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Q13976

- KGP1_HUMAN

UniProt

Q13976 - KGP1_HUMAN

Protein

cGMP-dependent protein kinase 1

Gene

PRKG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Serine/threonine protein kinase that acts as key mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but the contribution of each of these targets may vary substantially among cell types. Proteins that are phosphorylated by PRKG1 regulate platelet activation and adhesion, smooth muscle contraction, cardiac function, gene expression, feedback of the NO-signaling pathway, and other processes involved in several aspects of the CNS like axon guidance, hippocampal and cerebellar learning, circadian rhythm and nociception. Smooth muscle relaxation is mediated through lowering of intracellular free calcium, by desensitization of contractile proteins to calcium, and by decrease in the contractile state of smooth muscle or in platelet activation. Regulates intracellular calcium levels via several pathways: phosphorylates MRVI1/IRAG and inhibits IP3-induced Ca2+ release from intracellular stores, phosphorylation of KCNMA1 (BKCa) channels decreases intracellular Ca2+ levels, which leads to increased opening of this channel. PRKG1 phosphorylates the canonical transient receptor potential channel (TRPC) family which inactivates the associated inward calcium current. Another mode of action of NO/cGMP/PKGI signaling involves PKGI-mediated inactivation of the Ras homolog gene family member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of this protein in myriad processes: regulation of RHOA translocation; decreasing contraction; controlling vesicle trafficking, reduction of myosin light chain phosphorylation resulting in vasorelaxation. Activation of PRKG1 by NO signaling alters also gene expression in a number of tissues. In smooth muscle cells, increased cGMP and PRKG1 activity influence expression of smooth muscle-specific contractile proteins, levels of proteins in the NO/cGMP signaling pathway, down-regulation of the matrix proteins osteopontin and thrombospondin-1 to limit smooth muscle cell migration and phenotype. Regulates vasodilator-stimulated phosphoprotein (VASP) functions in platelets and smooth muscle.8 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    In the absence of cGMP, PRKG1 activity is suppressed by autoinhibitory contacts.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei390 – 3901ATPPROSITE-ProRule annotation
    Active sitei484 – 4841Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi167 – 1704cAMP or cGMP
    Nucleotide bindingi177 – 1782cAMP or cGMP
    Nucleotide bindingi366 – 3749ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium channel regulator activity Source: UniProtKB
    3. cGMP binding Source: UniProtKB-KW
    4. cGMP-dependent protein kinase activity Source: UniProtKB
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: ProtInc
    2. blood coagulation Source: Reactome
    3. dendrite development Source: Ensembl
    4. forebrain development Source: Ensembl
    5. negative regulation of platelet aggregation Source: UniProtKB
    6. neuron migration Source: Ensembl
    7. protein phosphorylation Source: ProtInc
    8. regulation of GTPase activity Source: UniProtKB
    9. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, cGMP, cGMP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.12. 2681.
    ReactomeiREACT_172761. Ca2+ pathway.
    REACT_23767. cGMP effects.
    REACT_23898. Rap1 signalling.
    SignaLinkiQ13976.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    cGMP-dependent protein kinase 1 (EC:2.7.11.12)
    Short name:
    cGK 1
    Short name:
    cGK1
    Alternative name(s):
    cGMP-dependent protein kinase I
    Short name:
    cGKI
    Gene namesi
    Name:PRKG1
    Synonyms:PRKG1B, PRKGR1A, PRKGR1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:9414. PRKG1.

    Subcellular locationi

    Cytoplasm By similarity
    Note: Colocalized with TRPC7 in the plasma membrane.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. Golgi apparatus Source: Ensembl
    4. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Aortic aneurysm, familial thoracic 8 (AAT8) [MIM:615436]: A disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti177 – 1771R → Q in AAT8; impairs cGMP binding; the mutant protein is constitutively active. 1 Publication
    VAR_070434

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi12 – 121L → A: Loss of binding to PPP1R12A. 1 Publication
    Mutagenesisi19 – 191I → A: Loss of binding to PPP1R12A. 1 Publication
    Mutagenesisi26 – 261L → P: Loss of binding to PPP1R12A. 1 Publication
    Mutagenesisi33 – 331I → A: Loss of binding to PPP1R12A. 1 Publication
    Mutagenesisi40 – 401L → A: Loss of binding to PPP1R12A. 1 Publication

    Keywords - Diseasei

    Aortic aneurysm, Disease mutation

    Organism-specific databases

    MIMi615436. phenotype.
    Orphaneti91387. Familial thoracic aortic aneurysm and aortic dissection.
    PharmGKBiPA33777.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 671670cGMP-dependent protein kinase 1PRO_0000086115Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Disulfide bondi43 – 43InterchainBy similarity
    Modified residuei59 – 591Phosphothreonine; by autocatalysisBy similarity

    Post-translational modificationi

    Autophosphorylation increases kinase activity.
    65 kDa monomer is produced by proteolytic cleavage.By similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ13976.
    PaxDbiQ13976.
    PRIDEiQ13976.

    PTM databases

    PhosphoSiteiQ13976.

    Expressioni

    Tissue specificityi

    Primarily expressed in lung and placenta.1 Publication

    Gene expression databases

    ArrayExpressiQ13976.
    BgeeiQ13976.
    CleanExiHS_PRKG1.
    GenevestigatoriQ13976.

    Organism-specific databases

    HPAiCAB009629.
    HPA007699.

    Interactioni

    Subunit structurei

    Isoform alpha: parallel homodimer or heterodimer and also heterotetramer. Interacts directly with PPP1R12A. Non-covalent dimer of dimer of PRKG1-PRKG1 and PPP1R12A-PPP1R12A. This interaction targets PRKG1 to stress fibers to mediate smooth muscle cell relaxation and vasodilation in responses to rises in cGMP. Isoform beta: antiparallel homodimer. Part of cGMP kinase signaling complex at least composed of ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and ITPR1 By similarity. Interacts with MRVI1. Forms a stable complex with ITPR1, MRVI1, and isoform beta of PRKG1. Interacts with TRPC7 (via ankyrin repeat domain). Isoform alpha interacts with RGS2. Interacts with GTF2I.By similarity9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BMPR2Q138732EBI-3952014,EBI-527196

    Protein-protein interaction databases

    BioGridi111578. 17 interactions.
    DIPiDIP-46288N.
    IntActiQ13976. 2 interactions.
    MINTiMINT-121708.
    STRINGi9606.ENSP00000363092.

    Structurei

    Secondary structure

    1
    671
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 4334
    Helixi90 – 10011
    Turni102 – 1065
    Helixi109 – 11810
    Beta strandi120 – 1245
    Beta strandi129 – 1313
    Beta strandi139 – 1457
    Beta strandi148 – 1525
    Beta strandi155 – 1606
    Beta strandi165 – 1673
    Helixi169 – 1735
    Beta strandi174 – 1763
    Beta strandi178 – 1858
    Beta strandi187 – 1937
    Helixi194 – 2018
    Helixi209 – 2168
    Helixi220 – 2234
    Helixi227 – 23610
    Beta strandi238 – 2425
    Beta strandi247 – 2493
    Beta strandi257 – 2648
    Beta strandi266 – 2705
    Beta strandi274 – 2763
    Beta strandi279 – 2846
    Helixi293 – 2953
    Beta strandi296 – 2983
    Beta strandi303 – 31715
    Helixi318 – 3247
    Turni325 – 3273
    Helixi329 – 3324

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZXANMR-A/B2-59[»]
    3NMDX-ray2.27A/B/C/D/E4-55[»]
    3OCPX-ray2.49A/B90-212[»]
    3OD0X-ray2.90A/B90-212[»]
    3OGJX-ray2.75A/B/C/D90-212[»]
    4KU7X-ray1.65A204-354[»]
    4KU8X-ray1.99A/B/C204-354[»]
    ProteinModelPortaliQ13976.
    SMRiQ13976. Positions 9-44, 60-655.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13976.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini360 – 619260Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini620 – 67152AGC-kinase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 102101Required for dimerizationAdd
    BLAST
    Regioni9 – 4436Leucine-zipperAdd
    BLAST
    Regioni50 – 7526Autoinhibitory domainBy similarityAdd
    BLAST
    Regioni103 – 220118cGMP-binding, high affinityAdd
    BLAST
    Regioni221 – 341121cGMP-binding, low affinityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili2 – 59581 PublicationAdd
    BLAST

    Domaini

    Composed of an N-terminal leucine-zipper domain followed by an autoinhibitory domain, which mediate homodimer formation and inhibit kinase activity, respectively. Next, two cGMP-binding domains are followed by the catalytic domain at the C-terminus. Binding of cGMP to cGMP-binding domains results in a conformational change that activates kinase activity by removing the autoinhibitory domain from the catalytic cleft leaving the catalytic domain free to phosphorylate downstream substrates. Isoforms alpha and beta have identical cGMP-binding and catalytic domains but differ in their leucine zipper and autoinhibitory sequences and therefore differ in their dimerization substrates and kinase enzyme activity.
    Heterotetramerization is mediated by the interaction between a coiled-coil of PRKG1 and the leucine/isoleucine zipper of PPP1R12A/MBS, the myosin-binding subunit of the myosin phosphatase.

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 2 cyclic nucleotide-binding domains.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233033.
    HOVERGENiHBG006211.
    InParanoidiP14619.
    KOiK07376.
    OMAiHQDLSRQ.
    PhylomeDBiQ13976.
    TreeFamiTF313261.

    Family and domain databases

    Gene3Di2.60.120.10. 2 hits.
    InterProiIPR000961. AGC-kinase_C.
    IPR016232. cGMP-dependent_protein_kinase.
    IPR002374. cGMP_dep_kinase.
    IPR018490. cNMP-bd-like.
    IPR018488. cNMP-bd_CS.
    IPR000595. cNMP-bd_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR014710. RmlC-like_jellyroll.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00027. cNMP_binding. 2 hits.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000559. cGMP-dep_kinase. 1 hit.
    PRINTSiPR00104. CGMPKINASE.
    SMARTiSM00100. cNMP. 2 hits.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF51206. SSF51206. 2 hits.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS00888. CNMP_BINDING_1. 2 hits.
    PS00889. CNMP_BINDING_2. 2 hits.
    PS50042. CNMP_BINDING_3. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform Alpha (identifier: Q13976-1) [UniParc]FASTAAdd to Basket

    Also known as: CGK1-alpha

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSELEEDFAK ILMLKEERIK ELEKRLSEKE EEIQELKRKL HKCQSVLPVP    50
    STHIGPRTTR AQGISAEPQT YRSFHDLRQA FRKFTKSERS KDLIKEAILD 100
    NDFMKNLELS QIQEIVDCMY PVEYGKDSCI IKEGDVGSLV YVMEDGKVEV 150
    TKEGVKLCTM GPGKVFGELA ILYNCTRTAT VKTLVNVKLW AIDRQCFQTI 200
    MMRTGLIKHT EYMEFLKSVP TFQSLPEEIL SKLADVLEET HYENGEYIIR 250
    QGARGDTFFI ISKGTVNVTR EDSPSEDPVF LRTLGKGDWF GEKALQGEDV 300
    RTANVIAAEA VTCLVIDRDS FKHLIGGLDD VSNKAYEDAE AKAKYEAEAA 350
    FFANLKLSDF NIIDTLGVGG FGRVELVQLK SEESKTFAMK ILKKRHIVDT 400
    RQQEHIRSEK QIMQGAHSDF IVRLYRTFKD SKYLYMLMEA CLGGELWTIL 450
    RDRGSFEDST TRFYTACVVE AFAYLHSKGI IYRDLKPENL ILDHRGYAKL 500
    VDFGFAKKIG FGKKTWTFCG TPEYVAPEII LNKGHDISAD YWSLGILMYE 550
    LLTGSPPFSG PDPMKTYNII LRGIDMIEFP KKIAKNAANL IKKLCRDNPS 600
    ERLGNLKNGV KDIQKHKWFE GFNWEGLRKG TLTPPIIPSV ASPTDTSNFD 650
    SFPEDNDEPP PDDNSGWDID F 671
    Length:671
    Mass (Da):76,364
    Last modified:January 23, 2007 - v3
    Checksum:i51389502A5E5FBD2
    GO
    Isoform Beta (identifier: Q13976-2) [UniParc] [UniParc]FASTAAdd to Basket

    Also known as: CGK1-beta

    The sequence of this isoform differs from the canonical sequence as follows:
         2-89: SELEEDFAKI...AFRKFTKSER → MGTLRDLQYA...TLPFYPKSPQ

    Show »
    Length:687
    Mass (Da):77,935
    Checksum:i7A59FA64EE85C0C3
    GO
    Isoform 3 (identifier: Q13976-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-15: MSELEEDFAKILMLK → MEKQNMFLHGSYILR
         16-297: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:389
    Mass (Da):44,185
    Checksum:i9792149F93773D55
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti177 – 1771R → Q in AAT8; impairs cGMP binding; the mutant protein is constitutively active. 1 Publication
    VAR_070434
    Natural varianti249 – 2491I → V.1 Publication
    Corresponds to variant rs56082459 [ dbSNP | Ensembl ].
    VAR_046773
    Natural varianti267 – 2671N → S.1 Publication
    Corresponds to variant rs34997494 [ dbSNP | Ensembl ].
    VAR_051632
    Natural varianti474 – 4741Y → F.1 Publication
    VAR_070435
    Natural varianti666 – 6661G → A.1 Publication
    VAR_070436

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1515MSELE…ILMLK → MEKQNMFLHGSYILR in isoform 3. 1 PublicationVSP_055541Add
    BLAST
    Alternative sequencei2 – 8988SELEE…TKSER → MGTLRDLQYALQEKIEELRQ RDALIDELELELDQKDELIQ KLQNELDKYRSVIRPATQQA QKQSASTLQGEPRTKRQAIS AEPTAFDIQDLSHVTLPFYP KSPQ in isoform Beta. 3 PublicationsVSP_038714Add
    BLAST
    Alternative sequencei16 – 297282Missing in isoform 3. 1 PublicationVSP_055542Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y07512 mRNA. Translation: CAA68810.1.
    D45864 mRNA. Translation: BAA08297.1.
    AK093436 mRNA. Translation: BAG52715.1.
    EF560730 mRNA. Translation: ABQ59040.1.
    Z92867
    , Z92869, Z92870, Z92871, Z92872, Z92873, Z92874, Z92875, Z92876, Z92877, Z92878, Z92879, Z92880, Z92881, Z92882, Z92883, Z92884, Z92885 Genomic DNA. Translation: CAB07436.1.
    Z92868
    , Z92869, Z92870, Z92871, Z92872, Z92873, Z92874, Z92875, Z92876, Z92877, Z92878, Z92879, Z92880, Z92881, Z92882, Z92883, Z92884, Z92885 Genomic DNA. Translation: CAB07437.1.
    AL391378
    , AC009986, AC022537, AC022025, AC027118, AL731537, AL928686, AL157399, AC026228 Genomic DNA. Translation: CAI39626.1.
    AL928686
    , AC009986, AC022537, AL731537, AL391378, AL157399, AC027118, AC026228, AC022025 Genomic DNA. Translation: CAI40743.1.
    AL157399
    , AC022025, AC009986, AL928686, AL731537, AL391378, AC027118, AC026228, AC022537 Genomic DNA. Translation: CAI41305.1.
    AL731537
    , AL928686, AL391378, AL157399, AC027118, AC026228, AC022537, AC022025, AC009986 Genomic DNA. Translation: CAI17115.1.
    AC068062 Genomic DNA. No translation available.
    AC069079 Genomic DNA. No translation available.
    AC073584 Genomic DNA. No translation available.
    AL596105 Genomic DNA. No translation available.
    AL607031 Genomic DNA. No translation available.
    CH471083 Genomic DNA. Translation: EAW54140.1.
    BC062688 mRNA. Translation: AAH62688.1.
    BC127090 mRNA. Translation: AAI27091.1.
    CCDSiCCDS44399.1. [Q13976-1]
    PIRiS05702.
    RefSeqiNP_001091982.1. NM_001098512.2. [Q13976-1]
    NP_006249.1. NM_006258.3.
    UniGeneiHs.407535.

    Genome annotation databases

    EnsembliENST00000373975; ENSP00000363086; ENSG00000185532. [Q13976-3]
    ENST00000373980; ENSP00000363092; ENSG00000185532. [Q13976-2]
    ENST00000401604; ENSP00000384200; ENSG00000185532. [Q13976-1]
    GeneIDi5592.
    KEGGihsa:5592.
    UCSCiuc001jjm.3. human. [Q13976-1]
    uc001jjo.3. human. [Q13976-2]

    Polymorphism databases

    DMDMi6225588.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y07512 mRNA. Translation: CAA68810.1 .
    D45864 mRNA. Translation: BAA08297.1 .
    AK093436 mRNA. Translation: BAG52715.1 .
    EF560730 mRNA. Translation: ABQ59040.1 .
    Z92867
    , Z92869 , Z92870 , Z92871 , Z92872 , Z92873 , Z92874 , Z92875 , Z92876 , Z92877 , Z92878 , Z92879 , Z92880 , Z92881 , Z92882 , Z92883 , Z92884 , Z92885 Genomic DNA. Translation: CAB07436.1 .
    Z92868
    , Z92869 , Z92870 , Z92871 , Z92872 , Z92873 , Z92874 , Z92875 , Z92876 , Z92877 , Z92878 , Z92879 , Z92880 , Z92881 , Z92882 , Z92883 , Z92884 , Z92885 Genomic DNA. Translation: CAB07437.1 .
    AL391378
    , AC009986 , AC022537 , AC022025 , AC027118 , AL731537 , AL928686 , AL157399 , AC026228 Genomic DNA. Translation: CAI39626.1 .
    AL928686
    , AC009986 , AC022537 , AL731537 , AL391378 , AL157399 , AC027118 , AC026228 , AC022025 Genomic DNA. Translation: CAI40743.1 .
    AL157399
    , AC022025 , AC009986 , AL928686 , AL731537 , AL391378 , AC027118 , AC026228 , AC022537 Genomic DNA. Translation: CAI41305.1 .
    AL731537
    , AL928686 , AL391378 , AL157399 , AC027118 , AC026228 , AC022537 , AC022025 , AC009986 Genomic DNA. Translation: CAI17115.1 .
    AC068062 Genomic DNA. No translation available.
    AC069079 Genomic DNA. No translation available.
    AC073584 Genomic DNA. No translation available.
    AL596105 Genomic DNA. No translation available.
    AL607031 Genomic DNA. No translation available.
    CH471083 Genomic DNA. Translation: EAW54140.1 .
    BC062688 mRNA. Translation: AAH62688.1 .
    BC127090 mRNA. Translation: AAI27091.1 .
    CCDSi CCDS44399.1. [Q13976-1 ]
    PIRi S05702.
    RefSeqi NP_001091982.1. NM_001098512.2. [Q13976-1 ]
    NP_006249.1. NM_006258.3.
    UniGenei Hs.407535.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZXA NMR - A/B 2-59 [» ]
    3NMD X-ray 2.27 A/B/C/D/E 4-55 [» ]
    3OCP X-ray 2.49 A/B 90-212 [» ]
    3OD0 X-ray 2.90 A/B 90-212 [» ]
    3OGJ X-ray 2.75 A/B/C/D 90-212 [» ]
    4KU7 X-ray 1.65 A 204-354 [» ]
    4KU8 X-ray 1.99 A/B/C 204-354 [» ]
    ProteinModelPortali Q13976.
    SMRi Q13976. Positions 9-44, 60-655.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111578. 17 interactions.
    DIPi DIP-46288N.
    IntActi Q13976. 2 interactions.
    MINTi MINT-121708.
    STRINGi 9606.ENSP00000363092.

    Chemistry

    BindingDBi Q13976.
    ChEMBLi CHEMBL4273.
    GuidetoPHARMACOLOGYi 1492.

    PTM databases

    PhosphoSitei Q13976.

    Polymorphism databases

    DMDMi 6225588.

    Proteomic databases

    MaxQBi Q13976.
    PaxDbi Q13976.
    PRIDEi Q13976.

    Protocols and materials databases

    DNASUi 5592.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373975 ; ENSP00000363086 ; ENSG00000185532 . [Q13976-3 ]
    ENST00000373980 ; ENSP00000363092 ; ENSG00000185532 . [Q13976-2 ]
    ENST00000401604 ; ENSP00000384200 ; ENSG00000185532 . [Q13976-1 ]
    GeneIDi 5592.
    KEGGi hsa:5592.
    UCSCi uc001jjm.3. human. [Q13976-1 ]
    uc001jjo.3. human. [Q13976-2 ]

    Organism-specific databases

    CTDi 5592.
    GeneCardsi GC10P052751.
    HGNCi HGNC:9414. PRKG1.
    HPAi CAB009629.
    HPA007699.
    MIMi 176894. gene.
    615436. phenotype.
    neXtProti NX_Q13976.
    Orphaneti 91387. Familial thoracic aortic aneurysm and aortic dissection.
    PharmGKBi PA33777.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233033.
    HOVERGENi HBG006211.
    InParanoidi P14619.
    KOi K07376.
    OMAi HQDLSRQ.
    PhylomeDBi Q13976.
    TreeFami TF313261.

    Enzyme and pathway databases

    BRENDAi 2.7.11.12. 2681.
    Reactomei REACT_172761. Ca2+ pathway.
    REACT_23767. cGMP effects.
    REACT_23898. Rap1 signalling.
    SignaLinki Q13976.

    Miscellaneous databases

    ChiTaRSi PRKG1. human.
    EvolutionaryTracei Q13976.
    GeneWikii PRKG1.
    GenomeRNAii 5592.
    NextBioi 21698.
    PROi Q13976.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13976.
    Bgeei Q13976.
    CleanExi HS_PRKG1.
    Genevestigatori Q13976.

    Family and domain databases

    Gene3Di 2.60.120.10. 2 hits.
    InterProi IPR000961. AGC-kinase_C.
    IPR016232. cGMP-dependent_protein_kinase.
    IPR002374. cGMP_dep_kinase.
    IPR018490. cNMP-bd-like.
    IPR018488. cNMP-bd_CS.
    IPR000595. cNMP-bd_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR014710. RmlC-like_jellyroll.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00027. cNMP_binding. 2 hits.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000559. cGMP-dep_kinase. 1 hit.
    PRINTSi PR00104. CGMPKINASE.
    SMARTi SM00100. cNMP. 2 hits.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51206. SSF51206. 2 hits.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS00888. CNMP_BINDING_1. 2 hits.
    PS00889. CNMP_BINDING_2. 2 hits.
    PS50042. CNMP_BINDING_3. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and predicted full-length amino acid sequence of the type I beta isozyme of cGMP-dependent protein kinase from human placenta. Tissue distribution and developmental changes in rat."
      Sandberg M., Natarajan V., Ronander I., Kalderon D., Walter U., Lohmann S.M., Jahnsen T.
      FEBS Lett. 255:321-329(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
      Tissue: Placenta.
    2. Sandberg M.
      Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "cDNA cloning and gene expression of human type Ialpha cGMP-dependent protein kinase."
      Tamura N., Itoh H., Ogawa Y., Nakagawa O., Harada M., Chun T., Suga S., Yoshimasa T., Nakao K.
      Hypertension 27:552-557(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
      Tissue: Lung.
    4. "Characterization of the human gene encoding the type I alpha and type I beta cGMP-dependent protein kinase (PRKG1)."
      Orstavik S., Natarajan V., Tasken K., Jahnsen T., Sandberg M.
      Genomics 42:311-318(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    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] (ISOFORM 3).
      Tissue: Testis.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
      Tissue: Cervix.
    7. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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] (ISOFORM BETA).
    10. "cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets."
      Butt E., Abel K., Krieger M., Palm D., Hoppe V., Hoppe J., Walter U.
      J. Biol. Chem. 269:14509-14517(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF VASP.
    11. "Regulation of myosin phosphatase by a specific interaction with cGMP-dependent protein kinase Ialpha."
      Surks H.K., Mochizuki N., Kasai Y., Georgescu S.P., Tang K.M., Ito M., Lincoln T.M., Mendelsohn M.E.
      Science 286:1583-1587(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R12A, SUBUNIT, MUTAGENESIS OF LEU-12; ILE-19; LEU-26; ILE-33 AND LEU-40, FUNCTION.
    12. Cited for: FUNCTION IN PHOSPHORYLATION OF RHOA.
    13. "cGMP-dependent protein kinase I beta physically and functionally interacts with the transcriptional regulator TFII-I."
      Casteel D.E., Zhuang S., Gudi T., Tang J., Vuica M., Desiderio S., Pilz R.B.
      J. Biol. Chem. 277:32003-32014(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF GTF2I, INTERACTION WITH GTF2I.
    14. "Regulation of cGMP-specific phosphodiesterase (PDE5) phosphorylation in smooth muscle cells."
      Rybalkin S.D., Rybalkina I.G., Feil R., Hofmann F., Beavo J.A.
      J. Biol. Chem. 277:3310-3317(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PDE5.
    15. "Regulator of G-protein signaling-2 mediates vascular smooth muscle relaxation and blood pressure."
      Tang K.M., Wang G.R., Lu P., Karas R.H., Aronovitz M., Heximer S.P., Kaltenbronn K.M., Blumer K.J., Siderovski D.P., Zhu Y., Mendelsohn M.E.
      Nat. Med. 9:1506-1512(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF RGS2, INTERACTION WITH RGS2.
    16. "Smooth muscle phosphatase is regulated in vivo by exclusion of phosphorylation of threonine 696 of MYPT1 by phosphorylation of Serine 695 in response to cyclic nucleotides."
      Wooldridge A.A., MacDonald J.A., Erdodi F., Ma C., Borman M.A., Hartshorne D.J., Haystead T.A.J.
      J. Biol. Chem. 279:34496-34504(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation and thrombus formation."
      Antl M., von Bruehl M.-L., Eiglsperger C., Werner M., Konrad I., Kocher T., Wilm M., Hofmann F., Massberg S., Schlossmann J.
      Blood 109:552-559(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE INHIBITION OF PLATELET AGGREGATION, FUNCTION IN PHOSPHORYLATION OF MRVI1, SUBCELLULAR LOCATION, INTERACTION WITH MRVI1 AND ITPR1.
    18. "Interactions between the leucine-zipper motif of cGMP-dependent protein kinase and the C-terminal region of the targeting subunit of myosin light chain phosphatase."
      Lee E., Hayes D.B., Langsetmo K., Sundberg E.J., Tao T.C.
      J. Mol. Biol. 373:1198-1212(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R12A.
    19. "Probing the interaction between the coiled coil leucine zipper of cGMP-dependent protein kinase Ialpha and the C terminus of the myosin binding subunit of the myosin light chain phosphatase."
      Sharma A.K., Zhou G.-P., Kupferman J., Surks H.K., Christensen E.N., Chou J.J., Mendelsohn M.E., Rigby A.C.
      J. Biol. Chem. 283:32860-32869(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R12A, SUBUNIT.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "cGMP-dependent protein kinases and cGMP phosphodiesterases in nitric oxide and cGMP action."
      Francis S.H., Busch J.L., Corbin J.D., Sibley D.
      Pharmacol. Rev. 62:525-563(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Functional regulation of transient receptor potential canonical 7 by cGMP-dependent protein kinase Ialpha."
      Yuasa K., Matsuda T., Tsuji A.
      Cell. Signal. 23:1179-1187(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM ALPHA) IN PHOSPHORYLATION OF TRPC7, INTERACTION WITH TRPC7, SUBCELLULAR LOCATION.
    24. "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].
    25. "Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Ialpha."
      Schnell J.R., Zhou G.-P., Zweckstetter M., Rigby A.C., Chou J.J.
      Protein Sci. 14:2421-2428(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2-58, INTERACTION WITH PPP1R12A, SUBUNIT, COILED-COIL.
    26. "A crystal structure of the cyclic GMP-dependent protein kinase I{beta} dimerization/docking domain reveals molecular details of isoform-specific anchoring."
      Casteel D.E., Smith-Nguyen E.V., Sankaran B., Roh S.H., Pilz R.B., Kim C.
      J. Biol. Chem. 285:32684-32688(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 4-55 (ISOFORM BETA), SUBUNIT.
    27. "Co-crystal structures of PKG Ibeta (92-227) with cGMP and cAMP reveal the molecular details of cyclic-nucleotide binding."
      Kim J.J., Casteel D.E., Huang G., Kwon T.H., Ren R.K., Zwart P., Headd J.J., Brown N.G., Chow D.C., Palzkill T., Kim C.
      PLoS ONE 6:E18413-E18413(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 92-227 (ISOFORM BETA) IN COMPLEX WITH CGMP AND CAMP.
    28. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-249 AND SER-267.
    29. Cited for: VARIANT AAT8 GLN-177, VARIANTS PHE-474 AND ALA-666, CHARACTERIZATION OF VARIANT AAT8 GLN-177.

    Entry informationi

    Entry nameiKGP1_HUMAN
    AccessioniPrimary (citable) accession number: Q13976
    Secondary accession number(s): A5YM56
    , B3KSF3, E2PU10, P14619, Q5JP05, Q5JSJ6, Q6P5T7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 146 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

    3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3