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Q05655

- KPCD_HUMAN

UniProt

Q05655 - KPCD_HUMAN

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Protein

Protein kinase C delta type

Gene

PRKCD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression as well as survival of several cancers, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. Negatively regulates B cell proliferation and also has an important function in self-antigen induced B cell tolerance induction. Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation. Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1. Is highly expressed in a number of cancer cells and promotes cell survival and resistance against chemotherapeutic drugs by inducing cyclin D1 (CCND1) and hyperphosphorylation of RB1, and via several pro-survival pathways, including NF-kappa-B, AKT1 and MAPK1/3 (ERK1/2). Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-formyl-methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways. May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin. The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion By similarity.By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Enzyme regulationi

Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are calcium-insensitive, but activated by diacylglycerol (DAG) and phosphatidylserine. Three specific sites; Thr-507 (activation loop of the kinase domain), Ser-645 (turn motif) and Ser-664 (hydrophobic region), need to be phosphorylated for its full activation. Activated by caspase-3 (CASP3) cleavage during apoptosis. After cleavage, the pseudosubstrate motif in the regulatory subunit is released from the substrate recognition site of the catalytic subunit, which enables PRKCD to become constitutively activated. The catalytic subunit which displays properties of a sphingosine-dependent protein kinase is activated by D-erythro-sphingosine (Sph) or N,N-dimethyl-D-erythrosphingosine (DMS) or N,N,N-trimethyl-D-erythrosphingosine (TMS), but not by ceramide or Sph-1-P and is strongly inhibited by phosphatidylserine By similarity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei48 – 481Interaction with phosphotyrosine-containing peptide
Sitei62 – 621Interaction with phosphotyrosine-containing peptide
Sitei67 – 671Interaction with phosphotyrosine-containing peptide
Sitei123 – 1231Interaction with phosphotyrosine-containing peptide
Sitei329 – 3302Cleavage; by caspase-3By similarity
Binding sitei378 – 3781ATPPROSITE-ProRule annotation
Active sitei473 – 4731Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri158 – 20851Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri230 – 28051Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi355 – 3639ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium-independent protein kinase C activity Source: BHF-UCL
  3. enzyme activator activity Source: UniProtKB
  4. enzyme binding Source: UniProtKB
  5. insulin receptor substrate binding Source: BHF-UCL
  6. metal ion binding Source: UniProtKB-KW
  7. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  8. protein kinase C activity Source: UniProtKB
  9. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. activation of phospholipase C activity Source: Reactome
  2. apoptotic process Source: UniProtKB
  3. B cell proliferation Source: Ensembl
  4. blood coagulation Source: Reactome
  5. cell cycle Source: UniProtKB-KW
  6. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  7. cellular senescence Source: BHF-UCL
  8. cytokine-mediated signaling pathway Source: Reactome
  9. defense response to bacterium Source: UniProtKB
  10. epidermal growth factor receptor signaling pathway Source: Reactome
  11. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  12. fibroblast growth factor receptor signaling pathway Source: Reactome
  13. gene expression Source: Reactome
  14. immunoglobulin mediated immune response Source: Ensembl
  15. innate immune response Source: Reactome
  16. interferon-gamma-mediated signaling pathway Source: Reactome
  17. interleukin-10 production Source: Ensembl
  18. interleukin-12 production Source: Ensembl
  19. intrinsic apoptotic signaling pathway in response to oxidative stress Source: ParkinsonsUK-UCL
  20. mRNA metabolic process Source: Reactome
  21. negative regulation of actin filament polymerization Source: UniProtKB
  22. negative regulation of filopodium assembly Source: UniProtKB
  23. negative regulation of glial cell apoptotic process Source: UniProtKB
  24. negative regulation of inflammatory response Source: BHF-UCL
  25. negative regulation of insulin receptor signaling pathway Source: BHF-UCL
  26. negative regulation of MAP kinase activity Source: BHF-UCL
  27. negative regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  28. negative regulation of platelet aggregation Source: UniProtKB
  29. negative regulation of protein binding Source: BHF-UCL
  30. neurotrophin TRK receptor signaling pathway Source: Reactome
  31. neutrophil activation Source: UniProtKB
  32. peptidyl-threonine phosphorylation Source: UniProtKB
  33. platelet activation Source: Reactome
  34. positive regulation of apoptotic signaling pathway Source: Ensembl
  35. positive regulation of ceramide biosynthetic process Source: BHF-UCL
  36. positive regulation of glucosylceramide catabolic process Source: BHF-UCL
  37. positive regulation of phospholipid scramblase activity Source: UniProtKB
  38. positive regulation of protein dephosphorylation Source: BHF-UCL
  39. positive regulation of response to DNA damage stimulus Source: UniProtKB
  40. positive regulation of sphingomyelin catabolic process Source: BHF-UCL
  41. positive regulation of superoxide anion generation Source: UniProtKB
  42. protein phosphorylation Source: UniProtKB
  43. protein stabilization Source: UniProtKB
  44. regulation of receptor activity Source: BHF-UCL
  45. RNA metabolic process Source: Reactome
  46. signal transduction Source: Reactome
  47. termination of signal transduction Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi2.7.11.13. 2681.
ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
REACT_111064. DAG and IP3 signaling.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_19333. G alpha (z) signalling events.
REACT_2202. Effects of PIP2 hydrolysis.
REACT_25078. Interferon gamma signaling.
REACT_25218. HuR stabilizes mRNA.
REACT_9000. Calmodulin induced events.
SignaLinkiQ05655.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C delta type (EC:2.7.11.13)
Alternative name(s):
Tyrosine-protein kinase PRKCD (EC:2.7.10.2)
nPKC-delta
Cleaved into the following 2 chains:
Alternative name(s):
Sphingosine-dependent protein kinase-1
Short name:
SDK1
Gene namesi
Name:PRKCD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:9399. PRKCD.

Subcellular locationi

GO - Cellular componenti

  1. cell-cell junction Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. endoplasmic reticulum Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProt
  6. mitochondrion Source: UniProtKB-KW
  7. nuclear matrix Source: Ensembl
  8. nucleoplasm Source: Reactome
  9. nucleus Source: UniProtKB
  10. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Immunodeficiency, common variable, 9 (CVID9) [MIM:615559]: A primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low. CVID9 patients have B-cell deficiency and severe autoimmunity.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi299 – 2991S → A: Loss of phosphorylation. 1 Publication
Mutagenesisi507 – 5071T → A: No effect on kinase activity. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

MIMi615559. phenotype.
Orphaneti3261. Autoimmune lymphoproliferative syndrome.
300345. Autosomal recessive systemic lupus erythematosus.
1572. Common variable immunodeficiency.
PharmGKBiPA33763.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 676676Protein kinase C delta typePRO_0000055694Add
BLAST
Chaini1 – 329329Protein kinase C delta type regulatory subunitBy similarityPRO_0000421667Add
BLAST
Chaini330 – 676347Protein kinase C delta type catalytic subunitBy similarityPRO_0000421668Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431PhosphothreonineBy similarity
Modified residuei64 – 641PhosphotyrosineBy similarity
Modified residuei130 – 1301Phosphoserine1 Publication
Modified residuei155 – 1551Phosphotyrosine1 Publication
Modified residuei218 – 2181Phosphothreonine1 Publication
Modified residuei299 – 2991Phosphoserine; by autocatalysis2 Publications
Modified residuei302 – 3021Phosphoserine; by autocatalysis2 Publications
Modified residuei304 – 3041Phosphoserine; by autocatalysis4 Publications
Modified residuei307 – 3071Phosphoserine1 Publication
Modified residuei313 – 3131Phosphotyrosine4 Publications
Modified residuei334 – 3341Phosphotyrosine; by SRC1 Publication
Modified residuei374 – 3741Phosphotyrosine1 Publication
Modified residuei503 – 5031Phosphoserine1 Publication
Modified residuei507 – 5071Phosphothreonine; by autocatalysis1 Publication
Modified residuei567 – 5671Phosphotyrosine1 Publication
Modified residuei645 – 6451Phosphoserine3 Publications
Modified residuei654 – 6541Phosphoserine1 Publication
Modified residuei658 – 6581Phosphoserine1 Publication
Modified residuei664 – 6641Phosphoserine5 Publications

Post-translational modificationi

Autophosphorylated and/or phosphorylated at Thr-507, within the activation loop; phosphorylation at Thr-507 is not a prerequisite for enzymatic activity. Autophosphorylated at Ser-299, Ser-302 and Ser-304. Upon TNFSF10/TRAIL treatment, phosphorylated at Tyr-155; phosphorylation is required for its translocation to the endoplasmic reticulum and cleavage by caspase-3. Phosphorylated at Tyr-313, Tyr-334 and Tyr-567; phosphorylation of Tyr-313 and Tyr-567 following thrombin stimulation potentiates its kinase activity. Phosphorylated by protein kinase PDPK1; phosphorylation is inhibited by the apoptotic C-terminal cleavage product of PKN2.11 Publications
Proteolytically cleaved into a catalytic subunit and a regulatory subunit by caspase-3 during apoptosis which results in kinase activation.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ05655.
PaxDbiQ05655.
PRIDEiQ05655.

PTM databases

PhosphoSiteiQ05655.

Miscellaneous databases

PMAP-CutDBQ05655.

Expressioni

Gene expression databases

BgeeiQ05655.
CleanExiHS_PRKCD.
ExpressionAtlasiQ05655. baseline and differential.
GenevestigatoriQ05655.

Organism-specific databases

HPAiCAB010469.
CAB013225.
HPA001863.
HPA001890.

Interactioni

Subunit structurei

Interacts with PDPK1 (via N-terminal region), RAD9A, CDCP1, MUC1 and VASP.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DIABLOQ9NR284EBI-704279,EBI-517508
FYNP062415EBI-704279,EBI-515315
GAP43P176774EBI-704279,EBI-1267511
IL32C6GKH13EBI-704279,EBI-9547476
IL32P24001-23EBI-704279,EBI-8800907

Protein-protein interaction databases

BioGridi111566. 70 interactions.
DIPiDIP-29954N.
IntActiQ05655. 22 interactions.
MINTiMINT-1346366.
STRINGi9606.ENSP00000331602.

Structurei

Secondary structure

676
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 1313
Beta strandi20 – 234
Beta strandi27 – 3812
Beta strandi41 – 455
Beta strandi58 – 625
Beta strandi68 – 769
Beta strandi79 – 879
Helixi88 – 969
Turni97 – 1004
Beta strandi101 – 1077
Beta strandi109 – 1113
Beta strandi113 – 12311
Helixi156 – 1583
Beta strandi161 – 1644
Beta strandi173 – 1753
Beta strandi181 – 1833
Beta strandi186 – 1894
Turni190 – 1923
Helixi200 – 2023

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YRKX-ray1.70A1-123[»]
2YUUNMR-A149-218[»]
ProteinModelPortaliQ05655.
SMRiQ05655. Positions 1-123, 149-668.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05655.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9090C2Add
BLAST
Domaini349 – 603255Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini604 – 67572AGC-kinase C-terminalAdd
BLAST

Domaini

The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor.
The C2 domain is a non-calcium binding domain. It binds proteins containing phosphotyrosine in a sequence-specific manner.

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 fingeri158 – 20851Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri230 – 28051Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118891.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiQ05655.
KOiK06068.
OMAiGEDEAKF.
OrthoDBiEOG77M8QM.
PhylomeDBiQ05655.
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.
IPR002219. PE/DAG-bd.
IPR027436. PKC_delta.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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.
PIRSF501104. Protein_kin_C_delta. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
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 (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q05655-1) [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

        10         20         30         40         50
MAPFLRIAFN SYELGSLQAE DEANQPFCAV KMKEALSTER GKTLVQKKPT
60 70 80 90 100
MYPEWKSTFD AHIYEGRVIQ IVLMRAAEEP VSEVTVGVSV LAERCKKNNG
110 120 130 140 150
KAEFWLDLQP QAKVLMSVQY FLEDVDCKQS MRSEDEAKFP TMNRRGAIKQ
160 170 180 190 200
AKIHYIKNHE FIATFFGQPT FCSVCKDFVW GLNKQGYKCR QCNAAIHKKC
210 220 230 240 250
IDKIIGRCTG TAANSRDTIF QKERFNIDMP HRFKVHNYMS PTFCDHCGSL
260 270 280 290 300
LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQRASR
310 320 330 340 350
RSDSASSEPV GIYQGFEKKT GVAGEDMQDN SGTYGKIWEG SSKCNINNFI
360 370 380 390 400
FHKVLGKGSF GKVLLGELKG RGEYFAIKAL KKDVVLIDDD VECTMVEKRV
410 420 430 440 450
LTLAAENPFL THLICTFQTK DHLFFVMEFL NGGDLMYHIQ DKGRFELYRA
460 470 480 490 500
TFYAAEIMCG LQFLHSKGII YRDLKLDNVL LDRDGHIKIA DFGMCKENIF
510 520 530 540 550
GESRASTFCG TPDYIAPEIL QGLKYTFSVD WWSFGVLLYE MLIGQSPFHG
560 570 580 590 600
DDEDELFESI RVDTPHYPRW ITKESKDILE KLFEREPTKR LGVTGNIKIH
610 620 630 640 650
PFFKTINWTL LEKRRLEPPF RPKVKSPRDY SNFDQEFLNE KARLSYSDKN
660 670
LIDSMDQSAF AGFSFVNPKF EHLLED
Length:676
Mass (Da):77,505
Last modified:September 2, 2008 - v2
Checksum:i013F4314A2EE331A
GO
Isoform 2 (identifier: Q05655-2) [UniParc]FASTAAdd to Basket

Also known as: PKCdeltaVIII

The sequence of this isoform differs from the canonical sequence as follows:
     328-328: Q → QGEAGSIAPLRFLFPLRPKKGDCPPFHCQVRQ

Note: Antiapoptotic isoform, resistant to caspase-3 cleavage.

Show »
Length:707
Mass (Da):80,953
Checksum:iF1380490CC52EF07
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti524 – 5241K → R in BAG36031. (PubMed:14702039)Curated
Sequence conflicti533 – 5331S → A no nucleotide entry (PubMed:7988719)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti348 – 3481N → S.
Corresponds to variant rs33911937 [ dbSNP | Ensembl ].
VAR_035347
Natural varianti375 – 3751F → S.1 Publication
Corresponds to variant rs1056998 [ dbSNP | Ensembl ].
VAR_006175
Natural varianti410 – 4101L → F.
Corresponds to variant rs34502209 [ dbSNP | Ensembl ].
VAR_035348
Natural varianti483 – 4831R → W.
Corresponds to variant rs35891605 [ dbSNP | Ensembl ].
VAR_046009
Natural varianti494 – 4941M → V.1 Publication
VAR_020610
Natural varianti593 – 5931V → M.1 Publication
VAR_006176

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei328 – 3281Q → QGEAGSIAPLRFLFPLRPKK GDCPPFHCQVRQ in isoform 2. 1 PublicationVSP_043899

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07860 mRNA. Translation: AAA03176.1.
L07861 mRNA. Translation: AAA03175.1.
AK313216 mRNA. Translation: BAG36031.1.
CH471055 Genomic DNA. Translation: EAW65279.1.
BC043350 mRNA. Translation: AAH43350.1.
Z22521 mRNA. Translation: CAA80249.1.
D10495 mRNA. Translation: BAA01381.1.
DQ516383 mRNA. Translation: ABF68960.1.
CCDSiCCDS2870.1. [Q05655-1]
PIRiS35704.
RefSeqiNP_006245.2. NM_006254.3. [Q05655-1]
NP_997704.1. NM_212539.1. [Q05655-1]
XP_006713321.1. XM_006713258.1. [Q05655-1]
XP_006713322.1. XM_006713259.1. [Q05655-1]
UniGeneiHs.155342.

Genome annotation databases

EnsembliENST00000330452; ENSP00000331602; ENSG00000163932. [Q05655-1]
ENST00000394729; ENSP00000378217; ENSG00000163932. [Q05655-1]
GeneIDi5580.
KEGGihsa:5580.
UCSCiuc003dgl.3. human. [Q05655-1]

Polymorphism databases

DMDMi205371776.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07860 mRNA. Translation: AAA03176.1 .
L07861 mRNA. Translation: AAA03175.1 .
AK313216 mRNA. Translation: BAG36031.1 .
CH471055 Genomic DNA. Translation: EAW65279.1 .
BC043350 mRNA. Translation: AAH43350.1 .
Z22521 mRNA. Translation: CAA80249.1 .
D10495 mRNA. Translation: BAA01381.1 .
DQ516383 mRNA. Translation: ABF68960.1 .
CCDSi CCDS2870.1. [Q05655-1 ]
PIRi S35704.
RefSeqi NP_006245.2. NM_006254.3. [Q05655-1 ]
NP_997704.1. NM_212539.1. [Q05655-1 ]
XP_006713321.1. XM_006713258.1. [Q05655-1 ]
XP_006713322.1. XM_006713259.1. [Q05655-1 ]
UniGenei Hs.155342.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YRK X-ray 1.70 A 1-123 [» ]
2YUU NMR - A 149-218 [» ]
ProteinModelPortali Q05655.
SMRi Q05655. Positions 1-123, 149-668.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111566. 70 interactions.
DIPi DIP-29954N.
IntActi Q05655. 22 interactions.
MINTi MINT-1346366.
STRINGi 9606.ENSP00000331602.

Chemistry

BindingDBi Q05655.
ChEMBLi CHEMBL2093867.
DrugBanki DB05013. Ingenol Mebutate.
DB00675. Tamoxifen.
GuidetoPHARMACOLOGYi 1485.

PTM databases

PhosphoSitei Q05655.

Polymorphism databases

DMDMi 205371776.

Proteomic databases

MaxQBi Q05655.
PaxDbi Q05655.
PRIDEi Q05655.

Protocols and materials databases

DNASUi 5580.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000330452 ; ENSP00000331602 ; ENSG00000163932 . [Q05655-1 ]
ENST00000394729 ; ENSP00000378217 ; ENSG00000163932 . [Q05655-1 ]
GeneIDi 5580.
KEGGi hsa:5580.
UCSCi uc003dgl.3. human. [Q05655-1 ]

Organism-specific databases

CTDi 5580.
GeneCardsi GC03P053190.
HGNCi HGNC:9399. PRKCD.
HPAi CAB010469.
CAB013225.
HPA001863.
HPA001890.
MIMi 176977. gene.
615559. phenotype.
neXtProti NX_Q05655.
Orphaneti 3261. Autoimmune lymphoproliferative syndrome.
300345. Autosomal recessive systemic lupus erythematosus.
1572. Common variable immunodeficiency.
PharmGKBi PA33763.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118891.
HOGENOMi HOG000233022.
HOVERGENi HBG108317.
InParanoidi Q05655.
KOi K06068.
OMAi GEDEAKF.
OrthoDBi EOG77M8QM.
PhylomeDBi Q05655.
TreeFami TF102004.

Enzyme and pathway databases

BRENDAi 2.7.11.13. 2681.
Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
REACT_111064. DAG and IP3 signaling.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_19333. G alpha (z) signalling events.
REACT_2202. Effects of PIP2 hydrolysis.
REACT_25078. Interferon gamma signaling.
REACT_25218. HuR stabilizes mRNA.
REACT_9000. Calmodulin induced events.
SignaLinki Q05655.

Miscellaneous databases

ChiTaRSi PRKCD. human.
EvolutionaryTracei Q05655.
GeneWikii PRKCD.
GenomeRNAii 5580.
NextBioi 21638.
PMAP-CutDB Q05655.
PROi Q05655.
SOURCEi Search...

Gene expression databases

Bgeei Q05655.
CleanExi HS_PRKCD.
ExpressionAtlasi Q05655. baseline and differential.
Genevestigatori Q05655.

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.
IPR002219. PE/DAG-bd.
IPR027436. PKC_delta.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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.
PIRSF501104. Protein_kin_C_delta. 1 hit.
PRINTSi PR00008. DAGPEDOMAIN.
SMARTi SM00109. C1. 2 hits.
SM00239. C2. 1 hit.
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

« Hide 'large scale' publications
  1. "Molecular and biochemical characterization of a recombinant human PKC-delta family member."
    Aris J.P., Basta P.V., Holmes W.D., Ballas L.M., Moomaw C., Rankl N.B., Blobel G., Loomis C.R., Burns D.J.
    Biochim. Biophys. Acta 1174:171-181(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-375 AND MET-593.
    Tissue: Liver.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1).
    Tissue: Skin.
  5. "Partial cDNA Sequence of human protein kinase C delta."
    Hug H.
    Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-365 (ISOFORM 1).
    Tissue: Hippocampus.
  6. "Functional analyses of mammalian protein kinase C isozymes in budding yeast and mammalian fibroblasts."
    Nomoto S., Watanabe Y., Ninomiya-Tsuji J., Yang L.-X., Kikuchi K., Hagiwara M., Hidaka H., Matsumoto K., Irie K.
    Genes Cells 2:601-614(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 51-676 (ISOFORM 1).
  7. "Identification of a novel antiapoptotic human protein kinase C delta isoform, PKCdeltaVIII in NT2 cells."
    Jiang K., Apostolatos A.H., Ghansah T., Watson J.E., Vickers T., Cooper D.R., Epling-Burnette P.K., Patel N.A.
    Biochemistry 47:787-797(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 224-371 (ISOFORM 2).
  8. "Identification of multiple, novel, protein kinase C-related gene products."
    Palmer R.H., Ridden J., Parker P.J.
    FEBS Lett. 356:5-8(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 432-533 (ISOFORM 1), VARIANT VAL-494.
  9. "Regulation of human eosinophil NADPH oxidase activity: a central role for PKCdelta."
    Bankers-Fulbright J.L., Kita H., Gleich G.J., O'Grady S.M.
    J. Cell. Physiol. 189:306-315(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "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: MUTAGENESIS OF THR-507.
  11. "Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment."
    Hodgkinson C.P., Sale G.J.
    Biochemistry 41:561-569(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDPK1, PHOSPHORYLATION.
  12. "Protein kinase C delta regulates function of the DF3/MUC1 carcinoma antigen in beta-catenin signaling."
    Ren J., Li Y., Kufe D.
    J. Biol. Chem. 277:17616-17622(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MUC1, FUNCTION.
  13. "Protein kinase Cdelta is responsible for constitutive and DNA damage-induced phosphorylation of Rad9."
    Yoshida K., Wang H.-G., Miki Y., Kufe D.
    EMBO J. 22:1431-1441(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD9A.
  14. "Roles of tyrosine phosphorylation and cleavage of protein kinase Cdelta in its protective effect against tumor necrosis factor-related apoptosis inducing ligand-induced apoptosis."
    Okhrimenko H., Lu W., Xiang C., Ju D., Blumberg P.M., Gomel R., Kazimirsky G., Brodie C.
    J. Biol. Chem. 280:23643-23652(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-155.
  15. "PKCdelta regulates collagen-induced platelet aggregation through inhibition of VASP-mediated filopodia formation."
    Pula G., Schuh K., Nakayama K., Nakayama K.I., Walter U., Poole A.W.
    Blood 108:4035-4044(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PLATELET AGGREGATION, INTERACTION WITH VASP.
  16. "Coincident regulation of PKCdelta in human platelets by phosphorylation of Tyr311 and Tyr565 and phospholipase C signalling."
    Hall K.J., Jones M.L., Poole A.W.
    Biochem. J. 406:501-509(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-313 AND TYR-567.
  17. "Novel phosphorylation site markers of protein kinase C delta activation."
    Durgan J., Michael N., Totty N., Parker P.J.
    FEBS Lett. 581:3377-3381(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-299; SER-302 AND SER-304, MUTAGENESIS OF SER-299.
  18. "The localization of protein kinase Cdelta in different subcellular sites affects its proapoptotic and antiapoptotic functions and the activation of distinct downstream signaling pathways."
    Gomel R., Xiang C., Finniss S., Lee H.K., Lu W., Okhrimenko H., Brodie C.
    Mol. Cancer Res. 5:627-639(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  20. "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-299; TYR-313; SER-503; SER-654; SER-658 AND SER-664, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-302; SER-304; SER-307 AND SER-664, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Lyn, PKC-delta, SHIP-1 interactions regulate GPVI-mediated platelet-dense granule secretion."
    Chari R., Kim S., Murugappan S., Sanjay A., Daniel J.L., Kunapuli S.P.
    Blood 114:3056-3063(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PLATELET RESPONSE.
  24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-218; TYR-313 AND SER-664, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "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 TYR-313 AND SER-664, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  26. "Regulation of TNF-induced oxygen radical production in human neutrophils: role of delta-PKC."
    Kilpatrick L.E., Sun S., Li H., Vary T.C., Korchak H.M.
    J. Leukoc. Biol. 87:153-164(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF NCF1, PHOSPHORYLATION AT THR-507 AND SER-645.
  27. "Protein kinase C delta (PKC delta): activation mechanisms and functions."
    Kikkawa U., Matsuzaki H., Yamamoto T.
    J. Biochem. 132:831-839(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  28. "Diverse functions of protein kinase C isoforms in platelet activation and thrombus formation."
    Harper M.T., Poole A.W.
    J. Thromb. Haemost. 8:454-462(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  29. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; TYR-374; SER-645 AND SER-664, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. "Two faces of protein kinase Cdelta: the contrasting roles of PKCdelta in cell survival and cell death."
    Basu A., Pal D.
    ScientificWorldJournal 10:2272-2284(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "PKC-delta and PKC-epsilon: Foes of the same family or strangers?"
    Duquesnes N., Lezoualc'h F., Crozatier B.
    J. Mol. Cell. Cardiol. 51:665-673(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  33. "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-304 AND SER-645, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "Protein kinase cdelta in apoptosis: a brief overview."
    Zhao M., Xia L., Chen G.Q.
    Arch. Immunol. Ther. Exp. 60:361-372(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  35. Cited for: INVOLVEMENT IN CVID9.
  36. "The C2 domain of PKCdelta is a phosphotyrosine binding domain."
    Benes C.H., Wu N., Elia A.E.H., Dharia T., Cantley L.C., Soltoff S.P.
    Cell 121:271-280(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-123 IN COMPLEX WITH PHOSPHOTYROSINE-CONTAINING PEPTIDE, INTERACTION WITH CDCP1.
  37. "Solution structure of the first phorbol esters/diacylglycerol binding domain of human protein kinase C, delta."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 149-218.

Entry informationi

Entry nameiKPCD_HUMAN
AccessioniPrimary (citable) accession number: Q05655
Secondary accession number(s): B0KZ81
, B2R834, Q15144, Q86XJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: September 2, 2008
Last modified: October 29, 2014
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. 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