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P62333

- PRS10_HUMAN

UniProt

P62333 - PRS10_HUMAN

Protein

26S protease regulatory subunit 10B

Gene

PSMC6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi174 – 1818ATPSequence Analysis

    GO - Molecular functioni

    1. ATPase activity Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. protein binding, bridging Source: UniProtKB

    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. ATP catabolic process Source: GOC
    7. cellular nitrogen compound metabolic process Source: Reactome
    8. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
    9. G1/S transition of mitotic cell cycle Source: Reactome
    10. gene expression Source: Reactome
    11. mitotic cell cycle Source: Reactome
    12. mRNA metabolic process Source: Reactome
    13. negative regulation of apoptotic process Source: Reactome
    14. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    15. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    16. protein polyubiquitination Source: Reactome
    17. regulation of apoptotic process Source: Reactome
    18. regulation of cellular amino acid metabolic process Source: Reactome
    19. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    20. RNA metabolic process Source: Reactome
    21. small molecule metabolic process Source: Reactome
    22. ubiquitin-dependent protein catabolic process Source: UniProtKB
    23. viral process Source: Reactome

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    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:
    26S protease regulatory subunit 10B
    Alternative name(s):
    26S proteasome AAA-ATPase subunit RPT4
    Proteasome 26S subunit ATPase 6
    Proteasome subunit p42
    Gene namesi
    Name:PSMC6
    Synonyms:SUG2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:9553. PSMC6.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB
    6. proteasome accessory complex Source: UniProtKB
    7. proteasome complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33898.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 38938926S protease regulatory subunit 10BPRO_0000084732Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei72 – 721N6-acetyllysine1 Publication
    Modified residuei206 – 2061N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP62333.
    PaxDbiP62333.
    PeptideAtlasiP62333.
    PRIDEiP62333.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00021926.

    PTM databases

    PhosphoSiteiP62333.

    Expressioni

    Gene expression databases

    ArrayExpressiP62333.
    BgeeiP62333.
    CleanExiHS_PSMC6.
    GenevestigatoriP62333.

    Organism-specific databases

    HPAiHPA042823.
    HPA048142.

    Interactioni

    Subunit structurei

    Found in the multi-protein complexes: the 26S proteasome (formed from the 20S proteasome and PA700), and the modulator. PA700 consists of 28 subunits arranged to form a cylinder-shaped complex by four stacked rings, each containing seven subunits. Interacts with PAAF1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PSMC1P621913EBI-357669,EBI-357598
    PSMC3P179805EBI-357669,EBI-359720
    PSMC4P436863EBI-357669,EBI-743997
    PSMC5P621958EBI-357669,EBI-357745
    PSMD9O002335EBI-357669,EBI-750973

    Protein-protein interaction databases

    BioGridi111679. 83 interactions.
    DIPiDIP-38150N.
    IntActiP62333. 32 interactions.
    MINTiMINT-5001174.
    STRINGi9606.ENSP00000401802.

    Structurei

    3D structure databases

    ProteinModelPortaliP62333.
    SMRiP62333. Positions 19-379.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AAA ATPase family.Curated

    Phylogenomic databases

    eggNOGiCOG1222.
    HOGENOMiHOG000225143.
    HOVERGENiHBG000109.
    InParanoidiP62333.
    KOiK03064.
    OrthoDBiEOG7TF78Z.
    PhylomeDBiP62333.
    TreeFamiTF106229.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR005937. 26S_Psome_P45.
    IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00004. AAA. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
    PROSITEiPS00674. AAA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P62333-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADPRDKALQ DYRKKLLEHK EIDGRLKELR EQLKELTKQY EKSENDLKAL    50
    QSVGQIVGEV LKQLTEEKFI VKATNGPRYV VGCRRQLDKS KLKPGTRVAL 100
    DMTTLTIMRY LPREVDPLVY NMSHEDPGNV SYSEIGGLSE QIRELREVIE 150
    LPLTNPELFQ RVGIIPPKGC LLYGPPGTGK TLLARAVASQ LDCNFLKVVS 200
    SSIVDKYIGE SARLIREMFN YARDHQPCII FMDEIDAIGG RRFSEGTSAD 250
    REIQRTLMEL LNQMDGFDTL HRVKMIMATN RPDTLDPALL RPGRLDRKIH 300
    IDLPNEQARL DILKIHAGPI TKHGEIDYEA IVKLSDGFNG ADLRNVCTEA 350
    GMFAIRADHD FVVQEDFMKA VRKVADSKKL ESKLDYKPV 389
    Length:389
    Mass (Da):44,173
    Last modified:July 5, 2004 - v1
    Checksum:iB26421295742CACD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti276 – 2761I → T in BAA11338. (PubMed:8674546)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D78275 mRNA. Translation: BAA11338.1.
    AF006305 mRNA. Translation: AAB61616.1.
    BT006843 mRNA. Translation: AAP35489.1.
    CR456709 mRNA. Translation: CAG32990.1.
    AK313670 mRNA. Translation: BAG36422.1.
    CH471078 Genomic DNA. Translation: EAW65645.1.
    BC005390 mRNA. Translation: AAH05390.1.
    PIRiS71316.
    RefSeqiNP_002797.3. NM_002806.3.
    UniGeneiHs.156171.

    Genome annotation databases

    EnsembliENST00000606149; ENSP00000475721; ENSG00000100519.
    GeneIDi5706.
    KEGGihsa:5706.
    UCSCiuc010tqx.2. human.

    Polymorphism databases

    DMDMi51702772.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D78275 mRNA. Translation: BAA11338.1 .
    AF006305 mRNA. Translation: AAB61616.1 .
    BT006843 mRNA. Translation: AAP35489.1 .
    CR456709 mRNA. Translation: CAG32990.1 .
    AK313670 mRNA. Translation: BAG36422.1 .
    CH471078 Genomic DNA. Translation: EAW65645.1 .
    BC005390 mRNA. Translation: AAH05390.1 .
    PIRi S71316.
    RefSeqi NP_002797.3. NM_002806.3.
    UniGenei Hs.156171.

    3D structure databases

    ProteinModelPortali P62333.
    SMRi P62333. Positions 19-379.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111679. 83 interactions.
    DIPi DIP-38150N.
    IntActi P62333. 32 interactions.
    MINTi MINT-5001174.
    STRINGi 9606.ENSP00000401802.

    PTM databases

    PhosphoSitei P62333.

    Polymorphism databases

    DMDMi 51702772.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00021926.

    Proteomic databases

    MaxQBi P62333.
    PaxDbi P62333.
    PeptideAtlasi P62333.
    PRIDEi P62333.

    Protocols and materials databases

    DNASUi 5706.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000606149 ; ENSP00000475721 ; ENSG00000100519 .
    GeneIDi 5706.
    KEGGi hsa:5706.
    UCSCi uc010tqx.2. human.

    Organism-specific databases

    CTDi 5706.
    GeneCardsi GC14P053173.
    H-InvDB HIX0011661.
    HGNCi HGNC:9553. PSMC6.
    HPAi HPA042823.
    HPA048142.
    MIMi 602708. gene.
    neXtProti NX_P62333.
    PharmGKBi PA33898.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1222.
    HOGENOMi HOG000225143.
    HOVERGENi HBG000109.
    InParanoidi P62333.
    KOi K03064.
    OrthoDBi EOG7TF78Z.
    PhylomeDBi P62333.
    TreeFami TF106229.

    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

    GeneWikii PSMC6.
    GenomeRNAii 5706.
    NextBioi 22170.
    PROi P62333.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62333.
    Bgeei P62333.
    CleanExi HS_PSMC6.
    Genevestigatori P62333.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR005937. 26S_Psome_P45.
    IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00004. AAA. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR01242. 26Sp45. 1 hit.
    PROSITEi PS00674. AAA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning of p42, a shared subunit of two proteasome regulatory proteins, reveals a novel member of the AAA protein family."
      Fujiwara T., Watanabe T.K., Tanaka K., Slaughter C.A., Demartino G.N.
      FEBS Lett. 387:184-188(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Aorta.
    2. "Human SUG2."
      Li Y., Benezra R.
      Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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].
    4. "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].
    5. "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].
      Tissue: Caudate nucleus.
    6. 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].
      Tissue: Urinary bladder.
    8. "Identification, purification, and characterization of a PA700-dependent activator of the proteasome."
      Demartino G.N., Proske R.J., Moomaw C.R., Strong A.A., Song X., Hisamatsu H., Tanaka K., Slaughter C.A.
      J. Biol. Chem. 271:3112-3118(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
    9. "Proteasomal ATPase-associated factor 1 negatively regulates proteasome activity by interacting with proteasomal ATPases."
      Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.
      Mol. Cell. Biol. 25:3842-3853(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAAF1.
    10. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
      Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
      Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-72 AND LYS-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPRS10_HUMAN
    AccessioniPrimary (citable) accession number: P62333
    Secondary accession number(s): B2R975
    , P49719, Q6IBU3, Q92524
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 115 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

    Caution

    Alternative initiation from an upstream conserved methionine cannot be fully excluded but is not experimentally supported while initiation from the displayed methionine is supported by PubMed:17323924.Curated

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3