UniProt ID | SPTC1_MOUSE | |
---|---|---|
UniProt AC | O35704 | |
Protein Name | Serine palmitoyltransferase 1 | |
Gene Name | Sptlc1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 473 | |
Subcellular Localization |
Endoplasmic reticulum membrane Single-pass membrane protein . |
|
Protein Description | Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates. The SPTLC1-SPTLC2-SPTSSB complex displays a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme has the ability to use a broader range of acyl-CoAs (By similarity).. | |
Protein Sequence | MATVAEQWVLVEMVQALYEAPAYHLILEGILILWIIRLVFSKTYKLQERSDLTAKEKEELIEEWQPEPLVPPVSKNHPALNYNIVSGPPTHNIVVNGKECVNFASFNFLGLLANPRVKATAFSSLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAIIYSYGFSTIASAIPAYSKRGDIIFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQEIEDQKNPRKARVTRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISIDDIDLISANMENALASVGGFCCGRSFVVDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPDIFAVLKKKCQNIHKSLQGVSGLKVVGESLSPALHLQLEESTGSREKDVKLLQAIVDQCMDKGIALTQARYLDKEEKCLPPPSIRVVVTVEQTEEELQRAASTIREAAQAVLL | |
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 |
---|---|---|---|---|---|
50 | Phosphorylation | TYKLQERSDLTAKEK CCCCHHHCCCCHHHH | 35.90 | 26643407 | |
86 | Phosphorylation | ALNYNIVSGPPTHNI CCCCCCCCCCCCCEE | 41.61 | - | |
158 | Phosphorylation | RLAKFMKTEEAIIYS HHHHHHCCCCHHHHH | 27.54 | 23984901 | |
164 | Phosphorylation | KTEEAIIYSYGFSTI CCCCHHHHHCCHHHH | 6.96 | 23984901 | |
165 | Phosphorylation | TEEAIIYSYGFSTIA CCCHHHHHCCHHHHH | 14.36 | 23984901 | |
166 | Phosphorylation | EEAIIYSYGFSTIAS CCHHHHHCCHHHHHH | 12.76 | 23984901 | |
169 | Phosphorylation | IIYSYGFSTIASAIP HHHHCCHHHHHHHCH | 17.97 | 23984901 | |
170 | Phosphorylation | IYSYGFSTIASAIPA HHHCCHHHHHHHCHH | 20.50 | 23984901 | |
173 | Phosphorylation | YGFSTIASAIPAYSK CCHHHHHHHCHHHCC | 23.92 | 23984901 | |
178 | Phosphorylation | IASAIPAYSKRGDII HHHHCHHHCCCCCEE | 14.90 | 23984901 | |
179 | Phosphorylation | ASAIPAYSKRGDIIF HHHCHHHCCCCCEEE | 20.27 | 23984901 | |
222 | Ubiquitination | ADLERLLKEQEIEDQ HHHHHHHHHHHHHHC | 63.04 | 22790023 | |
230 | Ubiquitination | EQEIEDQKNPRKARV HHHHHHCCCHHHHHH | 79.73 | 27667366 | |
375 | Ubiquitination | KKCQNIHKSLQGVSG HHHHHHHHHHCCCCC | 49.41 | 22790023 | |
376 | Phosphorylation | KCQNIHKSLQGVSGL HHHHHHHHHCCCCCC | 16.26 | 29109428 | |
438 | Glutathionylation | YLDKEEKCLPPPSIR HCCHHHCCCCCCCEE | 8.57 | 24333276 | |
443 | Phosphorylation | EKCLPPPSIRVVVTV HCCCCCCCEEEEEEE | 28.88 | 29899451 | |
449 | Phosphorylation | PSIRVVVTVEQTEEE CCEEEEEEECCCHHH | 13.50 | 29899451 | |
453 | Phosphorylation | VVVTVEQTEEELQRA EEEEECCCHHHHHHH | 31.68 | 29899451 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
164 | Y | Phosphorylation | Kinase | ABL | P00520 | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPTC1_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 SPTC1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ABCA1_MOUSE | Abca1 | physical | 18484747 | |
PARD3_MOUSE | Pard3 | physical | 18484747 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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