UniProt ID | KPSH1_HUMAN | |
---|---|---|
UniProt AC | P11801 | |
Protein Name | Serine/threonine-protein kinase H1 | |
Gene Name | PSKH1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 424 | |
Subcellular Localization |
Golgi apparatus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus speckle. Endoplasmic reticulum membrane Lipid-anchor. Cell membrane Lipid-anchor. Cytoplasm. Localized in the brefeldin A-sensitive Golgi compartment, at c |
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Protein Description | May be a SFC-associated serine kinase (splicing factor compartment-associated serine kinase) with a role in intranuclear SR protein (non-snRNP splicing factors containing a serine/arginine-rich domain) trafficking and pre-mRNA processing.. | |
Protein Sequence | MGCGTSKVLPEPPKDVQLDLVKKVEPFSGTKSDVYKHFITEVDSVGPVKAGFPAASQYAHPCPGPPTAGHTEPPSEPPRRARVAKYRAKFDPRVTAKYDIKALIGRGSFSRVVRVEHRATRQPYAIKMIETKYREGREVCESELRVLRRVRHANIIQLVEVFETQERVYMVMELATGGELFDRIIAKGSFTERDATRVLQMVLDGVRYLHALGITHRDLKPENLLYYHPGTDSKIIITDFGLASARKKGDDCLMKTTCGTPEYIAPEVLVRKPYTNSVDMWALGVIAYILLSGTMPFEDDNRTRLYRQILRGKYSYSGEPWPSVSNLAKDFIDRLLTVDPGARMTALQALRHPWVVSMAASSSMKNLHRSISQNLLKRASSRCQSTKSAQSTRSSRSTRSNKSRRVRERELRELNLRYQQQYNG | |
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 |
---|---|---|---|---|---|
2 | N-myristoyl glycine | ------MGCGTSKVL ------CCCCCCCCC | 20.68 | - | |
2 | Myristoylation | ------MGCGTSKVL ------CCCCCCCCC | 20.68 | 14644153 | |
3 | S-palmitoylation | -----MGCGTSKVLP -----CCCCCCCCCC | 5.33 | 14644153 | |
35 | Phosphorylation | SGTKSDVYKHFITEV CCCCHHHHHHHCEEC | 12.07 | - | |
95 | Phosphorylation | AKFDPRVTAKYDIKA HHCCCCCCEEEEHHH | 20.79 | 28555341 | |
164 | Phosphorylation | QLVEVFETQERVYMV HHEEEEHHHCHHHHE | 25.02 | - | |
176 | Phosphorylation | YMVMELATGGELFDR HHEEHHHHCCHHHHH | 59.34 | - | |
187 | Ubiquitination | LFDRIIAKGSFTERD HHHHHHHCCCCCHHH | 44.68 | - | |
238 | Phosphorylation | TDSKIIITDFGLASA CCCEEEEECCCHHHH | 18.18 | 26074081 | |
244 | Phosphorylation | ITDFGLASARKKGDD EECCCHHHHHHCCCC | 33.38 | 26074081 | |
380 | Phosphorylation | QNLLKRASSRCQSTK HHHHHHHHHHHHCCH | 23.50 | - | |
381 | Phosphorylation | NLLKRASSRCQSTKS HHHHHHHHHHHCCHH | 35.77 | - |
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 KPSH1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KPSH1_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 KPSH1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
HS90A_HUMAN | HSP90AA1 | physical | 22939624 | |
RDH13_HUMAN | RDH13 | physical | 21988832 |
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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Myristoylation | |
Reference | PubMed |
"Mutants of the protein serine kinase PSKH1 disassemble the Golgiapparatus."; Brede G., Solheim J., Stang E., Prydz H.; Exp. Cell Res. 291:299-312(2003). Cited for: MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-3, AND SUBCELLULARLOCATION. | |
Palmitoylation | |
Reference | PubMed |
"Mutants of the protein serine kinase PSKH1 disassemble the Golgiapparatus."; Brede G., Solheim J., Stang E., Prydz H.; Exp. Cell Res. 291:299-312(2003). Cited for: MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-3, AND SUBCELLULARLOCATION. |