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P01588

- EPO_HUMAN

UniProt

P01588 - EPO_HUMAN

Protein

Erythropoietin

Gene

EPO

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Erythropoietin is the principal hormone involved in the regulation of erythrocyte differentiation and the maintenance of a physiological level of circulating erythrocyte mass.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein kinase activator activity Source: Ensembl

    GO - Biological processi

    1. aging Source: Ensembl
    2. apoptotic process Source: Ensembl
    3. blood circulation Source: ProtInc
    4. cellular hyperosmotic response Source: BHF-UCL
    5. cellular response to hypoxia Source: Reactome
    6. embryo implantation Source: Ensembl
    7. erythrocyte maturation Source: UniProtKB-KW
    8. hemoglobin biosynthetic process Source: Ensembl
    9. negative regulation of calcium ion transport into cytosol Source: BHF-UCL
    10. negative regulation of cation channel activity Source: BHF-UCL
    11. negative regulation of erythrocyte apoptotic process Source: BHF-UCL
    12. negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress Source: BHF-UCL
    13. peptidyl-serine phosphorylation Source: Ensembl
    14. positive regulation of cell proliferation Source: BHF-UCL
    15. positive regulation of DNA replication Source: BHF-UCL
    16. positive regulation of neuron differentiation Source: Ensembl
    17. positive regulation of Ras protein signal transduction Source: BHF-UCL
    18. positive regulation of transcription, DNA-templated Source: BHF-UCL
    19. positive regulation of tyrosine phosphorylation of Stat5 protein Source: BHF-UCL
    20. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
    21. response to axon injury Source: Ensembl
    22. response to electrical stimulus Source: Ensembl
    23. response to estrogen Source: Ensembl
    24. response to hyperoxia Source: Ensembl
    25. response to interleukin-1 Source: Ensembl
    26. response to lipopolysaccharide Source: Ensembl
    27. response to salt stress Source: Ensembl
    28. response to testosterone Source: Ensembl
    29. response to vitamin A Source: Ensembl
    30. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Hormone

    Keywords - Biological processi

    Erythrocyte maturation

    Enzyme and pathway databases

    ReactomeiREACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
    SignaLinkiP01588.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Erythropoietin
    Alternative name(s):
    INN: Epoetin
    Gene namesi
    Name:EPO
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:3415. EPO.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: BHF-UCL
    2. extracellular region Source: Reactome
    3. extracellular space Source: BHF-UCL

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Microvascular complications of diabetes 2 (MVCD2) [MIM:612623]: Pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis.
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Pharmaceutical usei

    Used for the treatment of anemia. Available under the names Epogen (Amgen), Epogin (Chugai), Epomax (Elanex), Eprex (Janssen-Cilag), NeoRecormon or Recormon (Roche), Dynepo (Shire Pharmaceuticals) and Procrit (Ortho Biotech). Variations in the glycosylation pattern of EPO distinguishes these products. Epogen, Epogin, Eprex and Procrit are generically known as epoetin alfa, NeoRecormon and Recormon as epoetin beta, Dynepo as epoetin delta and Epomax as epoetin omega. Epoetin zeta is the name used for some 'biosimilars' forms of epoetin alfa and is available under the names Silapo (Stada) and Retacrit (Hospira). Darbepoetin alfa is a form created by 5 substitutions (Asn-57, Thr-59, Val-114, Asn-115 and Thr-117) that create 2 new N-glycosylation sites. It has a longer circulating half-life in vivo. It is available under the name Aranesp (Amgen). EPO is being much misused as a performance-enhancing drug in endurance athletes.

    Organism-specific databases

    MIMi612623. phenotype.
    PharmGKBiPA27833.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 27271 PublicationAdd
    BLAST
    Chaini28 – 193166ErythropoietinPRO_0000008401Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi34 ↔ 1881 Publication
    Glycosylationi51 – 511N-linked (GlcNAc...)1 PublicationCAR_000052
    Disulfide bondi56 ↔ 601 Publication
    Glycosylationi65 – 651N-linked (GlcNAc...)1 PublicationCAR_000166
    Glycosylationi110 – 1101N-linked (GlcNAc...)1 PublicationCAR_000192
    Glycosylationi153 – 1531O-linked (GalNAc...)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiP01588.

    PTM databases

    PhosphoSiteiP01588.
    UniCarbKBiP01588.

    Expressioni

    Tissue specificityi

    Produced by kidney or liver of adult mammals and by liver of fetal or neonatal mammals.

    Gene expression databases

    ArrayExpressiP01588.
    BgeeiP01588.
    CleanExiHS_EPO.
    GenevestigatoriP01588.

    Organism-specific databases

    HPAiCAB010336.
    HPA027572.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EPORP192352EBI-1027362,EBI-617321

    Protein-protein interaction databases

    BioGridi108370. 2 interactions.
    DIPiDIP-5731N.
    IntActiP01588. 2 interactions.
    STRINGi9606.ENSP00000252723.

    Structurei

    Secondary structure

    1
    193
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi32 – 343
    Helixi36 – 5217
    Helixi53 – 553
    Beta strandi57 – 604
    Beta strandi61 – 688
    Helixi75 – 784
    Beta strandi79 – 813
    Helixi83 – 10927
    Helixi118 – 13821
    Helixi141 – 1477
    Beta strandi160 – 1645
    Helixi165 – 17713
    Helixi179 – 18810

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BUYNMR-A28-193[»]
    1CN4X-ray2.80C28-193[»]
    1EERX-ray1.90A28-193[»]
    ProteinModelPortaliP01588.
    SMRiP01588. Positions 28-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01588.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the EPO/TPO family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG43828.
    HOGENOMiHOG000052505.
    HOVERGENiHBG003978.
    InParanoidiP01588.
    KOiK05437.
    OMAiNVTMGCA.
    OrthoDBiEOG7DVDCR.
    PhylomeDBiP01588.
    TreeFamiTF333413.

    Family and domain databases

    Gene3Di1.20.1250.10. 1 hit.
    InterProiIPR009079. 4_helix_cytokine-like_core.
    IPR012351. 4_helix_cytokine_core.
    IPR019767. EPO/TPO_CS.
    IPR001323. EPO_TPO.
    IPR003013. Erythroptn.
    [Graphical view]
    PANTHERiPTHR10370. PTHR10370. 1 hit.
    PfamiPF00758. EPO_TPO. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001951. EPO. 1 hit.
    PRINTSiPR00272. ERYTHROPTN.
    SUPFAMiSSF47266. SSF47266. 1 hit.
    PROSITEiPS00817. EPO_TPO. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P01588-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGVHECPAWL WLLLSLLSLP LGLPVLGAPP RLICDSRVLE RYLLEAKEAE    50
    NITTGCAEHC SLNENITVPD TKVNFYAWKR MEVGQQAVEV WQGLALLSEA 100
    VLRGQALLVN SSQPWEPLQL HVDKAVSGLR SLTTLLRALG AQKEAISPPD 150
    AASAAPLRTI TADTFRKLFR VYSNFLRGKL KLYTGEACRT GDR 193
    Length:193
    Mass (Da):21,307
    Last modified:July 21, 1986 - v1
    Checksum:iC91F0E4C26A52033
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 401E → Q in CAA26095. (PubMed:3838366)Curated
    Sequence conflicti85 – 851Q → QQ AA sequence (PubMed:3949763)Curated
    Sequence conflicti140 – 1401G → R in CAA26095. (PubMed:3838366)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti131 – 1322SL → NF in a hepatocellular carcinoma.
    VAR_009870
    Natural varianti149 – 1491P → Q in a hepatocellular carcinoma. 1 Publication
    VAR_009871

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02158 Genomic DNA. Translation: CAA26095.1.
    X02157 mRNA. Translation: CAA26094.1.
    M11319 Genomic DNA. Translation: AAA52400.1.
    AF053356 Genomic DNA. Translation: AAC78791.1.
    AF202308, AF202306, AF202307 Genomic DNA. Translation: AAF23132.1.
    AH009004 Genomic DNA. Translation: AAF23133.1.
    AF202311 Genomic DNA. Translation: AAF17572.1.
    AF202314, AF202312, AF202313 Genomic DNA. Translation: AAF23134.1.
    AC009488 Genomic DNA. Translation: AAP22357.1.
    BC093628 mRNA. Translation: AAH93628.1.
    BC111937 mRNA. Translation: AAI11938.1.
    S65458 mRNA. Translation: AAD13964.1.
    CCDSiCCDS5705.1.
    PIRiA01855. ZUHU.
    RefSeqiNP_000790.2. NM_000799.2.
    UniGeneiHs.2303.

    Genome annotation databases

    EnsembliENST00000252723; ENSP00000252723; ENSG00000130427.
    GeneIDi2056.
    KEGGihsa:2056.
    UCSCiuc003uwi.3. human.

    Polymorphism databases

    DMDMi119526.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    R&D Systems' cytokine source book: Erythropoietin
    Wikipedia

    Erythropoietin entry

    Protein Spotlight

    Journey into a tiny world - Issue 84 of July 2007

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02158 Genomic DNA. Translation: CAA26095.1 .
    X02157 mRNA. Translation: CAA26094.1 .
    M11319 Genomic DNA. Translation: AAA52400.1 .
    AF053356 Genomic DNA. Translation: AAC78791.1 .
    AF202308 , AF202306 , AF202307 Genomic DNA. Translation: AAF23132.1 .
    AH009004 Genomic DNA. Translation: AAF23133.1 .
    AF202311 Genomic DNA. Translation: AAF17572.1 .
    AF202314 , AF202312 , AF202313 Genomic DNA. Translation: AAF23134.1 .
    AC009488 Genomic DNA. Translation: AAP22357.1 .
    BC093628 mRNA. Translation: AAH93628.1 .
    BC111937 mRNA. Translation: AAI11938.1 .
    S65458 mRNA. Translation: AAD13964.1 .
    CCDSi CCDS5705.1.
    PIRi A01855. ZUHU.
    RefSeqi NP_000790.2. NM_000799.2.
    UniGenei Hs.2303.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BUY NMR - A 28-193 [» ]
    1CN4 X-ray 2.80 C 28-193 [» ]
    1EER X-ray 1.90 A 28-193 [» ]
    ProteinModelPortali P01588.
    SMRi P01588. Positions 28-193.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108370. 2 interactions.
    DIPi DIP-5731N.
    IntActi P01588. 2 interactions.
    STRINGi 9606.ENSP00000252723.

    Chemistry

    ChEMBLi CHEMBL5837.
    DrugBanki DB00012. Darbepoetin alfa.
    DB00016. Epoetin alfa.

    PTM databases

    PhosphoSitei P01588.
    UniCarbKBi P01588.

    Polymorphism databases

    DMDMi 119526.

    Proteomic databases

    PRIDEi P01588.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000252723 ; ENSP00000252723 ; ENSG00000130427 .
    GeneIDi 2056.
    KEGGi hsa:2056.
    UCSCi uc003uwi.3. human.

    Organism-specific databases

    CTDi 2056.
    GeneCardsi GC07P100318.
    HGNCi HGNC:3415. EPO.
    HPAi CAB010336.
    HPA027572.
    MIMi 133170. gene.
    612623. phenotype.
    neXtProti NX_P01588.
    PharmGKBi PA27833.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG43828.
    HOGENOMi HOG000052505.
    HOVERGENi HBG003978.
    InParanoidi P01588.
    KOi K05437.
    OMAi NVTMGCA.
    OrthoDBi EOG7DVDCR.
    PhylomeDBi P01588.
    TreeFami TF333413.

    Enzyme and pathway databases

    Reactomei REACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
    SignaLinki P01588.

    Miscellaneous databases

    EvolutionaryTracei P01588.
    GeneWikii Erythropoietin.
    GenomeRNAii 2056.
    NextBioi 8361.
    PROi P01588.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P01588.
    Bgeei P01588.
    CleanExi HS_EPO.
    Genevestigatori P01588.

    Family and domain databases

    Gene3Di 1.20.1250.10. 1 hit.
    InterProi IPR009079. 4_helix_cytokine-like_core.
    IPR012351. 4_helix_cytokine_core.
    IPR019767. EPO/TPO_CS.
    IPR001323. EPO_TPO.
    IPR003013. Erythroptn.
    [Graphical view ]
    PANTHERi PTHR10370. PTHR10370. 1 hit.
    Pfami PF00758. EPO_TPO. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001951. EPO. 1 hit.
    PRINTSi PR00272. ERYTHROPTN.
    SUPFAMi SSF47266. SSF47266. 1 hit.
    PROSITEi PS00817. EPO_TPO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Large-scale sequencing of two regions in human chromosome 7q22: analysis of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17 genes."
      Gloeckner G., Scherer S., Schattevoy R., Boright A.P., Weber J., Tsui L.-C., Rosenthal A.
      Genome Res. 8:1060-1073(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Erythropoietin gene sequence in the Quechua, a high altitude native population."
      Rupert J.L., Hochachka P.W.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "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].
    6. "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: Brain.
    7. "Gene expression of mutant erythropoietin in hepatocellular carcinoma."
      Funakoshi A., Muta H., Baba T., Shimizu S.
      Biochem. Biophys. Res. Commun. 195:717-722(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-193, VARIANTS HEPATOCELLULAR CARCINOMA 131-ASN-PHE-132 AND GLN-149.
    8. "Structural characterization of human erythropoietin."
      Lai P.H., Everett R., Wang F.F., Arakawa T., Goldwasser E.
      J. Biol. Chem. 261:3116-3121(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-193, DISULFIDE BONDS.
      Tissue: Urine.
    9. "Isolation of human erythropoietin with monoclonal antibodies."
      Yanagawa S., Hirade K., Ohnota H., Sasaki R., Chiba H., Ueda M., Goto M.
      J. Biol. Chem. 259:2707-2710(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 28-57.
    10. "Comparative study of the asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells."
      Takeuchi M., Takasaki S., Miyazaki H., Kato T., Hoshi S., Kochibe N., Kobata A.
      J. Biol. Chem. 263:3657-3663(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE OF CARBOHYDRATES.
    11. "Site-specific glycosylation of human recombinant erythropoietin: analysis of glycopeptides or peptides at each glycosylation site by fast atom bombardment mass spectrometry."
      Sasaki H., Ochi N., Dell A., Fukuda M.
      Biochemistry 27:8618-8626(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE OF CARBOHYDRATES.
    12. "Structures and functional roles of the sugar chains of human erythropoietins."
      Takeuchi M., Kobata A.
      Glycobiology 1:337-346(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE OF CARBOHYDRATES.
    13. "Sugar profiling proves that human serum erythropoietin differs from recombinant human erythropoietin."
      Skibeli V., Nissen-Lie G., Torjesen P.
      Blood 98:3626-3634(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE OF CARBOHYDRATES.
    14. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 28-193.
    15. "NMR structure of human erythropoietin and a comparison with its receptor bound conformation."
      Cheetham J.C., Smith D.M., Aoki K.H., Stevenson J.L., Hoeffel T.J., Syed R.S., Egrie J., Harvey T.S.
      Nat. Struct. Biol. 5:861-866(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 28-193.
    16. Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO MICROVASCULAR COMPLICATIONS OF DIABETES TYPE 2.

    Entry informationi

    Entry nameiEPO_HUMAN
    AccessioniPrimary (citable) accession number: P01588
    Secondary accession number(s): Q2M2L6
    , Q549U2, Q9UDZ0, Q9UEZ5, Q9UHA0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 157 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, Direct protein sequencing, Pharmaceutical, 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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3