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P31321

- KAP1_HUMAN

UniProt

P31321 - KAP1_HUMAN

Protein

cAMP-dependent protein kinase type I-beta regulatory subunit

Gene

PRKAR1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 4 (05 May 2009)
      Previous versions | rss
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    Functioni

    Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei202 – 2021cAMP 1
    Binding sitei211 – 2111cAMP 1
    Binding sitei326 – 3261cAMP 2
    Binding sitei335 – 3351cAMP 2

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi137 – 254118cAMP 1Add
    BLAST
    Nucleotide bindingi255 – 381127cAMP 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 kinase A catalytic subunit binding Source: BHF-UCL

    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. learning or memory Source: Ensembl
    10. negative regulation of cAMP-dependent protein kinase activity Source: BHF-UCL
    11. neurotrophin TRK receptor signaling pathway Source: Reactome
    12. protein phosphorylation Source: UniProtKB
    13. regulation of insulin secretion Source: Reactome
    14. signal transduction Source: Reactome
    15. small molecule metabolic process Source: Reactome
    16. transmembrane transport Source: Reactome
    17. 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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    cAMP-dependent protein kinase type I-beta regulatory subunit
    Gene namesi
    Name:PRKAR1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:9390. PRKAR1B.

    Subcellular locationi

    Cell membrane 1 Publication

    GO - Cellular componenti

    1. cAMP-dependent protein kinase complex Source: UniProtKB
    2. cytosol Source: Reactome
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33756.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 381380cAMP-dependent protein kinase type I-beta regulatory subunitPRO_0000205381Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineCurated
    Disulfide bondi18 – 18Interchain (with C-39)By similarity
    Modified residuei21 – 211Nitrated tyrosine1 Publication
    Disulfide bondi39 – 39Interchain (with C-18)By similarity
    Modified residuei77 – 771Phosphoserine1 Publication
    Modified residuei83 – 831Phosphoserine2 Publications

    Post-translational modificationi

    The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity.

    Keywords - PTMi

    Acetylation, Disulfide bond, Nitration, Phosphoprotein

    Proteomic databases

    MaxQBiP31321.
    PaxDbiP31321.
    PRIDEiP31321.

    PTM databases

    PhosphoSiteiP31321.

    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

    ArrayExpressiP31321.
    BgeeiP31321.
    CleanExiHS_PRKAR1B.
    GenevestigatoriP31321.

    Organism-specific databases

    HPAiHPA026719.

    Interactioni

    Subunit structurei

    The inactive holoenzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP releases the two active catalytic monomers and the regulatory dimer. Interacts with PRKX; regulates this cAMP-dependent protein kinase. Interacts with C2orf88/smAKAP; this interaction may target PRKAR1B to the plasma membrane.2 Publications

    Protein-protein interaction databases

    BioGridi111561. 14 interactions.
    IntActiP31321. 8 interactions.
    MINTiMINT-240609.
    STRINGi9606.ENSP00000353415.

    Structurei

    Secondary structure

    1
    381
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 246
    Turni27 – 315
    Helixi32 – 4110
    Helixi46 – 6823

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4DINX-ray3.70B1-381[»]
    4F9KX-ray2.80A/B/C/D11-73[»]
    ProteinModelPortaliP31321.
    SMRiP31321. Positions 14-380.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 136135Dimerization and phosphorylationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi96 – 1005Pseudophosphorylation motif

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0664.
    HOGENOMiHOG000196669.
    HOVERGENiHBG002025.
    InParanoidiP31321.
    KOiK04739.
    OMAiCKQIMAR.
    OrthoDBiEOG72JWG6.
    PhylomeDBiP31321.
    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.

    P31321-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASPPACPSE EDESLKGCEL YVQLHGIQQV LKDCIVHLCI SKPERPMKFL    50
    REHFEKLEKE ENRQILARQK SNSQSDSHDE EVSPTPPNPV VKARRRRGGV 100
    SAEVYTEEDA VSYVRKVIPK DYKTMTALAK AISKNVLFAH LDDNERSDIF 150
    DAMFPVTHIA GETVIQQGNE GDNFYVVDQG EVDVYVNGEW VTNISEGGSF 200
    GELALIYGTP RAATVKAKTD LKLWGIDRDS YRRILMGSTL RKRKMYEEFL 250
    SKVSILESLE KWERLTVADA LEPVQFEDGE KIVVQGEPGD DFYIITEGTA 300
    SVLQRRSPNE EYVEVGRLGP SDYFGEIALL LNRPRAATVV ARGPLKCVKL 350
    DRPRFERVLG PCSEILKRNI QRYNSFISLT V 381
    Length:381
    Mass (Da):43,073
    Last modified:May 5, 2009 - v4
    Checksum:i1ED7BFEC30897191
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti270 – 2701A → R in AAC37564. (PubMed:1708242)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M65066 mRNA. Translation: AAC37564.1.
    AK315951 mRNA. Translation: BAH14322.1.
    AK315990 mRNA. Translation: BAH14361.1.
    BC026734 mRNA. Translation: AAH26734.1.
    BC036828 mRNA. Translation: AAH36828.2.
    CCDSiCCDS34579.1.
    PIRiJH0392. OKHUR1.
    RefSeqiNP_001158230.1. NM_001164758.1.
    NP_001158231.1. NM_001164759.1.
    NP_001158232.1. NM_001164760.1.
    NP_001158233.1. NM_001164761.1.
    NP_001158234.1. NM_001164762.1.
    NP_002726.1. NM_002735.2.
    UniGeneiHs.520851.

    Genome annotation databases

    EnsembliENST00000360274; ENSP00000353415; ENSG00000188191.
    ENST00000403562; ENSP00000385349; ENSG00000188191.
    ENST00000406797; ENSP00000385749; ENSG00000188191.
    ENST00000537384; ENSP00000440449; ENSG00000188191.
    ENST00000544935; ENSP00000444487; ENSG00000188191.
    GeneIDi5575.
    KEGGihsa:5575.
    UCSCiuc003siu.2. human.

    Polymorphism databases

    DMDMi229463042.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M65066 mRNA. Translation: AAC37564.1 .
    AK315951 mRNA. Translation: BAH14322.1 .
    AK315990 mRNA. Translation: BAH14361.1 .
    BC026734 mRNA. Translation: AAH26734.1 .
    BC036828 mRNA. Translation: AAH36828.2 .
    CCDSi CCDS34579.1.
    PIRi JH0392. OKHUR1.
    RefSeqi NP_001158230.1. NM_001164758.1.
    NP_001158231.1. NM_001164759.1.
    NP_001158232.1. NM_001164760.1.
    NP_001158233.1. NM_001164761.1.
    NP_001158234.1. NM_001164762.1.
    NP_002726.1. NM_002735.2.
    UniGenei Hs.520851.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4DIN X-ray 3.70 B 1-381 [» ]
    4F9K X-ray 2.80 A/B/C/D 11-73 [» ]
    ProteinModelPortali P31321.
    SMRi P31321. Positions 14-380.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111561. 14 interactions.
    IntActi P31321. 8 interactions.
    MINTi MINT-240609.
    STRINGi 9606.ENSP00000353415.

    Chemistry

    BindingDBi P31321.

    PTM databases

    PhosphoSitei P31321.

    Polymorphism databases

    DMDMi 229463042.

    Proteomic databases

    MaxQBi P31321.
    PaxDbi P31321.
    PRIDEi P31321.

    Protocols and materials databases

    DNASUi 5575.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360274 ; ENSP00000353415 ; ENSG00000188191 .
    ENST00000403562 ; ENSP00000385349 ; ENSG00000188191 .
    ENST00000406797 ; ENSP00000385749 ; ENSG00000188191 .
    ENST00000537384 ; ENSP00000440449 ; ENSG00000188191 .
    ENST00000544935 ; ENSP00000444487 ; ENSG00000188191 .
    GeneIDi 5575.
    KEGGi hsa:5575.
    UCSCi uc003siu.2. human.

    Organism-specific databases

    CTDi 5575.
    GeneCardsi GC07M000588.
    HGNCi HGNC:9390. PRKAR1B.
    HPAi HPA026719.
    MIMi 176911. gene.
    neXtProti NX_P31321.
    PharmGKBi PA33756.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0664.
    HOGENOMi HOG000196669.
    HOVERGENi HBG002025.
    InParanoidi P31321.
    KOi K04739.
    OMAi CKQIMAR.
    OrthoDBi EOG72JWG6.
    PhylomeDBi P31321.
    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.

    Miscellaneous databases

    ChiTaRSi PRKAR1B. human.
    GeneWikii PRKAR1B.
    GenomeRNAii 5575.
    NextBioi 21612.
    PROi P31321.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P31321.
    Bgeei P31321.
    CleanExi HS_PRKAR1B.
    Genevestigatori P31321.

    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, cDNA structure and tissue-specific expression of the human regulatory subunit RI beta of cAMP-dependent protein kinases."
      Solberg R., Tasken K., Keiserud A., Jahnsen T.
      Biochem. Biophys. Res. Commun. 176:166-172(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Human regulatory subunit RI beta of cAMP-dependent protein kinases: expression, holoenzyme formation and microinjection into living cells."
      Solberg R., Tasken K., Wen W., Coghlan V.M., Meinkoth J.L., Scott J.D., Jahnsen T., Taylor S.S.
      Exp. Cell Res. 214:595-605(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 98-100.
      Tissue: Testis.
    3. "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: Amygdala and Brain.
    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].
      Tissue: Brain and Cervix.
    5. "Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry."
      Zhan X., Desiderio D.M.
      Anal. Biochem. 354:279-289(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Pituitary adenoma.
    6. "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.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "Regulation of cAMP-dependent protein kinases: the human protein kinase X (PrKX) reveals the role of the catalytic subunit alphaH-alphaI loop."
      Diskar M., Zenn H.M., Kaupisch A., Kaufholz M., Brockmeyer S., Sohmen D., Berrera M., Zaccolo M., Boshart M., Herberg F.W., Prinz A.
      J. Biol. Chem. 285:35910-35918(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PRKX.
    10. "A small novel A-kinase anchoring protein (AKAP) that localizes specifically protein kinase A-regulatory subunit I (PKA-RI) to the plasma membrane."
      Burgers P.P., Ma Y., Margarucci L., Mackey M., van der Heyden M.A., Ellisman M., Scholten A., Taylor S.S., Heck A.J.
      J. Biol. Chem. 287:43789-43797(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH C2ORF88/SMAKAP, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiKAP1_HUMAN
    AccessioniPrimary (citable) accession number: P31321
    Secondary accession number(s): Q8N422
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 140 of the entry and version 4 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 7
      Human chromosome 7: 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