| UniProt ID | HEBP2_HUMAN | |
|---|---|---|
| UniProt AC | Q9Y5Z4 | |
| Protein Name | Heme-binding protein 2 | |
| Gene Name | HEBP2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 205 | |
| Subcellular Localization | Cytoplasm . Mitochondrion . Mainly localized to the cytoplasm with a much lower abundance in the mitochondrion. | |
| Protein Description | Can promote mitochondrial permeability transition and facilitate necrotic cell death under different types of stress conditions.. | |
| Protein Sequence | MAEPLQPDPGAAEDAAAQAVETPGWKAPEDAGPQPGSYEIRHYGPAKWVSTSVESMDWDSAIQTGFTKLNSYIQGKNEKEMKIKMTAPVTSYVEPGSGPFSESTITISLYIPSEQQFDPPRPLESDVFIEDRAEMTVFVRSFDGFSSAQKNQEQLLTLASILREDGKVFDEKVYYTAGYNSPVKLLNRNNEVWLIQKNEPTKENE | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MAEPLQPDP ------CCCCCCCCC | 27.41 | 22223895 | |
| 22 | Phosphorylation | AAAQAVETPGWKAPE HHHHHHCCCCCCCCC | 22.09 | 28355574 | |
| 37 | Phosphorylation | DAGPQPGSYEIRHYG CCCCCCCCEEEEEEC | 26.69 | 26437602 | |
| 41 | Methylation | QPGSYEIRHYGPAKW CCCCEEEEEECCCEE | 12.68 | 115478391 | |
| 76 | Ubiquitination | LNSYIQGKNEKEMKI HHHHHCCCCCCCCEE | 45.62 | - | |
| 82 | Ubiquitination | GKNEKEMKIKMTAPV CCCCCCCEEEEECCC | 40.02 | - | |
| 135 | Sulfoxidation | FIEDRAEMTVFVRSF EECCCCEEEEEEEEC | 3.65 | 21406390 | |
| 136 | Phosphorylation | IEDRAEMTVFVRSFD ECCCCEEEEEEEECC | 11.42 | - | |
| 141 | Phosphorylation | EMTVFVRSFDGFSSA EEEEEEEECCCCCCH | 23.53 | 26437602 | |
| 146 | Phosphorylation | VRSFDGFSSAQKNQE EEECCCCCCHHCCHH | 30.23 | - | |
| 147 | Phosphorylation | RSFDGFSSAQKNQEQ EECCCCCCHHCCHHH | 32.24 | - | |
| 151 (in isoform 2) | Ubiquitination | - | 38.24 | 21890473 | |
| 163 (in isoform 2) | Ubiquitination | - | 37.99 | 21890473 | |
| 172 | Ubiquitination | DGKVFDEKVYYTAGY CCCCCCEEEEEECCC | 37.06 | 21890473 | |
| 172 (in isoform 1) | Ubiquitination | - | 37.06 | 21890473 | |
| 174 | Phosphorylation | KVFDEKVYYTAGYNS CCCCEEEEEECCCCC | 13.23 | 28152594 | |
| 175 | Phosphorylation | VFDEKVYYTAGYNSP CCCEEEEEECCCCCC | 7.97 | 28152594 | |
| 176 | Phosphorylation | FDEKVYYTAGYNSPV CCEEEEEECCCCCCE | 8.91 | 28152594 | |
| 179 | Phosphorylation | KVYYTAGYNSPVKLL EEEEECCCCCCEEEE | 15.25 | 19413330 | |
| 181 | Phosphorylation | YYTAGYNSPVKLLNR EEECCCCCCEEEECC | 23.68 | 19664994 | |
| 184 | Ubiquitination | AGYNSPVKLLNRNNE CCCCCCEEEECCCCC | 51.12 | 21890473 | |
| 184 (in isoform 1) | Ubiquitination | - | 51.12 | 21890473 | |
| 184 | Acetylation | AGYNSPVKLLNRNNE CCCCCCEEEECCCCC | 51.12 | 23236377 |
| 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 HEBP2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HEBP2_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 HEBP2_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of HEBP2_HUMAN !! | ||||
| 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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| Acetylation | |
| Reference | PubMed |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT TYR-179 AND SER-181, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASSSPECTROMETRY. | |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT TYR-179 AND SER-181, AND MASS SPECTROMETRY. | |
