UniProt ID | SPCS3_HUMAN | |
---|---|---|
UniProt AC | P61009 | |
Protein Name | Signal peptidase complex subunit 3 | |
Gene Name | SPCS3 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 180 | |
Subcellular Localization |
Microsome membrane Single-pass type II membrane protein . Endoplasmic reticulum membrane Single-pass type II membrane protein . |
|
Protein Description | Component of the microsomal signal peptidase complex which removes signal peptides and other N-terminal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum.. | |
Protein Sequence | MNTVLSRANSLFAFSLSVMAALTFGCFITTAFKDRSVPVRLHVSRIMLKNVEDFTGPRERSDLGFITFDITADLENIFDWNVKQLFLYLSAEYSTKNNALNQVVLWDKIVLRGDNPKLLLKDMKTKYFFFDDGNGLKGNRNVTLTLSWNVVPNAGILPLVTGSGHVSVPFPDTYEITKSY | |
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 |
---|---|---|---|---|---|
3 | Phosphorylation | -----MNTVLSRANS -----CCCHHHHHHH | 22.86 | 24043423 | |
6 | Phosphorylation | --MNTVLSRANSLFA --CCCHHHHHHHHHH | 25.63 | 24043423 | |
10 | Phosphorylation | TVLSRANSLFAFSLS CHHHHHHHHHHHHHH | 24.71 | 24043423 | |
15 | Phosphorylation | ANSLFAFSLSVMAAL HHHHHHHHHHHHHHH | 19.12 | 24043423 | |
17 | Phosphorylation | SLFAFSLSVMAALTF HHHHHHHHHHHHHHH | 14.51 | 24043423 | |
23 | Phosphorylation | LSVMAALTFGCFITT HHHHHHHHHCHHHHH | 17.16 | 24043423 | |
29 | Phosphorylation | LTFGCFITTAFKDRS HHHCHHHHHHCCCCC | 7.57 | 24043423 | |
30 | Phosphorylation | TFGCFITTAFKDRSV HHCHHHHHHCCCCCC | 25.86 | 24043423 | |
49 | Ubiquitination | HVSRIMLKNVEDFTG EEEEEEECCHHHCCC | 41.38 | 27667366 | |
49 | Acetylation | HVSRIMLKNVEDFTG EEEEEEECCHHHCCC | 41.38 | 27452117 | |
49 | 2-Hydroxyisobutyrylation | HVSRIMLKNVEDFTG EEEEEEECCHHHCCC | 41.38 | - | |
55 | Phosphorylation | LKNVEDFTGPRERSD ECCHHHCCCCCCCCC | 59.61 | 24719451 | |
71 | Phosphorylation | GFITFDITADLENIF CEEEEEEECCHHHHC | 18.90 | - | |
108 | Ubiquitination | NQVVLWDKIVLRGDN CCEEEEEEEEECCCC | 24.11 | 22817900 | |
117 | Ubiquitination | VLRGDNPKLLLKDMK EECCCCCCEEEECCC | 59.00 | 22817900 | |
121 | Ubiquitination | DNPKLLLKDMKTKYF CCCCEEEECCCCCEE | 56.60 | 22817900 | |
121 | 2-Hydroxyisobutyrylation | DNPKLLLKDMKTKYF CCCCEEEECCCCCEE | 56.60 | - | |
124 | Ubiquitination | KLLLKDMKTKYFFFD CEEEECCCCCEEEEE | 52.58 | 22817900 | |
125 | Phosphorylation | LLLKDMKTKYFFFDD EEEECCCCCEEEEEC | 25.08 | 27174698 | |
126 | Ubiquitination | LLKDMKTKYFFFDDG EEECCCCCEEEEECC | 34.24 | 21906983 | |
126 | 2-Hydroxyisobutyrylation | LLKDMKTKYFFFDDG EEECCCCCEEEEECC | 34.24 | - | |
126 | Acetylation | LLKDMKTKYFFFDDG EEECCCCCEEEEECC | 34.24 | 27452117 | |
127 | Phosphorylation | LKDMKTKYFFFDDGN EECCCCCEEEEECCC | 15.73 | 25693802 | |
137 | Ubiquitination | FDDGNGLKGNRNVTL EECCCCCCCCCEEEE | 56.38 | 27667366 | |
141 | N-linked_Glycosylation | NGLKGNRNVTLTLSW CCCCCCCEEEEEEEE | 34.82 | 19159218 |
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 SPCS3_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPCS3_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 SPCS3_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of SPCS3_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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N-linked Glycosylation | |
Reference | PubMed |
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-141, AND MASSSPECTROMETRY. |