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Protein

Serine/threonine-protein kinase D2

Gene

PRKD2

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

Functioni

Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. May potentiate mitogenesis induced by the neuropeptide bombesin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression. In response to oxidative stress, is phosphorylated at Tyr-438 by ABL1, which leads to the activation of PRKD2 without increasing its catalytic activity, and mediates activation of NF-kappa-B. In response to the activation of the gastrin receptor CCKBR, is phosphorylated at Ser-244 by CSNK1D and CSNK1E, translocates to the nucleus, phosphorylates HDAC7, leading to nuclear export of HDAC7 and inhibition of HDAC7 transcriptional repression of NR4A1/NUR77. Upon TCR stimulation, is activated independently of ZAP70, translocates from the cytoplasm to the nucleus and is required for interleukin-2 (IL2) promoter up-regulation. During adaptive immune responses, is required in peripheral T-lymphocytes for the production of the effector cytokines IL2 and IFNG after TCR engagement and for optimal induction of antibody responses to antigens. In epithelial cells stimulated with lysophosphatidic acid (LPA), is activated through a PKC-dependent pathway and mediates LPA-stimulated interleukin-8 (IL8) secretion via a NF-kappa-B-dependent pathway. During TCR-induced T-cell activation, interacts with and is activated by the tyrosine kinase LCK, which results in the activation of the NFAT transcription factors. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane and in polarized cells is involved in the transport of proteins from the TGN to the basolateral membrane. Plays an important role in endothelial cell proliferation and migration prior to angiogenesis, partly through modulation of the expression of KDR/VEGFR2 and FGFR1, two key growth factor receptors involved in angiogenesis. In secretory pathway, is required for the release of chromogranin-A (CHGA)-containing secretory granules from the TGN. Downstream of PRKCA, plays important roles in angiotensin-2-induced monocyte adhesion to endothelial cells. Plays a regulatory role in angiogenesis and tumor growth by phosphorylating a downstream mediator CIB1 isoform 2, resulting in vascular endothelial growth factor A (VEGFA) secretion.10 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

Activated by DAG and phorbol esters. Phorbol-ester/DAG-type domains bind DAG, mediating translocation to membranes. Autophosphorylation of Ser-710 and phosphorylation of Ser-706 by PKC relieves auto-inhibition by the PH domain.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei580 – 5801ATPPROSITE-ProRule annotation
Active sitei674 – 6741Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri138 – 18851Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri264 – 31451Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi557 – 5659ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • protein kinase activity Source: BHF-UCL
  • protein kinase C activity Source: UniProtKB-EC
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • adaptive immune response Source: UniProtKB-KW
  • angiogenesis Source: UniProtKB-KW
  • cell adhesion Source: UniProtKB-KW
  • cell death Source: BHF-UCL
  • cellular response to vascular endothelial growth factor stimulus Source: BHF-UCL
  • endothelial tube morphogenesis Source: BHF-UCL
  • intracellular signal transduction Source: BHF-UCL
  • mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • peptidyl-serine phosphorylation Source: BHF-UCL
  • positive regulation of angiogenesis Source: UniProtKB
  • positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
  • positive regulation of cell adhesion Source: UniProtKB
  • positive regulation of CREB transcription factor activity Source: BHF-UCL
  • positive regulation of DNA biosynthetic process Source: UniProtKB
  • positive regulation of endothelial cell chemotaxis Source: BHF-UCL
  • positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  • positive regulation of endothelial cell migration Source: UniProtKB
  • positive regulation of endothelial cell proliferation Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of fibroblast growth factor receptor signaling pathway Source: UniProtKB
  • positive regulation of histone deacetylase activity Source: BHF-UCL
  • positive regulation of interleukin-2 production Source: UniProtKB
  • positive regulation of interleukin-8 production Source: UniProtKB
  • positive regulation of intracellular signal transduction Source: BHF-UCL
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • positive regulation of T cell receptor signaling pathway Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
  • protein autophosphorylation Source: BHF-UCL
  • protein kinase D signaling Source: BHF-UCL
  • protein phosphorylation Source: UniProtKB
  • T cell receptor signaling pathway Source: BHF-UCL
  • vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Adaptive immunity, Angiogenesis, Cell adhesion, Immunity

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi2.7.11.13. 2681.
SignaLinkiQ9BZL6.
SIGNORiQ9BZL6.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase D2 (EC:2.7.11.13)
Alternative name(s):
nPKC-D2
Gene namesi
Name:PRKD2
Synonyms:PKD2
ORF Names:HSPC187
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:17293. PRKD2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • Golgi apparatus Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: BHF-UCL
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi244 – 2441S → E: Constitutive kinase activity; when associated with E-706 and E-710. 1 Publication
Mutagenesisi275 – 2751P → G: Increase in ability to bind phorbol ester, slight increase in ability to bind DAG. 1 Publication
Mutagenesisi438 – 4381Y → F: Loss of phosphorylation. 1 Publication
Mutagenesisi695 – 6951D → A: Loss of kinase activity. 1 Publication
Mutagenesisi706 – 7061S → E: Constitutive kinase activity; when associated with E-710 or with E-244 and E-710. 1 Publication
Mutagenesisi710 – 7101S → E: Constitutive kinase activity; when associated with E-706 or with E-244 and E-706. 1 Publication

Organism-specific databases

PharmGKBiPA134903505.

Chemistry

ChEMBLiCHEMBL4900.
GuidetoPHARMACOLOGYi2173.

Polymorphism and mutation databases

BioMutaiPRKD2.
DMDMi296434570.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 878878Serine/threonine-protein kinase D2PRO_0000055716Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei197 – 1971PhosphoserineCombined sources
Modified residuei198 – 1981PhosphoserineCombined sources
Modified residuei200 – 2001PhosphoserineCombined sources
Modified residuei203 – 2031PhosphoserineCombined sources
Modified residuei206 – 2061PhosphoserineCombined sources
Modified residuei212 – 2121PhosphoserineBy similarity
Modified residuei214 – 2141PhosphoserineCombined sources
Modified residuei244 – 2441Phosphoserine; by CSNK1D and CSNK1E1 Publication
Modified residuei438 – 4381Phosphotyrosine; by ABL11 Publication
Modified residuei518 – 5181PhosphoserineCombined sources
Modified residuei706 – 7061Phosphoserine; by PKC1 Publication
Modified residuei710 – 7101PhosphoserineCombined sources1 Publication
Modified residuei717 – 7171PhosphotyrosineCombined sources
Modified residuei876 – 8761Phosphoserine; by autocatalysisCombined sources2 Publications

Post-translational modificationi

Phosphorylation of Ser-876 correlates with the activation status of the kinase. Ser-706 is probably phosphorylated by PKC. Phosphorylation at Ser-244 by CSNK1D and CSNK1E promotes nuclear localization and substrate targeting. Phosphorylation at Ser-244, Ser-706 and Ser-710 is required for nuclear localization. Phosphorylated at Tyr-438 by ABL1 in response to oxidative stress.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9BZL6.
MaxQBiQ9BZL6.
PaxDbiQ9BZL6.
PeptideAtlasiQ9BZL6.
PRIDEiQ9BZL6.

PTM databases

iPTMnetiQ9BZL6.
PhosphoSiteiQ9BZL6.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiENSG00000105287.
CleanExiHS_PKD2.
HS_PRKD2.
ExpressionAtlasiQ9BZL6. baseline and differential.
GenevisibleiQ9BZL6. HS.

Organism-specific databases

HPAiHPA021490.
HPA056727.

Interactioni

Subunit structurei

Interacts (via C-terminus) with LCK. Interacts (via N-terminal AP-rich region) with CIB1 isoform 2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HDAC7Q8WUI46EBI-1384325,EBI-1048378

Protein-protein interaction databases

BioGridi117384. 38 interactions.
IntActiQ9BZL6. 35 interactions.
MINTiMINT-1179710.
STRINGi9606.ENSP00000291281.

Chemistry

BindingDBiQ9BZL6.

Structurei

Secondary structure

1
878
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi399 – 4068Combined sources
Beta strandi409 – 4113Combined sources
Beta strandi415 – 4217Combined sources
Beta strandi423 – 43311Combined sources
Beta strandi438 – 4425Combined sources
Turni443 – 4453Combined sources
Beta strandi448 – 4525Combined sources
Beta strandi456 – 4583Combined sources
Beta strandi465 – 4706Combined sources
Beta strandi486 – 4883Combined sources
Helixi495 – 50713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2COANMR-A398-509[»]
3BGMX-ray1.60C526-534[»]
4NNXX-ray2.10C526-534[»]
4NNYX-ray1.90C526-534[»]
ProteinModelPortaliQ9BZL6.
SMRiQ9BZL6. Positions 138-188, 237-357, 395-509, 537-846.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BZL6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini397 – 509113PHPROSITE-ProRule annotationAdd
BLAST
Domaini551 – 807257Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PH domain.PROSITE-ProRule annotation
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 fingeri138 – 18851Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri264 – 31451Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG4236. Eukaryota.
ENOG410XQZ3. LUCA.
HOGENOMiHOG000015135.
HOVERGENiHBG003564.
InParanoidiQ9BZL6.
KOiK06070.
PhylomeDBiQ9BZL6.
TreeFamiTF314320.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015727. Protein_Kinase_C_mu-related.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR22968. PTHR22968. 1 hit.
PfamiPF00130. C1_1. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000552. PKC_mu_nu_D2. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 2 hits.
SM00233. PH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 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.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BZL6-1) [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
MATAPSYPAG LPGSPGPGSP PPPGGLELQS PPPLLPQIPA PGSGVSFHIQ
60 70 80 90 100
IGLTREFVLL PAASELAHVK QLACSIVDQK FPECGFYGLY DKILLFKHDP
110 120 130 140 150
TSANLLQLVR SSGDIQEGDL VEVVLSASAT FEDFQIRPHA LTVHSYRAPA
160 170 180 190 200
FCDHCGEMLF GLVRQGLKCD GCGLNYHKRC AFSIPNNCSG ARKRRLSSTS
210 220 230 240 250
LASGHSVRLG TSESLPCTAE ELSRSTTELL PRRPPSSSSS SSASSYTGRP
260 270 280 290 300
IELDKMLLSK VKVPHTFLIH SYTRPTVCQA CKKLLKGLFR QGLQCKDCKF
310 320 330 340 350
NCHKRCATRV PNDCLGEALI NGDVPMEEAT DFSEADKSAL MDESEDSGVI
360 370 380 390 400
PGSHSENALH ASEEEEGEGG KAQSSLGYIP LMRVVQSVRH TTRKSSTTLR
410 420 430 440 450
EGWVVHYSNK DTLRKRHYWR LDCKCITLFQ NNTTNRYYKE IPLSEILTVE
460 470 480 490 500
SAQNFSLVPP GTNPHCFEIV TANATYFVGE MPGGTPGGPS GQGAEAARGW
510 520 530 540 550
ETAIRQALMP VILQDAPSAP GHAPHRQASL SISVSNSQIQ ENVDIATVYQ
560 570 580 590 600
IFPDEVLGSG QFGVVYGGKH RKTGRDVAVK VIDKLRFPTK QESQLRNEVA
610 620 630 640 650
ILQSLRHPGI VNLECMFETP EKVFVVMEKL HGDMLEMILS SEKGRLPERL
660 670 680 690 700
TKFLITQILV ALRHLHFKNI VHCDLKPENV LLASADPFPQ VKLCDFGFAR
710 720 730 740 750
IIGEKSFRRS VVGTPAYLAP EVLLNQGYNR SLDMWSVGVI MYVSLSGTFP
760 770 780 790 800
FNEDEDINDQ IQNAAFMYPA SPWSHISAGA IDLINNLLQV KMRKRYSVDK
810 820 830 840 850
SLSHPWLQEY QTWLDLRELE GKMGERYITH ESDDVRWEQF AAEHPLPGSG
860 870
LPTDRDLGGA CPPQDHDMQG LAERISVL
Length:878
Mass (Da):96,750
Last modified:May 18, 2010 - v2
Checksum:i8BAB45FB5B1718E7
GO
Isoform 2 (identifier: Q9BZL6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-157: Missing.

Note: No experimental confirmation available.
Show »
Length:721
Mass (Da):80,143
Checksum:i8A97CE2220C63C8D
GO

Sequence cautioni

The sequence AAF36107 differs from that shown. Reason: Frameshift at positions 604, 606, 738, 744, 755, 758, 833 and 854. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti790 – 7901V → L in AAF36107 (PubMed:11042152).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti324 – 3241V → M.1 Publication
Corresponds to variant rs45455991 [ dbSNP | Ensembl ].
VAR_042330
Natural varianti496 – 4961A → V.1 Publication
Corresponds to variant rs55716765 [ dbSNP | Ensembl ].
VAR_042331
Natural varianti604 – 6041S → G.1 Publication
Corresponds to variant rs34325043 [ dbSNP | Ensembl ].
VAR_042332
Natural varianti773 – 7731W → R.1 Publication
Corresponds to variant rs55933311 [ dbSNP | Ensembl ].
VAR_042333
Natural varianti835 – 8351V → A.1 Publication3 Publications
Corresponds to variant rs314665 [ dbSNP | Ensembl ].
VAR_061531
Natural varianti848 – 8481G → E in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042334
Natural varianti870 – 8701G → E in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042335

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 157157Missing in isoform 2. 1 PublicationVSP_057279Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF309082 mRNA. Translation: AAK01149.1.
AK074673 mRNA. Translation: BAC11127.1.
AK095884 mRNA. Translation: BAG53158.1.
AC008635 Genomic DNA. No translation available.
AC093503 Genomic DNA. No translation available.
KC877745 Genomic DNA. No translation available.
AL050147 mRNA. Translation: CAB43292.1.
AF151021 mRNA. Translation: AAF36107.1. Frameshift.
CCDSiCCDS12689.1. [Q9BZL6-1]
CCDS59401.1. [Q9BZL6-2]
PIRiT08777.
RefSeqiNP_001073349.1. NM_001079880.1.
NP_001073350.1. NM_001079881.1.
NP_001073351.1. NM_001079882.1.
NP_057541.2. NM_016457.4.
XP_005258773.2. XM_005258716.2.
UniGeneiHs.466987.

Genome annotation databases

EnsembliENST00000291281; ENSP00000291281; ENSG00000105287.
ENST00000433867; ENSP00000393978; ENSG00000105287.
ENST00000600194; ENSP00000472744; ENSG00000105287.
ENST00000601806; ENSP00000469106; ENSG00000105287.
GeneIDi25865.
KEGGihsa:25865.
UCSCiuc002pfi.4. human. [Q9BZL6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF309082 mRNA. Translation: AAK01149.1.
AK074673 mRNA. Translation: BAC11127.1.
AK095884 mRNA. Translation: BAG53158.1.
AC008635 Genomic DNA. No translation available.
AC093503 Genomic DNA. No translation available.
KC877745 Genomic DNA. No translation available.
AL050147 mRNA. Translation: CAB43292.1.
AF151021 mRNA. Translation: AAF36107.1. Frameshift.
CCDSiCCDS12689.1. [Q9BZL6-1]
CCDS59401.1. [Q9BZL6-2]
PIRiT08777.
RefSeqiNP_001073349.1. NM_001079880.1.
NP_001073350.1. NM_001079881.1.
NP_001073351.1. NM_001079882.1.
NP_057541.2. NM_016457.4.
XP_005258773.2. XM_005258716.2.
UniGeneiHs.466987.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2COANMR-A398-509[»]
3BGMX-ray1.60C526-534[»]
4NNXX-ray2.10C526-534[»]
4NNYX-ray1.90C526-534[»]
ProteinModelPortaliQ9BZL6.
SMRiQ9BZL6. Positions 138-188, 237-357, 395-509, 537-846.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117384. 38 interactions.
IntActiQ9BZL6. 35 interactions.
MINTiMINT-1179710.
STRINGi9606.ENSP00000291281.

Chemistry

BindingDBiQ9BZL6.
ChEMBLiCHEMBL4900.
GuidetoPHARMACOLOGYi2173.

PTM databases

iPTMnetiQ9BZL6.
PhosphoSiteiQ9BZL6.

Polymorphism and mutation databases

BioMutaiPRKD2.
DMDMi296434570.

Proteomic databases

EPDiQ9BZL6.
MaxQBiQ9BZL6.
PaxDbiQ9BZL6.
PeptideAtlasiQ9BZL6.
PRIDEiQ9BZL6.

Protocols and materials databases

DNASUi25865.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000291281; ENSP00000291281; ENSG00000105287.
ENST00000433867; ENSP00000393978; ENSG00000105287.
ENST00000600194; ENSP00000472744; ENSG00000105287.
ENST00000601806; ENSP00000469106; ENSG00000105287.
GeneIDi25865.
KEGGihsa:25865.
UCSCiuc002pfi.4. human. [Q9BZL6-1]

Organism-specific databases

CTDi25865.
GeneCardsiPRKD2.
HGNCiHGNC:17293. PRKD2.
HPAiHPA021490.
HPA056727.
MIMi607074. gene.
neXtProtiNX_Q9BZL6.
PharmGKBiPA134903505.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4236. Eukaryota.
ENOG410XQZ3. LUCA.
HOGENOMiHOG000015135.
HOVERGENiHBG003564.
InParanoidiQ9BZL6.
KOiK06070.
PhylomeDBiQ9BZL6.
TreeFamiTF314320.

Enzyme and pathway databases

BRENDAi2.7.11.13. 2681.
SignaLinkiQ9BZL6.
SIGNORiQ9BZL6.

Miscellaneous databases

ChiTaRSiPRKD2. human.
EvolutionaryTraceiQ9BZL6.
GeneWikiiPRKD2.
GenomeRNAii25865.
PROiQ9BZL6.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000105287.
CleanExiHS_PKD2.
HS_PRKD2.
ExpressionAtlasiQ9BZL6. baseline and differential.
GenevisibleiQ9BZL6. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015727. Protein_Kinase_C_mu-related.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR22968. PTHR22968. 1 hit.
PfamiPF00130. C1_1. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000552. PKC_mu_nu_D2. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 2 hits.
SM00233. PH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiKPCD2_HUMAN
AccessioniPrimary (citable) accession number: Q9BZL6
Secondary accession number(s): M0R2R2
, Q8NCK8, Q8TB08, Q9P0T6, Q9Y3X8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: May 18, 2010
Last modified: September 7, 2016
This is version 172 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 19
    Human chromosome 19: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.