UniProt ID | H17B6_HUMAN | |
---|---|---|
UniProt AC | O14756 | |
Protein Name | 17-beta-hydroxysteroid dehydrogenase type 6 | |
Gene Name | HSD17B6 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 317 | |
Subcellular Localization |
Microsome membrane Peripheral membrane protein Lumenal side . Early endosome membrane Peripheral membrane protein Lumenal side . |
|
Protein Description | NAD-dependent oxidoreductase with broad substrate specificity that shows both oxidative and reductive activity (in vitro). Has 17-beta-hydroxysteroid dehydrogenase activity towards various steroids (in vitro). Converts 5-alpha-androstan-3-alpha,17-beta-diol to androsterone and estradiol to estrone (in vitro). Has 3-alpha-hydroxysteroid dehydrogenase activity towards androsterone (in vitro). Has retinol dehydrogenase activity towards all-trans-retinol (in vitro). Can convert androsterone to epi-androsterone. Androsterone is first oxidized to 5-alpha-androstane-3,17-dione and then reduced to epi-andosterone. Can act on both C-19 and C-21 3-alpha-hydroxysteroids.. | |
Protein Sequence | MWLYLAAFVGLYYLLHWYRERQVVSHLQDKYVFITGCDSGFGNLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKMESIAAATQWVKEHVGDRGLWGLVNNAGILTPITLCEWLNTEDSMNMLKVNLIGVIQVTLSMLPLVRRARGRIVNVSSILGRVAFFVGGYCVSKYGVEAFSDILRREIQHFGVKISIVEPGYFRTGMTNMTQSLERMKQSWKEAPKHIKETYGQQYFDALYNIMKEGLLNCSTNLNLVTDCMEHALTSVHPRTRYSAGWDAKFFFIPLSYLPTSLADYILTRSWPKPAQAV | |
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 |
---|---|---|---|---|---|
64 | Ubiquitination | LAACLTEKGAEQLRG HHHHHCHHHHHHHCC | 59.18 | - | |
161 | N-linked_Glycosylation | RARGRIVNVSSILGR HHCCCEEEHHHHHHH | 26.11 | UniProtKB CARBOHYD | |
202 | Phosphorylation | QHFGVKISIVEPGYF HHHCCEEEEECCCCC | 18.18 | - | |
215 | N-linked_Glycosylation | YFRTGMTNMTQSLER CCCCCCCHHHHHHHH | 23.70 | UniProtKB CARBOHYD | |
256 | N-linked_Glycosylation | IMKEGLLNCSTNLNL HHHHCCCCCCCCCHH | 23.80 | UniProtKB CARBOHYD | |
274 | Phosphorylation | CMEHALTSVHPRTRY HHHHHHHCCCCCCCC | 21.19 | 22210691 | |
279 | Phosphorylation | LTSVHPRTRYSAGWD HHCCCCCCCCCCCCC | 38.11 | 22210691 | |
281 | Phosphorylation | SVHPRTRYSAGWDAK CCCCCCCCCCCCCCE | 11.40 | 22210691 |
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 H17B6_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of H17B6_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 H17B6_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
AT12A_HUMAN | ATP12A | physical | 26186194 | |
NFH_HUMAN | NEFH | physical | 26186194 | |
AT2B1_HUMAN | ATP2B1 | physical | 26186194 | |
AT2B4_HUMAN | ATP2B4 | physical | 26186194 | |
AT2B2_HUMAN | ATP2B2 | physical | 26186194 | |
AT2B3_HUMAN | ATP2B3 | physical | 26186194 | |
TATD1_HUMAN | TATDN1 | physical | 26186194 | |
PRDC1_HUMAN | PRTFDC1 | physical | 26186194 | |
SNX3_HUMAN | SNX3 | physical | 26186194 | |
KPRP_HUMAN | KPRP | physical | 26186194 | |
AT2B3_HUMAN | ATP2B3 | physical | 28514442 | |
AT2B4_HUMAN | ATP2B4 | physical | 28514442 | |
PRDC1_HUMAN | PRTFDC1 | physical | 28514442 | |
TATD1_HUMAN | TATDN1 | physical | 28514442 | |
AT2B1_HUMAN | ATP2B1 | physical | 28514442 | |
PP14B_HUMAN | PPP1R14B | physical | 28514442 | |
GNA1_HUMAN | GNPNAT1 | physical | 28514442 | |
AT12A_HUMAN | ATP12A | physical | 28514442 | |
SNX3_HUMAN | SNX3 | physical | 28514442 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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