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Protein

Serine/threonine-protein kinase D1

Gene

PRKD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. Phosphorylates the epidermal growth factor receptor (EGFR) on dual threonine residues, which leads to the suppression of epidermal growth factor (EGF)-induced MAPK8/JNK1 activation and subsequent JUN phosphorylation. Phosphorylates RIN1, inducing RIN1 binding to 14-3-3 proteins YWHAB, YWHAE and YWHAZ and increased competition with RAF1 for binding to GTP-bound form of Ras proteins (NRAS, HRAS and KRAS). Acts downstream of the heterotrimeric G-protein beta/gamma-subunit complex to maintain the structural integrity of the Golgi membranes, and is required for protein transport along the secretory pathway. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane. May act by activating the lipid kinase phosphatidylinositol 4-kinase beta (PI4KB) at the TGN for the local synthesis of phosphorylated inositol lipids, which induces a sequential production of DAG, phosphatidic acid (PA) and lyso-PA (LPA) that are necessary for membrane fission and generation of specific transport carriers to the cell surface. Under oxidative stress, is phosphorylated at Tyr-463 via SRC-ABL1 and contributes to cell survival by activating IKK complex and subsequent nuclear translocation and activation of NFKB1. Involved in cell migration by regulating integrin alpha-5/beta-3 recycling and promoting its recruitment in newly forming focal adhesion. In osteoblast differentiation, mediates the bone morphogenetic protein 2 (BMP2)-induced nuclear export of HDAC7, which results in the inhibition of HDAC7 transcriptional repression of RUNX2. In neurons, plays an important role in neuronal polarity by regulating the biogenesis of TGN-derived dendritic vesicles, and is involved in the maintenance of dendritic arborization and Golgi structure in hippocampal cells. May potentiate mitogenesis induced by the neuropeptide bombesin or vasopressin 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. Plays an important role in the proliferative response induced by low calcium in keratinocytes, through sustained activation of MAPK1/3 (ERK1/2) pathway. Downstream of novel PKC signaling, plays a role in cardiac hypertrophy by phosphorylating HDAC5, which in turn triggers XPO1/CRM1-dependent nuclear export of HDAC5, MEF2A transcriptional activation and induction of downstream target genes that promote myocyte hypertrophy and pathological cardiac remodeling. Mediates cardiac troponin I (TNNI3) phosphorylation at the PKA sites, which results in reduced myofilament calcium sensitivity, and accelerated crossbridge cycling kinetics. The PRKD1-HDAC5 pathway is also involved in angiogenesis by mediating VEGFA-induced specific subset of gene expression, cell migration, and tube formation. In response to VEGFA, is necessary and required for HDAC7 phosphorylation which induces HDAC7 nuclear export and endothelial cell proliferation and migration. During apoptosis induced by cytarabine and other genotoxic agents, PRKD1 is cleaved by caspase-3 at Asp-378, resulting in activation of its kinase function and increased sensitivity of cells to the cytotoxic effects of genotoxic agents. In epithelial cells, is required for transducing flagellin-stimulated inflammatory responses by binding and phosphorylating TLR5, which contributes to MAPK14/p38 activation and production of inflammatory cytokines. May play a role in inflammatory response by mediating activation of NF-kappa-B. May be involved in pain transmission by directly modulating TRPV1 receptor. Plays a role in activated KRAS-mediated stabilization of ZNF304 in colorectal cancer (CRC) cells (PubMed:24623306). Regulates nuclear translocation of transcription factor TFEB in macrophages upon live S.enterica infection (By similarity).By similarity11 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Activity regulationi

Activated by DAG and phorbol esters. Phorbol-ester/DAG-type domain 1 binds DAG with high affinity and appears to play the dominant role in mediating translocation to the cell membrane and trans-Golgi network. Phorbol-ester/DAG-type domain 2 binds phorbol ester with higher affinity. Autophosphorylation of Ser-742 and phosphorylation of Ser-738 by PKC relieves auto-inhibition by the PH domain. Phosphorylation on Tyr-463 by the SRC-ABL1 pathway in response to oxidative stress, is also required for activation. Activated by DAPK1 under oxidative stress.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei612ATP1
Active sitei706Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri146 – 196Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri270 – 320Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51
Nucleotide bindingi589 – 597ATPPROSITE-ProRule annotation9

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processAngiogenesis, Apoptosis, Differentiation, Immunity, Inflammatory response, Innate immunity, Neurogenesis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.11.13 2681
ReactomeiR-HSA-1660661 Sphingolipid de novo biosynthesis
SignaLinkiQ15139
SIGNORiQ15139

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase D1 (EC:2.7.11.13)
Alternative name(s):
Protein kinase C mu type
Protein kinase D
nPKC-D1
nPKC-mu
Gene namesi
Name:PRKD1
Synonyms:PKD, PKD1, PRKCM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiHostDB:ENSG00000184304.14
HGNCiHGNC:9407 PRKD1
MIMi605435 gene
neXtProtiNX_Q15139

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Congenital heart defects and ectodermal dysplasia (CHDED)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant syndrome characterized by atrial and/or ventricular septal congenital heart defects and variable features of ectodermal dysplasia, including sparse hair, dry skin, thin skin, fragile nails, premature loss of primary teeth, and small widely spaced teeth. Patients manifest developmental disabilities ranging from motor delay and delayed speech to global developmental retardation.
See also OMIM:617364
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078602299L → W in CHDED. 1 PublicationCorresponds to variant dbSNP:rs1057519636Ensembl.1
Natural variantiVAR_078603592G → R in CHDED. 1 PublicationCorresponds to variant dbSNP:rs1057519635Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi157P → G: Increase in ability to bind phorbol ester, loss of ability to bind DAG. 1 Publication1
Mutagenesisi281P → G: No effect on ability to bind phorbol ester, slight increase in ability to bind DAG. 1 Publication1
Mutagenesisi432Y → E: Decreased phosphorylation level when coexpressed with SRC in HeLa cells. Unchanged phosphorylation level when coexpressed with ABL. 1 Publication1
Mutagenesisi432Y → F: Decreased phosphorylation level when coexpressed with SRC in HeLa cells. Unchanged phosphorylation level when coexpressed with ABL. Unaltered kinase activity. Decreased kinase activity; when associated with F-463 and F-502. 1 Publication1
Mutagenesisi463Y → E: Constitutive activation and constitutive phosphorylation of S-738 and S-742. 1 Publication1
Mutagenesisi463Y → F: Decreased phosphorylation level when coexpressed with either SRC or ABL in HeLa cells. Decreased kinase activity. 1 Publication1
Mutagenesisi502Y → E: Loss of activation. 1 Publication1
Mutagenesisi502Y → F: Decreased phosphorylation level when coexpressed with SRC in HeLa cells. Unchanged phosphorylation level when coexpressed with ABL. Unaltered kinase activity. Decreased kinase activity; when associated with F-432 and F-502. 1 Publication1
Mutagenesisi612K → W: Loss of kinase activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Ectodermal dysplasia

Organism-specific databases

DisGeNETi5587
MalaCardsiPRKD1
MIMi617364 phenotype
OpenTargetsiENSG00000184304
Orphaneti276145 Malignant epithelial tumor of salivary glands
PharmGKBiPA33771

Chemistry databases

ChEMBLiCHEMBL3863
GuidetoPHARMACOLOGYi1489

Polymorphism and mutation databases

BioMutaiPRKD1
DMDMi209572639

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000557141 – 912Serine/threonine-protein kinase D1Add BLAST912

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei95Phosphotyrosine1 Publication1
Modified residuei205PhosphoserineCombined sources1
Modified residuei208PhosphoserineCombined sources1
Modified residuei219PhosphoserineBy similarity1
Modified residuei223PhosphoserineBy similarity1
Modified residuei345PhosphoserineCombined sources1
Modified residuei397Phosphoserine; by MAPK131 Publication1
Modified residuei401Phosphoserine; by MAPK131 Publication1
Modified residuei432Phosphotyrosine1 Publication1
Modified residuei448PhosphoserineCombined sources1
Modified residuei463Phosphotyrosine; by ABL2 Publications1
Modified residuei473PhosphoserineCombined sources1
Modified residuei502Phosphotyrosine1 Publication1
Modified residuei548PhosphoserineBy similarity1
Modified residuei738Phosphoserine; by PKC/PRKCD1 Publication1
Modified residuei742Phosphoserine; by autocatalysis and PKC/PRKCD1 Publication1
Modified residuei749PhosphotyrosineBy similarity1
Modified residuei910Phosphoserine; by autocatalysis1 Publication1

Post-translational modificationi

Phosphorylated at Ser-397 and Ser-401 by MAPK13 during regulation of insulin secretion in pancreatic beta cells (PubMed:19135240). Phosphorylated by DAPK1 (PubMed:17703233). Phosphorylated at Tyr-95 and by ABL at Tyr-463, which primes the kinase in response to oxidative stress, and promotes a second step activating phosphorylation at Ser-738/Ser-742 by PKRD (PubMed:12637538, PubMed:15024053, PubMed:17804414). Phosphorylated on Ser-910 upon S.enterica infection in macrophages (By similarity).By similarity5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ15139
MaxQBiQ15139
PaxDbiQ15139
PeptideAtlasiQ15139
PRIDEiQ15139
ProteomicsDBi60458

PTM databases

iPTMnetiQ15139
PhosphoSitePlusiQ15139

Expressioni

Inductioni

Up-regulated by the intestine-specific transcription factor CDX1 in an activated KRAS-dependent manner in colorectal cancer (CRC) cells (PubMed:24623306).1 Publication

Gene expression databases

BgeeiENSG00000184304 Expressed in 184 organ(s), highest expression level in urinary bladder
CleanExiHS_PKD1
HS_PRKD1
ExpressionAtlasiQ15139 baseline and differential
GenevisibleiQ15139 HS

Organism-specific databases

HPAiCAB018367
HPA029834

Interactioni

Subunit structurei

Interacts (via N-terminus) with ADAP1/CENTA1 (PubMed:12893243). Interacts with MAPK13 (PubMed:19135240). Interacts with DAPK1 in an oxidative stress-regulated manner (PubMed:17703233). Interacts with USP28; the interaction induces phosphorylation of USP28 and activated KRAS-mediated stabilization of ZNF304 (PubMed:24623306). Interacts with AKAP13 (via C-terminal domain) (By similarity).By similarity4 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi111573, 38 interactors
DIPiDIP-38481N
IntActiQ15139, 11 interactors
STRINGi9606.ENSP00000333568

Chemistry databases

BindingDBiQ15139

Structurei

3D structure databases

ProteinModelPortaliQ15139
SMRiQ15139
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini422 – 541PHPROSITE-ProRule annotationAdd BLAST120
Domaini583 – 839Protein kinasePROSITE-ProRule annotationAdd BLAST257

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi17 – 26Poly-Ala10
Compositional biasi200 – 203Poly-Arg4

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri146 – 196Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri270 – 320Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG4236 Eukaryota
ENOG410XQZ3 LUCA
GeneTreeiENSGT00930000150929
HOVERGENiHBG003564
InParanoidiQ15139
KOiK06070
PhylomeDBiQ15139
TreeFamiTF314320

Family and domain databases

CDDicd00029 C1, 2 hits
Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR020454 DAG/PE-bd
IPR011009 Kinase-like_dom_sf
IPR002219 PE/DAG-bd
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR015727 Protein_Kinase_C_mu-related
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR22968 PTHR22968, 1 hit
PfamiView protein in Pfam
PF00130 C1_1, 2 hits
PF00169 PH, 1 hit
PF00069 Pkinase, 1 hit
PIRSFiPIRSF000552 PKC_mu_nu_D2, 1 hit
PRINTSiPR00008 DAGPEDOMAIN
SMARTiView protein in SMART
SM00109 C1, 2 hits
SM00233 PH, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50003 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

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

Q15139-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSAPPVLRPP SPLLPVAAAA AAAAAALVPG SGPGPAPFLA PVAAPVGGIS
60 70 80 90 100
FHLQIGLSRE PVLLLQDSSG DYSLAHVREM ACSIVDQKFP ECGFYGMYDK
110 120 130 140 150
ILLFRHDPTS ENILQLVKAA SDIQEGDLIE VVLSASATFE DFQIRPHALF
160 170 180 190 200
VHSYRAPAFC DHCGEMLWGL VRQGLKCEGC GLNYHKRCAF KIPNNCSGVR
210 220 230 240 250
RRRLSNVSLT GVSTIRTSSA ELSTSAPDEP LLQKSPSESF IGREKRSNSQ
260 270 280 290 300
SYIGRPIHLD KILMSKVKVP HTFVIHSYTR PTVCQYCKKL LKGLFRQGLQ
310 320 330 340 350
CKDCRFNCHK RCAPKVPNNC LGEVTINGDL LSPGAESDVV MEEGSDDNDS
360 370 380 390 400
ERNSGLMDDM EEAMVQDAEM AMAECQNDSG EMQDPDPDHE DANRTISPST
410 420 430 440 450
SNNIPLMRVV QSVKHTKRKS STVMKEGWMV HYTSKDTLRK RHYWRLDSKC
460 470 480 490 500
ITLFQNDTGS RYYKEIPLSE ILSLEPVKTS ALIPNGANPH CFEITTANVV
510 520 530 540 550
YYVGENVVNP SSPSPNNSVL TSGVGADVAR MWEIAIQHAL MPVIPKGSSV
560 570 580 590 600
GTGTNLHRDI SVSISVSNCQ IQENVDISTV YQIFPDEVLG SGQFGIVYGG
610 620 630 640 650
KHRKTGRDVA IKIIDKLRFP TKQESQLRNE VAILQNLHHP GVVNLECMFE
660 670 680 690 700
TPERVFVVME KLHGDMLEMI LSSEKGRLPE HITKFLITQI LVALRHLHFK
710 720 730 740 750
NIVHCDLKPE NVLLASADPF PQVKLCDFGF ARIIGEKSFR RSVVGTPAYL
760 770 780 790 800
APEVLRNKGY NRSLDMWSVG VIIYVSLSGT FPFNEDEDIH DQIQNAAFMY
810 820 830 840 850
PPNPWKEISH EAIDLINNLL QVKMRKRYSV DKTLSHPWLQ DYQTWLDLRE
860 870 880 890 900
LECKIGERYI THESDDLRWE KYAGEQGLQY PTHLINPSAS HSDTPETEET
910
EMKALGERVS IL
Length:912
Mass (Da):101,704
Last modified:October 14, 2008 - v2
Checksum:i0BC9414C335D2DBB
GO

Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8WBA3F8WBA3_HUMAN
Serine/threonine-protein kinase
PRKD1
920Annotation score:
F8VZ98F8VZ98_HUMAN
Serine/threonine-protein kinase D1
PRKD1
117Annotation score:
H0YHL5H0YHL5_HUMAN
Serine/threonine-protein kinase D1
PRKD1
157Annotation score:
H0YHS9H0YHS9_HUMAN
Serine/threonine-protein kinase D1
PRKD1
80Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti135A → R in CAA53384 (PubMed:8119958).Curated1
Sequence conflicti877G → R in CAA53384 (PubMed:8119958).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035468152H → Y in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_042324225S → P1 Publication1
Natural variantiVAR_078602299L → W in CHDED. 1 PublicationCorresponds to variant dbSNP:rs1057519636Ensembl.1
Natural variantiVAR_042325478K → Q1 PublicationCorresponds to variant dbSNP:rs55852813Ensembl.1
Natural variantiVAR_042326585P → S in a metastatic melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_078603592G → R in CHDED. 1 PublicationCorresponds to variant dbSNP:rs1057519635Ensembl.1
Natural variantiVAR_042327677R → M in a lung bronchoalveolar carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042328679P → L1 PublicationCorresponds to variant dbSNP:rs34588699Ensembl.1
Natural variantiVAR_046988825R → K. Corresponds to variant dbSNP:rs11161065Ensembl.1
Natural variantiVAR_035469857E → K in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_042329891H → R1 PublicationCorresponds to variant dbSNP:rs45582934Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75756 mRNA Translation: CAA53384.1
AK314170 mRNA Translation: BAG36853.1
AL135858 Genomic DNA No translation available.
CH471078 Genomic DNA Translation: EAW65971.1
CCDSiCCDS9637.1
PIRiA53215
RefSeqiNP_002733.2, NM_002742.2
UniGeneiHs.508999

Genome annotation databases

EnsembliENST00000331968; ENSP00000333568; ENSG00000184304
ENST00000616995; ENSP00000482645; ENSG00000184304
GeneIDi5587
KEGGihsa:5587
UCSCiuc001wqh.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75756 mRNA Translation: CAA53384.1
AK314170 mRNA Translation: BAG36853.1
AL135858 Genomic DNA No translation available.
CH471078 Genomic DNA Translation: EAW65971.1
CCDSiCCDS9637.1
PIRiA53215
RefSeqiNP_002733.2, NM_002742.2
UniGeneiHs.508999

3D structure databases

ProteinModelPortaliQ15139
SMRiQ15139
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111573, 38 interactors
DIPiDIP-38481N
IntActiQ15139, 11 interactors
STRINGi9606.ENSP00000333568

Chemistry databases

BindingDBiQ15139
ChEMBLiCHEMBL3863
GuidetoPHARMACOLOGYi1489

PTM databases

iPTMnetiQ15139
PhosphoSitePlusiQ15139

Polymorphism and mutation databases

BioMutaiPRKD1
DMDMi209572639

Proteomic databases

EPDiQ15139
MaxQBiQ15139
PaxDbiQ15139
PeptideAtlasiQ15139
PRIDEiQ15139
ProteomicsDBi60458

Protocols and materials databases

DNASUi5587
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331968; ENSP00000333568; ENSG00000184304
ENST00000616995; ENSP00000482645; ENSG00000184304
GeneIDi5587
KEGGihsa:5587
UCSCiuc001wqh.4 human

Organism-specific databases

CTDi5587
DisGeNETi5587
EuPathDBiHostDB:ENSG00000184304.14
GeneCardsiPRKD1
H-InvDBiHIX0037727
HGNCiHGNC:9407 PRKD1
HPAiCAB018367
HPA029834
MalaCardsiPRKD1
MIMi605435 gene
617364 phenotype
neXtProtiNX_Q15139
OpenTargetsiENSG00000184304
Orphaneti276145 Malignant epithelial tumor of salivary glands
PharmGKBiPA33771
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4236 Eukaryota
ENOG410XQZ3 LUCA
GeneTreeiENSGT00930000150929
HOVERGENiHBG003564
InParanoidiQ15139
KOiK06070
PhylomeDBiQ15139
TreeFamiTF314320

Enzyme and pathway databases

BRENDAi2.7.11.13 2681
ReactomeiR-HSA-1660661 Sphingolipid de novo biosynthesis
SignaLinkiQ15139
SIGNORiQ15139

Miscellaneous databases

ChiTaRSiPRKD1 human
GeneWikiiProtein_kinase_D1
GenomeRNAii5587
PROiPR:Q15139
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000184304 Expressed in 184 organ(s), highest expression level in urinary bladder
CleanExiHS_PKD1
HS_PRKD1
ExpressionAtlasiQ15139 baseline and differential
GenevisibleiQ15139 HS

Family and domain databases

CDDicd00029 C1, 2 hits
Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR020454 DAG/PE-bd
IPR011009 Kinase-like_dom_sf
IPR002219 PE/DAG-bd
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR015727 Protein_Kinase_C_mu-related
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR22968 PTHR22968, 1 hit
PfamiView protein in Pfam
PF00130 C1_1, 2 hits
PF00169 PH, 1 hit
PF00069 Pkinase, 1 hit
PIRSFiPIRSF000552 PKC_mu_nu_D2, 1 hit
PRINTSiPR00008 DAGPEDOMAIN
SMARTiView protein in SMART
SM00109 C1, 2 hits
SM00233 PH, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50003 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
ProtoNetiSearch...

Entry informationi

Entry nameiKPCD1_HUMAN
AccessioniPrimary (citable) accession number: Q15139
Secondary accession number(s): A6NL64, B2RAF6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 14, 2008
Last modified: November 7, 2018
This is version 190 of the entry and version 2 of the sequence. See 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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