UniProt ID | SSRB_HUMAN | |
---|---|---|
UniProt AC | P43308 | |
Protein Name | Translocon-associated protein subunit beta | |
Gene Name | SSR2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 183 | |
Subcellular Localization |
Endoplasmic reticulum membrane Single-pass type I membrane protein. |
|
Protein Description | TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.. | |
Protein Sequence | MRLLSFVVLALFAVTQAEEGARLLASKSLLNRYAVEGRDLTLQYNIYNVGSSAALDVELSDDSFPPEDFGIVSGMLNVKWDRIAPASNVSHTVVLRPLKAGYFNFTSATITYLAQEDGPVVIGSTSAPGQGGILAQREFDRRFSPHFLDWAAFGVMTLPSIGIPLLLWYSSKRKYDTPKTKKN | |
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 |
---|---|---|---|---|---|
27 | Ubiquitination | GARLLASKSLLNRYA HHHHHHCHHHHHHHH | 39.24 | 21963094 | |
27 | 2-Hydroxyisobutyrylation | GARLLASKSLLNRYA HHHHHHCHHHHHHHH | 39.24 | - | |
32 | Methylation | ASKSLLNRYAVEGRD HCHHHHHHHHHCCCC | 22.28 | 115917889 | |
46 | Ubiquitination | DLTLQYNIYNVGSSA CEEEEEEEEECCCCE | 1.94 | 21906983 | |
87 | O-linked_Glycosylation | WDRIAPASNVSHTVV CEEECCCCCCCEEEE | 36.38 | 30059200 | |
88 | N-linked_Glycosylation | DRIAPASNVSHTVVL EEECCCCCCCEEEEE | 41.22 | 12754519 | |
90 | O-linked_Glycosylation | IAPASNVSHTVVLRP ECCCCCCCEEEEECE | 20.07 | 30059200 | |
104 | N-linked_Glycosylation | PLKAGYFNFTSATIT EECCCCCEECEEEEE | 30.70 | 12754519 | |
125 | O-linked_Glycosylation | GPVVIGSTSAPGQGG CCEEEECCCCCCCCC | 24.56 | OGP | |
157 | Phosphorylation | WAAFGVMTLPSIGIP HHHHCCCCCHHCCCC | 32.86 | 27251275 | |
160 | Phosphorylation | FGVMTLPSIGIPLLL HCCCCCHHCCCCHHH | 36.24 | 27251275 | |
169 | Phosphorylation | GIPLLLWYSSKRKYD CCCHHHHHHCCCCCC | 11.75 | 27251275 | |
171 | Phosphorylation | PLLLWYSSKRKYDTP CHHHHHHCCCCCCCC | 22.30 | 27251275 | |
177 | Phosphorylation | SSKRKYDTPKTKKN- HCCCCCCCCCCCCC- | 24.48 | 21857030 | |
182 | Ubiquitination | YDTPKTKKN------ CCCCCCCCC------ | 73.46 | 24816145 | |
201 | Ubiquitination | ------------------------- ------------------------- | 24816145 |
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 SSRB_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SSRB_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 SSRB_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SRPRA_HUMAN | SRPR | physical | 3021779 | |
RPN1_HUMAN | RPN1 | physical | 26344197 | |
QCR2_HUMAN | UQCRC2 | physical | 26344197 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
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-88 AND ASN-104, AND MASSSPECTROMETRY. | |
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry."; Zhang H., Li X.-J., Martin D.B., Aebersold R.; Nat. Biotechnol. 21:660-666(2003). Cited for: GLYCOSYLATION AT ASN-88 AND ASN-104. |