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P56589

- PEX3_HUMAN

UniProt

P56589 - PEX3_HUMAN

Protein

Peroxisomal biogenesis factor 3

Gene

PEX3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (15 Dec 1998)
      Previous versions | rss
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    Functioni

    Involved in peroxisome biosynthesis and integrity. Assembles membrane vesicles before the matrix proteins are translocated. As a docking factor for PEX19, is necessary for the import of peroxisomal membrane proteins in the peroxisomes.2 Publications

    GO - Molecular functioni

    1. lipid binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein dimerization activity Source: UniProtKB

    GO - Biological processi

    1. peroxisome membrane biogenesis Source: Ensembl
    2. peroxisome organization Source: UniProtKB
    3. protein import into peroxisome membrane Source: UniProtKB
    4. transmembrane transport Source: Reactome

    Keywords - Biological processi

    Peroxisome biogenesis

    Enzyme and pathway databases

    ReactomeiREACT_111158. ABCA transporters in lipid homeostasis.

    Protein family/group databases

    TCDBi9.A.17.1.2. the integral membrane peroxisomal protein importer-2 (ppi2) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal biogenesis factor 3
    Alternative name(s):
    Peroxin-3
    Peroxisomal assembly protein PEX3
    Gene namesi
    Name:PEX3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:8858. PEX3.

    Subcellular locationi

    Peroxisome membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. endoplasmic reticulum Source: UniProtKB
    3. integral component of peroxisomal membrane Source: UniProtKB
    4. intracellular membrane-bounded organelle Source: HPA
    5. membrane Source: UniProtKB
    6. nucleus Source: HPA
    7. peroxisomal membrane Source: UniProtKB
    8. peroxisome Source: UniProtKB
    9. protein complex Source: UniProtKB
    10. protein-lipid complex Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Peroxisome

    Pathology & Biotechi

    Involvement in diseasei

    Peroxisome biogenesis disorder complementation group 12 (PBD-CG12) [MIM:614882]: A peroxisomal disorder arising from a failure of protein import into the peroxisomal membrane or matrix. The peroxisome biogenesis disorders (PBD group) are genetically heterogeneous with at least 14 distinct genetic groups as concluded from complementation studies. Include disorders are: Zellweger syndrome (ZWS), neonatal adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and classical rhizomelic chondrodysplasia punctata (RCDP). ZWS, NALD and IRD are distinct from RCDP and constitute a clinical continuum of overlapping phenotypes known as the Zellweger spectrum (PBD-ZSS).
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Peroxisome biogenesis disorder 10A (PBD10A) [MIM:614882]: A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and clinically characterized by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti138 – 1381G → E in PBD10A. 1 Publication
    VAR_009304

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi125 – 1251L → P: Abolishes binding to PEX19 without affecting targeting to peroxisomes; when associated with D-134. 1 Publication
    Mutagenesisi134 – 1341N → D: Abolishes binding to PEX19 without affecting targeting to peroxisomes; when associated with P-125. 1 Publication

    Keywords - Diseasei

    Disease mutation, Peroxisome biogenesis disorder, Zellweger syndrome

    Organism-specific databases

    MIMi614882. phenotype.
    Orphaneti772. Infantile Refsum disease.
    44. Neonatal adrenoleukodystrophy.
    912. Zellweger syndrome.
    PharmGKBiPA33200.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 373373Peroxisomal biogenesis factor 3PRO_0000208737Add
    BLAST

    Proteomic databases

    MaxQBiP56589.
    PaxDbiP56589.
    PeptideAtlasiP56589.
    PRIDEiP56589.

    PTM databases

    PhosphoSiteiP56589.

    Expressioni

    Tissue specificityi

    Found in all examined tissues.

    Gene expression databases

    ArrayExpressiP56589.
    BgeeiP56589.
    CleanExiHS_PEX3.
    GenevestigatoriP56589.

    Organism-specific databases

    HPAiHPA042830.

    Interactioni

    Subunit structurei

    Interacts with PEX19.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PEX19P4085520EBI-594885,EBI-594747

    Protein-protein interaction databases

    BioGridi114076. 9 interactions.
    IntActiP56589. 4 interactions.
    MINTiMINT-241504.
    STRINGi9606.ENSP00000356563.

    Structurei

    Secondary structure

    1
    373
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi41 – 8343
    Helixi86 – 938
    Helixi100 – 14243
    Beta strandi147 – 1515
    Helixi158 – 1658
    Helixi166 – 1683
    Helixi169 – 1724
    Helixi174 – 19118
    Beta strandi199 – 2013
    Helixi202 – 21716
    Helixi234 – 2374
    Helixi246 – 2483
    Helixi255 – 27117
    Helixi274 – 29623
    Beta strandi319 – 3213
    Helixi322 – 3309
    Helixi333 – 3364
    Turni339 – 3413
    Helixi344 – 3496
    Helixi352 – 36615

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3AJBX-ray2.50A49-373[»]
    3MK4X-ray2.42A41-373[»]
    ProteinModelPortaliP56589.
    SMRiP56589. Positions 52-368.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP56589.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1515CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini37 – 11680PeroxisomalSequence AnalysisAdd
    BLAST
    Topological domaini141 – 373233CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei16 – 3621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei117 – 14024HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 4545Targeting to peroxisomesAdd
    BLAST
    Regioni120 – 13617Interaction with PEX19Add
    BLAST

    Sequence similaritiesi

    Belongs to the peroxin-3 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG259038.
    HOGENOMiHOG000007212.
    HOVERGENiHBG000467.
    InParanoidiP56589.
    KOiK13336.
    OMAiARRQFHF.
    OrthoDBiEOG71ZP1Q.
    PhylomeDBiP56589.
    TreeFamiTF352826.

    Family and domain databases

    InterProiIPR006966. Peroxin-3.
    [Graphical view]
    PfamiPF04882. Peroxin-3. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P56589-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRSVWNFLK RHKKKCIFLG TVLGGVYILG KYGQKKIREI QEREAAEYIA    50
    QARRQYHFES NQRTCNMTVL SMLPTLREAL MQQLNSESLT ALLKNRPSNK 100
    LEIWEDLKII SFTRSTVAVY STCMLVVLLR VQLNIIGGYI YLDNAAVGKN 150
    GTTILAPPDV QQQYLSSIQH LLGDGLTELI TVIKQAVQKV LGSVSLKHSL 200
    SLLDLEQKLK EIRNLVEQHK SSSWINKDGS KPLLCHYMMP DEETPLAVQA 250
    CGLSPRDITT IKLLNETRDM LESPDFSTVL NTCLNRGFSR LLDNMAEFFR 300
    PTEQDLQHGN SMNSLSSVSL PLAKIIPIVN GQIHSVCSET PSHFVQDLLT 350
    MEQVKDFAAN VYEAFSTPQQ LEK 373
    Length:373
    Mass (Da):42,140
    Last modified:December 15, 1998 - v1
    Checksum:i3515A1F29656B7CC
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti82 – 821Q → R.
    Corresponds to variant rs35220041 [ dbSNP | Ensembl ].
    VAR_053572
    Natural varianti138 – 1381G → E in PBD10A. 1 Publication
    VAR_009304

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001625 mRNA. Translation: CAA04879.1.
    AJ131389 mRNA. Translation: CAA10362.1.
    AJ009866
    , AJ009867, AJ009868, AJ009869, AJ009870, AJ009871, AJ009872, AJ009873, AJ009874 Genomic DNA. Translation: CAA08904.1.
    AB035307 mRNA. Translation: BAA97993.1.
    AY277600 mRNA. Translation: AAQ18039.1.
    CR542062 mRNA. Translation: CAG46859.1.
    AL031320 Genomic DNA. Translation: CAB53744.1.
    CH471051 Genomic DNA. Translation: EAW47866.1.
    BC014551 mRNA. Translation: AAH14551.1.
    BC015506 mRNA. Translation: AAH15506.1.
    CCDSiCCDS5199.1.
    RefSeqiNP_003621.1. NM_003630.2.
    UniGeneiHs.592832.
    Hs.7277.

    Genome annotation databases

    EnsembliENST00000367591; ENSP00000356563; ENSG00000034693.
    GeneIDi8504.
    KEGGihsa:8504.
    UCSCiuc003qjl.3. human.

    Polymorphism databases

    DMDMi3914303.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001625 mRNA. Translation: CAA04879.1 .
    AJ131389 mRNA. Translation: CAA10362.1 .
    AJ009866
    , AJ009867 , AJ009868 , AJ009869 , AJ009870 , AJ009871 , AJ009872 , AJ009873 , AJ009874 Genomic DNA. Translation: CAA08904.1 .
    AB035307 mRNA. Translation: BAA97993.1 .
    AY277600 mRNA. Translation: AAQ18039.1 .
    CR542062 mRNA. Translation: CAG46859.1 .
    AL031320 Genomic DNA. Translation: CAB53744.1 .
    CH471051 Genomic DNA. Translation: EAW47866.1 .
    BC014551 mRNA. Translation: AAH14551.1 .
    BC015506 mRNA. Translation: AAH15506.1 .
    CCDSi CCDS5199.1.
    RefSeqi NP_003621.1. NM_003630.2.
    UniGenei Hs.592832.
    Hs.7277.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3AJB X-ray 2.50 A 49-373 [» ]
    3MK4 X-ray 2.42 A 41-373 [» ]
    ProteinModelPortali P56589.
    SMRi P56589. Positions 52-368.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114076. 9 interactions.
    IntActi P56589. 4 interactions.
    MINTi MINT-241504.
    STRINGi 9606.ENSP00000356563.

    Protein family/group databases

    TCDBi 9.A.17.1.2. the integral membrane peroxisomal protein importer-2 (ppi2) family.

    PTM databases

    PhosphoSitei P56589.

    Polymorphism databases

    DMDMi 3914303.

    Proteomic databases

    MaxQBi P56589.
    PaxDbi P56589.
    PeptideAtlasi P56589.
    PRIDEi P56589.

    Protocols and materials databases

    DNASUi 8504.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367591 ; ENSP00000356563 ; ENSG00000034693 .
    GeneIDi 8504.
    KEGGi hsa:8504.
    UCSCi uc003qjl.3. human.

    Organism-specific databases

    CTDi 8504.
    GeneCardsi GC06P143772.
    GeneReviewsi PEX3.
    HGNCi HGNC:8858. PEX3.
    HPAi HPA042830.
    MIMi 603164. gene.
    614882. phenotype.
    neXtProti NX_P56589.
    Orphaneti 772. Infantile Refsum disease.
    44. Neonatal adrenoleukodystrophy.
    912. Zellweger syndrome.
    PharmGKBi PA33200.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG259038.
    HOGENOMi HOG000007212.
    HOVERGENi HBG000467.
    InParanoidi P56589.
    KOi K13336.
    OMAi ARRQFHF.
    OrthoDBi EOG71ZP1Q.
    PhylomeDBi P56589.
    TreeFami TF352826.

    Enzyme and pathway databases

    Reactomei REACT_111158. ABCA transporters in lipid homeostasis.

    Miscellaneous databases

    EvolutionaryTracei P56589.
    GeneWikii PEX3.
    GenomeRNAii 8504.
    NextBioi 31825.
    PROi P56589.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P56589.
    Bgeei P56589.
    CleanExi HS_PEX3.
    Genevestigatori P56589.

    Family and domain databases

    InterProi IPR006966. Peroxin-3.
    [Graphical view ]
    Pfami PF04882. Peroxin-3. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the gene encoding the human peroxisomal assembly protein Pex3p."
      Kammerer S., Holzinger A., Welsch U., Roscher A.A.
      FEBS Lett. 429:53-60(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Identification and characterization of the human peroxin PEX3."
      Soukupova M., Sprenger C., Gorgas K., Kunau W.H., Dodt G.
      Eur. J. Cell Biol. 78:357-374(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The human PEX3 gene encoding a peroxisomal assembly protein: genomic organization, positional mapping, and mutation analysis in candidate phenotypes."
      Muntau A.C., Holzinger A., Mayerhofer P.U., Gartner J., Roscher A.A., Kammerer S.
      Biochem. Biophys. Res. Commun. 268:704-710(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The peroxin pex3p initiates membrane assembly in peroxisome biogenesis."
      Ghaedi K., Tamura S., Okumoto K., Matsuzono Y., Fujiki Y.
      Mol. Biol. Cell 11:2085-2102(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CHARACTERIZATION, VARIANT PBD10A GLU-138.
      Tissue: Liver.
    5. "Identification of a human transforming gene."
      Kim J.W.
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. 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: Skin and Uterus.
    10. "PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis."
      Sacksteder K.A., Jones J.M., South S.T., Li X., Liu Y., Gould S.J.
      J. Cell Biol. 148:931-944(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PEX19.
    11. "Human pex19p binds peroxisomal integral membrane proteins at regions distinct from their sorting sequences."
      Fransen M., Wylin T., Brees C., Mannaerts G.P., Van Veldhoven P.P.
      Mol. Cell. Biol. 21:4413-4424(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PEX19, SUBCELLULAR LOCATION.
    12. "PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins."
      Fang Y., Morrell J.C., Jones J.M., Gould S.J.
      J. Cell Biol. 164:863-875(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LEU-125 AND ASN-134.
    13. "Defective peroxisome membrane synthesis due to mutations in human PEX3 causes Zellweger syndrome, complementation group G."
      Muntau A.C., Mayerhofer P.U., Paton B.C., Kammerer S., Roscher A.A.
      Am. J. Hum. Genet. 67:967-975(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN PBD-CG12 AND PBD10A.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Structural basis for docking of peroxisomal membrane protein carrier Pex19p onto its receptor Pex3p."
      Sato Y., Shibata H., Nakatsu T., Nakano H., Kashiwayama Y., Imanaka T., Kato H.
      EMBO J. 29:4083-4093(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 49-373 IN COMPLEX WITH PEX19, SUBUNIT.
    16. "Insights into peroxisome function from the structure of PEX3 in complex with a soluble fragment of PEX19."
      Schmidt F., Treiber N., Zocher G., Bjelic S., Steinmetz M.O., Kalbacher H., Stehle T., Dodt G.
      J. Biol. Chem. 285:25410-25417(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 41-373 IN COMPLEX WITH PEX19, SUBUNIT.

    Entry informationi

    Entry nameiPEX3_HUMAN
    AccessioniPrimary (citable) accession number: P56589
    Secondary accession number(s): Q6FGP5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 129 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 6
      Human chromosome 6: 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