PRKD3 | ENSG00000115825 | NCBI 23683

Details for: PRKD3

Gene ID: 23683

Symbol: PRKD3

Ensembl ID: ENSG00000115825

Description: protein kinase D3

Associated with

Metabolism
(R-HSA-1430728)
Metabolism of lipids
(R-HSA-556833)
Sphingolipid de novo biosynthesis
(R-HSA-1660661)
Sphingolipid metabolism
(R-HSA-428157)
Atp binding
(GO:0005524)
Cytosol
(GO:0005829)
Diacylglycerol-dependent serine/threonine kinase activity
(GO:0004697)
Intracellular signal transduction
(GO:0035556)
Kinase activity
(GO:0016301)
Metal ion binding
(GO:0046872)
Nucleoplasm
(GO:0005654)
Phospholipase c-activating g protein-coupled receptor signaling pathway
(GO:0007200)
Plasma membrane
(GO:0005886)
Protein binding
(GO:0005515)
Protein kinase c-activating g protein-coupled receptor signaling pathway
(GO:0007205)
Protein phosphorylation
(GO:0006468)
Protein serine/threonine kinase activity
(GO:0004674)
Protein serine kinase activity
(GO:0106310)
Sphingolipid biosynthetic process
(GO:0030148)

Other Information

Proteins

Serine/threonine-protein kinase D3

Genular Protein ID: 400956723

Symbol: KPCD3_HUMAN

Name: Serine/threonine-protein kinase D3

UniProtKB Accession Codes:

O94806 D6W587 Q53TR7 Q8NEL8

Database IDs:

Citations:

PubMed ID: 10231560

Title: PKCnu, a new member of the protein kinase C family, composes a fourth subfamily with PKCmu.

PubMed ID: 10231560

DOI: 10.1016/s0167-4889(99)00040-3

PubMed ID: 15815621

Title: Generation and annotation of the DNA sequences of human chromosomes 2 and 4.

PubMed ID: 15815621

DOI: 10.1038/nature03466

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 18076381

Title: Selective binding of phorbol esters and diacylglycerol by individual C1 domains of the PKD family.

PubMed ID: 18076381

DOI: 10.1042/bj20071334

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19369195

Title: Large-scale proteomics analysis of the human kinome.

PubMed ID: 19369195

DOI: 10.1074/mcp.m800588-mcp200

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 17344846

Title: Patterns of somatic mutation in human cancer genomes.

PubMed ID: 17344846

DOI: 10.1038/nature05610

Sequence Information:

Length: 890
Mass: 100471
Checksum: 66D5E7E7235064F5
Sequence:

MSANNSPPSA QKSVLPTAIP AVLPAASPCS SPKTGLSARL SNGSFSAPSL TNSRGSVHTV 
SFLLQIGLTR ESVTIEAQEL SLSAVKDLVC SIVYQKFPEC GFFGMYDKIL LFRHDMNSEN 
ILQLITSADE IHEGDLVEVV LSALATVEDF QIRPHTLYVH SYKAPTFCDY CGEMLWGLVR 
QGLKCEGCGL NYHKRCAFKI PNNCSGVRKR RLSNVSLPGP GLSVPRPLQP EYVALPSEES 
HVHQEPSKRI PSWSGRPIWM EKMVMCRVKV PHTFAVHSYT RPTICQYCKR LLKGLFRQGM 
QCKDCKFNCH KRCASKVPRD CLGEVTFNGE PSSLGTDTDI PMDIDNNDIN SDSSRGLDDT 
EEPSPPEDKM FFLDPSDLDV ERDEEAVKTI SPSTSNNIPL MRVVQSIKHT KRKSSTMVKE 
GWMVHYTSRD NLRKRHYWRL DSKCLTLFQN ESGSKYYKEI PLSEILRISS PRDFTNISQG 
SNPHCFEIIT DTMVYFVGEN NGDSSHNPVL AATGVGLDVA QSWEKAIRQA LMPVTPQASV 
CTSPGQGKDH KDLSTSISVS NCQIQENVDI STVYQIFADE VLGSGQFGIV YGGKHRKTGR 
DVAIKVIDKM RFPTKQESQL RNEVAILQNL HHPGIVNLEC MFETPERVFV VMEKLHGDML 
EMILSSEKSR LPERITKFMV TQILVALRNL HFKNIVHCDL KPENVLLASA EPFPQVKLCD 
FGFARIIGEK SFRRSVVGTP AYLAPEVLRS KGYNRSLDMW SVGVIIYVSL SGTFPFNEDE 
DINDQIQNAA FMYPPNPWRE ISGEAIDLIN NLLQVKMRKR YSVDKSLSHP WLQDYQTWLD 
LREFETRIGE RYITHESDDA RWEIHAYTHN LVYPKHFIMA PNPDDMEEDP

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: PRKD3

Associated with

Other Information

PKCnu, a new member of the protein kinase C family, composes a fourth subfamily with PKCmu. PubMed ID: 10231560

Generation and annotation of the DNA sequences of human chromosomes 2 and 4. PubMed ID: 15815621

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PubMed ID: 16964243

Selective binding of phorbol esters and diacylglycerol by individual C1 domains of the PKD family. PubMed ID: 18076381

Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. PubMed ID: 18691976

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Large-scale proteomics analysis of the human kinome. PubMed ID: 19369195

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

Patterns of somatic mutation in human cancer genomes. PubMed ID: 17344846