Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P51857 (AK1D1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:AKR1D1
Synonyms:SRD5B1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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 regulation

Subject to inhibition by high substrate concentrations. Inhibited by testosterone concentrations above 10 µM. Ref.11

Subcellular location

Cytoplasm.

Tissue specificity

Highly expressed in liver. Expressed in testis and weakly in colon. Ref.2

Involvement in disease

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. Ref.15 Ref.16

Sequence similarities

Belongs to the aldo/keto reductase family.

Biophysicochemical properties

Kinetic parameters:

KM=2.7 µM for testosterone Ref.11

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P51857-1)

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.
Isoform 2 (identifier: P51857-2)

The sequence of this isoform differs from the canonical sequence as follows:
     286-326: IFDFSLTEEEMKDIEALNKNVRFVELLMWRDHPEYPFHDEY → VARSS
Note: No experimental confirmation available.
Isoform 3 (identifier: P51857-3)

The sequence of this isoform differs from the canonical sequence as follows:
     153-193: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3263263-oxo-5-beta-steroid 4-dehydrogenase
PRO_0000124669

Regions

Nucleotide binding22 – 265NADP
Nucleotide binding169 – 1702NADP
Nucleotide binding219 – 2246NADP
Nucleotide binding273 – 28311NADP

Sites

Active site581Proton donor
Binding site261Substrate
Binding site531NADP
Binding site581Substrate
Binding site891Substrate
Binding site1201Substrate
Binding site1321Substrate
Binding site1931NADP
Binding site2301Substrate

Natural variations

Alternative sequence153 – 19341Missing in isoform 3.
VSP_042913
Alternative sequence286 – 32641IFDFS…FHDEY → VARSS in isoform 2.
VSP_042901
Natural variant1061L → F in CBAS2. Ref.15
VAR_033007
Natural variant1331P → R in CBAS2. Ref.16
VAR_044430
Natural variant1981P → L in CBAS2. Ref.15
VAR_033008
Natural variant2611R → C in CBAS2. Ref.16
VAR_044431

Experimental info

Mutagenesis581Y → A: Loss of activity. Ref.11
Mutagenesis1201E → A: Loss of activity. Ref.11
Sequence conflict141D → V in BAF82114. Ref.3

Secondary structure

...................................................... 326
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 1FE02B95398A0A6F

FASTA32637,377
        10         20         30         40         50         60 
MDLSAASHRI PLSDGNSIPI IGLGTYSEPK STPKGACATS VKVAIDTGYR HIDGAYIYQN 

        70         80         90        100        110        120 
EHEVGEAIRE KIAEGKVRRE DIFYCGKLWA TNHVPEMVRP TLERTLRVLQ LDYVDLYIIE 

       130        140        150        160        170        180 
VPMAFKPGDE IYPRDENGKW LYHKSNLCAT WEAMEACKDA GLVKSLGVSN FNRRQLELIL 

       190        200        210        220        230        240 
NKPGLKHKPV SNQVECHPYF TQPKLLKFCQ QHDIVITAYS PLGTSRNPIW VNVSSPPLLK 

       250        260        270        280        290        300 
DALLNSLGKR YNKTAAQIVL RFNIQRGVVV IPKSFNLERI KENFQIFDFS LTEEEMKDIE 

       310        320 
ALNKNVRFVE LLMWRDHPEY PFHDEY 

« Hide

Isoform 2 [UniParc].

Checksum: F2C7686DA906C0EC
Show »

FASTA29032,748
Isoform 3 [UniParc].

Checksum: 5017C36EB0EB13D9
Show »

FASTA28532,890

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z28339 mRNA. Translation: CAA82193.1.
AF283659 expand/collapse EMBL AC list , 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.
CCDSCCDS55169.1. [P51857-2]
CCDS55170.1. [P51857-3]
CCDS5846.1. [P51857-1]
PIRS41120.
RefSeqNP_001177835.1. NM_001190906.1. [P51857-3]
NP_001177836.1. NM_001190907.1. [P51857-2]
NP_005980.1. NM_005989.3. [P51857-1]
UniGeneHs.201667.
Hs.740214.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP51857.
SMRP51857. Positions 2-326.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000242375.

PTM databases

PhosphoSiteP51857.

Polymorphism databases

DMDM1703007.

Proteomic databases

MaxQBP51857.
PaxDbP51857.
PRIDEP51857.

Protocols and materials databases

DNASU6718.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000242375; ENSP00000242375; ENSG00000122787. [P51857-1]
ENST00000411726; ENSP00000402374; ENSG00000122787. [P51857-3]
ENST00000432161; ENSP00000389197; ENSG00000122787. [P51857-2]
GeneID6718.
KEGGhsa:6718.
UCSCuc003vtz.3. human. [P51857-1]
uc011kqe.1. human. [P51857-2]
uc011kqf.2. human. [P51857-3]

Organism-specific databases

CTD6718.
GeneCardsGC07P137687.
HGNCHGNC:388. AKR1D1.
HPAHPA057002.
MIM235555. phenotype.
604741. gene.
neXtProtNX_P51857.
Orphanet79303. Congenital bile acid synthesis defect type 2.
PharmGKBPA24681.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0656.
HOGENOMHOG000250272.
HOVERGENHBG000020.
InParanoidP51857.
KOK00251.
OMALYQNEHE.
OrthoDBEOG70KGQF.
PhylomeDBP51857.
TreeFamTF106492.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKP51857.

Gene expression databases

ArrayExpressP51857.
BgeeP51857.
CleanExHS_AKR1D1.
GenevestigatorP51857.

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

EvolutionaryTraceP51857.
GenomeRNAi6718.
NextBio26206.
PROP51857.
SOURCESearch...

Entry information

Entry nameAK1D1_HUMAN
AccessionPrimary (citable) accession number: P51857
Secondary accession number(s): A1L4P6 expand/collapse secondary AC list , A8K060, B4DPN3, B4DPN8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 125 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 7

Human chromosome 7: entries, gene names and cross-references to MIM