UniProt ID | DHI1_HUMAN | |
---|---|---|
UniProt AC | P28845 | |
Protein Name | Corticosteroid 11-beta-dehydrogenase isozyme 1 | |
Gene Name | HSD11B1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 292 | |
Subcellular Localization |
Endoplasmic reticulum membrane Single-pass type II membrane protein . |
|
Protein Description | Catalyzes reversibly the conversion of cortisol to the inactive metabolite cortisone. Catalyzes reversibly the conversion of 7-ketocholesterol to 7-beta-hydroxycholesterol. In intact cells, the reaction runs only in one direction, from 7-ketocholesterol to 7-beta-hydroxycholesterol (By similarity).. | |
Protein Sequence | MAFMKKYLLPILGLFMAYYYYSANEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAHVVVTARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQAGKLMGGLDMLILNHITNTSLNLFHDDIHHVRKSMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMVAAYSASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMKAVSGIVHMQAAPKEECALEIIKGGALRQEEVYYDSSLWTTLLIRNPCRKILEFLYSTSYNMDRFINK | |
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 |
---|---|---|---|---|---|
22 | Phosphorylation | FMAYYYYSANEEFRP HHHHHHHCCCHHHCH | 14.43 | 24719451 | |
56 | Methylation | EMAYHLAKMGAHVVV HHHHHHHHCCCEEEE | 44.20 | 23644510 | |
67 | Phosphorylation | HVVVTARSKETLQKV EEEEEECCHHHHHHH | 32.17 | 30576142 | |
123 | N-linked_Glycosylation | LILNHITNTSLNLFH HHHHCCCCCCCCCCC | 27.37 | 19159218 | |
162 | N-linked_Glycosylation | LPMLKQSNGSIVVVS HHHHHHCCCCEEEEE | 45.82 | 19159218 | |
195 | Phosphorylation | FALDGFFSSIRKEYS HHHHHHHHHHHHHHC | 23.69 | 29978859 | |
196 | Phosphorylation | ALDGFFSSIRKEYSV HHHHHHHHHHHHHCC | 22.66 | 29978859 | |
207 | N-linked_Glycosylation | EYSVSRVNVSITLCV HHCCCCCCEEEEEEH | 22.25 | UniProtKB CARBOHYD | |
280 | Phosphorylation | RKILEFLYSTSYNMD HHHHHHHHHHCCCHH | 18.41 | 23663014 | |
281 | Phosphorylation | KILEFLYSTSYNMDR HHHHHHHHHCCCHHH | 17.02 | 23663014 | |
282 | Phosphorylation | ILEFLYSTSYNMDRF HHHHHHHHCCCHHHH | 22.98 | 23663014 | |
283 | Phosphorylation | LEFLYSTSYNMDRFI HHHHHHHCCCHHHHC | 14.47 | 23663014 | |
284 | Phosphorylation | EFLYSTSYNMDRFIN HHHHHHCCCHHHHCC | 18.00 | 23663014 |
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 DHI1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DHI1_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 DHI1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
DAD1_HUMAN | DAD1 | physical | 26186194 | |
TMX2_HUMAN | TMX2 | physical | 26186194 | |
CGT_HUMAN | UGT8 | physical | 26186194 | |
BI1_HUMAN | TMBIM6 | physical | 26186194 | |
GLBL2_HUMAN | GLB1L2 | physical | 26186194 | |
C42S2_HUMAN | CDC42SE2 | physical | 26186194 | |
RAB18_HUMAN | RAB18 | physical | 26186194 | |
NHLC3_HUMAN | NHLRC3 | physical | 26186194 | |
TOR1A_HUMAN | TOR1A | physical | 26186194 | |
FA69A_HUMAN | FAM69A | physical | 26186194 | |
TMX4_HUMAN | TMX4 | physical | 26186194 | |
MANEA_HUMAN | MANEA | physical | 26186194 | |
CGT_HUMAN | UGT8 | physical | 28514442 | |
NPTX1_HUMAN | NPTX1 | physical | 28514442 | |
TMX4_HUMAN | TMX4 | physical | 28514442 | |
BI1_HUMAN | TMBIM6 | physical | 28514442 |
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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-123 AND ASN-162, AND MASSSPECTROMETRY. |