UniProt ID | LSG1_MOUSE | |
---|---|---|
UniProt AC | Q3UM18 | |
Protein Name | Large subunit GTPase 1 homolog | |
Gene Name | Lsg1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 644 | |
Subcellular Localization | Cytoplasm. Nucleus. Endoplasmic reticulum. Shuttles between the Cajal bodies in the nucleus and the endoplasmic reticulum.. | |
Protein Description | GTPase required for the XPO1/CRM1-mediated nuclear export of the 60S ribosomal subunit. Probably acts by mediating the release of NMD3 from the 60S ribosomal subunit after export into the cytoplasm (By similarity).. | |
Protein Sequence | MGRRRAPGGGSLGRVLIRQQTQRSRSHRHTDSWLHTSELNDGYDWGRLNLQSVTEQSSLEDFLATAELAGTEFVAEKLNIKFVPPEARTGLLSFEESQRIKKLHEENRQFLCIPRRPNWDRKTSPEELKQAEKDNFLKWRRQLVRLEEEQKLILTPFERNLDFWRQLWRVIERSDIVVQIVDARNPLLFRCEDLECYVKEIDAAKENVILINKADLLTAEQRFAWAVHFEKEGVKVIFWSALAETDHLNGDLKEEVDSVAGDTNKTESESSSLDANEIPHRDLISLSEESASDSGDSKYEDCQEDEEEDWQTCSEEDSVPEEEEGCNADSETQNRKNAENQQVNNDSYLVSKQELLELFKKLHTGKKVKDGQLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHTKHFQTLYVEPGLCLCDCPGLVMPSFVSTKAEMICNGILPIDQMRDHVPPVSLVCQNIPRRVLEVTYGINIIKPREDEDPYRPPTSEELLTAYGCMRGFMTAHGQPDQPRSARYILKDYVGGKLLYCHPPPGKDPVAFQHQHQQLLESKVKGGELRLQPGKGRKAKQIENVVDKTFFHQENVRALTKGVQAVMGYKPGHGLVTAAAASAENVPGKPWKKHGNRNKKEKSRRLYKHLDV | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
14 | Methylation | PGGGSLGRVLIRQQT CCCCHHHHHHHHHCC | 25.92 | 25058859 | |
14 | Dimethylation | PGGGSLGRVLIRQQT CCCCHHHHHHHHHCC | 25.92 | - | |
21 | Phosphorylation | RVLIRQQTQRSRSHR HHHHHHCCHHCCCCC | 20.01 | 29514104 | |
93 | Phosphorylation | EARTGLLSFEESQRI HHHCCCCCHHHHHHH | 35.34 | - | |
97 | Phosphorylation | GLLSFEESQRIKKLH CCCCHHHHHHHHHHH | 19.98 | - | |
155 | Phosphorylation | EEQKLILTPFERNLD HHHHEEECCHHHCHH | 20.95 | 22871156 | |
258 | Phosphorylation | DLKEEVDSVAGDTNK CCHHHHHHHCCCCCC | 21.02 | 25521595 | |
263 | Phosphorylation | VDSVAGDTNKTESES HHHHCCCCCCCCCCC | 37.38 | 17242355 | |
266 | Phosphorylation | VAGDTNKTESESSSL HCCCCCCCCCCCCCC | 46.98 | 25338131 | |
268 | Phosphorylation | GDTNKTESESSSLDA CCCCCCCCCCCCCCC | 48.27 | 17242355 | |
270 | Phosphorylation | TNKTESESSSLDANE CCCCCCCCCCCCCCC | 34.21 | 17242355 | |
271 | Phosphorylation | NKTESESSSLDANEI CCCCCCCCCCCCCCC | 30.76 | 28973931 | |
272 | Phosphorylation | KTESESSSLDANEIP CCCCCCCCCCCCCCC | 39.28 | 25195567 | |
292 | Phosphorylation | SLSEESASDSGDSKY ECCCCCCCCCCCCCC | 41.40 | 25293948 | |
294 | Phosphorylation | SEESASDSGDSKYED CCCCCCCCCCCCCCC | 41.84 | 25293948 | |
297 | Phosphorylation | SASDSGDSKYEDCQE CCCCCCCCCCCCCCC | 40.43 | 25293948 | |
399 | Phosphorylation | IMGNKKVSVSATPGH HCCCCEEEEECCCCC | 21.16 | 25338131 | |
472 | Phosphorylation | PRRVLEVTYGINIIK CHHHEEEEEEEEEEC | 13.47 | 24719451 | |
473 | Phosphorylation | RRVLEVTYGINIIKP HHHEEEEEEEEEECC | 22.60 | 24719451 | |
517 | Phosphorylation | GQPDQPRSARYILKD CCCCCCCCHHHHHHH | 24.63 | 23737553 | |
520 | Phosphorylation | DQPRSARYILKDYVG CCCCCHHHHHHHCCC | 15.43 | 23737553 |
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 LSG1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LSG1_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 LSG1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of LSG1_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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