoylationKAQNTWGCGSSLRTA
ECCCCCCCCHHHHHH
3.4428526873
524PhosphorylationQNTWGCGSSLRTALI
CCCCCCCHHHHHHHH
30.2129514104
525PhosphorylationNTWGCGSSLRTALIN
CCCCCCHHHHHHHHC
13.738477740
528PhosphorylationGCGSSLRTALINSTG
CCCHHHHHHHHCCCC
30.9828066266
533PhosphorylationLRTALINSTGEEVAM
HHHHHHCCCCHHHHH
30.6926824392
534PhosphorylationRTALINSTGEEVAMR
HHHHHCCCCHHHHHH
44.0925521595
546PhosphorylationAMRKLVRSLTMVEDN
HHHHHHHHCCCCCCC
22.2527087446
548PhosphorylationRKLVRSLTMVEDNED
HHHHHHCCCCCCCCC
22.0326824392
570PhosphorylationLLHHHRGSHCSGSGD
HHHHCCCCCCCCCCC
22.6827087446
570 (in isoform 2)Phosphorylation-22.6828507225
572GlutathionylationHHHRGSHCSGSGDPA
HHCCCCCCCCCCCHH
5.4424333276
572 (in isoform 2)Phosphorylation-5.4429514104
573PhosphorylationHHRGSHCSGSGDPAE
HCCCCCCCCCCCHHH
30.4825521595
575PhosphorylationRGSHCSGSGDPAEYN
CCCCCCCCCCHHHHC
24.5926824392
581PhosphorylationGSGDPAEYNLRSRTV
CCCCHHHHCCCCCEE
22.9225619855
585PhosphorylationPAEYNLRSRTVLCGT
HHHHCCCCCEEEECC
35.1525619855
587PhosphorylationEYNLRSRTVLCGTCG
HHCCCCCEEEECCCC
21.0525619855
592PhosphorylationSRTVLCGTCGQPADK
CCEEEECCCCCCCHH
16.6825619855
611O-linked_GlycosylationAGAQVGGSISSGSSA
CCCCCCCCCCCCCCC
17.2321540332
611PhosphorylationAGAQVGGSISSGSSA
CCCCCCCCCCCCCCC
17.2325619855
613O-linked_GlycosylationAQVGGSISSGSSASS
CCCCCCCCCCCCCCE
30.2821540332
613PhosphorylationAQVGGSISSGSSASS
CCCCCCCCCCCCCCE
30.2825619855
614O-linked_GlycosylationQVGGSISSGSSASSV
CCCCCCCCCCCCCEE
40.8121540332
614PhosphorylationQVGGSISSGSSASSV
CCCCCCCCCCCCCEE
40.8125619855
616PhosphorylationGGSISSGSSASSVTV
CCCCCCCCCCCEEEE
25.3626824392
617PhosphorylationGSISSGSSASSVTVT
CCCCCCCCCCEEEEE
35.3827087446
619PhosphorylationISSGSSASSVTVTRS
CCCCCCCCEEEEEEE
27.5625619855
620PhosphorylationSSGSSASSVTVTRSF
CCCCCCCEEEEEEEE
22.8627087446
622PhosphorylationGSSASSVTVTRSFRS
CCCCCEEEEEEEECC
20.3625619855
624PhosphorylationSASSVTVTRSFRSVG
CCCEEEEEEEECCCC
15.9525619855
626PhosphorylationSSVTVTRSFRSVGGS
CEEEEEEEECCCCCC
18.6926643407
629PhosphorylationTVTRSFRSVGGSGGG
EEEEEECCCCCCCCC
24.0925521595
633PhosphorylationSFRSVGGSGGGSFGD
EECCCCCCCCCCCCC
28.4725521595
637PhosphorylationVGGSGGGSFGDNLVT
CCCCCCCCCCCCHHH
29.3627087446
644O-linked_GlycosylationSFGDNLVTRSYLLGN
CCCCCHHHHHHHCCC
19.6421540332
644PhosphorylationSFGDNLVTRSYLLGN
CCCCCHHHHHHHCCC
19.6425619855
646PhosphorylationGDNLVTRSYLLGNSS
CCCHHHHHHHCCCCC
15.6927717184
647PhosphorylationDNLVTRSYLLGNSSP
CCHHHHHHHCCCCCC
11.5822802335
652PhosphorylationRSYLLGNSSPRSQSS
HHHHCCCCCCCCCCC
39.6622802335
653PhosphorylationSYLLGNSSPRSQSSQ
HHHCCCCCCCCCCCC
28.4726824392
662FarnesylationRSQSSQNCSIM----
CCCCCCCCCCC----
1.95-
662MethylationRSQSSQNCSIM----
CCCCCCCCCCC----
1.95-

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
5SPhosphorylationKinasePKC_GROUP-PhosphoELM
5SPhosphorylationKinasePRKCAP20444
GPS
5SPhosphorylationKinasePKC-FAMILY-GPS
22SPhosphorylationKinaseMAPK1P63085
GPS
199TPhosphorylationKinasePRKCAP20444
GPS
199TPhosphorylationKinasePKC_GROUP-PhosphoELM
199TPhosphorylationKinasePKC-FAMILY-GPS
390SPhosphorylationKinaseCDK1P06493
PSP
390SPhosphorylationKinaseCDK_GROUP-PhosphoELM
390SPhosphorylationKinaseCDK-FAMILY-GPS
392SPhosphorylationKinaseCDK-FAMILY-GPS
392SPhosphorylationKinaseCDK_GROUP-PhosphoELM
392SPhosphorylationKinaseCDK1P06493
PSP
392SPhosphorylationKinaseCDK1P11440
PSP
404SPhosphorylationKinaseP70-SUBFAMILY-GPS
404SPhosphorylationKinaseP70S6K_GROUP-PhosphoELM
416TPhosphorylationKinasePKC-FAMILY-GPS
416TPhosphorylationKinasePRKCAP20444
GPS
416TPhosphorylationKinasePKC_GROUP-PhosphoELM
480TPhosphorylationKinasePKC-FAMILY-GPS
480TPhosphorylationKinasePKC_GROUP-PhosphoELM
480TPhosphorylationKinasePRKCAP20444
GPS
525SPhosphorylationKinasePRKCAP20444
GPS
575SPhosphorylationKinasePRKCAP17252
GPS
652SPhosphorylationKinasePRKCAP20444
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
392SPhosphorylation

1959608
407SPhosphorylation

1959608
409SPhosphorylation

1959608

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 LMNA_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LMNB1_MOUSELmnb1physical
21327095
LMNB2_MOUSELmnb2physical
21327095
HNRH2_MOUSEHnrnph2physical
21327095
DX39B_MOUSEDdx39bphysical
21327095
LBR_MOUSELbrphysical
21327095
TOIP1_MOUSETor1aip1physical
21327095
SUN2_MOUSESun2physical
21327095
SUN1_MOUSESun1physical
21327095
HNRL1_MOUSEHnrnpul1physical
21327095
MYH9_MOUSEMyh9physical
21327095
1433G_MOUSEYwhagphysical
21327095
RAB5A_MOUSERab5aphysical
21327095
EMD_MOUSEEmdphysical
21327095
DDX3Y_MOUSEDdx3yphysical
21327095
RBM10_MOUSERbm10physical
21327095
1433S_MOUSESfnphysical
21327095
RED_MOUSEIkphysical
21327095
UBC9_MOUSEUbe2iphysical
21327095
PPIL1_MOUSEPpil1physical
21327095
TOP2A_MOUSETop2aphysical
21327095
RAB2A_MOUSERab2aphysical
21327095
ENPL_MOUSEHsp90b1physical
21327095
MAN1_MOUSELemd3physical
21327095
TNPO1_MOUSETnpo1physical
21327095
SYNE2_MOUSESyne2physical
21327095
RAB5C_MOUSERab5cphysical
21327095
ACTG_MOUSEActg1physical
21327095
RAB7A_MOUSERab7physical
21327095
H14_MOUSEHist1h1ephysical
21327095
ANXA3_MOUSEAnxa3physical
21327095
EIF3I_MOUSEEif3iphysical
21327095
RAB10_MOUSERab10physical
21327095
LUC7L_MOUSELuc7lphysical
21327095
CBX5_MOUSECbx5physical
21327095
ARC1B_MOUSEArpc1bphysical
21327095
RAB6B_MOUSERab6bphysical
21327095
PIPNB_MOUSEPitpnbphysical
21327095
TIF1B_MOUSETrim28physical
21327095
SC22B_MOUSESec22bphysical
21327095
PAIRB_MOUSESerbp1physical
21327095
STRAP_MOUSEStrapphysical
21327095
MTAP_MOUSEMtapphysical
21327095
LAR4B_MOUSELarp4bphysical
21327095
CNN3_MOUSECnn3physical
21327095
PSB5_MOUSEPsmb5physical
21327095
GT251_MOUSEGlt25d1physical
21327095
ESTD_MOUSEEsdphysical
21327095
XRCC6_MOUSEXrcc6physical
21327095
DESP_HUMANDSPphysical
26496610
DNJB1_HUMANDNAJB1physical
26496610
LMNB1_HUMANLMNB1physical
26496610
MTDC_HUMANMTHFD2physical
26496610
HAUS5_HUMANHAUS5physical
26496610
DCAF8_HUMANDCAF8physical
26496610
LMNB2_HUMANLMNB2physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LMNA_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-22; SER-390 AND SER-392,AND MASS 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-301; SER-390; SER-392;SER-398; SER-406; SER-407; SER-409; SER-414; SER-573; SER-575; SER-629AND SER-633, 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-12; THR-19; SER-22;SER-633 AND SER-637, AND MASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390 AND SER-392, ANDMASS SPECTROMETRY.
"Identification of phosphorylation sites on murine nuclear lamin C byRP-HPLC and microsequencing.";
Eggert M., Radomski N., Tripier D., Traub P., Jost E.;
FEBS Lett. 292:205-209(1991).
Cited for: PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION AT SER-392; SER-407 ANDSER-409.

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