LBR_MOUSE - dbPTM
LBR_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LBR_MOUSE
UniProt AC Q3U9G9
Protein Name Lamin-B receptor
Gene Name Lbr
Organism Mus musculus (Mouse).
Sequence Length 626
Subcellular Localization Nucleus inner membrane
Multi-pass membrane protein.
Protein Description Anchors the lamina and the heterochromatin to the inner nuclear membrane..
Protein Sequence MPSRKFVEGEVVRGRWPGSSLYYEVEILSHDNKSQLYTVKYKDGTELELKESDIKPLKSFKQRKSGSISSSPSRRRGSRSRSRSRSRSRSPGRAPKGSRRSVSASHEGDVKEKKEKEMRREILQVKLTPLVLKPFGNSVSVYNGEPEHMEKNATPYKDKQERIILSTEDRYIVTQYSLRPRREEVKAKEIESEEQNLVTKGPAPLGTFQVTTPQRKDLEFGGVPGAVLIMLGLPACVLLLLLQCRQKDPGLLHFPPPLPALHELWEPRVCGVYLLWFFVQALFHLLPVGKVAEGTPLVDGRRLQYRLNGLYAFILTSAALGAAVFWGVELCYLYTHFLQLALAATGFSVLLSAYLYVRSLRAPREELSPASSGNAVYDFFIGRELNPRLGAFDLKFFCELRPGLIGWVVINLVMLLMEMKIQERAAPSLAMILVNSFQLLYVVDALWNEEALLTSMDIMHDGFGFMLAFGDLVWVPFTYSLQAFYLVSHPHDLSWPLASVIIALKLCGYVIFRCANSQKNAFRKNPTDPKLAHLKTIHTSTGKSLLVSGWWGFVRHPNYLGDLIMALAWSLPCGFNHLLPYFYIIYFTALLIHREARDEHQCRRKYGLAWEKYCQRVPYRIFPYIY
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
5Acetylation---MPSRKFVEGEVV
---CCCCCEEECEEE
59.0923806337
5Ubiquitination---MPSRKFVEGEVV
---CCCCCEEECEEE
59.0922790023
19PhosphorylationVRGRWPGSSLYYEVE
ECCCCCCCCEEEEEE
17.0622871156
34PhosphorylationILSHDNKSQLYTVKY
EEECCCCCCEEEEEE
31.5022871156
42UbiquitinationQLYTVKYKDGTELEL
CEEEEEECCCCEEEE
43.9222790023
45PhosphorylationTVKYKDGTELELKES
EEEECCCCEEEEEHH
47.7518779572
50UbiquitinationDGTELELKESDIKPL
CCCEEEEEHHHCCCC
45.88-
55AcetylationELKESDIKPLKSFKQ
EEEHHHCCCCHHHHC
49.65-
59PhosphorylationSDIKPLKSFKQRKSG
HHCCCCHHHHCCCCC
45.4125159016
65PhosphorylationKSFKQRKSGSISSSP
HHHHCCCCCCCCCCH
39.7127087446
67PhosphorylationFKQRKSGSISSSPSR
HHCCCCCCCCCCHHH
26.7927087446
69PhosphorylationQRKSGSISSSPSRRR
CCCCCCCCCCHHHCC
26.8527087446
70PhosphorylationRKSGSISSSPSRRRG
CCCCCCCCCHHHCCC
44.6027087446
71PhosphorylationKSGSISSSPSRRRGS
CCCCCCCCHHHCCCC
21.8027087446
73PhosphorylationGSISSSPSRRRGSRS
CCCCCCHHHCCCCCC
40.1321082442
86PhosphorylationRSRSRSRSRSRSPGR
CCCCCCCCCCCCCCC
35.5422817900
88PhosphorylationRSRSRSRSRSPGRAP
CCCCCCCCCCCCCCC
38.0525266776
90PhosphorylationRSRSRSRSPGRAPKG
CCCCCCCCCCCCCCC
32.7123684622
98PhosphorylationPGRAPKGSRRSVSAS
CCCCCCCCCCCCCCC
30.5526824392
98O-linked_GlycosylationPGRAPKGSRRSVSAS
CCCCCCCCCCCCCCC
30.5512438562
101PhosphorylationAPKGSRRSVSASHEG
CCCCCCCCCCCCCCC
21.2227087446
103PhosphorylationKGSRRSVSASHEGDV
CCCCCCCCCCCCCCH
25.8727087446
105PhosphorylationSRRSVSASHEGDVKE
CCCCCCCCCCCCHHH
17.9927087446
111UbiquitinationASHEGDVKEKKEKEM
CCCCCCHHHHHHHHH
69.43-
113UbiquitinationHEGDVKEKKEKEMRR
CCCCHHHHHHHHHHH
61.59-
128PhosphorylationEILQVKLTPLVLKPF
HHHHHCCCCEEECCC
14.6225159016
133UbiquitinationKLTPLVLKPFGNSVS
CCCCEEECCCCCEEE
30.7122790023
138PhosphorylationVLKPFGNSVSVYNGE
EECCCCCEEEEECCC
19.0225159016
140PhosphorylationKPFGNSVSVYNGEPE
CCCCCEEEEECCCHH
20.7825159016
142PhosphorylationFGNSVSVYNGEPEHM
CCCEEEEECCCHHHH
15.2225159016
151UbiquitinationGEPEHMEKNATPYKD
CCHHHHCCCCCCCCC
44.2922790023
154PhosphorylationEHMEKNATPYKDKQE
HHHCCCCCCCCCHHC
36.2225266776
157UbiquitinationEKNATPYKDKQERII
CCCCCCCCCHHCEEE
60.70-
166PhosphorylationKQERIILSTEDRYIV
HHCEEEEECCCCEEE
21.2428066266
167PhosphorylationQERIILSTEDRYIVT
HCEEEEECCCCEEEE
38.1628066266
171PhosphorylationILSTEDRYIVTQYSL
EEECCCCEEEEECCC
16.4425159016
174PhosphorylationTEDRYIVTQYSLRPR
CCCCEEEEECCCCCC
16.5425159016
176PhosphorylationDRYIVTQYSLRPRRE
CCEEEEECCCCCCHH
10.5824224561
177PhosphorylationRYIVTQYSLRPRREE
CEEEEECCCCCCHHH
14.2124704852
188UbiquitinationRREEVKAKEIESEEQ
CHHHHHHHHHCHHHH
54.2122790023
188AcetylationRREEVKAKEIESEEQ
CHHHHHHHHHCHHHH
54.2123806337
192PhosphorylationVKAKEIESEEQNLVT
HHHHHHCHHHHHCCC
52.6928833060
200UbiquitinationEEQNLVTKGPAPLGT
HHHHCCCCCCCCCCE
56.25-
211PhosphorylationPLGTFQVTTPQRKDL
CCCEEEECCCCCCCC
23.2128066266
212PhosphorylationLGTFQVTTPQRKDLE
CCEEEECCCCCCCCC
20.6828066266
527PhosphorylationNAFRKNPTDPKLAHL
CCCCCCCCCHHHHHC
74.4627180971
605AcetylationDEHQCRRKYGLAWEK
CHHHHHHHHCCHHHH
25.07-
612AcetylationKYGLAWEKYCQRVPY
HHCCHHHHHHHHCCC
40.3923806337
612UbiquitinationKYGLAWEKYCQRVPY
HHCCHHHHHHHHCCC
40.3922790023

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
86SPhosphorylationKinaseCDK1P11440
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LBR_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 LBR_MOUSE !!

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 LBR_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-101 AND SER-103, ANDMASS SPECTROMETRY.

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