UniProt ID | GEMI7_HUMAN | |
---|---|---|
UniProt AC | Q9H840 | |
Protein Name | Gem-associated protein 7 | |
Gene Name | GEMIN7 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 131 | |
Subcellular Localization | Nucleus, nucleoplasm . Nucleus, gem . Cytoplasm . Found both in the nucleoplasm and in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm. | |
Protein Description | The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus.. | |
Protein Sequence | MQTPVNIPVPVLRLPRGPDGFSRGFAPDGRRAPLRPEVPEIQECPIAQESLESQEQRARAALRERYLRSLLAMVGHQVSFTLHEGVRVAAHFGATDLDVANFYVSQLQTPIGVQAEALLRCSDIISYTFKP | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MQTPVNIP -------CCCCCCCC | 10.12 | 22223895 | |
3 | Phosphorylation | -----MQTPVNIPVP -----CCCCCCCCCC | 28.10 | 29255136 | |
16 | Methylation | VPVLRLPRGPDGFSR CCEEECCCCCCCCCC | 74.08 | - | |
23 | Methylation | RGPDGFSRGFAPDGR CCCCCCCCCCCCCCC | 41.82 | - | |
44 | Glutathionylation | EVPEIQECPIAQESL CCCCHHCCCCCHHHH | 1.37 | 22555962 | |
50 | Phosphorylation | ECPIAQESLESQEQR CCCCCHHHHHHHHHH | 25.92 | - | |
53 | Phosphorylation | IAQESLESQEQRARA CCHHHHHHHHHHHHH | 44.29 | - | |
128 | Phosphorylation | CSDIISYTFKP---- CHHHHEEECCC---- | 20.56 | - |
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 GEMI7_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GEMI7_HUMAN !! |
* 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 GEMI7_HUMAN !! |
Kegg Disease | ||||||
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There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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