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P51857

- AK1D1_HUMAN

UniProt

P51857 - AK1D1_HUMAN

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Protein
3-oxo-5-beta-steroid 4-dehydrogenase
Gene
AKR1D1, SRD5B1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites. The bile acid intermediates 7-alpha,12-alpha-dihydroxy-4-cholesten-3-one and 7-alpha-hydroxy-4-cholesten-3-one can also act as substrates.

Catalytic activityi

5-beta-cholestan-3-one + NADP+ = cholest-4-en-3-one + NADPH.
17,21-dihydroxy-5-beta-pregnane-3,11,20-trione + NADP+ = cortisone.

Enzyme regulationi

Subject to inhibition by high substrate concentrations. Inhibited by testosterone concentrations above 10 µM.1 Publication

Kineticsi

  1. KM=2.7 µM for testosterone1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei26 – 261Substrate
Binding sitei53 – 531NADP
Active sitei58 – 581Proton donor
Binding sitei58 – 581Substrate
Binding sitei89 – 891Substrate
Binding sitei120 – 1201Substrate
Binding sitei132 – 1321Substrate
Binding sitei193 – 1931NADP
Binding sitei230 – 2301Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 265NADP
Nucleotide bindingi169 – 1702NADP
Nucleotide bindingi219 – 2246NADP
Nucleotide bindingi273 – 28311NADP
Add
BLAST

GO - Molecular functioni

  1. delta4-3-oxosteroid 5beta-reductase activity Source: UniProtKB-EC
  2. steroid binding Source: UniProtKB

GO - Biological processi

  1. C21-steroid hormone metabolic process Source: UniProtKB
  2. androgen metabolic process Source: UniProtKB
  3. bile acid biosynthetic process Source: UniProtKB
  4. bile acid catabolic process Source: UniProtKB-KW
  5. bile acid metabolic process Source: Reactome
  6. cholesterol catabolic process Source: UniProtKB
  7. digestion Source: UniProtKB
  8. oxidation-reduction process Source: UniProtKB
  9. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Bile acid catabolism, Lipid degradation, Lipid metabolism, Steroid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_11048. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
SABIO-RKP51857.

Names & Taxonomyi

Protein namesi
Recommended name:
3-oxo-5-beta-steroid 4-dehydrogenase (EC:1.3.1.3)
Alternative name(s):
Aldo-keto reductase family 1 member D1
Delta(4)-3-ketosteroid 5-beta-reductase
Delta(4)-3-oxosteroid 5-beta-reductase
Gene namesi
Name:AKR1D1
Synonyms:SRD5B1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:388. AKR1D1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Congenital bile acid synthesis defect 2 (CBAS2) [MIM:235555]: A condition characterized by jaundice, intrahepatic cholestasis and hepatic failure. Patients with this liver disease show absence or low levels of chenodeoxycholic acid and cholic acid in plasma and urine.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061L → F in CBAS2. 1 Publication
VAR_033007
Natural varianti133 – 1331P → R in CBAS2. 1 Publication
VAR_044430
Natural varianti198 – 1981P → L in CBAS2. 1 Publication
VAR_033008
Natural varianti261 – 2611R → C in CBAS2. 1 Publication
VAR_044431

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581Y → A: Loss of activity. 1 Publication
Mutagenesisi120 – 1201E → A: Loss of activity. 1 Publication

Keywords - Diseasei

Disease mutation, Intrahepatic cholestasis

Organism-specific databases

MIMi235555. phenotype.
Orphaneti79303. Congenital bile acid synthesis defect type 2.
PharmGKBiPA24681.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3263263-oxo-5-beta-steroid 4-dehydrogenase
PRO_0000124669Add
BLAST

Proteomic databases

MaxQBiP51857.
PaxDbiP51857.
PRIDEiP51857.

PTM databases

PhosphoSiteiP51857.

Expressioni

Tissue specificityi

Highly expressed in liver. Expressed in testis and weakly in colon.1 Publication

Gene expression databases

ArrayExpressiP51857.
BgeeiP51857.
CleanExiHS_AKR1D1.
GenevestigatoriP51857.

Organism-specific databases

HPAiHPA057002.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000242375.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 113
Beta strandi17 – 215
Turni29 – 313
Helixi36 – 4712
Beta strandi51 – 533
Helixi56 – 583
Helixi61 – 7313
Helixi79 – 813
Beta strandi83 – 886
Helixi90 – 923
Helixi95 – 973
Helixi98 – 10912
Beta strandi114 – 1207
Helixi147 – 15913
Beta strandi162 – 1709
Helixi173 – 1808
Beta strandi191 – 1955
Helixi203 – 2119
Beta strandi215 – 2206
Turni228 – 2303
Helixi238 – 2403
Helixi242 – 2509
Helixi255 – 26511
Helixi277 – 2848
Helixi293 – 3008
Helixi312 – 3143
Beta strandi321 – 3244

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BURX-ray1.62A/B1-326[»]
3BUVX-ray1.35A/B1-326[»]
3BV7X-ray1.79A/B1-326[»]
3CAQX-ray2.20A/B1-326[»]
3CASX-ray2.00A/B1-326[»]
3CAVX-ray1.90A/B1-326[»]
3CMFX-ray1.90A/B1-326[»]
3COTX-ray2.03A/B1-326[»]
3DOPX-ray2.00A/B1-326[»]
3G1RX-ray1.70A/B1-326[»]
3UZWX-ray1.89A/B1-326[»]
3UZXX-ray1.64A/B1-326[»]
3UZYX-ray1.83A/B1-326[»]
3UZZX-ray1.82A/B1-326[»]
ProteinModelPortaliP51857.
SMRiP51857. Positions 2-326.

Miscellaneous databases

EvolutionaryTraceiP51857.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0656.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiP51857.
KOiK00251.
OMAiLYQNEHE.
OrthoDBiEOG70KGQF.
PhylomeDBiP51857.
TreeFamiTF106492.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P51857-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MDLSAASHRI PLSDGNSIPI IGLGTYSEPK STPKGACATS VKVAIDTGYR    50
HIDGAYIYQN EHEVGEAIRE KIAEGKVRRE DIFYCGKLWA TNHVPEMVRP 100
TLERTLRVLQ LDYVDLYIIE VPMAFKPGDE IYPRDENGKW LYHKSNLCAT 150
WEAMEACKDA GLVKSLGVSN FNRRQLELIL NKPGLKHKPV SNQVECHPYF 200
TQPKLLKFCQ QHDIVITAYS PLGTSRNPIW VNVSSPPLLK DALLNSLGKR 250
YNKTAAQIVL RFNIQRGVVV IPKSFNLERI KENFQIFDFS LTEEEMKDIE 300
ALNKNVRFVE LLMWRDHPEY PFHDEY 326
Length:326
Mass (Da):37,377
Last modified:October 1, 1996 - v1
Checksum:i1FE02B95398A0A6F
GO
Isoform 2 (identifier: P51857-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     286-326: IFDFSLTEEEMKDIEALNKNVRFVELLMWRDHPEYPFHDEY → VARSS

Note: No experimental confirmation available.

Show »
Length:290
Mass (Da):32,748
Checksum:iF2C7686DA906C0EC
GO
Isoform 3 (identifier: P51857-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     153-193: Missing.

Note: No experimental confirmation available.

Show »
Length:285
Mass (Da):32,890
Checksum:i5017C36EB0EB13D9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061L → F in CBAS2. 1 Publication
VAR_033007
Natural varianti133 – 1331P → R in CBAS2. 1 Publication
VAR_044430
Natural varianti198 – 1981P → L in CBAS2. 1 Publication
VAR_033008
Natural varianti261 – 2611R → C in CBAS2. 1 Publication
VAR_044431

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei153 – 19341Missing in isoform 3.
VSP_042913Add
BLAST
Alternative sequencei286 – 32641IFDFS…FHDEY → VARSS in isoform 2.
VSP_042901Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141D → V in BAF82114. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z28339 mRNA. Translation: CAA82193.1.
AF283659
, AF283651, AF283652, AF283653, AF283654, AF283655, AF283656, AF283657, AF283658 Genomic DNA. Translation: AAG39381.1.
AK289425 mRNA. Translation: BAF82114.1.
AK298421 mRNA. Translation: BAG60645.1.
AK298428 mRNA. Translation: BAG60650.1.
AC009263 Genomic DNA. No translation available.
AC024082 Genomic DNA. No translation available.
AC083867 Genomic DNA. No translation available.
CH236950 Genomic DNA. Translation: EAL24049.1.
CH471070 Genomic DNA. Translation: EAW83881.1.
BC130625 mRNA. Translation: AAI30626.1.
BC130627 mRNA. Translation: AAI30628.1.
CCDSiCCDS55169.1. [P51857-2]
CCDS55170.1. [P51857-3]
CCDS5846.1. [P51857-1]
PIRiS41120.
RefSeqiNP_001177835.1. NM_001190906.1. [P51857-3]
NP_001177836.1. NM_001190907.1. [P51857-2]
NP_005980.1. NM_005989.3. [P51857-1]
UniGeneiHs.201667.
Hs.740214.

Genome annotation databases

EnsembliENST00000242375; ENSP00000242375; ENSG00000122787. [P51857-1]
ENST00000411726; ENSP00000402374; ENSG00000122787. [P51857-3]
ENST00000432161; ENSP00000389197; ENSG00000122787. [P51857-2]
GeneIDi6718.
KEGGihsa:6718.
UCSCiuc003vtz.3. human. [P51857-1]
uc011kqe.1. human. [P51857-2]
uc011kqf.2. human. [P51857-3]

Polymorphism databases

DMDMi1703007.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z28339 mRNA. Translation: CAA82193.1 .
AF283659
, AF283651 , AF283652 , AF283653 , AF283654 , AF283655 , AF283656 , AF283657 , AF283658 Genomic DNA. Translation: AAG39381.1 .
AK289425 mRNA. Translation: BAF82114.1 .
AK298421 mRNA. Translation: BAG60645.1 .
AK298428 mRNA. Translation: BAG60650.1 .
AC009263 Genomic DNA. No translation available.
AC024082 Genomic DNA. No translation available.
AC083867 Genomic DNA. No translation available.
CH236950 Genomic DNA. Translation: EAL24049.1 .
CH471070 Genomic DNA. Translation: EAW83881.1 .
BC130625 mRNA. Translation: AAI30626.1 .
BC130627 mRNA. Translation: AAI30628.1 .
CCDSi CCDS55169.1. [P51857-2 ]
CCDS55170.1. [P51857-3 ]
CCDS5846.1. [P51857-1 ]
PIRi S41120.
RefSeqi NP_001177835.1. NM_001190906.1. [P51857-3 ]
NP_001177836.1. NM_001190907.1. [P51857-2 ]
NP_005980.1. NM_005989.3. [P51857-1 ]
UniGenei Hs.201667.
Hs.740214.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3BUR X-ray 1.62 A/B 1-326 [» ]
3BUV X-ray 1.35 A/B 1-326 [» ]
3BV7 X-ray 1.79 A/B 1-326 [» ]
3CAQ X-ray 2.20 A/B 1-326 [» ]
3CAS X-ray 2.00 A/B 1-326 [» ]
3CAV X-ray 1.90 A/B 1-326 [» ]
3CMF X-ray 1.90 A/B 1-326 [» ]
3COT X-ray 2.03 A/B 1-326 [» ]
3DOP X-ray 2.00 A/B 1-326 [» ]
3G1R X-ray 1.70 A/B 1-326 [» ]
3UZW X-ray 1.89 A/B 1-326 [» ]
3UZX X-ray 1.64 A/B 1-326 [» ]
3UZY X-ray 1.83 A/B 1-326 [» ]
3UZZ X-ray 1.82 A/B 1-326 [» ]
ProteinModelPortali P51857.
SMRi P51857. Positions 2-326.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000242375.

PTM databases

PhosphoSitei P51857.

Polymorphism databases

DMDMi 1703007.

Proteomic databases

MaxQBi P51857.
PaxDbi P51857.
PRIDEi P51857.

Protocols and materials databases

DNASUi 6718.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000242375 ; ENSP00000242375 ; ENSG00000122787 . [P51857-1 ]
ENST00000411726 ; ENSP00000402374 ; ENSG00000122787 . [P51857-3 ]
ENST00000432161 ; ENSP00000389197 ; ENSG00000122787 . [P51857-2 ]
GeneIDi 6718.
KEGGi hsa:6718.
UCSCi uc003vtz.3. human. [P51857-1 ]
uc011kqe.1. human. [P51857-2 ]
uc011kqf.2. human. [P51857-3 ]

Organism-specific databases

CTDi 6718.
GeneCardsi GC07P137687.
HGNCi HGNC:388. AKR1D1.
HPAi HPA057002.
MIMi 235555. phenotype.
604741. gene.
neXtProti NX_P51857.
Orphaneti 79303. Congenital bile acid synthesis defect type 2.
PharmGKBi PA24681.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0656.
HOGENOMi HOG000250272.
HOVERGENi HBG000020.
InParanoidi P51857.
KOi K00251.
OMAi LYQNEHE.
OrthoDBi EOG70KGQF.
PhylomeDBi P51857.
TreeFami TF106492.

Enzyme and pathway databases

Reactomei REACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_11048. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
SABIO-RK P51857.

Miscellaneous databases

EvolutionaryTracei P51857.
GenomeRNAii 6718.
NextBioi 26206.
PROi P51857.
SOURCEi Search...

Gene expression databases

ArrayExpressi P51857.
Bgeei P51857.
CleanExi HS_AKR1D1.
Genevestigatori P51857.

Family and domain databases

Gene3Di 3.20.20.100. 1 hit.
InterProi IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view ]
PANTHERi PTHR11732. PTHR11732. 1 hit.
Pfami PF00248. Aldo_ket_red. 1 hit.
[Graphical view ]
PIRSFi PIRSF000097. AKR. 1 hit.
PRINTSi PR00069. ALDKETRDTASE.
SUPFAMi SSF51430. SSF51430. 1 hit.
PROSITEi PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of cDNA of human delta 4-3-oxosteroid 5 beta-reductase and substrate specificity of the expressed enzyme."
    Kondo K.-H., Kai M.-H., Setoguchi Y., Eggertsen G., Sjoeblom P., Setoguchi T., Okuda K., Bjoerkhem I.
    Eur. J. Biochem. 219:357-363(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "Genomic organization of a human 5beta-reductase and its pseudogene and substrate selectivity of the expressed enzyme."
    Charbonneau A., The V.L.
    Biochim. Biophys. Acta 1517:228-235(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, TISSUE SPECIFICITY.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Tissue: Liver and Mammary gland.
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "The crystal structure of human Delta4-3-ketosteroid 5beta-reductase defines the functional role of the residues of the catalytic tetrad in the steroid double bond reduction mechanism."
    Faucher F., Cantin L., Luu-The V., Labrie F., Breton R.
    Biochemistry 47:8261-8270(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH NADP.
  10. "Crystal structures of human Delta4-3-ketosteroid 5beta-reductase (AKR1D1) reveal the presence of an alternative binding site responsible for substrate inhibition."
    Faucher F., Cantin L., Luu-The V., Labrie F., Breton R.
    Biochemistry 47:13537-13546(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH NADP.
  11. "Crystal structure of human liver delta(4)-3-ketosteroid 5beta-reductase (AKR1D1) and implications for substrate binding and catalysis."
    Di Costanzo L., Drury J.E., Penning T.M., Christianson D.W.
    J. Biol. Chem. 283:16830-16839(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEXES WITH NADP; TESTOSTERONE; PROGESTERONE AND CORTISONE, MUTAGENESIS OF TYR-58 AND GLU-120, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  12. "Inhibition of human steroid 5beta-reductase (AKR1D1) by finasteride and structure of the enzyme-inhibitor complex."
    Drury J.E., Di Costanzo L., Penning T.M., Christianson D.W.
    J. Biol. Chem. 284:19786-19790(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH NADP.
  13. "Structure and catalytic mechanism of human steroid 5beta-reductase (AKR1D1)."
    Di Costanzo L., Drury J.E., Christianson D.W., Penning T.M.
    Mol. Cell. Endocrinol. 301:191-198(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH NADP.
  14. "Conversion of human steroid 5beta-reductase (AKR1D1) into 3beta-hydroxysteroid dehydrogenase by single point mutation E120H: example of perfect enzyme engineering."
    Chen M., Drury J.E., Christianson D.W., Penning T.M.
    J. Biol. Chem. 287:16609-16622(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) IN COMPLEX WITH NADP AND TESTOSTERONE.
  15. "Mutations in SRD5B1 (AKR1D1), the gene encoding delta(4)-3-oxosteroid 5beta-reductase, in hepatitis and liver failure in infancy."
    Lemonde H.A., Custard E.J., Bouquet J., Duran M., Overmars H., Scambler P.J., Clayton P.T.
    Gut 52:1494-1499(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CBAS2 PHE-106 AND LEU-198.
  16. "SRD5B1 (AKR1D1) gene analysis in delta(4)-3-oxosteroid 5beta-reductase deficiency: evidence for primary genetic defect."
    Gonzales E., Cresteil D., Baussan C., Dabadie A., Gerhardt M.F., Jacquemin E.
    J. Hepatol. 40:716-718(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CBAS2 ARG-133 AND CYS-261.

Entry informationi

Entry nameiAK1D1_HUMAN
AccessioniPrimary (citable) accession number: P51857
Secondary accession number(s): A1L4P6
, A8K060, B4DPN3, B4DPN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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