| |
|---|---|
| Accession Number: | P04035 |
| Protein Name: | HMDH aka HMGCR |
| Length: | 888 |
| Molecular Weight: | 97476.00 |
| Species: | Homo sapiens (Human) [9606] |
| Number of TMSs: | 7 |
| Location1 / Topology2 / Orientation3: | Endoplasmic reticulum membrane1 / Multi-pass membrane protein2 |
| Substrate | electron |
Cross database links:
| RefSeq: | NP_000850.1 NP_001124468.1 |
|---|---|
| Entrez Gene ID: | 3156 |
| Pfam: | PF00368 |
| OMIM: |
142910 gene+phenotype |
| BioCyc: | MetaCyc:ENSG00000113161-MONOMER |
| KEGG: | hsa:3156 |
Gene Ontology
GO:0005789
C:endoplasmic reticulum membrane
GO:0016021
C:integral to membrane
GO:0005778
C:peroxisomal membrane
GO:0004420
F:hydroxymethylglutaryl-CoA reductase (NADPH)...
GO:0050661
F:NADP or NADPH binding
GO:0006695
P:cholesterol biosynthetic process
GO:0015936
P:coenzyme A metabolic process
GO:0008354
P:germ cell migration
GO:0008406
P:gonad development
GO:0008299
P:isoprenoid biosynthetic process
GO:0055114
P:oxidation reduction
| |
References (5)[1] “Human 3-hydroxy-3-methylglutaryl coenzyme A reductase. Conserved domains responsible for catalytic activity and sterol-regulated degradation.” Luskey K.L.et.al. 2991281 [2] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).” The MGC Project Teamet.al. 15489334 [3] “Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis.” Istvan E.S.et.al. 10698924 | |
| Structure: | |
| [...more] | |
External Searches:
|
Analyze:
| Predict TMSs (Predict number of transmembrane segments) | ||||
| FASTA formatted sequence |
|
|||
1: MLSRLFRMHG LFVASHPWEV IVGTVTLTIC MMSMNMFTGN NKICGWNYEC PKFEEDVLSS 61: DIIILTITRC IAILYIYFQF QNLRQLGSKY ILGIAGLFTI FSSFVFSTVV IHFLDKELTG 121: LNEALPFFLL LIDLSRASTL AKFALSSNSQ DEVRENIARG MAILGPTFTL DALVECLVIG 181: VGTMSGVRQL EIMCCFGCMS VLANYFVFMT FFPACVSLVL ELSRESREGR PIWQLSHFAR 241: VLEEEENKPN PVTQRVKMIM SLGLVLVHAH SRWIADPSPQ NSTADTSKVS LGLDENVSKR 301: IEPSVSLWQF YLSKMISMDI EQVITLSLAL LLAVKYIFFE QTETESTLSL KNPITSPVVT 361: QKKVPDNCCR REPMLVRNNQ KCDSVEEETG INRERKVEVI KPLVAETDTP NRATFVVGNS 421: SLLDTSSVLV TQEPEIELPR EPRPNEECLQ ILGNAEKGAK FLSDAEIIQL VNAKHIPAYK 481: LETLMETHER GVSIRRQLLS KKLSEPSSLQ YLPYRDYNYS LVMGACCENV IGYMPIPVGV 541: AGPLCLDEKE FQVPMATTEG CLVASTNRGC RAIGLGGGAS SRVLADGMTR GPVVRLPRAC 601: DSAEVKAWLE TSEGFAVIKE AFDSTSRFAR LQKLHTSIAG RNLYIRFQSR SGDAMGMNMI 661: SKGTEKALSK LHEYFPEMQI LAVSGNYCTD KKPAAINWIE GRGKSVVCEA VIPAKVVREV 721: LKTTTEAMIE VNINKNLVGS AMAGSIGGYN AHAANIVTAI YIACGQDAAQ NVGSSNCITL 781: MEASGPTNED LYISCTMPSI EIGTVGGGTN LLPQQACLQM LGVQGACKDN PGENARQLAR 841: IVCGTVMAGE LSLMAALAAG HLVKSHMIHN RSKINLQDLQ GACTKKTA