LMNB1_MOUSE - dbPTM
LMNB1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LMNB1_MOUSE
UniProt AC P14733
Protein Name Lamin-B1
Gene Name Lmnb1
Organism Mus musculus (Mouse).
Sequence Length 588
Subcellular Localization Nucleus inner membrane
Lipid-anchor
Nucleoplasmic side.
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..
Protein Sequence MATATPVQQQRAGSRASAPATPLSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSRVTVSRASSSRSVRTTRGKRKRVDVEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSVSYKYTSRYVLKAGQTVTVWAANAGVTASPPTDLIWKNQNSWGTGEDVKVILKNSQGEEVAQRSTVFKTTIPEEEEEEEEEPIGVAVEEERFHQQGAPRASNKSCAIM
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------MATATPVQQ
------CCCCCHHHH		13.12-
3Phosphorylation-----MATATPVQQQ
-----CCCCCHHHHH		29.7529472430
5Phosphorylation---MATATPVQQQRA
---CCCCCHHHHHHC		21.4526824392
14PhosphorylationVQQQRAGSRASAPAT
HHHHHCCCCCCCCCC		24.5625521595
15MethylationQQQRAGSRASAPATP
HHHHCCCCCCCCCCC		31.4816289129
17PhosphorylationQRAGSRASAPATPLS
HHCCCCCCCCCCCCC		33.4027087446
21PhosphorylationSRASAPATPLSPTRL
CCCCCCCCCCCHHHH		24.5727087446
24PhosphorylationSAPATPLSPTRLSRL
CCCCCCCCHHHHHHH		25.9826824392
26PhosphorylationPATPLSPTRLSRLQE
CCCCCCHHHHHHHHH		40.6522942356
29PhosphorylationPLSPTRLSRLQEKEE
CCCHHHHHHHHHHHH		27.8828833060
34AcetylationRLSRLQEKEELRELN
HHHHHHHHHHHHHHH		43.4523954790
59PhosphorylationRSLETENSALQLQVT
HCCCCCCCCEEEEEE		24.9127566939
80UbiquitinationGRELTGLKALYETEL
CCCCHHHHHHHHHHH		37.3822790023
85PhosphorylationGLKALYETELADARR
HHHHHHHHHHHHHHH		23.81-
103UbiquitinationDTARERAKLQIELGK
HHHHHHHHHHHHHCC		47.33-
103MalonylationDTARERAKLQIELGK
HHHHHHHHHHHHHCC		47.3326320211
110UbiquitinationKLQIELGKFKAEHDQ
HHHHHHCCCHHHHHH		57.2122790023
110AcetylationKLQIELGKFKAEHDQ
HHHHHHCCCHHHHHH		57.2123954790
112UbiquitinationQIELGKFKAEHDQLL
HHHHCCCHHHHHHHH		57.2422790023
112AcetylationQIELGKFKAEHDQLL
HHHHCCCHHHHHHHH		57.2423806337
125UbiquitinationLLLNYAKKESDLSGA
HHHHHHHHHHCCCCC		55.04-
127PhosphorylationLNYAKKESDLSGAQI
HHHHHHHHCCCCCCH		53.3728833060
130PhosphorylationAKKESDLSGAQIKLR
HHHHHCCCCCCHHHH		36.7528464351
135UbiquitinationDLSGAQIKLREYEAA
CCCCCCHHHHHHHHH		29.4322790023
139PhosphorylationAQIKLREYEAALNSK
CCHHHHHHHHHHCCH		12.3925195567
158AcetylationATALGDKKSLEGDLE
HHHHCCHHHHCCCHH		66.08-
158UbiquitinationATALGDKKSLEGDLE
HHHHCCHHHHCCCHH		66.0822790023
159PhosphorylationTALGDKKSLEGDLED
HHHCCHHHHCCCHHH		37.0823984901
168AcetylationEGDLEDLKDQIAQLE
CCCHHHHHHHHHHHH		60.9719859047
177PhosphorylationQIAQLEASLSAAKKQ
HHHHHHHHHHHHHHH		17.3027600695
179PhosphorylationAQLEASLSAAKKQLA
HHHHHHHHHHHHHHC		24.5627600695
182UbiquitinationEASLSAAKKQLADET
HHHHHHHHHHHCCCH		40.54-
183UbiquitinationASLSAAKKQLADETL
HHHHHHHHHHCCCHH		45.9022790023
189PhosphorylationKKQLADETLLKVDLE
HHHHCCCHHHHCCHH		37.6321454597
192AcetylationLADETLLKVDLENRC
HCCCHHHHCCHHHHH		36.4923954790
201PhosphorylationDLENRCQSLTEDLEF
CHHHHHHHHHHCHHH		40.6725266776
203PhosphorylationENRCQSLTEDLEFRK
HHHHHHHHHCHHHHH		32.4723984901
210UbiquitinationTEDLEFRKNMYEEEI
HHCHHHHHHHHHHHH		51.9222790023
226PhosphorylationETRRKHETRLVEVDS
HHHHHHCEEEEEECC		29.0824899341
233PhosphorylationTRLVEVDSGRQIEYE
EEEEEECCCCCEEHH		40.8425266776
242AcetylationRQIEYEYKLAQALHE
CCEEHHHHHHHHHHH		25.9622826441
262AcetylationDAQVRLYKEELEQTY
HHHHHHHHHHHHHHH		49.6723806337
262UbiquitinationDAQVRLYKEELEQTY
HHHHHHHHHHHHHHH		49.6722790023
272AcetylationLEQTYHAKLENARLS
HHHHHHHHHHHHHHC		42.9223806337
272UbiquitinationLEQTYHAKLENARLS
HHHHHHHHHHHHHHC		42.9222790023
279PhosphorylationKLENARLSSEMNTST
HHHHHHHCHHCCHHH		20.7821659605
280PhosphorylationLENARLSSEMNTSTV
HHHHHHCHHCCHHHH		45.5226643407
284PhosphorylationRLSSEMNTSTVNSAR
HHCHHCCHHHHHHHH		25.1926643407
285PhosphorylationLSSEMNTSTVNSARE
HCHHCCHHHHHHHHH		25.9221082442
286PhosphorylationSSEMNTSTVNSAREE
CHHCCHHHHHHHHHH		22.9728066266
289PhosphorylationMNTSTVNSAREELME
CCHHHHHHHHHHHHH		25.1128066266
297PhosphorylationAREELMESRMRIESL
HHHHHHHHHHHHHHH		19.8830635358
303PhosphorylationESRMRIESLSSQLSN
HHHHHHHHHHHHHHH		31.0526824392
305PhosphorylationRMRIESLSSQLSNLQ
HHHHHHHHHHHHHHH		25.8928833060
306PhosphorylationMRIESLSSQLSNLQK
HHHHHHHHHHHHHHH		40.2028833060
309PhosphorylationESLSSQLSNLQKESR
HHHHHHHHHHHHHHH		28.0528833060
313MalonylationSQLSNLQKESRACLE
HHHHHHHHHHHHHHH		61.9026320211
313UbiquitinationSQLSNLQKESRACLE
HHHHHHHHHHHHHHH		61.9027667366
331AcetylationELEDMLAKERDNSRR
HHHHHHHHHHHCHHH		49.6923806337
331UbiquitinationELEDMLAKERDNSRR
HHHHHHHHHHHCHHH		49.6922790023
359PhosphorylationDQMQQQLSDYEQLLD
HHHHHHHCCHHHHHH		33.5322817900
376PhosphorylationLALDMEISAYRKLLE
HHHHCHHHHHHHHHC		13.1226824392
378PhosphorylationLDMEISAYRKLLEGE
HHCHHHHHHHHHCCH		11.0729895711
380AcetylationMEISAYRKLLEGEEE
CHHHHHHHHHCCHHH		44.7623954790
380UbiquitinationMEISAYRKLLEGEEE
CHHHHHHHHHCCHHH		44.7622790023
390MalonylationEGEEERLKLSPSPSS
CCHHHHHCCCCCCCC		53.8126320211
390UbiquitinationEGEEERLKLSPSPSS
CCHHHHHCCCCCCCC		53.8127667366
392PhosphorylationEEERLKLSPSPSSRV
HHHHHCCCCCCCCCE		23.0326824392
394PhosphorylationERLKLSPSPSSRVTV
HHHCCCCCCCCCEEE		33.7626824392
396PhosphorylationLKLSPSPSSRVTVSR
HCCCCCCCCCEEEEC		34.8027149854
397PhosphorylationKLSPSPSSRVTVSRA
CCCCCCCCCEEEECC		33.8727149854
400PhosphorylationPSPSSRVTVSRASSS
CCCCCCEEEECCCCC		16.2027600695
402PhosphorylationPSSRVTVSRASSSRS
CCCCEEEECCCCCCC		16.8623684622
405PhosphorylationRVTVSRASSSRSVRT
CEEEECCCCCCCCCC		27.9527087446
406PhosphorylationVTVSRASSSRSVRTT
EEEECCCCCCCCCCC		28.8725338131
407PhosphorylationTVSRASSSRSVRTTR
EEECCCCCCCCCCCC		26.5324453211
409PhosphorylationSRASSSRSVRTTRGK
ECCCCCCCCCCCCCC		20.2121659605
414MethylationSRSVRTTRGKRKRVD
CCCCCCCCCCCEECC		48.28-
475MalonylationGGWEMIRKIGDTSVS
CCHHHHHHHCCCEEE		39.8726320211
482PhosphorylationKIGDTSVSYKYTSRY
HHCCCEEEEEEEEEE		18.7028285833
484MalonylationGDTSVSYKYTSRYVL
CCCEEEEEEEEEEEE		34.2526320211
484AcetylationGDTSVSYKYTSRYVL
CCCEEEEEEEEEEEE		34.2523954790
533MalonylationEDVKVILKNSQGEEV
CCEEEEEECCCCCCH		43.3526320211
533UbiquitinationEDVKVILKNSQGEEV
CCEEEEEECCCCCCH		43.3527667366
535PhosphorylationVKVILKNSQGEEVAQ
EEEEEECCCCCCHHH		37.6723375375
544PhosphorylationGEEVAQRSTVFKTTI
CCCHHHHCEEEEECC		19.49-
548UbiquitinationAQRSTVFKTTIPEEE
HHHCEEEEECCCHHH		40.1822790023
581PhosphorylationQQGAPRASNKSCAIM
HCCCCCCCCCCCCCC		46.1829514104
585MethylationPRASNKSCAIM----
CCCCCCCCCCC----		2.96-
585FarnesylationPRASNKSCAIM----
CCCCCCCCCCC----		2.96-
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 LMNB1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LMNB1_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 LMNB1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MLP3B_MOUSEMap1lc3bphysical
26524528
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LMNB1_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-392 AND SER-394, ANDMASS 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-17; THR-21 AND SER-24,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-17 AND THR-21, AND MASSSPECTROMETRY.

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