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Q04828 (AK1C1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldo-keto reductase family 1 member C1

EC=1.1.1.-
Alternative name(s):
20-alpha-hydroxysteroid dehydrogenase
Short name=20-alpha-HSD
EC=1.1.1.149
Chlordecone reductase homolog HAKRC
Dihydrodiol dehydrogenase 1/2
Short name=DD1/DD2
High-affinity hepatic bile acid-binding protein
Short name=HBAB
Indanol dehydrogenase
EC=1.1.1.112
Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
EC=1.3.1.20
Gene names
Name:AKR1C1
Synonyms:DDH, DDH1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts progesterone to its inactive form, 20-alpha-dihydroxyprogesterone (20-alpha-OHP). In the liver and intestine, may have a role in the transport of bile. May have a role in monitoring the intrahepatic bile acid concentration. Has a low bile-binding ability. May play a role in myelin formation. Ref.6 Ref.11

Catalytic activity

17-alpha,20-alpha-dihydroxypregn-4-en-3-one + NAD(P)+ = 17-alpha-hydroxyprogesterone + NAD(P)H. Ref.6 Ref.11

Trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH. Ref.6 Ref.11

Indan-1-ol + NAD(P)+ = indanone + NAD(P)H. Ref.6 Ref.11

Enzyme regulation

Inhibited by hexestrol with an IC50 of 9.5 µM, 1,10-phenanthroline with an IC50 of 55 µM, 1,7-phenanthroline with an IC50 of 72 µM, flufenamic acid with an IC50 of 6.0 µM, indomethacin with an IC50 of 140 µM, ibuprofen with an IC50 of 950 µM, lithocholic acid with an IC50 of 25 µM, ursodeoxycholic acid with an IC50 of 340 µM and chenodeoxycholic acid with an IC50 of 570 µM. Ref.11

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in all tissues tested including liver, prostate, testis, adrenal gland, brain, uterus, mammary gland and keratinocytes. Highest levels found in liver, mammary gland and brain. Ref.6

Sequence similarities

Belongs to the aldo/keto reductase family.

Biophysicochemical properties

Kinetic parameters:

KM=5 µM for (s)-tetralol Ref.6 Ref.11

KM=38 µM for (s)-indan-1-ol

KM=580 µM for benzene dihydrodiol

KM=3 µM for 5-beta-pregnane-3-alpha,20-alpha-diol

KM=3 µM for 5-beta-pregnan-20-alpha-ol-3-one

KM=12 µM for 4-pregnen-20-alpha-ol-3-one

KM=133 µM for 9-alpha,11-beta-PGF2

KM=2 µM for 5-beta-pregnan-3-alpha-ol-20-one

KM=1 µM for 5-beta-androstane-3,17-dione

KM=12 µM for PGD2

KM=0.6 µM for 20-alpha-hydroxyprogesterone (with NADH)

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbile acid and bile salt transport

Traceable author statement Ref.1. Source: UniProtKB

bile acid metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

cellular response to jasmonic acid stimulus

Inferred from direct assay PubMed 19487289. Source: UniProtKB

cholesterol homeostasis

Traceable author statement Ref.1. Source: UniProtKB

daunorubicin metabolic process

Inferred from mutant phenotype PubMed 20837989. Source: UniProtKB

digestion

Inferred from direct assay Ref.1. Source: UniProtKB

doxorubicin metabolic process

Inferred from mutant phenotype PubMed 20837989. Source: UniProtKB

epithelial cell differentiation

Inferred from direct assay PubMed 21492153. Source: UniProt

intestinal cholesterol absorption

Traceable author statement Ref.1. Source: UniProtKB

oxidation-reduction process

Inferred from direct assay PubMed 19442656PubMed 21232532Ref.1. Source: UniProtKB

phototransduction, visible light

Traceable author statement. Source: Reactome

progesterone metabolic process

Inferred from direct assay PubMed 21232532. Source: UniProtKB

protein homooligomerization

Inferred from direct assay Ref.1. Source: UniProtKB

response to organophosphorus

Inferred from expression pattern PubMed 16079077. Source: UniProtKB

retinal metabolic process

Inferred from direct assay PubMed 21851338. Source: UniProtKB

retinoid metabolic process

Traceable author statement. Source: Reactome

xenobiotic metabolic process

Non-traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentcytosol

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_function17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

alditol:NADP+ 1-oxidoreductase activity

Inferred from direct assay PubMed 21232532. Source: UniProtKB

aldo-keto reductase (NADP) activity

Traceable author statement PubMed 7789999. Source: UniProtKB

androsterone dehydrogenase (B-specific) activity

Inferred from direct assay Ref.1. Source: UniProtKB

bile acid binding

Inferred from direct assay Ref.1. Source: UniProtKB

carboxylic acid binding

Inferred from direct assay Ref.1. Source: UniProtKB

indanol dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

ketosteroid monooxygenase activity

Inferred from direct assay PubMed 21232532. Source: UniProtKB

oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor

Inferred from direct assay PubMed 19442656PubMed 20837989. Source: UniProtKB

phenanthrene 9,10-monooxygenase activity

Inferred from direct assay PubMed 21851338. Source: UniProtKB

trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 323323Aldo-keto reductase family 1 member C1
PRO_0000124633

Regions

Nucleotide binding20 – 245NADP
Nucleotide binding166 – 1672NADP
Nucleotide binding216 – 2227NADP
Nucleotide binding270 – 28011NADP

Sites

Active site551Proton donor By similarity
Binding site241Substrate
Binding site501NADP
Binding site1171Substrate By similarity
Binding site1901NADP
Binding site2221Substrate
Binding site2271Substrate
Site541Important for substrate specificity By similarity
Site841Lowers pKa of active site Tyr By similarity
Site2221May be involved in the mediating step between the transformation of progesterone and the release of the cofactor

Natural variations

Natural variant1701R → H.
Corresponds to variant rs17295755 [ dbSNP | Ensembl ].
VAR_048214
Natural variant1721Q → L.
Corresponds to variant rs17354444 [ dbSNP | Ensembl ].
VAR_048215

Experimental info

Mutagenesis1271E → D: 30-fold decrease in k(cat)/K(m) value for progesterone reduction; no effect on the K(m) value. Ref.13
Mutagenesis2221H → I: Marked decrease in k(cat)/K(m) value for progesterone; 24-fold decrease for progesterone reduction; 18-fold decrease for 20alpha-OHProg oxidation. 95-fold decrease in K(m) value for NADPH. Ref.13
Mutagenesis2221H → S: Marked decrease in k(cat)/K(m) value for progesterone; 10-fold decrease for progesterone reduction; 3-fold decrease for 20alpha-OHProg oxidation. 10-fold decrease in K(m) value for NADPH. Ref.13
Mutagenesis3041R → L: 70-fold decrease in progesterone reduction. No effect on DHT reduction. Ref.13
Mutagenesis3051Y → F: No effect on progesterone reduction. Ref.13
Mutagenesis3071T → V: No effect on progesterone reduction. Ref.13
Mutagenesis3091D → V: No effect on progesterone reduction. Ref.13
Sequence conflict31S → A no nucleotide entry Ref.4
Sequence conflict951V → D no nucleotide entry Ref.4
Sequence conflict951V → D in AAD14012. Ref.10
Sequence conflict1581G → E no nucleotide entry Ref.4
Sequence conflict1581G → E in AAD14012. Ref.10
Sequence conflict171 – 1722RQ → ST no nucleotide entry Ref.4
Sequence conflict171 – 1722RQ → ST in AAD14012. Ref.10
Sequence conflict183 – 1842KY → QV no nucleotide entry Ref.4
Sequence conflict183 – 1842KY → QV in AAD14012. Ref.10
Sequence conflict2221H → L no nucleotide entry Ref.4
Sequence conflict2221H → L in AAD14012. Ref.10
Sequence conflict3191F → I no nucleotide entry Ref.4
Sequence conflict3191F → I in AAD14012. Ref.10

Secondary structure

........................................................ 323
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q04828 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 9CB215478FBD29D5

FASTA32336,788
        10         20         30         40         50         60 
MDSKYQCVKL NDGHFMPVLG FGTYAPAEVP KSKALEATKL AIEAGFRHID SAHLYNNEEQ 

        70         80         90        100        110        120 
VGLAIRSKIA DGSVKREDIF YTSKLWCNSH RPELVRPALE RSLKNLQLDY VDLYLIHFPV 

       130        140        150        160        170        180 
SVKPGEEVIP KDENGKILFD TVDLCATWEA VEKCKDAGLA KSIGVSNFNR RQLEMILNKP 

       190        200        210        220        230        240 
GLKYKPVCNQ VECHPYFNQR KLLDFCKSKD IVLVAYSALG SHREEPWVDP NSPVLLEDPV 

       250        260        270        280        290        300 
LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTS EEMKAIDGLN 

       310        320 
RNVRYLTLDI FAGPPNYPFS DEY 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family."
Stolz A., Hammond L., Lou H., Takikawa H., Ronk M., Shively J.E.
J. Biol. Chem. 268:10448-10457(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high affinity bile acid binding."
Lou H., Hammond L., Sharma V., Sparkes R.S., Lusis A.J., Stolz A.
J. Biol. Chem. 269:8416-8422(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.
[3]"Regulation of human dihydrodiol dehydrogenase by Michael acceptor xenobiotics."
Ciaccio P.J., Jaiswal A.K., Tew K.D.
J. Biol. Chem. 269:15558-15562(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Colon.
[4]"Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans."
Khanna M., Qin K.-N., Cheng K.-C.
J. Steroid Biochem. Mol. Biol. 53:41-46(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[5]"Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes."
Nishizawa M., Nakajima T., Yasuda K., Kanzaki H., Sasaguri Y., Watanabe K., Ito S.
Genes Cells 5:111-125(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[6]"Characterization of a human 20alpha-hydroxysteroid dehydrogenase."
Zhang Y., Dufort I., Rheault P., Luu-The V.
J. Mol. Endocrinol. 25:221-228(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
Tissue: Skin fibroblast.
[7]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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].
Tissue: Lung and Testis.
[10]"Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase."
Qin K.-N., New M.I., Cheng K.-C.
J. Steroid Biochem. Mol. Biol. 46:673-679(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-323.
Tissue: Liver.
[11]"Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells."
Hara A., Matsuura K., Tamada Y., Sato K., Miyabe Y., Deyashiki Y., Ishida N.
Biochem. J. 313:373-376(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 10-31; 40-61; 69-126; 137-153; 162-206; 209-230; 250-267; 271-289 AND 295-323, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[12]"Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder."
Deyashiki Y., Ogasawara A., Nakayama T., Nakanishi M., Miyabe Y., Sato K., Hara A.
Biochem. J. 299:545-552(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-323, PROTEIN SEQUENCE OF 18-31; 105-131; 176-193 AND 271-294.
Tissue: Liver.
[13]"Human 20alpha-hydroxysteroid dehydrogenase: crystallographic and site-directed mutagenesis studies lead to the identification of an alternative binding site for C21-steroids."
Couture J.-F., Legrand P., Cantin L., Luu-The V., Labrie F., Breton R.
J. Mol. Biol. 331:593-604(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NADP AND 20ALPHA-HYDROXY-PROGESTERONE, MUTAGENESIS OF GLU-127; HIS-222; ARG-304; TYR-305; THR-307 AND ASP-309.
[14]"Probing the inhibitor selectivity pocket of human 20alpha-hydroxysteroid dehydrogenase (AKR1C1) with X-ray crystallography and site-directed mutagenesis."
El-Kabbani O., Dhagat U., Soda M., Endo S., Matsunaga T., Hara A.
Bioorg. Med. Chem. Lett. 21:2564-2567(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) IN COMPLEX WITH NADP AND 3-CHLORO-5-PHENYLSALICYLIC ACID.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86609 mRNA. Translation: AAB02880.1.
U05861 expand/collapse EMBL AC list , U05853, U05854, U05855, U05857, U05858, U05859, U05860 Genomic DNA. Translation: AAA18115.1.
U05684 mRNA. Translation: AAA16227.1.
AB031083 mRNA. Translation: BAA92883.1.
AB032150 Genomic DNA. Translation: BAA92886.1.
BT007197 mRNA. Translation: AAP35861.1.
AL713867, AC091817 Genomic DNA. Translation: CAI16409.1.
BC015490 mRNA. Translation: AAH15490.1.
BC020216 mRNA. Translation: AAH20216.1.
BC040210 mRNA. Translation: AAH40210.1.
S68290 mRNA. Translation: AAD14012.1.
D26124 mRNA. Translation: BAA05121.1.
CCDSCCDS7061.1.
PIRA53436.
I73675.
S59619.
S61515.
RefSeqNP_001344.2. NM_001353.5.
UniGeneHs.460260.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MRQX-ray1.59A2-323[»]
3C3UX-ray1.80A1-323[»]
3GUGX-ray1.90A1-323[»]
3NTYX-ray1.87A1-323[»]
ProteinModelPortalQ04828.
SMRQ04828. Positions 2-323.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108012. 3 interactions.
IntActQ04828. 3 interactions.
MINTMINT-5001209.
STRING9606.ENSP00000370254.

Chemistry

BindingDBQ04828.
ChEMBLCHEMBL5905.
DrugBankDB00157. NADH.

PTM databases

PhosphoSiteQ04828.

Polymorphism databases

DMDM416877.

Proteomic databases

MaxQBQ04828.
PaxDbQ04828.
PRIDEQ04828.

Protocols and materials databases

DNASU1645.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380872; ENSP00000370254; ENSG00000187134.
ENST00000434459; ENSP00000412248; ENSG00000187134.
ENST00000578362; ENSP00000462940; ENSG00000266592.
ENST00000582412; ENSP00000462966; ENSG00000266592.
GeneID1645.
KEGGhsa:1645.
UCSCuc001iho.3. human.

Organism-specific databases

CTD1645.
GeneCardsGC10P004995.
HGNCHGNC:384. AKR1C1.
HPACAB010874.
CAB047303.
MIM600449. gene.
neXtProtNX_Q04828.
PharmGKBPA24677.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0656.
HOGENOMHOG000250272.
HOVERGENHBG000020.
InParanoidQ04828.
KOK00089.
K00212.
OMAEMREDED.
PhylomeDBQ04828.
TreeFamTF106492.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKQ04828.

Gene expression databases

ArrayExpressQ04828.
BgeeQ04828.
CleanExHS_AKR1C1.
GenevestigatorQ04828.

Family and domain databases

Gene3D3.20.20.100. 1 hit.
InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERPTHR11732. PTHR11732. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFPIRSF000097. AKR. 1 hit.
PRINTSPR00069. ALDKETRDTASE.
SUPFAMSSF51430. SSF51430. 1 hit.
PROSITEPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ04828.
GeneWikiAKR1C1.
GenomeRNAi1645.
NextBio6768.
PROQ04828.
SOURCESearch...

Entry information

Entry nameAK1C1_HUMAN
AccessionPrimary (citable) accession number: Q04828
Secondary accession number(s): P52896 expand/collapse secondary AC list , Q5SR15, Q7M4N2, Q9UCX2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 9, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM