| UniProt ID | SIRB1_HUMAN | |
|---|---|---|
| UniProt AC | O00241 | |
| Protein Name | Signal-regulatory protein beta-1 | |
| Gene Name | SIRPB1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 398 | |
| Subcellular Localization |
Membrane Single-pass type I membrane protein. |
|
| Protein Description | Immunoglobulin-like cell surface receptor involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. Participates also in the recruitment of tyrosine kinase SYK.. | |
| Protein Sequence | MPVPASWPHLPSPFLLMTLLLGRLTGVAGEDELQVIQPEKSVSVAAGESATLRCAMTSLIPVGPIMWFRGAGAGRELIYNQKEGHFPRVTTVSELTKRNNLDFSISISNITPADAGTYYCVKFRKGSPDDVEFKSGAGTELSVRAKPSAPVVSGPAVRATPEHTVSFTCESHGFSPRDITLKWFKNGNELSDFQTNVDPAGDSVSYSIHSTARVVLTRGDVHSQVICEIAHITLQGDPLRGTANLSEAIRVPPTLEVTQQPMRAENQANVTCQVSNFYPRGLQLTWLENGNVSRTETASTLIENKDGTYNWMSWLLVNTCAHRDDVVLTCQVEHDGQQAVSKSYALEISAHQKEHGSDITHEAALAPTAPLLVALLLGPKLLLVVGVSAIYICWKQKA | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 82 | Ubiquitination | RELIYNQKEGHFPRV CHHEECCCCCCCCCE | 63.12 | - | |
| 97 | Ubiquitination | TTVSELTKRNNLDFS EEHHHHHHHCCCEEE | 66.79 | - | |
| 119 | Phosphorylation | PADAGTYYCVKFRKG HHCCCEEEEEEECCC | 7.21 | - | |
| 135 | Phosphorylation | PDDVEFKSGAGTELS CCCCEEECCCCCEEE | 38.91 | 29978859 | |
| 139 | Phosphorylation | EFKSGAGTELSVRAK EEECCCCCEEEEEEC | 32.97 | 29978859 | |
| 142 | Phosphorylation | SGAGTELSVRAKPSA CCCCCEEEEEECCCC | 11.88 | 29978859 | |
| 148 | Phosphorylation | LSVRAKPSAPVVSGP EEEEECCCCCEEECC | 44.49 | 30243723 | |
| 153 | Phosphorylation | KPSAPVVSGPAVRAT CCCCCEEECCEEECC | 39.01 | 30243723 | |
| 182 | Ubiquitination | SPRDITLKWFKNGNE CCCCEEEEEEECCCC | 41.77 | - | |
| 182 (in isoform 1) | Ubiquitination | - | 41.77 | 21890473 | |
| 191 | Phosphorylation | FKNGNELSDFQTNVD EECCCCCCCCCCCCC | 30.15 | - | |
| 244 | N-linked_Glycosylation | DPLRGTANLSEAIRV CCCCCCCCHHHHCCC | 43.89 | 16335952 | |
| 269 | N-linked_Glycosylation | MRAENQANVTCQVSN CCHHHCCCCEEEEEC | 21.62 | UniProtKB CARBOHYD | |
| 291 | N-linked_Glycosylation | LTWLENGNVSRTETA EEEEECCCCCCEEEC | 39.92 | UniProtKB CARBOHYD |
| 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 SIRB1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SIRB1_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 SIRB1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| TYOBP_HUMAN | TYROBP | physical | 10604985 | |
| TYOBP_HUMAN | TYROBP | physical | 10940905 | |
| KSYK_HUMAN | SYK | physical | 10940905 | |
| RBPMS_HUMAN | RBPMS | physical | 25416956 |
| 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 |
| "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-244, AND MASSSPECTROMETRY. | |