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P13861

- KAP2_HUMAN

UniProt

P13861 - KAP2_HUMAN

Protein

cAMP-dependent protein kinase type II-alpha regulatory subunit

Gene

PRKAR2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      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 sitei208 – 2081cAMP 1
    Binding sitei217 – 2171cAMP 1
    Binding sitei338 – 3381cAMP 2
    Binding sitei347 – 3471cAMP 2

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi139 – 260122cAMP 1Add
    BLAST
    Nucleotide bindingi261 – 404144cAMP 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: UniProtKB
    4. protein binding Source: IntAct
    5. protein kinase A catalytic subunit binding Source: BHF-UCL
    6. 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. fibroblast growth factor receptor signaling pathway Source: Reactome
    8. innate immune response Source: Reactome
    9. intracellular signal transduction Source: ProtInc
    10. negative regulation of cAMP-dependent protein kinase activity Source: BHF-UCL
    11. neurotrophin TRK receptor signaling pathway Source: Reactome
    12. regulation of insulin secretion Source: Reactome
    13. signal transduction Source: Reactome
    14. small molecule metabolic process Source: Reactome
    15. transmembrane transport Source: Reactome
    16. water transport Source: Reactome

    Keywords - Ligandi

    cAMP, cAMP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_15334. DARPP-32 events.
    REACT_15530. PKA activation.
    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.
    SignaLinkiP13861.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    cAMP-dependent protein kinase type II-alpha regulatory subunit
    Gene namesi
    Name:PRKAR2A
    Synonyms:PKR2, PRKAR2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:9391. PRKAR2A.

    Subcellular locationi

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

    GO - Cellular componenti

    1. AMP-activated protein kinase complex Source: BHF-UCL
    2. cAMP-dependent protein kinase complex Source: InterPro
    3. centrosome Source: UniProtKB
    4. cytoplasm Source: UniProtKB
    5. cytosol Source: Reactome
    6. extracellular vesicular exosome Source: UniProt
    7. membrane Source: UniProtKB
    8. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33757.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 404403cAMP-dependent protein kinase type II-alpha regulatory subunitPRO_0000205385Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei48 – 481Phosphoserine1 Publication
    Modified residuei54 – 541Phosphothreonine2 Publications
    Modified residuei58 – 581Phosphoserine2 Publications
    Modified residuei78 – 781Phosphoserine4 Publications
    Modified residuei80 – 801Phosphoserine4 Publications
    Modified residuei99 – 991Phosphoserine; by PKA4 Publications
    Modified residuei215 – 2151Phosphothreonine; by PDPK1By similarity

    Post-translational modificationi

    Phosphorylated by the activated catalytic chain.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP13861.
    PaxDbiP13861.
    PRIDEiP13861.

    2D gel databases

    OGPiP13861.

    PTM databases

    PhosphoSiteiP13861.

    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

    ArrayExpressiP13861.
    BgeeiP13861.
    CleanExiHS_PRKAR2A.
    GenevestigatoriP13861.

    Organism-specific databases

    HPAiCAB005023.

    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 AKAP4 and CBFA2T3. Interacts with the phosphorylated form of PJA2. Interacts with MYRIP. This interaction may link PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P03259-25EBI-2556122,EBI-7225021From a different organism.
    AKAP1Q926673EBI-2556122,EBI-2119593
    AKAP3O759692EBI-2556122,EBI-9033101

    Protein-protein interaction databases

    BioGridi111562. 38 interactions.
    DIPiDIP-552N.
    IntActiP13861. 19 interactions.
    MINTiMINT-5000495.
    STRINGi9606.ENSP00000265563.

    Structurei

    Secondary structure

    1
    404
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 2415
    Helixi29 – 4315

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IZXX-ray1.30A/B4-44[»]
    2KYGNMR-A/B1-45[»]
    ProteinModelPortaliP13861.
    SMRiP13861. Positions 4-396.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13861.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 138137Dimerization and phosphorylationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0664.
    HOGENOMiHOG000196668.
    HOVERGENiHBG002025.
    InParanoidiP13861.
    KOiK04739.
    OMAiLEMSERM.
    PhylomeDBiP13861.
    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.

    P13861-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHIQIPPGL TELLQGYTVE VLRQQPPDLV EFAVEYFTRL REARAPASVL    50
    PAATPRQSLG HPPPEPGPDR VADAKGDSES EEDEDLEVPV PSRFNRRVSV 100
    CAETYNPDEE EEDTDPRVIH PKTDEQRCRL QEACKDILLF KNLDQEQLSQ 150
    VLDAMFERIV KADEHVIDQG DDGDNFYVIE RGTYDILVTK DNQTRSVGQY 200
    DNRGSFGELA LMYNTPRAAT IVATSEGSLW GLDRVTFRRI IVKNNAKKRK 250
    MFESFIESVP LLKSLEVSER MKIVDVIGEK IYKDGERIIT QGEKADSFYI 300
    IESGEVSILI RSRTKSNKDG GNQEVEIARC HKGQYFGELA LVTNKPRAAS 350
    AYAVGDVKCL VMDVQAFERL LGPCMDIMKR NISHYEEQLV KMFGSSVDLG 400
    NLGQ 404
    Length:404
    Mass (Da):45,518
    Last modified:January 23, 2007 - v2
    Checksum:iC7D6E8E476E1DB65
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14968 mRNA. Translation: CAA33094.1.
    X99455 Genomic DNA. Translation: CAA67817.1.
    CCDSiCCDS2778.1.
    PIRiS03885. OKHU2R.
    RefSeqiNP_004148.1. NM_004157.2.
    XP_005265370.1. XM_005265313.1.
    UniGeneiHs.631923.

    Genome annotation databases

    EnsembliENST00000265563; ENSP00000265563; ENSG00000114302.
    ENST00000454963; ENSP00000394041; ENSG00000114302.
    GeneIDi5576.
    KEGGihsa:5576.
    UCSCiuc003cux.1. human.

    Polymorphism databases

    DMDMi125198.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14968 mRNA. Translation: CAA33094.1 .
    X99455 Genomic DNA. Translation: CAA67817.1 .
    CCDSi CCDS2778.1.
    PIRi S03885. OKHU2R.
    RefSeqi NP_004148.1. NM_004157.2.
    XP_005265370.1. XM_005265313.1.
    UniGenei Hs.631923.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IZX X-ray 1.30 A/B 4-44 [» ]
    2KYG NMR - A/B 1-45 [» ]
    ProteinModelPortali P13861.
    SMRi P13861. Positions 4-396.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111562. 38 interactions.
    DIPi DIP-552N.
    IntActi P13861. 19 interactions.
    MINTi MINT-5000495.
    STRINGi 9606.ENSP00000265563.

    Chemistry

    BindingDBi P13861.

    PTM databases

    PhosphoSitei P13861.

    Polymorphism databases

    DMDMi 125198.

    2D gel databases

    OGPi P13861.

    Proteomic databases

    MaxQBi P13861.
    PaxDbi P13861.
    PRIDEi P13861.

    Protocols and materials databases

    DNASUi 5576.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265563 ; ENSP00000265563 ; ENSG00000114302 .
    ENST00000454963 ; ENSP00000394041 ; ENSG00000114302 .
    GeneIDi 5576.
    KEGGi hsa:5576.
    UCSCi uc003cux.1. human.

    Organism-specific databases

    CTDi 5576.
    GeneCardsi GC03M048762.
    HGNCi HGNC:9391. PRKAR2A.
    HPAi CAB005023.
    MIMi 176910. gene.
    neXtProti NX_P13861.
    PharmGKBi PA33757.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0664.
    HOGENOMi HOG000196668.
    HOVERGENi HBG002025.
    InParanoidi P13861.
    KOi K04739.
    OMAi LEMSERM.
    PhylomeDBi P13861.
    TreeFami TF314920.

    Enzyme and pathway databases

    Reactomei REACT_15334. DARPP-32 events.
    REACT_15530. PKA activation.
    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.
    SignaLinki P13861.

    Miscellaneous databases

    ChiTaRSi PRKAR2A. human.
    EvolutionaryTracei P13861.
    GeneWikii PRKAR2A.
    GenomeRNAii 5576.
    NextBioi 21620.
    PROi P13861.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13861.
    Bgeei P13861.
    CleanExi HS_PRKAR2A.
    Genevestigatori P13861.

    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. "Human testis cDNA for the regulatory subunit RII alpha of cAMP-dependent protein kinase encodes an alternate amino-terminal region."
      Oyen O., Myklebust F., Scott J.D., Hansson V., Jahnsen T.
      FEBS Lett. 246:57-64(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Testis.
    2. "Molecular cloning, upstream sequence and promoter studies of the human gene for the regulatory subunit RII alpha of cAMP-dependent protein kinase."
      Foss K.B., Solberg R., Simard J., Myklebust F., Hansson V., Jahnsen T., Tasken K.
      Biochim. Biophys. Acta 1350:98-108(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-87.
    3. "Identification and characterization of myeloid translocation gene 16b as a novel a kinase anchoring protein in T lymphocytes."
      Schillace R.V., Andrews S.F., Liberty G.A., Davey M.P., Carr D.W.
      J. Immunol. 168:1590-1599(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBFA2T3.
    4. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Pituitary.
    6. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
      Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
      Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Prostate cancer.
    7. Cited for: INTERACTION WITH MYRIP.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-58; SER-78; SER-80 AND SER-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    12. "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].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-78; SER-80 AND SER-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-54; SER-58; SER-78 AND SER-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PJA2.
    18. "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-78 AND SER-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiKAP2_HUMAN
    AccessioniPrimary (citable) accession number: P13861
    Secondary accession number(s): Q16823
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 154 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 3
      Human chromosome 3: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3