UniProt ID | NB5R2_HUMAN | |
---|---|---|
UniProt AC | Q6BCY4 | |
Protein Name | NADH-cytochrome b5 reductase 2 | |
Gene Name | CYB5R2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 276 | |
Subcellular Localization | ||
Protein Description | NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction (By similarity). Responsible for NADH-dependent lucigenin chemiluminescence in spermatozoa by reducing both lucigenin and 2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt (WST-1).. | |
Protein Sequence | MNSRRREPITLQDPEAKYPLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYFKNVHPQYPEGGKMTQYLENMKIGETIFFRGPRGRLFYHGPGNLGIRPDQTSEPKKTLADHLGMIAGGTGITPMLQLIRHITKDPSDRTRMSLIFANQTEEDILVRKELEEIARTHPDQFNLWYTLDRPPIGWKYSSGFVTADMIKEHLPPPAKSTLILVCGPPPLIQTAAHPNLEKLGYTQDMIFTY | |
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 |
---|---|---|---|---|---|
17 | Acetylation | TLQDPEAKYPLPLIE CCCCCCCCCCCCCEE | 45.82 | 25038526 | |
18 | Phosphorylation | LQDPEAKYPLPLIEK CCCCCCCCCCCCEEH | 19.63 | - | |
25 | Acetylation | YPLPLIEKEKISHNT CCCCCEEHHHCCCCC | 58.26 | 25038526 | |
41 | Phosphorylation | RFRFGLPSPDHVLGL CEECCCCCCCCCCCC | 48.26 | - | |
145 | Phosphorylation | QTSEPKKTLADHLGM CCCCCCCCHHHHHHH | 33.05 | - | |
157 | Phosphorylation | LGMIAGGTGITPMLQ HHHHCCCCCHHHHHH | 25.21 | 20068231 | |
160 | Phosphorylation | IAGGTGITPMLQLIR HCCCCCHHHHHHHHH | 12.18 | 20068231 | |
177 | Phosphorylation | TKDPSDRTRMSLIFA HCCCCCCCEEEEEEC | 35.40 | 22817900 | |
177 (in isoform 1) | Phosphorylation | - | 35.40 | - | |
234 | Acetylation | FVTADMIKEHLPPPA EEEHHHHHHHCCCCC | 32.23 | 25038526 | |
243 | Phosphorylation | HLPPPAKSTLILVCG HCCCCCCEEEEEEEC | 30.47 | 21406692 | |
244 | Phosphorylation | LPPPAKSTLILVCGP CCCCCCEEEEEEECC | 19.67 | 21406692 | |
257 | Phosphorylation | GPPPLIQTAAHPNLE CCCCHHHCCCCCCHH | 20.86 | 21406692 |
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 NB5R2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NB5R2_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 NB5R2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
FFAR2_HUMAN | FFAR2 | physical | 21988832 |
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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Phosphorylation | |
Reference | PubMed |
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177, AND MASSSPECTROMETRY. |