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Q92530

- PSMF1_HUMAN

UniProt

Q92530 - PSMF1_HUMAN

Protein

Proteasome inhibitor PI31 subunit

Gene

PSMF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (20 Mar 2007)
      Previous versions | rss
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    Functioni

    Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28.1 Publication

    GO - Molecular functioni

    1. endopeptidase inhibitor activity Source: UniProtKB
    2. proteasome binding Source: UniProtKB
    3. protein binding Source: IntAct

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
    3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
    4. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    5. apoptotic process Source: Reactome
    6. cellular nitrogen compound metabolic process Source: Reactome
    7. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
    8. G1/S transition of mitotic cell cycle Source: Reactome
    9. gene expression Source: Reactome
    10. mitotic cell cycle Source: Reactome
    11. mRNA metabolic process Source: Reactome
    12. negative regulation of apoptotic process Source: Reactome
    13. negative regulation of endopeptidase activity Source: GOC
    14. negative regulation of proteasomal protein catabolic process Source: UniProtKB
    15. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    16. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    17. protein polyubiquitination Source: Reactome
    18. regulation of apoptotic process Source: Reactome
    19. regulation of cellular amino acid metabolic process Source: Reactome
    20. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    21. RNA metabolic process Source: Reactome
    22. small molecule metabolic process Source: Reactome
    23. ubiquitin-dependent protein catabolic process Source: UniProtKB
    24. viral process Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_111178. ER-Phagosome pathway.
    REACT_1156. Orc1 removal from chromatin.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_13565. Regulation of ornithine decarboxylase (ODC).
    REACT_150471. Separation of Sister Chromatids.
    REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_172638. Asymmetric localization of PCP proteins.
    REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
    REACT_200766. degradation of AXIN.
    REACT_200841. degradation of DVL.
    REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_9031. Vpu mediated degradation of CD4.
    REACT_9453. Vif-mediated degradation of APOBEC3G.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome inhibitor PI31 subunit
    Short name:
    hPI31
    Gene namesi
    Name:PSMF1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:9571. PSMF1.

    Subcellular locationi

    Cytoplasm 1 Publication. Endoplasmic reticulum 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProtKB
    3. endoplasmic reticulum Source: UniProtKB
    4. membrane Source: UniProtKB
    5. nucleoplasm Source: Reactome
    6. proteasome core complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Proteasome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi6 – 61V → R: Abolishes homodimerization. 1 Publication
    Mutagenesisi83 – 831I → E: Abolishes interaction with FBXO7, but has no effect on homodimerization; when associated with E-90. 1 Publication
    Mutagenesisi90 – 901I → E: Abolishes interaction with FBXO7, but has no effect on homodimerization; when associated with E-83. 1 Publication

    Organism-specific databases

    PharmGKBiPA33917.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 271270Proteasome inhibitor PI31 subunitPRO_0000220920Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei252 – 2521Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ92530.
    PaxDbiQ92530.
    PRIDEiQ92530.

    PTM databases

    PhosphoSiteiQ92530.

    Expressioni

    Gene expression databases

    ArrayExpressiQ92530.
    BgeeiQ92530.
    CleanExiHS_PSMF1.
    GenevestigatoriQ92530.

    Organism-specific databases

    HPAiHPA041122.
    HPA041300.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Interacts with FBXO7. Interacts with the 20S proteasome.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RBFOX1Q9NWB12EBI-945916,EBI-945906

    Protein-protein interaction databases

    BioGridi114872. 27 interactions.
    IntActiQ92530. 11 interactions.
    MINTiMINT-1633308.
    STRINGi9606.ENSP00000327704.

    Structurei

    Secondary structure

    1
    271
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 118
    Helixi12 – 143
    Helixi18 – 3114
    Turni32 – 343
    Beta strandi35 – 439
    Beta strandi51 – 533
    Turni56 – 594
    Beta strandi62 – 7211
    Beta strandi77 – 859
    Beta strandi88 – 958
    Turni96 – 994
    Beta strandi100 – 1078
    Helixi108 – 1114
    Helixi120 – 1234
    Helixi127 – 13711

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VT8X-ray2.60A/B1-151[»]
    ProteinModelPortaliQ92530.
    SMRiQ92530. Positions 1-142.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92530.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 150149Important for homodimerization and interaction with FBXO7Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi154 – 271118Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the proteasome inhibitor PI31 family.Curated

    Phylogenomic databases

    eggNOGiNOG255866.
    HOGENOMiHOG000231957.
    HOVERGENiHBG053746.
    InParanoidiQ92530.
    KOiK06700.
    OMAiDFHRTYK.
    PhylomeDBiQ92530.
    TreeFamiTF106238.

    Family and domain databases

    InterProiIPR021625. FP_dom.
    IPR013886. PI31_Prot_Reg.
    [Graphical view]
    PfamiPF08577. PI31_Prot_C. 1 hit.
    PF11566. PI31_Prot_N. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q92530-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGLEVLFAS AAPAITCRQD ALVCFLHWEV VTHGYFGLGV GDQPGPNDKK    50
    SELLPAGWNN NKDLYVLRYE YKDGSRKLLV KAITVESSMI LNVLEYGSQQ 100
    VADLTLNLDD YIDAEHLGDF HRTYKNSEEL RSRIVSGIIT PIHEQWEKAN 150
    VSSPHREFPP ATAREVDPLR IPPHHPHTSR QPPWCDPLGP FVVGGEDLDP 200
    FGPRRGGMIV DPLRSGFPRA LIDPSSGLPN RLPPGAVPPG ARFDPFGPIG 250
    TSPPGPNPDH LPPPGYDDMY L 271
    Length:271
    Mass (Da):29,817
    Last modified:March 20, 2007 - v2
    Checksum:iC669F8210AFAD727
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361F → C.3 Publications
    Corresponds to variant rs1803415 [ dbSNP | Ensembl ].
    VAR_024564
    Natural varianti174 – 1741H → R.
    Corresponds to variant rs2235587 [ dbSNP | Ensembl ].
    VAR_022153

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D88378 mRNA. Translation: BAA13603.1.
    AL031665 Genomic DNA. Translation: CAC10383.1.
    CH471133 Genomic DNA. Translation: EAX10650.1.
    CH471133 Genomic DNA. Translation: EAX10651.1.
    BC126462 mRNA. Translation: AAI26463.1.
    CCDSiCCDS13010.1.
    RefSeqiNP_006805.2. NM_006814.3.
    NP_848693.2. NM_178578.2.
    UniGeneiHs.471917.

    Genome annotation databases

    EnsembliENST00000333082; ENSP00000327704; ENSG00000125818.
    ENST00000335877; ENSP00000338039; ENSG00000125818.
    GeneIDi9491.
    KEGGihsa:9491.
    UCSCiuc002wel.4. human.

    Polymorphism databases

    DMDMi134047876.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D88378 mRNA. Translation: BAA13603.1 .
    AL031665 Genomic DNA. Translation: CAC10383.1 .
    CH471133 Genomic DNA. Translation: EAX10650.1 .
    CH471133 Genomic DNA. Translation: EAX10651.1 .
    BC126462 mRNA. Translation: AAI26463.1 .
    CCDSi CCDS13010.1.
    RefSeqi NP_006805.2. NM_006814.3.
    NP_848693.2. NM_178578.2.
    UniGenei Hs.471917.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VT8 X-ray 2.60 A/B 1-151 [» ]
    ProteinModelPortali Q92530.
    SMRi Q92530. Positions 1-142.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114872. 27 interactions.
    IntActi Q92530. 11 interactions.
    MINTi MINT-1633308.
    STRINGi 9606.ENSP00000327704.

    PTM databases

    PhosphoSitei Q92530.

    Polymorphism databases

    DMDMi 134047876.

    Proteomic databases

    MaxQBi Q92530.
    PaxDbi Q92530.
    PRIDEi Q92530.

    Protocols and materials databases

    DNASUi 9491.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000333082 ; ENSP00000327704 ; ENSG00000125818 .
    ENST00000335877 ; ENSP00000338039 ; ENSG00000125818 .
    GeneIDi 9491.
    KEGGi hsa:9491.
    UCSCi uc002wel.4. human.

    Organism-specific databases

    CTDi 9491.
    GeneCardsi GC20P001041.
    HGNCi HGNC:9571. PSMF1.
    HPAi HPA041122.
    HPA041300.
    neXtProti NX_Q92530.
    PharmGKBi PA33917.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG255866.
    HOGENOMi HOG000231957.
    HOVERGENi HBG053746.
    InParanoidi Q92530.
    KOi K06700.
    OMAi DFHRTYK.
    PhylomeDBi Q92530.
    TreeFami TF106238.

    Enzyme and pathway databases

    Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_111178. ER-Phagosome pathway.
    REACT_1156. Orc1 removal from chromatin.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_13565. Regulation of ornithine decarboxylase (ODC).
    REACT_150471. Separation of Sister Chromatids.
    REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_172638. Asymmetric localization of PCP proteins.
    REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
    REACT_200766. degradation of AXIN.
    REACT_200841. degradation of DVL.
    REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_9031. Vpu mediated degradation of CD4.
    REACT_9453. Vif-mediated degradation of APOBEC3G.

    Miscellaneous databases

    ChiTaRSi PSMF1. human.
    EvolutionaryTracei Q92530.
    GeneWikii PSMF1.
    GenomeRNAii 9491.
    NextBioi 35560.
    PROi Q92530.

    Gene expression databases

    ArrayExpressi Q92530.
    Bgeei Q92530.
    CleanExi HS_PSMF1.
    Genevestigatori Q92530.

    Family and domain databases

    InterProi IPR021625. FP_dom.
    IPR013886. PI31_Prot_Reg.
    [Graphical view ]
    Pfami PF08577. PI31_Prot_C. 1 hit.
    PF11566. PI31_Prot_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning, expression, and functional characterization of PI31, a proline-rich inhibitor of the proteasome."
      McCutchen-Maloney S.L., Matsuda K., Shimbara N., Binns D.D., Tanaka K., Slaughter C.A., DeMartino G.N.
      J. Biol. Chem. 275:18557-18565(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CYS-36, FUNCTION, SUBUNIT.
    2. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT CYS-36.
    4. "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], VARIANT CYS-36.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "Structure of a conserved dimerization domain within the F-box protein Fbxo7 and the PI31 proteasome inhibitor."
      Kirk R., Laman H., Knowles P.P., Murray-Rust J., Lomonosov M., Meziane E.K., McDonald N.Q.
      J. Biol. Chem. 283:22325-22335(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-151, INTERACTION WITH FBXO7, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF VAL-6; ILE-83 AND ILE-90.

    Entry informationi

    Entry nameiPSMF1_HUMAN
    AccessioniPrimary (citable) accession number: Q92530
    Secondary accession number(s): A0AVQ9, D3DVW3, Q9H4I1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: March 20, 2007
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 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 20
      Human chromosome 20: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3