| 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 | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 5 | Acetylation | ---MPSRKFVEGEVV ---CCCCCEEECEEE | 59.09 | 23806337 | |
| 5 | Ubiquitination | ---MPSRKFVEGEVV ---CCCCCEEECEEE | 59.09 | 22790023 | |
| 19 | Phosphorylation | VRGRWPGSSLYYEVE ECCCCCCCCEEEEEE | 17.06 | 22871156 | |
| 34 | Phosphorylation | ILSHDNKSQLYTVKY EEECCCCCCEEEEEE | 31.50 | 22871156 | |
| 42 | Ubiquitination | QLYTVKYKDGTELEL CEEEEEECCCCEEEE | 43.92 | 22790023 | |
| 45 | Phosphorylation | TVKYKDGTELELKES EEEECCCCEEEEEHH | 47.75 | 18779572 | |
| 50 | Ubiquitination | DGTELELKESDIKPL CCCEEEEEHHHCCCC | 45.88 | - | |
| 55 | Acetylation | ELKESDIKPLKSFKQ EEEHHHCCCCHHHHC | 49.65 | - | |
| 59 | Phosphorylation | SDIKPLKSFKQRKSG HHCCCCHHHHCCCCC | 45.41 | 25159016 | |
| 65 | Phosphorylation | KSFKQRKSGSISSSP HHHHCCCCCCCCCCH | 39.71 | 27087446 | |
| 67 | Phosphorylation | FKQRKSGSISSSPSR HHCCCCCCCCCCHHH | 26.79 | 27087446 | |
| 69 | Phosphorylation | QRKSGSISSSPSRRR CCCCCCCCCCHHHCC | 26.85 | 27087446 | |
| 70 | Phosphorylation | RKSGSISSSPSRRRG CCCCCCCCCHHHCCC | 44.60 | 27087446 | |
| 71 | Phosphorylation | KSGSISSSPSRRRGS CCCCCCCCHHHCCCC | 21.80 | 27087446 | |
| 73 | Phosphorylation | GSISSSPSRRRGSRS CCCCCCHHHCCCCCC | 40.13 | 21082442 | |
| 86 | Phosphorylation | RSRSRSRSRSRSPGR CCCCCCCCCCCCCCC | 35.54 | 22817900 | |
| 88 | Phosphorylation | RSRSRSRSRSPGRAP CCCCCCCCCCCCCCC | 38.05 | 25266776 | |
| 90 | Phosphorylation | RSRSRSRSPGRAPKG CCCCCCCCCCCCCCC | 32.71 | 23684622 | |
| 98 | Phosphorylation | PGRAPKGSRRSVSAS CCCCCCCCCCCCCCC | 30.55 | 26824392 | |
| 98 | O-linked_Glycosylation | PGRAPKGSRRSVSAS CCCCCCCCCCCCCCC | 30.55 | 12438562 | |
| 101 | Phosphorylation | APKGSRRSVSASHEG CCCCCCCCCCCCCCC | 21.22 | 27087446 | |
| 103 | Phosphorylation | KGSRRSVSASHEGDV CCCCCCCCCCCCCCH | 25.87 | 27087446 | |
| 105 | Phosphorylation | SRRSVSASHEGDVKE CCCCCCCCCCCCHHH | 17.99 | 27087446 | |
| 111 | Ubiquitination | ASHEGDVKEKKEKEM CCCCCCHHHHHHHHH | 69.43 | - | |
| 113 | Ubiquitination | HEGDVKEKKEKEMRR CCCCHHHHHHHHHHH | 61.59 | - | |
| 128 | Phosphorylation | EILQVKLTPLVLKPF HHHHHCCCCEEECCC | 14.62 | 25159016 | |
| 133 | Ubiquitination | KLTPLVLKPFGNSVS CCCCEEECCCCCEEE | 30.71 | 22790023 | |
| 138 | Phosphorylation | VLKPFGNSVSVYNGE EECCCCCEEEEECCC | 19.02 | 25159016 | |
| 140 | Phosphorylation | KPFGNSVSVYNGEPE CCCCCEEEEECCCHH | 20.78 | 25159016 | |
| 142 | Phosphorylation | FGNSVSVYNGEPEHM CCCEEEEECCCHHHH | 15.22 | 25159016 | |
| 151 | Ubiquitination | GEPEHMEKNATPYKD CCHHHHCCCCCCCCC | 44.29 | 22790023 | |
| 154 | Phosphorylation | EHMEKNATPYKDKQE HHHCCCCCCCCCHHC | 36.22 | 25266776 | |
| 157 | Ubiquitination | EKNATPYKDKQERII CCCCCCCCCHHCEEE | 60.70 | - | |
| 166 | Phosphorylation | KQERIILSTEDRYIV HHCEEEEECCCCEEE | 21.24 | 28066266 | |
| 167 | Phosphorylation | QERIILSTEDRYIVT HCEEEEECCCCEEEE | 38.16 | 28066266 | |
| 171 | Phosphorylation | ILSTEDRYIVTQYSL EEECCCCEEEEECCC | 16.44 | 25159016 | |
| 174 | Phosphorylation | TEDRYIVTQYSLRPR CCCCEEEEECCCCCC | 16.54 | 25159016 | |
| 176 | Phosphorylation | DRYIVTQYSLRPRRE CCEEEEECCCCCCHH | 10.58 | 24224561 | |
| 177 | Phosphorylation | RYIVTQYSLRPRREE CEEEEECCCCCCHHH | 14.21 | 24704852 | |
| 188 | Ubiquitination | RREEVKAKEIESEEQ CHHHHHHHHHCHHHH | 54.21 | 22790023 | |
| 188 | Acetylation | RREEVKAKEIESEEQ CHHHHHHHHHCHHHH | 54.21 | 23806337 | |
| 192 | Phosphorylation | VKAKEIESEEQNLVT HHHHHHCHHHHHCCC | 52.69 | 28833060 | |
| 200 | Ubiquitination | EEQNLVTKGPAPLGT HHHHCCCCCCCCCCE | 56.25 | - | |
| 211 | Phosphorylation | PLGTFQVTTPQRKDL CCCEEEECCCCCCCC | 23.21 | 28066266 | |
| 212 | Phosphorylation | LGTFQVTTPQRKDLE CCEEEECCCCCCCCC | 20.68 | 28066266 | |
| 527 | Phosphorylation | NAFRKNPTDPKLAHL CCCCCCCCCHHHHHC | 74.46 | 27180971 | |
| 605 | Acetylation | DEHQCRRKYGLAWEK CHHHHHHHHCCHHHH | 25.07 | - | |
| 612 | Acetylation | KYGLAWEKYCQRVPY HHCCHHHHHHHHCCC | 40.39 | 23806337 | |
| 612 | Ubiquitination | KYGLAWEKYCQRVPY HHCCHHHHHHHHCCC | 40.39 | 22790023 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 86 | S | Phosphorylation | Kinase | CDK1 | P11440 | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LBR_MOUSE !! | ||||||
* 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 !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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. | |