LMNB1_RAT - dbPTM
LMNB1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LMNB1_RAT
UniProt AC P70615
Protein Name Lamin-B1
Gene Name Lmnb1
Organism Rattus norvegicus (Rat).
Sequence Length 587
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 MATATPVQQRAGSRASAPATPFSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSARGGMMESRMRIESLSSQLSNLQKDSRACLERIQELEDMLAKERDNSRRMLSDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSRVTVSRASSSRSVRTTRGKRKRVDVEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSVSYKYTSRYVLKAGQTVTVWAANAGVTASPPTDLIWKNQNSWGTGEDVKVVLKNSQGEEVAQRSTVFKTTIPEEEEEEEEEPIGVPLEEERFHQQGTPRASNKSCAIM
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
------CCCCCCCHH		13.12-
3Phosphorylation-----MATATPVQQR
-----CCCCCCCHHC		29.75-
5Phosphorylation---MATATPVQQRAG
---CCCCCCCHHCCC		21.4523984901
14MethylationVQQRAGSRASAPATP
CHHCCCCCCCCCCCC		31.48-
16PhosphorylationQRAGSRASAPATPFS
HCCCCCCCCCCCCCC		33.40-
20PhosphorylationSRASAPATPFSPTRL
CCCCCCCCCCCHHHH		24.6516641100
23PhosphorylationSAPATPFSPTRLSRL
CCCCCCCCHHHHHHH		26.9416641100
25PhosphorylationPATPFSPTRLSRLQE
CCCCCCHHHHHHHHH		42.94-
28PhosphorylationPFSPTRLSRLQEKEE
CCCHHHHHHHHHHHH		27.88-
33AcetylationRLSRLQEKEELRELN
HHHHHHHHHHHHHHH		43.4522902405
49AcetylationRLAVYIDKVRSLETE
HHHHHHHHHHCCCCC		29.9522902405
79AcetylationGRELTGLKALYETEL
CCCCHHHHHHHHHHH		37.3822902405
102AcetylationDTARERAKLQIELGK
HHHHHHHHHHHHHCC		47.3322902405
109AcetylationKLQIELGKFKAEHDQ
HHHHHHCCCHHHHHH		57.2122902405
111AcetylationQIELGKFKAEHDQLL
HHHHCCCHHHHHHHH		57.2422902405
123AcetylationQLLLNYAKKESDLSG
HHHHHHHHHHHCCCC		46.8722902405
126PhosphorylationLNYAKKESDLSGAQI
HHHHHHHHCCCCCCH		53.3722673903
134AcetylationDLSGAQIKLREYEAA
CCCCCCHHHHHHHHH		29.4322902405
156AcetylationLATALGDKKSLEGDL
HHHHHCCHHHHCCCH		42.3322902405
157AcetylationATALGDKKSLEGDLE
HHHHCCHHHHCCCHH		66.0822902405
157UbiquitinationATALGDKKSLEGDLE
HHHHCCHHHHCCCHH		66.08-
158PhosphorylationTALGDKKSLEGDLED
HHHCCHHHHCCCHHH		37.0830417516
176PhosphorylationQIAQLEASLSAAKKQ
HHHHHHHHHHHHHHH		17.3030181290
178PhosphorylationAQLEASLSAAKKQLA
HHHHHHHHHHHHHHC		24.5630181290
181AcetylationEASLSAAKKQLADET
HHHHHHHHHHHCCCH		40.5422902405
182UbiquitinationASLSAAKKQLADETL
HHHHHHHHHHCCCHH		45.90-
200PhosphorylationDLENRCQSLTEDLEF
CHHHHHHHHHHCHHH		40.67-
232PhosphorylationTRLVEVDSGRQIEYE
EEEEEECCCCCEEHH		40.8425575281
238PhosphorylationDSGRQIEYEYKLAQA
CCCCCEEHHHHHHHH		26.6225575281
240PhosphorylationGRQIEYEYKLAQALH
CCCEEHHHHHHHHHH		15.4825575281
241AcetylationRQIEYEYKLAQALHE
CCEEHHHHHHHHHHH		25.9622902405
261AcetylationDAQVRLYKEELEQTY
HHHHHHHHHHHHHHH		49.6722902405
271AcetylationLEQTYHAKLENARLS
HHHHHHHHHHHHHHC		42.9225786129
278PhosphorylationKLENARLSSEMNTST
HHHHHHHCHHCCHHH		20.7827097102
279PhosphorylationLENARLSSEMNTSTV
HHHHHHCHHCCHHHH		45.5227097102
283PhosphorylationRLSSEMNTSTVNSAR
HHCHHCCHHHHHHHC		25.1927097102
284PhosphorylationLSSEMNTSTVNSARG
HCHHCCHHHHHHHCC		25.9227097102
285PhosphorylationSSEMNTSTVNSARGG
CHHCCHHHHHHHCCC		22.9727097102
288PhosphorylationMNTSTVNSARGGMME
CCHHHHHHHCCCHHH		18.2722668510
302PhosphorylationESRMRIESLSSQLSN
HHHHHHHHHHHHHHH		31.0527097102
304PhosphorylationRMRIESLSSQLSNLQ
HHHHHHHHHHHHHCH		25.8928432305
305PhosphorylationMRIESLSSQLSNLQK
HHHHHHHHHHHHCHH		40.2027097102
308PhosphorylationESLSSQLSNLQKDSR
HHHHHHHHHCHHHHH		28.0527097102
330AcetylationELEDMLAKERDNSRR
HHHHHHHHHHHCHHC		49.6922902405
342AcetylationSRRMLSDKEREMAEI
HHCCCCHHHHHHHHH		56.1222902405
375PhosphorylationLALDMEISAYRKLLE
HHHHCHHHHHHHHHC		13.1223984901
377PhosphorylationLDMEISAYRKLLEGE
HHCHHHHHHHHHCCH		11.0723984901
379AcetylationMEISAYRKLLEGEEE
CHHHHHHHHHCCHHH		44.7622631275
391PhosphorylationEEERLKLSPSPSSRV
HHHHHCCCCCCCCCE		23.0329779826
393PhosphorylationERLKLSPSPSSRVTV
HHHCCCCCCCCCEEE		33.7627097102
395PhosphorylationLKLSPSPSSRVTVSR
HCCCCCCCCCEEEEC		34.8027097102
396PhosphorylationKLSPSPSSRVTVSRA
CCCCCCCCCEEEECC		33.8727097102
401PhosphorylationPSSRVTVSRASSSRS
CCCCEEEECCCCCCC		16.8628689409
404PhosphorylationRVTVSRASSSRSVRT
CEEEECCCCCCCCCC		27.9521630457
405PhosphorylationVTVSRASSSRSVRTT
EEEECCCCCCCCCCC		28.8721630457
406PhosphorylationTVSRASSSRSVRTTR
EEECCCCCCCCCCCC		26.5321630457
408PhosphorylationSRASSSRSVRTTRGK
ECCCCCCCCCCCCCC		20.21-
412PhosphorylationSSRSVRTTRGKRKRV
CCCCCCCCCCCCEEC		27.1924259510
413MethylationSRSVRTTRGKRKRVD
CCCCCCCCCCCEECC		48.28-
478PhosphorylationMIRKIGDTSVSYKYT
HHHHHCCCEEEEEEE		26.3023353032
483AcetylationGDTSVSYKYTSRYVL
CCCEEEEEEEEEEEE		34.2525786129
484PhosphorylationDTSVSYKYTSRYVLK
CCEEEEEEEEEEEEE		11.1723353032
488PhosphorylationSYKYTSRYVLKAGQT
EEEEEEEEEEECCCE		15.2023353032
528AcetylationWGTGEDVKVVLKNSQ
CCCCCCEEEEEECCC		38.6622902405
534PhosphorylationVKVVLKNSQGEEVAQ
EEEEEECCCCCCHHH		37.67-
576PhosphorylationERFHQQGTPRASNKS
HHHHHCCCCCCCCCC		12.7929779826
584FarnesylationPRASNKSCAIM----
CCCCCCCCCCC----		2.96-
584MethylationPRASNKSCAIM----
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_RAT !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LMNB1_RAT !!
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_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LMNB1_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites.";
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20 AND SER-23, AND MASSSPECTROMETRY.

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