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P56937

- DHB7_HUMAN

UniProt

P56937 - DHB7_HUMAN

Protein

3-keto-steroid reductase

Gene

HSD17B7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (30 May 2000)
      Previous versions | rss
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    Functioni

    Responsible for the reduction of the keto group on the C-3 of sterols.1 Publication

    Catalytic activityi

    A 3-beta-hydroxysteroid + NADP+ = a 3-oxosteroid + NADPH.
    17-beta-estradiol + NAD(P)+ = estrone + NAD(P)H.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei171 – 1711SubstrateBy similarity
    Active sitei193 – 1931Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi8 – 158NADSequence Analysis

    GO - Molecular functioni

    1. 3-keto sterol reductase activity Source: UniProtKB-EC
    2. estradiol 17-beta-dehydrogenase activity Source: ProtInc

    GO - Biological processi

    1. cholesterol biosynthetic process Source: Reactome
    2. estrogen biosynthetic process Source: UniProtKB-UniPathway
    3. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis

    Keywords - Ligandi

    NAD, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05604-MONOMER.
    ReactomeiREACT_9405. Cholesterol biosynthesis.
    SABIO-RKP56937.
    UniPathwayiUPA00769.
    UPA00770; UER00758.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-keto-steroid reductase (EC:1.1.1.270)
    Alternative name(s):
    17-beta-hydroxysteroid dehydrogenase 7
    Short name:
    17-beta-HSD 7
    Estradiol 17-beta-dehydrogenase 7 (EC:1.1.1.62)
    Gene namesi
    Name:HSD17B7
    ORF Names:UNQ2563/PRO6243
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:5215. HSD17B7.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29483.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3413413-keto-steroid reductasePRO_0000054586Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi37 – 371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi229 – 2291N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Phosphorylated.

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiP56937.
    PaxDbiP56937.
    PRIDEiP56937.

    PTM databases

    PhosphoSiteiP56937.

    Expressioni

    Tissue specificityi

    Highly expressed in adrenal gland, liver, lung and thymus. Expressed in breast, ovaries, pituitary gland, pregnant uterus, prostate, kidney, lymph node, small intestine, spinal cord and trachea. Weakly expressed in all other tissues tested. Isoform 3 is expressed in eye ciliary epithelial cells and neuroendocrine cells.

    Gene expression databases

    BgeeiP56937.
    CleanExiHS_HSD17B7.
    GenevestigatoriP56937.

    Organism-specific databases

    HPAiHPA047496.

    Interactioni

    Protein-protein interaction databases

    BioGridi119563. 7 interactions.
    IntActiP56937. 5 interactions.
    STRINGi9606.ENSP00000254521.

    Structurei

    3D structure databases

    ProteinModelPortaliP56937.
    SMRiP56937. Positions 2-228.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 229229ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini251 – 34191CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei230 – 25021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1028.
    HOGENOMiHOG000253921.
    HOVERGENiHBG058236.
    InParanoidiP56937.
    KOiK13373.
    OMAiCHSDNPS.
    PhylomeDBiP56937.
    TreeFamiTF105433.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P56937-1) [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

    MRKVVLITGA SSGIGLALCK RLLAEDDELH LCLACRNMSK AEAVCAALLA    50
    SHPTAEVTIV QVDVSNLQSV FRASKELKQR FQRLDCIYLN AGIMPNPQLN 100
    IKALFFGLFS RKVIHMFSTA EGLLTQGDKI TADGLQEVFE TNVFGHFILI 150
    RELEPLLCHS DNPSQLIWTS SRSARKSNFS LEDFQHSKGK EPYSSSKYAT 200
    DLLSVALNRN FNQQGLYSNV ACPGTALTNL TYGILPPFIW TLLMPAILLL 250
    RFFANAFTLT PYNGTEALVW LFHQKPESLN PLIKYLSATT GFGRNYIMTQ 300
    KMDLDEDTAE KFYQKLLELE KHIRVTIQKT DNQARLSGSC L 341
    Length:341
    Mass (Da):38,206
    Last modified:May 30, 2000 - v1
    Checksum:iFE4892B2602F549B
    GO
    Isoform 2 (identifier: P56937-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         112-119: Missing.

    Show »
    Length:333
    Mass (Da):37,262
    Checksum:i187F2F8818D93869
    GO
    Isoform 3 (identifier: P56937-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         215-249: Missing.

    Show »
    Length:306
    Mass (Da):34,476
    Checksum:i61F696BEDA3B9EAE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti52 – 532HP → PT in AAF14537. (PubMed:10544267)Curated
    Sequence conflicti61 – 611Q → P in AAF14537. (PubMed:10544267)Curated
    Sequence conflicti86 – 861C → R in CAC88111. (PubMed:12732193)Curated
    Sequence conflicti105 – 1051F → L in CAC88111. (PubMed:12732193)Curated
    Sequence conflicti135 – 1351L → F in AAP97275. 1 PublicationCurated
    Sequence conflicti273 – 2764HQKP → PPKA in AAP97275. 1 PublicationCurated
    Sequence conflicti288 – 2958ATTGFGRN → GTTALEEI in AAP97275. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei112 – 1198Missing in isoform 2. 1 PublicationVSP_006029
    Alternative sequencei215 – 24935Missing in isoform 3. 1 PublicationVSP_012766Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF098786 mRNA. Translation: AAF09266.2.
    AF162767
    , AF162759, AF162760, AF162761, AF162762, AF162763, AF162764, AF162765, AF162766 Genomic DNA. Translation: AAF14537.1.
    AJ249179 mRNA. Translation: CAC20418.1.
    AJ250550
    , AJ250551, AJ250552, AJ250553, AJ250554, AJ250555, AJ250556, AJ250557, AJ250558 Genomic DNA. Translation: CAC88111.1.
    AF145023 mRNA. Translation: AAP97275.1.
    AY358962 mRNA. Translation: AAQ89321.1.
    AK290741 mRNA. Translation: BAF83430.1.
    BT007075 mRNA. Translation: AAP35738.1.
    AL392003, AL445197 Genomic DNA. Translation: CAI13457.1.
    AL445197, AL392003 Genomic DNA. Translation: CAI15947.1.
    CH471067 Genomic DNA. Translation: EAW90716.1.
    BC007068 mRNA. Translation: AAH07068.1.
    BC065246 mRNA. Translation: AAH65246.1.
    CCDSiCCDS1242.1. [P56937-1]
    RefSeqiNP_057455.1. NM_016371.2. [P56937-1]
    UniGeneiHs.492925.

    Genome annotation databases

    EnsembliENST00000254521; ENSP00000254521; ENSG00000132196. [P56937-1]
    GeneIDi51478.
    KEGGihsa:51478.
    UCSCiuc001gci.3. human. [P56937-1]

    Polymorphism databases

    DMDMi8134404.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF098786 mRNA. Translation: AAF09266.2 .
    AF162767
    , AF162759 , AF162760 , AF162761 , AF162762 , AF162763 , AF162764 , AF162765 , AF162766 Genomic DNA. Translation: AAF14537.1 .
    AJ249179 mRNA. Translation: CAC20418.1 .
    AJ250550
    , AJ250551 , AJ250552 , AJ250553 , AJ250554 , AJ250555 , AJ250556 , AJ250557 , AJ250558 Genomic DNA. Translation: CAC88111.1 .
    AF145023 mRNA. Translation: AAP97275.1 .
    AY358962 mRNA. Translation: AAQ89321.1 .
    AK290741 mRNA. Translation: BAF83430.1 .
    BT007075 mRNA. Translation: AAP35738.1 .
    AL392003 , AL445197 Genomic DNA. Translation: CAI13457.1 .
    AL445197 , AL392003 Genomic DNA. Translation: CAI15947.1 .
    CH471067 Genomic DNA. Translation: EAW90716.1 .
    BC007068 mRNA. Translation: AAH07068.1 .
    BC065246 mRNA. Translation: AAH65246.1 .
    CCDSi CCDS1242.1. [P56937-1 ]
    RefSeqi NP_057455.1. NM_016371.2. [P56937-1 ]
    UniGenei Hs.492925.

    3D structure databases

    ProteinModelPortali P56937.
    SMRi P56937. Positions 2-228.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119563. 7 interactions.
    IntActi P56937. 5 interactions.
    STRINGi 9606.ENSP00000254521.

    Chemistry

    BindingDBi P56937.
    ChEMBLi CHEMBL5999.
    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P56937.

    Polymorphism databases

    DMDMi 8134404.

    Proteomic databases

    MaxQBi P56937.
    PaxDbi P56937.
    PRIDEi P56937.

    Protocols and materials databases

    DNASUi 51478.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000254521 ; ENSP00000254521 ; ENSG00000132196 . [P56937-1 ]
    GeneIDi 51478.
    KEGGi hsa:51478.
    UCSCi uc001gci.3. human. [P56937-1 ]

    Organism-specific databases

    CTDi 51478.
    GeneCardsi GC01P162760.
    HGNCi HGNC:5215. HSD17B7.
    HPAi HPA047496.
    MIMi 606756. gene.
    neXtProti NX_P56937.
    PharmGKBi PA29483.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1028.
    HOGENOMi HOG000253921.
    HOVERGENi HBG058236.
    InParanoidi P56937.
    KOi K13373.
    OMAi CHSDNPS.
    PhylomeDBi P56937.
    TreeFami TF105433.

    Enzyme and pathway databases

    UniPathwayi UPA00769 .
    UPA00770 ; UER00758 .
    BioCyci MetaCyc:HS05604-MONOMER.
    Reactomei REACT_9405. Cholesterol biosynthesis.
    SABIO-RK P56937.

    Miscellaneous databases

    GeneWikii HSD17B7.
    GenomeRNAii 51478.
    NextBioi 55124.
    PROi P56937.
    SOURCEi Search...

    Gene expression databases

    Bgeei P56937.
    CleanExi HS_HSD17B7.
    Genevestigatori P56937.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00106. adh_short. 1 hit.
    [Graphical view ]
    PRINTSi PR00081. GDHRDH.
    ProtoNeti Search...

    Publicationsi

    1. "Determination of cDNA, gene structure and chromosomal localization of the novel human 17beta-hydroxysteroid dehydrogenase type 7."
      Krazeisen A., Breitling R., Imai K., Fritz S., Moeller G., Adamski J.
      FEBS Lett. 460:373-379(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
    2. Krazeisen A., Breitling R., Imai K., Fritz S., Moeller G., Adamski J.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Production, purification, and functional analysis of recombinant human and mouse 17beta-hydroxysteroid dehydrogenase type 7."
      Toern S., Nokelainen P., Kurkela R., Pulkka A., Menjivar M., Ghosh S., Coca-Prados M., Peltoketo H., Isomaa V., Vihko P.
      Biochem. Biophys. Res. Commun. 305:37-45(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 3).
      Tissue: Placenta.
    4. "Cloning of a new human cDNA homologous to Rattus norvegicus ovarian-specific protein."
      Zhou Y., Yu L., Zhao S.Y.
      Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "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].
    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] (ISOFORM 1).
    8. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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).
      Tissue: Skin and Urinary bladder.
    11. "Closing the gap: identification of human 3-ketosteroid reductase, the last unknown enzyme of mammalian cholesterol biosynthesis."
      Marijanovic Z., Laubner D., Moeller G., Gege C., Husen B., Adamski J., Breitling R.
      Mol. Endocrinol. 17:1715-1725(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, FUNCTION.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDHB7_HUMAN
    AccessioniPrimary (citable) accession number: P56937
    Secondary accession number(s): Q5T246
    , Q7Z4V9, Q8WWS2, Q9UF00
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 146 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3