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P31323

- KAP3_HUMAN

UniProt

P31323 - KAP3_HUMAN

Protein

cAMP-dependent protein kinase type II-beta regulatory subunit

Gene

PRKAR2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (23 Sep 2008)
      Previous versions | rss
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    Functioni

    Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei223 – 2231cAMP 1
    Binding sitei232 – 2321cAMP 1
    Binding sitei352 – 3521cAMP 2
    Binding sitei361 – 3611cAMP 2

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi154 – 275122cAMP 1Add
    BLAST
    Nucleotide bindingi276 – 418143cAMP 2Add
    BLAST

    GO - Molecular functioni

    1. cAMP binding Source: UniProtKB-KW
    2. cAMP-dependent protein kinase inhibitor activity Source: BHF-UCL
    3. cAMP-dependent protein kinase regulator activity Source: BHF-UCL
    4. protein kinase A catalytic subunit binding Source: BHF-UCL
    5. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. activation of phospholipase C activity Source: Reactome
    2. activation of protein kinase A activity Source: Reactome
    3. blood coagulation Source: Reactome
    4. cellular response to glucagon stimulus Source: Reactome
    5. energy reserve metabolic process Source: Reactome
    6. epidermal growth factor receptor signaling pathway Source: Reactome
    7. fatty acid metabolic process Source: Ensembl
    8. fibroblast growth factor receptor signaling pathway Source: Reactome
    9. G2/M transition of mitotic cell cycle Source: Reactome
    10. innate immune response Source: Reactome
    11. intracellular signal transduction Source: ProtInc
    12. learning Source: Ensembl
    13. mitotic cell cycle Source: Reactome
    14. negative regulation of cAMP-dependent protein kinase activity Source: BHF-UCL
    15. neurotrophin TRK receptor signaling pathway Source: Reactome
    16. regulation of insulin secretion Source: Reactome
    17. signal transduction Source: Reactome
    18. small molecule metabolic process Source: Reactome
    19. transmembrane transport Source: Reactome
    20. water transport Source: Reactome

    Keywords - Ligandi

    cAMP, cAMP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15334. DARPP-32 events.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_15530. PKA activation.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_1946. PKA activation in glucagon signalling.
    REACT_24023. Regulation of water balance by renal Aquaporins.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    cAMP-dependent protein kinase type II-beta regulatory subunit
    Gene namesi
    Name:PRKAR2B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:9392. PRKAR2B.

    Subcellular locationi

    Cytoplasm 1 Publication. Cell membrane 1 Publication
    Note: Colocalizes with PJA2 in the cytoplasm and at the cell membrane.

    GO - Cellular componenti

    1. cAMP-dependent protein kinase complex Source: InterPro
    2. centrosome Source: UniProtKB
    3. cytoplasm Source: UniProtKB
    4. cytosol Source: Reactome
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33758.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedCurated
    Chaini2 – 418417cAMP-dependent protein kinase type II-beta regulatory subunitPRO_0000205390Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineCurated
    Modified residuei83 – 831Phosphoserine1 Publication
    Modified residuei85 – 851Phosphoserine1 Publication
    Modified residuei114 – 1141Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated by the activated catalytic chain.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP31323.
    PaxDbiP31323.
    PRIDEiP31323.

    2D gel databases

    OGPiP31323.

    PTM databases

    PhosphoSiteiP31323.

    Expressioni

    Tissue specificityi

    Four types of regulatory chains are found: I-alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible.

    Gene expression databases

    ArrayExpressiP31323.
    BgeeiP31323.
    CleanExiHS_PRKAR2B.
    GenevestigatoriP31323.

    Organism-specific databases

    HPAiHPA008421.

    Interactioni

    Subunit structurei

    The inactive form of the enzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP produces two active catalytic monomers and a regulatory dimer that binds four cAMP molecules. Interacts with the phosphorylated form of PJA2.1 Publication

    Protein-protein interaction databases

    BioGridi111563. 12 interactions.
    DIPiDIP-554N.
    IntActiP31323. 6 interactions.
    MINTiMINT-2782562.
    STRINGi9606.ENSP00000265717.

    Structurei

    3D structure databases

    ProteinModelPortaliP31323.
    SMRiP31323. Positions 8-410.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 153152Dimerization and phosphorylationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 cyclic nucleotide-binding domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0664.
    HOGENOMiHOG000196668.
    HOVERGENiHBG002025.
    InParanoidiP31323.
    KOiK04739.
    OMAiPMHSDSE.
    OrthoDBiEOG76T9RR.
    PhylomeDBiP31323.
    TreeFamiTF314920.

    Family and domain databases

    Gene3Di2.60.120.10. 2 hits.
    InterProiIPR002373. cAMP/cGMP_kin.
    IPR012198. cAMP_dep_PK_reg_su.
    IPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
    IPR018490. cNMP-bd-like.
    IPR018488. cNMP-bd_CS.
    IPR000595. cNMP-bd_dom.
    IPR014710. RmlC-like_jellyroll.
    [Graphical view]
    PfamiPF00027. cNMP_binding. 2 hits.
    PF02197. RIIa. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000548. PK_regulatory. 1 hit.
    PRINTSiPR00103. CAMPKINASE.
    SMARTiSM00100. cNMP. 2 hits.
    SM00394. RIIa. 1 hit.
    [Graphical view]
    SUPFAMiSSF47391. SSF47391. 1 hit.
    SSF51206. SSF51206. 2 hits.
    PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
    PS00889. CNMP_BINDING_2. 2 hits.
    PS50042. CNMP_BINDING_3. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P31323-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSIEIPAGLT ELLQGFTVEV LRHQPADLLE FALQHFTRLQ QENERKGTAR    50
    FGHEGRTWGD LGAAAGGGTP SKGVNFAEEP MQSDSEDGEE EEAAPADAGA 100
    FNAPVINRFT RRASVCAEAY NPDEEEDDAE SRIIHPKTDD QRNRLQEACK 150
    DILLFKNLDP EQMSQVLDAM FEKLVKDGEH VIDQGDDGDN FYVIDRGTFD 200
    IYVKCDGVGR CVGNYDNRGS FGELALMYNT PRAATITATS PGALWGLDRV 250
    TFRRIIVKNN AKKRKMYESF IESLPFLKSL EFSERLKVVD VIGTKVYNDG 300
    EQIIAQGDSA DSFFIVESGE VKITMKRKGK SEVEENGAVE IARCSRGQYF 350
    GELALVTNKP RAASAHAIGT VKCLAMDVQA FERLLGPCME IMKRNIATYE 400
    EQLVALFGTN MDIVEPTA 418
    Length:418
    Mass (Da):46,302
    Last modified:September 23, 2008 - v3
    Checksum:i83F402CCFFEFD186
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti341 – 3422IA → MP in AAA60099. (PubMed:2851102)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti335 – 3351E → D.
    Corresponds to variant rs3729881 [ dbSNP | Ensembl ].
    VAR_046549

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31158 mRNA. Translation: AAA60099.1.
    AK291441 mRNA. Translation: BAF84130.1.
    CH236947 Genomic DNA. Translation: EAL24395.1.
    CH471070 Genomic DNA. Translation: EAW83390.1.
    CCDSiCCDS5740.1.
    PIRiA40915. OKHUR2.
    RefSeqiNP_002727.2. NM_002736.2.
    UniGeneiHs.433068.

    Genome annotation databases

    EnsembliENST00000265717; ENSP00000265717; ENSG00000005249.
    GeneIDi5577.
    KEGGihsa:5577.
    UCSCiuc003vdx.3. human.

    Polymorphism databases

    DMDMi206729918.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31158 mRNA. Translation: AAA60099.1 .
    AK291441 mRNA. Translation: BAF84130.1 .
    CH236947 Genomic DNA. Translation: EAL24395.1 .
    CH471070 Genomic DNA. Translation: EAW83390.1 .
    CCDSi CCDS5740.1.
    PIRi A40915. OKHUR2.
    RefSeqi NP_002727.2. NM_002736.2.
    UniGenei Hs.433068.

    3D structure databases

    ProteinModelPortali P31323.
    SMRi P31323. Positions 8-410.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111563. 12 interactions.
    DIPi DIP-554N.
    IntActi P31323. 6 interactions.
    MINTi MINT-2782562.
    STRINGi 9606.ENSP00000265717.

    Chemistry

    BindingDBi P31323.

    PTM databases

    PhosphoSitei P31323.

    Polymorphism databases

    DMDMi 206729918.

    2D gel databases

    OGPi P31323.

    Proteomic databases

    MaxQBi P31323.
    PaxDbi P31323.
    PRIDEi P31323.

    Protocols and materials databases

    DNASUi 5577.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265717 ; ENSP00000265717 ; ENSG00000005249 .
    GeneIDi 5577.
    KEGGi hsa:5577.
    UCSCi uc003vdx.3. human.

    Organism-specific databases

    CTDi 5577.
    GeneCardsi GC07P106685.
    H-InvDB HIX0025309.
    HGNCi HGNC:9392. PRKAR2B.
    HPAi HPA008421.
    MIMi 176912. gene.
    neXtProti NX_P31323.
    PharmGKBi PA33758.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0664.
    HOGENOMi HOG000196668.
    HOVERGENi HBG002025.
    InParanoidi P31323.
    KOi K04739.
    OMAi PMHSDSE.
    OrthoDBi EOG76T9RR.
    PhylomeDBi P31323.
    TreeFami TF314920.

    Enzyme and pathway databases

    Reactomei REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15334. DARPP-32 events.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_15530. PKA activation.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_1946. PKA activation in glucagon signalling.
    REACT_24023. Regulation of water balance by renal Aquaporins.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.

    Miscellaneous databases

    GeneWikii PRKAR2B.
    GenomeRNAii 5577.
    NextBioi 21624.
    PROi P31323.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P31323.
    Bgeei P31323.
    CleanExi HS_PRKAR2B.
    Genevestigatori P31323.

    Family and domain databases

    Gene3Di 2.60.120.10. 2 hits.
    InterProi IPR002373. cAMP/cGMP_kin.
    IPR012198. cAMP_dep_PK_reg_su.
    IPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
    IPR018490. cNMP-bd-like.
    IPR018488. cNMP-bd_CS.
    IPR000595. cNMP-bd_dom.
    IPR014710. RmlC-like_jellyroll.
    [Graphical view ]
    Pfami PF00027. cNMP_binding. 2 hits.
    PF02197. RIIa. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000548. PK_regulatory. 1 hit.
    PRINTSi PR00103. CAMPKINASE.
    SMARTi SM00100. cNMP. 2 hits.
    SM00394. RIIa. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47391. SSF47391. 1 hit.
    SSF51206. SSF51206. 2 hits.
    PROSITEi PS00888. CNMP_BINDING_1. 2 hits.
    PS00889. CNMP_BINDING_2. 2 hits.
    PS50042. CNMP_BINDING_3. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, complementary deoxyribonucleic acid structure and predicted full-length amino acid sequence of the hormone-inducible regulatory subunit of 3'-5'-cyclic adenosine monophosphate-dependent protein kinase from human testis."
      Levy F.O., Oeyen O., Sandberg M., Tasken K., Eskild W., Hansson V., Jahnsen T.
      Mol. Endocrinol. 2:1364-1373(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Testis.
    2. "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: Brain.
    3. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PJA2.
    10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-85 AND SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiKAP3_HUMAN
    AccessioniPrimary (citable) accession number: P31323
    Secondary accession number(s): A4D0R9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 139 of the entry and version 3 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 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3