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Q04759

- KPCT_HUMAN

UniProt

Q04759 - KPCT_HUMAN

Protein

Protein kinase C theta type

Gene

PRKCQ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 3 (27 Mar 2002)
      Previous versions | rss
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    Functioni

    Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that mediates non-redundant functions in T-cell receptor (TCR) signaling, including T-cells activation, proliferation, differentiation and survival, by mediating activation of multiple transcription factors such as NF-kappa-B, JUN, NFATC1 and NFATC2. In TCR-CD3/CD28-co-stimulated T-cells, is required for the activation of NF-kappa-B and JUN, which in turn are essential for IL2 production, and participates to the calcium-dependent NFATC1 and NFATC2 transactivation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11 on several serine residues, inducing CARD11 association with lipid rafts and recruitment of the BCL10-MALT1 complex, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. May also play an indirect role in activation of the non-canonical NF-kappa-B (NFKB2) pathway. In the signaling pathway leading to JUN activation, acts by phosphorylating the mediator STK39/SPAK and may not act through MAP kinases signaling. Plays a critical role in TCR/CD28-induced NFATC1 and NFATC2 transactivation by participating in the regulation of reduced inositol 1,4,5-trisphosphate generation and intracellular calcium mobilization. After costimulation of T-cells through CD28 can phosphorylate CBLB and is required for the ubiquitination and subsequent degradation of CBLB, which is a prerequisite for the activation of TCR. During T-cells differentiation, plays an important role in the development of T-helper 2 (Th2) cells following immune and inflammatory responses, and, in the development of inflammatory autoimmune diseases, is necessary for the activation of IL17-producing Th17 cells. May play a minor role in Th1 response. Upon TCR stimulation, mediates T-cell protective survival signal by phosphorylating BAD, thus protecting T-cells from BAD-induced apoptosis, and by up-regulating BCL-X(L)/BCL2L1 levels through NF-kappa-B and JUN pathways. In platelets, regulates signal transduction downstream of the ITGA2B, CD36/GP4, F2R/PAR1 and F2RL3/PAR4 receptors, playing a positive role in 'outside-in' signaling and granule secretion signal transduction. May relay signals from the activated ITGA2B receptor by regulating the uncoupling of WASP and WIPF1, thereby permitting the regulation of actin filament nucleation and branching activity of the Arp2/3 complex. May mediate inhibitory effects of free fatty acids on insulin signaling by phosphorylating IRS1, which in turn blocks IRS1 tyrosine phosphorylation and downstream activation of the PI3K/AKT pathway. Phosphorylates MSN (moesin) in the presence of phosphatidylglycerol or phosphatidylinositol. Phosphorylates PDPK1 at 'Ser-504' and 'Ser-532' and negatively regulates its ability to phosphorylate PKB/AKT1.8 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are calcium-insensitive, but activated by diacylglycerol (DAG) and phosphatidylserine. Three specific sites; Thr-538 (activation loop of the kinase domain), Ser-676 (turn motif) and Ser-695 (hydrophobic region), need to be phosphorylated for its full activation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei409 – 4091ATP
    Active sitei504 – 5041Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri159 – 20951Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri231 – 28151Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi386 – 3949ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. protein kinase C activity Source: UniProtKB-EC
    5. protein serine/threonine kinase activity Source: UniProtKB
    6. ubiquitin-protein transferase activity Source: Reactome

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. axon guidance Source: Reactome
    3. blood coagulation Source: Reactome
    4. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    5. Fc-epsilon receptor signaling pathway Source: Reactome
    6. inflammatory response Source: UniProtKB-KW
    7. innate immune response Source: Reactome
    8. intracellular signal transduction Source: UniProtKB
    9. membrane protein ectodomain proteolysis Source: BHF-UCL
    10. negative regulation of insulin receptor signaling pathway Source: UniProtKB
    11. negative regulation of T cell apoptotic process Source: UniProtKB
    12. phototransduction, visible light Source: Reactome
    13. platelet activation Source: Reactome
    14. positive regulation of interleukin-17 production Source: UniProtKB
    15. positive regulation of interleukin-2 biosynthetic process Source: Ensembl
    16. positive regulation of interleukin-4 production Source: UniProtKB
    17. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    18. positive regulation of T cell activation Source: UniProtKB
    19. positive regulation of T cell proliferation Source: Ensembl
    20. positive regulation of T-helper 17 type immune response Source: UniProtKB
    21. positive regulation of T-helper 2 cell activation Source: UniProtKB
    22. protein ubiquitination Source: GOC
    23. regulation of cell growth Source: UniProtKB
    24. regulation of platelet aggregation Source: UniProtKB
    25. regulation of rhodopsin mediated signaling pathway Source: Reactome
    26. regulation of transcription, DNA-templated Source: UniProtKB
    27. rhodopsin mediated signaling pathway Source: Reactome
    28. T cell receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Immunity, Inflammatory response

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BRENDAi2.7.11.13. 2681.
    ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
    REACT_12555. Downstream TCR signaling.
    REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
    REACT_163994. FCERI mediated NF-kB activation.
    REACT_19333. G alpha (z) signalling events.
    REACT_2202. Effects of PIP2 hydrolysis.
    REACT_22237. Netrin-1 signaling.
    SignaLinkiQ04759.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein kinase C theta type (EC:2.7.11.13)
    Alternative name(s):
    nPKC-theta
    Gene namesi
    Name:PRKCQ
    Synonyms:PRKCT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:9410. PRKCQ.

    Subcellular locationi

    Cytoplasm. Cell membrane; Peripheral membrane protein
    Note: In resting T-cells, mostly localized in cytoplasm. In response to TCR stimulation, associates with lipid rafts and then localizes in the immunological synapse.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. immunological synapse Source: Ensembl
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi90 – 901Y → F: Loss of function in T-cells proliferation. No effect on kinase activity. 1 Publication
    Mutagenesisi148 – 1481A → E: Constitutively active form. 1 Publication
    Mutagenesisi219 – 2191T → A: Loss of transactivation of the IL2 promoter and translocation to the plasma membrane. No effect on kinase activity. 1 Publication
    Mutagenesisi409 – 4091K → A or E: Loss of kinase activity. 1 Publication
    Mutagenesisi538 – 5381T → A: Loss of kinase activity. 2 Publications
    Mutagenesisi676 – 6761S → A: Reduction in kinase activity. 1 Publication
    Mutagenesisi695 – 6951S → A: Reduction in kinase activity. 2 Publications

    Organism-specific databases

    PharmGKBiPA33773.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 706706Protein kinase C theta typePRO_0000055708Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei90 – 901Phosphotyrosine; by LCK1 Publication
    Modified residuei219 – 2191Phosphothreonine; by autocatalysis1 Publication
    Modified residuei348 – 3481Phosphoserine1 Publication
    Modified residuei538 – 5381Phosphothreonine; by PDPK13 Publications
    Modified residuei676 – 6761Phosphoserine4 Publications
    Modified residuei685 – 6851Phosphoserine3 Publications
    Modified residuei695 – 6951Phosphoserine7 Publications

    Post-translational modificationi

    Autophosphorylation at Thr-219 is required for targeting to the TCR and cellular function of PRKCQ upon antigen receptor ligation. Following TCR stimulation, phosphorylated at Tyr-90 and Ser-685.9 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ04759.
    PaxDbiQ04759.
    PRIDEiQ04759.

    PTM databases

    PhosphoSiteiQ04759.

    Miscellaneous databases

    PMAP-CutDBQ04759.

    Expressioni

    Tissue specificityi

    Expressed in skeletal muscle, T-cells, megakaryoblastic cells and platelets.1 Publication

    Gene expression databases

    ArrayExpressiQ04759.
    BgeeiQ04759.
    CleanExiHS_PRKCQ.
    GenevestigatoriQ04759.

    Interactioni

    Subunit structurei

    Interacts with GLRX3 (via N-terminus). Interacts with ECT2. Part of a lipid raft complex composed at least of BCL10, CARD11, MALT1 and IKBKB.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BTKQ061872EBI-374762,EBI-624835
    FYNP062417EBI-374762,EBI-515315
    GLRX3O760035EBI-374762,EBI-374781
    HSF1Q006132EBI-374762,EBI-719620
    Irs1P355702EBI-374762,EBI-520230From a different organism.
    LCKP062392EBI-374762,EBI-1348
    MAP4K3Q8IVH84EBI-374762,EBI-1758170
    PRKCZQ055133EBI-374762,EBI-295351

    Protein-protein interaction databases

    BioGridi111574. 27 interactions.
    IntActiQ04759. 18 interactions.
    MINTiMINT-4649766.
    STRINGi9606.ENSP00000263125.

    Structurei

    Secondary structure

    1
    706
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 139
    Beta strandi28 – 3912
    Beta strandi42 – 5211
    Beta strandi56 – 627
    Beta strandi69 – 757
    Beta strandi83 – 897
    Helixi90 – 989
    Turni99 – 1013
    Beta strandi103 – 1086
    Beta strandi110 – 1123
    Beta strandi114 – 1218
    Beta strandi155 – 1595
    Beta strandi161 – 1655
    Beta strandi174 – 1763
    Beta strandi187 – 1893
    Beta strandi191 – 1933
    Beta strandi196 – 1994
    Helixi200 – 2023
    Beta strandi234 – 2363
    Beta strandi246 – 2483
    Beta strandi255 – 2573
    Beta strandi259 – 2657
    Turni271 – 2766
    Turni281 – 2833
    Helixi377 – 3793
    Beta strandi380 – 3889
    Beta strandi390 – 39910
    Turni400 – 4023
    Beta strandi405 – 4128
    Helixi413 – 4186
    Helixi422 – 43514
    Beta strandi444 – 4496
    Beta strandi451 – 4599
    Helixi466 – 4738
    Helixi478 – 49720
    Helixi507 – 5093
    Beta strandi510 – 5123
    Beta strandi518 – 5203
    Helixi543 – 5453
    Helixi548 – 5514
    Helixi559 – 57416
    Helixi584 – 59310
    Helixi604 – 61310
    Helixi618 – 6203
    Helixi628 – 6303
    Helixi632 – 6343
    Helixi639 – 6435
    Turni667 – 6704
    Helixi680 – 6856
    Turni690 – 6934

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XJDX-ray2.00A362-706[»]
    2ENJNMR-A1-125[»]
    2ENNNMR-A144-213[»]
    2ENZNMR-A227-284[»]
    2JEDX-ray2.32A/B361-706[»]
    ProteinModelPortaliQ04759.
    SMRiQ04759. Positions 3-126, 144-281, 375-700.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04759.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 123116C2Add
    BLAST
    Domaini380 – 634255Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini635 – 70672AGC-kinase C-terminalAdd
    BLAST

    Domaini

    The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the C2 domain is a non-calcium binding domain.

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 C2 domain.Curated
    Contains 2 phorbol-ester/DAG-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri159 – 20951Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri231 – 28151Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233022.
    HOVERGENiHBG108317.
    InParanoidiQ04759.
    KOiK18052.
    OMAiREPQGIS.
    OrthoDBiEOG77M8QM.
    PhylomeDBiQ04759.
    TreeFamiTF102004.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    InterProiIPR000961. AGC-kinase_C.
    IPR000008. C2_dom.
    IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR027264. PKC_theta.
    IPR017892. Pkinase_C.
    IPR014376. Prot_kin_PKC_delta.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00130. C1_1. 2 hits.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000551. PKC_delta. 1 hit.
    PIRSF501105. Protein_kin_C_theta. 1 hit.
    PRINTSiPR00008. DAGPEDOMAIN.
    SMARTiSM00109. C1. 2 hits.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS00479. ZF_DAG_PE_1. 2 hits.
    PS50081. ZF_DAG_PE_2. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q04759-1) [UniParc]FASTAAdd to Basket

    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

    MSPFLRIGLS NFDCGSCQSC QGEAVNPYCA VLVKEYVESE NGQMYIQKKP    50
    TMYPPWDSTF DAHINKGRVM QIIVKGKNVD LISETTVELY SLAERCRKNN 100
    GKTEIWLELK PQGRMLMNAR YFLEMSDTKD MNEFETEGFF ALHQRRGAIK 150
    QAKVHHVKCH EFTATFFPQP TFCSVCHEFV WGLNKQGYQC RQCNAAIHKK 200
    CIDKVIAKCT GSAINSRETM FHKERFKIDM PHRFKVYNYK SPTFCEHCGT 250
    LLWGLARQGL KCDACGMNVH HRCQTKVANL CGINQKLMAE ALAMIESTQQ 300
    ARCLRDTEQI FREGPVEIGL PCSIKNEARP PCLPTPGKRE PQGISWESPL 350
    DEVDKMCHLP EPELNKERPS LQIKLKIEDF ILHKMLGKGS FGKVFLAEFK 400
    KTNQFFAIKA LKKDVVLMDD DVECTMVEKR VLSLAWEHPF LTHMFCTFQT 450
    KENLFFVMEY LNGGDLMYHI QSCHKFDLSR ATFYAAEIIL GLQFLHSKGI 500
    VYRDLKLDNI LLDKDGHIKI ADFGMCKENM LGDAKTNTFC GTPDYIAPEI 550
    LLGQKYNHSV DWWSFGVLLY EMLIGQSPFH GQDEEELFHS IRMDNPFYPR 600
    WLEKEAKDLL VKLFVREPEK RLGVRGDIRQ HPLFREINWE ELERKEIDPP 650
    FRPKVKSPFD CSNFDKEFLN EKPRLSFADR ALINSMDQNM FRNFSFMNPG 700
    MERLIS 706
    Length:706
    Mass (Da):81,865
    Last modified:March 27, 2002 - v3
    Checksum:iB3C53AB892D5210A
    GO
    Isoform 2 (identifier: Q04759-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         550-612: Missing.

    Show »
    Length:643
    Mass (Da):74,287
    Checksum:iA3B688EBE8809B9E
    GO
    Isoform 3 (identifier: Q04759-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-126: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:581
    Mass (Da):67,560
    Checksum:iABB524BD5B3E2898
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti700 – 7001G → R in AAA75571. (PubMed:7686153)Curated
    Sequence conflicti700 – 7001G → R in AAU29340. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti240 – 2401K → N in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_042319
    Natural varianti306 – 3061D → V.1 Publication
    Corresponds to variant rs45590231 [ dbSNP | Ensembl ].
    VAR_042320
    Natural varianti330 – 3301P → L.3 Publications
    Corresponds to variant rs2236379 [ dbSNP | Ensembl ].
    VAR_020401
    Natural varianti354 – 3541D → N.1 Publication
    Corresponds to variant rs34524148 [ dbSNP | Ensembl ].
    VAR_042321

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 126125Missing in isoform 3. 1 PublicationVSP_054550Add
    BLAST
    Alternative sequencei550 – 61263Missing in isoform 2. 1 PublicationVSP_017294Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01087 mRNA. Translation: AAA75571.1.
    L07032 mRNA. Translation: AAA60101.1.
    AY702977 mRNA. Translation: AAU29340.1.
    AK293935 mRNA. Translation: BAG57313.1.
    AL158043 Genomic DNA. Translation: CAC12904.2.
    AL137145 Genomic DNA. Translation: CAC10200.2.
    BC101465 mRNA. Translation: AAI01466.1.
    BC113359 mRNA. Translation: AAI13360.1.
    CCDSiCCDS55701.1. [Q04759-2]
    CCDS60482.1. [Q04759-3]
    CCDS7079.1. [Q04759-1]
    PIRiA45416.
    RefSeqiNP_001229342.1. NM_001242413.2. [Q04759-2]
    NP_001269573.1. NM_001282644.1.
    NP_001269574.1. NM_001282645.1. [Q04759-3]
    NP_006248.1. NM_006257.4. [Q04759-1]
    XP_006717528.1. XM_006717465.1. [Q04759-1]
    UniGeneiHs.498570.

    Genome annotation databases

    EnsembliENST00000263125; ENSP00000263125; ENSG00000065675. [Q04759-1]
    ENST00000397176; ENSP00000380361; ENSG00000065675. [Q04759-2]
    ENST00000539722; ENSP00000441752; ENSG00000065675. [Q04759-3]
    GeneIDi5588.
    KEGGihsa:5588.
    UCSCiuc001iji.1. human. [Q04759-1]
    uc009xim.2. human. [Q04759-2]

    Polymorphism databases

    DMDMi20141582.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01087 mRNA. Translation: AAA75571.1 .
    L07032 mRNA. Translation: AAA60101.1 .
    AY702977 mRNA. Translation: AAU29340.1 .
    AK293935 mRNA. Translation: BAG57313.1 .
    AL158043 Genomic DNA. Translation: CAC12904.2 .
    AL137145 Genomic DNA. Translation: CAC10200.2 .
    BC101465 mRNA. Translation: AAI01466.1 .
    BC113359 mRNA. Translation: AAI13360.1 .
    CCDSi CCDS55701.1. [Q04759-2 ]
    CCDS60482.1. [Q04759-3 ]
    CCDS7079.1. [Q04759-1 ]
    PIRi A45416.
    RefSeqi NP_001229342.1. NM_001242413.2. [Q04759-2 ]
    NP_001269573.1. NM_001282644.1.
    NP_001269574.1. NM_001282645.1. [Q04759-3 ]
    NP_006248.1. NM_006257.4. [Q04759-1 ]
    XP_006717528.1. XM_006717465.1. [Q04759-1 ]
    UniGenei Hs.498570.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XJD X-ray 2.00 A 362-706 [» ]
    2ENJ NMR - A 1-125 [» ]
    2ENN NMR - A 144-213 [» ]
    2ENZ NMR - A 227-284 [» ]
    2JED X-ray 2.32 A/B 361-706 [» ]
    ProteinModelPortali Q04759.
    SMRi Q04759. Positions 3-126, 144-281, 375-700.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111574. 27 interactions.
    IntActi Q04759. 18 interactions.
    MINTi MINT-4649766.
    STRINGi 9606.ENSP00000263125.

    Chemistry

    BindingDBi Q04759.
    ChEMBLi CHEMBL2096620.
    GuidetoPHARMACOLOGYi 1488.

    PTM databases

    PhosphoSitei Q04759.

    Polymorphism databases

    DMDMi 20141582.

    Proteomic databases

    MaxQBi Q04759.
    PaxDbi Q04759.
    PRIDEi Q04759.

    Protocols and materials databases

    DNASUi 5588.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263125 ; ENSP00000263125 ; ENSG00000065675 . [Q04759-1 ]
    ENST00000397176 ; ENSP00000380361 ; ENSG00000065675 . [Q04759-2 ]
    ENST00000539722 ; ENSP00000441752 ; ENSG00000065675 . [Q04759-3 ]
    GeneIDi 5588.
    KEGGi hsa:5588.
    UCSCi uc001iji.1. human. [Q04759-1 ]
    uc009xim.2. human. [Q04759-2 ]

    Organism-specific databases

    CTDi 5588.
    GeneCardsi GC10M006509.
    HGNCi HGNC:9410. PRKCQ.
    MIMi 600448. gene.
    neXtProti NX_Q04759.
    PharmGKBi PA33773.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233022.
    HOVERGENi HBG108317.
    InParanoidi Q04759.
    KOi K18052.
    OMAi REPQGIS.
    OrthoDBi EOG77M8QM.
    PhylomeDBi Q04759.
    TreeFami TF102004.

    Enzyme and pathway databases

    BRENDAi 2.7.11.13. 2681.
    Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
    REACT_12555. Downstream TCR signaling.
    REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
    REACT_163994. FCERI mediated NF-kB activation.
    REACT_19333. G alpha (z) signalling events.
    REACT_2202. Effects of PIP2 hydrolysis.
    REACT_22237. Netrin-1 signaling.
    SignaLinki Q04759.

    Miscellaneous databases

    ChiTaRSi PRKCQ. human.
    EvolutionaryTracei Q04759.
    GeneWikii PRKCQ.
    GenomeRNAii 5588.
    NextBioi 21674.
    PMAP-CutDB Q04759.
    PROi Q04759.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q04759.
    Bgeei Q04759.
    CleanExi HS_PRKCQ.
    Genevestigatori Q04759.

    Family and domain databases

    Gene3Di 2.60.40.150. 1 hit.
    InterProi IPR000961. AGC-kinase_C.
    IPR000008. C2_dom.
    IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR027264. PKC_theta.
    IPR017892. Pkinase_C.
    IPR014376. Prot_kin_PKC_delta.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00130. C1_1. 2 hits.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000551. PKC_delta. 1 hit.
    PIRSF501105. Protein_kin_C_theta. 1 hit.
    PRINTSi PR00008. DAGPEDOMAIN.
    SMARTi SM00109. C1. 2 hits.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS00479. ZF_DAG_PE_1. 2 hits.
    PS50081. ZF_DAG_PE_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of a cDNA encoding a novel isoenzyme of protein kinase C (nPKC). A new member of the nPKC family expressed in skeletal muscle, megakaryoblastic cells, and platelets."
      Chang J.D., Xu Y., Raychowdhury M.K., Ware J.A.
      J. Biol. Chem. 268:14208-14214(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT LEU-330.
    2. Erratum
      Chang J.D., Xu Y., Raychowdhury M.K., Ware J.A.
      J. Biol. Chem. 269:31322-31322(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    3. "Molecular cloning and characterization of PKC theta, a novel member of the protein kinase C (PKC) gene family expressed predominantly in hematopoietic cells."
      Baier G., Telford D., Giampa L., Coggeshall K.M., Baier-Bitterlich G., Isakov N., Altman A.
      J. Biol. Chem. 268:4997-5004(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Blood.
    4. Li H., Ke R., Zhou G., Shen C., Zhong G., Lin L., Yang S.
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-330.
    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: Cerebellum.
    6. "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].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    8. "Protein kinase C-theta isoenzyme selective stimulation of the transcription factor complex AP-1 in T lymphocytes."
      Baier-Bitterlich G., Uberall F., Bauer B., Fresser F., Wachter H., Grunicke H., Utermann G., Altman A., Baier G.
      Mol. Cell. Biol. 16:1842-1850(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ACTIVATION OF JUN.
    9. "Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain."
      Witte S., Villalba M., Bi K., Liu Y., Isakov N., Altman A.
      J. Biol. Chem. 275:1902-1909(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GLRX3.
    10. "Regulation of protein kinase Ctheta function during T cell activation by Lck-mediated tyrosine phosphorylation."
      Liu Y., Witte S., Liu Y.C., Doyle M., Elly C., Altman A.
      J. Biol. Chem. 275:3603-3609(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-90, MUTAGENESIS OF TYR-90; ALA-148 AND LYS-409.
    11. "Protein kinase C-theta mediates a selective T cell survival signal via phosphorylation of BAD."
      Villalba M., Bushway P., Altman A.
      J. Immunol. 166:5955-5963(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF BAD.
    12. "Phosphorylation of the protein kinase C-theta activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor-kappaB induction."
      Liu Y., Graham C., Li A., Fisher R.J., Shaw S.
      Biochem. J. 361:255-265(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-538; SER-676 AND SER-695, MUTAGENESIS OF THR-538 AND SER-695.
    13. "SPAK kinase is a substrate and target of PKCtheta in T-cell receptor-induced AP-1 activation pathway."
      Li Y., Hu J., Vita R., Sun B., Tabata H., Altman A.
      EMBO J. 23:1112-1122(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF STK39/SPAK.
    14. "Protein kinase C Theta inhibits insulin signaling by phosphorylating IRS1 at Ser(1101)."
      Li Y., Soos T.J., Li X., Wu J., Degennaro M., Sun X., Littman D.R., Birnbaum M.J., Polakiewicz R.D.
      J. Biol. Chem. 279:45304-45307(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF IRS1.
    15. "Nucleotide exchange factor ECT2 interacts with the polarity protein complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta activity."
      Liu X.F., Ishida H., Raziuddin R., Miki T.
      Mol. Cell. Biol. 24:6665-6675(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ECT2.
    16. "Critical role of novel Thr-219 autophosphorylation for the cellular function of PKCtheta in T lymphocytes."
      Thuille N., Heit I., Fresser F., Krumbock N., Bauer B., Leuthaeusser S., Dammeier S., Graham C., Copeland T.D., Shaw S., Baier G.
      EMBO J. 24:3869-3880(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-219; THR-538; SER-676 AND SER-695, MUTAGENESIS OF THR-219; THR-538; SER-676 AND SER-695.
    17. Cited for: FUNCTION IN PHOSPHORYLATION OF CARD11, SUBUNIT.
    18. "Protein kinase C-theta-mediated signals enhance CD4+ T cell survival by up-regulating Bcl-xL."
      Manicassamy S., Gupta S., Huang Z., Sun Z.
      J. Immunol. 176:6709-6716(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ACTIVATION OF BCL-X(L)/BCL2L1.
    19. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348; SER-685 AND SER-695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676 AND SER-695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "PKC-theta modulates the strength of T cell responses by targeting Cbl-b for ubiquitination and degradation."
      Gruber T., Hermann-Kleiter N., Hinterleitner R., Fresser F., Schneider R., Gastl G., Penninger J.M., Baier G.
      Sci. Signal. 2:RA30-RA30(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CBLB.
    22. "Protein kinase C(theta) in T cell activation."
      Isakov N., Altman A.
      Annu. Rev. Immunol. 20:761-794(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    23. "Protein kinase C-theta (PKC theta): a key enzyme in T cell life and death."
      Altman A., Villalba M.
      J. Biochem. 132:841-846(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    24. Cited for: REVIEW.
    25. "Selective function of PKC-theta in T cells."
      Manicassamy S., Gupta S., Sun Z.
      Cell. Mol. Immunol. 3:263-270(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    26. "Protein kinase C theta (PKCtheta): a key player in T cell life and death."
      Hayashi K., Altman A.
      Pharmacol. Res. 55:537-544(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    27. "T-cell fate and function: PKC-theta and beyond."
      Marsland B.J., Kopf M.
      Trends Immunol. 29:179-185(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    28. "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-685, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "Protein kinase C-theta in platelet activation."
      Cohen S., Braiman A., Shubinsky G., Isakov N.
      FEBS Lett. 585:3208-3215(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN PLATELET ACTIVATION.
    31. "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-685 AND SER-695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 362-706, PHOSPHORYLATION AT THR-538 AND SER-695.
    33. "The crystal structure of the kinase domain of the protein kinase C theta in complex with Nvp-Xaa228."
      Stark W., Bitsch F., Berner A., Buelens F., Graff P., Depersin H., Fendrich G., Geiser M., Knecht R., Rahuel J., Rummel G., Schlaeppi J.M., Schmitz R., Strauss A., Wagner J.
      Submitted (JAN-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 361-706, PHOSPHORYLATION AT SER-676 AND SER-695.
    34. "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] ASN-240; VAL-306; LEU-330 AND ASN-354.

    Entry informationi

    Entry nameiKPCT_HUMAN
    AccessioniPrimary (citable) accession number: Q04759
    Secondary accession number(s): B4DF52
    , Q14DH6, Q3MJF1, Q64FY5, Q9H508, Q9H549
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: March 27, 2002
    Last modified: October 1, 2014
    This is version 168 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, 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