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Protein

Serine/threonine-protein kinase D3

Gene

PRKD3

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

Functioni

Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress (By similarity).By similarity

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 1 and 2 bind both DAG and phorbol ester with high affinity and mediate translocation to the cell membrane. Autophosphorylation of Ser-735 and phosphorylation of Ser-731 by PKC relieves auto-inhibition by the PH domain.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei605 – 6051ATPPROSITE-ProRule annotation
Active sitei699 – 6991Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri154 – 20451Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri271 – 32151Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi582 – 5909ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • kinase activity Source: CACAO
  • metal ion binding Source: UniProtKB-KW
  • protein kinase C activity Source: ProtInc

GO - Biological processi

  • intracellular signal transduction Source: InterPro
  • protein kinase C-activating G-protein coupled receptor signaling pathway Source: ProtInc
  • protein phosphorylation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi2.7.11.13. 2681.
SignaLinkiO94806.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase D3 (EC:2.7.11.13)
Alternative name(s):
Protein kinase C nu type
Protein kinase EPK2
nPKC-nu
Gene namesi
Name:PRKD3
Synonyms:EPK2, PRKCN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:9408. PRKD3.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Membrane 1 Publication

  • Note: Translocation to the cell membrane is required for kinase activation.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi156 – 1561T → A: Slight loss in ability to bind DAG and phorbol-ester; when associated with F-158. 1 Publication
Mutagenesisi158 – 1581Y → F: Slight loss in ability to bind DAG and phorbol-ester; when associated with A-156. 1 Publication
Mutagenesisi165 – 1651P → G: No effect on ability to bind phorbol ester, loss of ability to bind DAG, reduced DAG-induced membrane translocation. 1 Publication
Mutagenesisi166 – 1661T → A: Slight loss in ability to bind DAG and phorbol-ester. 1 Publication
Mutagenesisi170 – 1701Y → F: Slight loss in ability to bind DAG and phorbol-ester. 1 Publication
Mutagenesisi282 – 2821P → G: No effect on ability to bind phorbol ester, increase in ability to bind DAG. 1 Publication
Mutagenesisi284 – 2841I → V: Slight increase in ability to bind DAG, no effect on phorbol-ester binding.
Mutagenesisi293 – 2931K → W: Increased ability to bind DAG, no effect on phorbol-ester binding. 1 Publication

Organism-specific databases

PharmGKBiPA33772.

Polymorphism and mutation databases

BioMutaiPRKD3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 890890Serine/threonine-protein kinase D3PRO_0000055717Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61Phosphoserine1 Publication
Modified residuei27 – 271Phosphoserine4 Publications
Modified residuei37 – 371Phosphoserine1 Publication
Modified residuei41 – 411Phosphoserine4 Publications
Modified residuei44 – 441Phosphoserine2 Publications
Modified residuei213 – 2131Phosphoserine2 Publications
Modified residuei216 – 2161Phosphoserine2 Publications
Modified residuei364 – 3641Phosphoserine4 Publications
Modified residuei391 – 3911PhosphoserineBy similarity
Modified residuei395 – 3951PhosphoserineBy similarity
Modified residuei426 – 4261PhosphotyrosineBy similarity
Modified residuei442 – 4421PhosphoserineBy similarity
Modified residuei457 – 4571PhosphotyrosineBy similarity
Modified residuei535 – 5351Phosphothreonine2 Publications
Modified residuei731 – 7311Phosphoserine; by PKCBy similarity
Modified residuei735 – 7351Phosphoserine; by autocatalysisBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO94806.
PaxDbiO94806.
PRIDEiO94806.

PTM databases

PhosphoSiteiO94806.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiO94806.
CleanExiHS_PRKD3.
ExpressionAtlasiO94806. baseline and differential.
GenevestigatoriO94806.

Organism-specific databases

HPAiHPA029529.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
VAMP2P630277EBI-1255366,EBI-520113

Protein-protein interaction databases

BioGridi117199. 8 interactions.
IntActiO94806. 10 interactions.
MINTiMINT-5003932.
STRINGi9606.ENSP00000234179.

Structurei

Secondary structure

1
890
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi417 – 42913Combined sources
Beta strandi434 – 44310Combined sources
Beta strandi445 – 4495Combined sources
Turni462 – 4643Combined sources
Beta strandi477 – 4793Combined sources
Beta strandi485 – 4895Combined sources
Beta strandi494 – 4974Combined sources
Turni508 – 5147Combined sources
Helixi517 – 53216Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9ZNMR-A417-532[»]
ProteinModelPortaliO94806.
SMRiO94806. Positions 155-204, 241-321, 414-532, 537-837.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO94806.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini416 – 532117PHPROSITE-ProRule annotationAdd
BLAST
Domaini576 – 832257Protein 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 fingeri154 – 20451Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri271 – 32151Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000121901.
HOGENOMiHOG000015135.
HOVERGENiHBG003564.
InParanoidiO94806.
KOiK06070.
OMAiHYTSRDT.
OrthoDBiEOG75B84N.
PhylomeDBiO94806.
TreeFamiTF314320.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015727. Protein_Kinase_C_mu-related.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR22968. PTHR22968. 1 hit.
PfamiPF00130. C1_1. 2 hits.
PF00169. PH. 1 hit.
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]
SUPFAMiSSF56112. 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: O94806-1) [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
MSANNSPPSA QKSVLPTAIP AVLPAASPCS SPKTGLSARL SNGSFSAPSL
60 70 80 90 100
TNSRGSVHTV SFLLQIGLTR ESVTIEAQEL SLSAVKDLVC SIVYQKFPEC
110 120 130 140 150
GFFGMYDKIL LFRHDMNSEN ILQLITSADE IHEGDLVEVV LSALATVEDF
160 170 180 190 200
QIRPHTLYVH SYKAPTFCDY CGEMLWGLVR QGLKCEGCGL NYHKRCAFKI
210 220 230 240 250
PNNCSGVRKR RLSNVSLPGP GLSVPRPLQP EYVALPSEES HVHQEPSKRI
260 270 280 290 300
PSWSGRPIWM EKMVMCRVKV PHTFAVHSYT RPTICQYCKR LLKGLFRQGM
310 320 330 340 350
QCKDCKFNCH KRCASKVPRD CLGEVTFNGE PSSLGTDTDI PMDIDNNDIN
360 370 380 390 400
SDSSRGLDDT EEPSPPEDKM FFLDPSDLDV ERDEEAVKTI SPSTSNNIPL
410 420 430 440 450
MRVVQSIKHT KRKSSTMVKE GWMVHYTSRD NLRKRHYWRL DSKCLTLFQN
460 470 480 490 500
ESGSKYYKEI PLSEILRISS PRDFTNISQG SNPHCFEIIT DTMVYFVGEN
510 520 530 540 550
NGDSSHNPVL AATGVGLDVA QSWEKAIRQA LMPVTPQASV CTSPGQGKDH
560 570 580 590 600
KDLSTSISVS NCQIQENVDI STVYQIFADE VLGSGQFGIV YGGKHRKTGR
610 620 630 640 650
DVAIKVIDKM RFPTKQESQL RNEVAILQNL HHPGIVNLEC MFETPERVFV
660 670 680 690 700
VMEKLHGDML EMILSSEKSR LPERITKFMV TQILVALRNL HFKNIVHCDL
710 720 730 740 750
KPENVLLASA EPFPQVKLCD FGFARIIGEK SFRRSVVGTP AYLAPEVLRS
760 770 780 790 800
KGYNRSLDMW SVGVIIYVSL SGTFPFNEDE DINDQIQNAA FMYPPNPWRE
810 820 830 840 850
ISGEAIDLIN NLLQVKMRKR YSVDKSLSHP WLQDYQTWLD LREFETRIGE
860 870 880 890
RYITHESDDA RWEIHAYTHN LVYPKHFIMA PNPDDMEEDP
Length:890
Mass (Da):100,471
Last modified:May 1, 1999 - v1
Checksum:i66D5E7E7235064F5
GO
Isoform 2 (identifier: O94806-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     595-611: HRKTGRDVAIKVIDKMR → QLQPFAYCTHYFKNWKM
     612-890: Missing.

Show »
Length:611
Mass (Da):68,123
Checksum:i1714FAD7DA82C942
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti42 – 421N → D.
Corresponds to variant rs11896614 [ dbSNP | Ensembl ].
VAR_037147
Natural varianti128 – 1281A → T.1 Publication
Corresponds to variant rs17852819 [ dbSNP | Ensembl ].
VAR_037148
Natural varianti225 – 2251P → S.
Corresponds to variant rs34280934 [ dbSNP | Ensembl ].
VAR_050561
Natural varianti445 – 4451L → I.
Corresponds to variant rs55912911 [ dbSNP | Ensembl ].
VAR_061532
Natural varianti546 – 5461Q → R.1 Publication
Corresponds to variant rs17856887 [ dbSNP | Ensembl ].
VAR_037149
Natural varianti716 – 7161V → M in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_042336

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei595 – 61117HRKTG…IDKMR → QLQPFAYCTHYFKNWKM in isoform 2. 1 PublicationVSP_029405Add
BLAST
Alternative sequencei612 – 890279Missing in isoform 2. 1 PublicationVSP_029406Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015982 mRNA. Translation: BAA36514.1.
AC007390 Genomic DNA. Translation: AAY14817.1.
CH471053 Genomic DNA. Translation: EAX00398.1.
CH471053 Genomic DNA. Translation: EAX00399.1.
BC030706 mRNA. Translation: AAH30706.1.
CCDSiCCDS1789.1. [O94806-1]
RefSeqiNP_005804.1. NM_005813.4. [O94806-1]
XP_005264294.1. XM_005264237.2. [O94806-1]
UniGeneiHs.660757.
Hs.716034.

Genome annotation databases

EnsembliENST00000234179; ENSP00000234179; ENSG00000115825. [O94806-1]
ENST00000379066; ENSP00000368356; ENSG00000115825. [O94806-1]
GeneIDi23683.
KEGGihsa:23683.
UCSCiuc002rqd.3. human. [O94806-1]
uc002rqf.1. human. [O94806-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015982 mRNA. Translation: BAA36514.1.
AC007390 Genomic DNA. Translation: AAY14817.1.
CH471053 Genomic DNA. Translation: EAX00398.1.
CH471053 Genomic DNA. Translation: EAX00399.1.
BC030706 mRNA. Translation: AAH30706.1.
CCDSiCCDS1789.1. [O94806-1]
RefSeqiNP_005804.1. NM_005813.4. [O94806-1]
XP_005264294.1. XM_005264237.2. [O94806-1]
UniGeneiHs.660757.
Hs.716034.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9ZNMR-A417-532[»]
ProteinModelPortaliO94806.
SMRiO94806. Positions 155-204, 241-321, 414-532, 537-837.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117199. 8 interactions.
IntActiO94806. 10 interactions.
MINTiMINT-5003932.
STRINGi9606.ENSP00000234179.

Chemistry

BindingDBiO94806.
ChEMBLiCHEMBL2595.
GuidetoPHARMACOLOGYi2174.

PTM databases

PhosphoSiteiO94806.

Polymorphism and mutation databases

BioMutaiPRKD3.

Proteomic databases

MaxQBiO94806.
PaxDbiO94806.
PRIDEiO94806.

Protocols and materials databases

DNASUi23683.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000234179; ENSP00000234179; ENSG00000115825. [O94806-1]
ENST00000379066; ENSP00000368356; ENSG00000115825. [O94806-1]
GeneIDi23683.
KEGGihsa:23683.
UCSCiuc002rqd.3. human. [O94806-1]
uc002rqf.1. human. [O94806-2]

Organism-specific databases

CTDi23683.
GeneCardsiGC02M037477.
H-InvDBHIX0030377.
HGNCiHGNC:9408. PRKD3.
HPAiHPA029529.
MIMi607077. gene.
neXtProtiNX_O94806.
PharmGKBiPA33772.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000121901.
HOGENOMiHOG000015135.
HOVERGENiHBG003564.
InParanoidiO94806.
KOiK06070.
OMAiHYTSRDT.
OrthoDBiEOG75B84N.
PhylomeDBiO94806.
TreeFamiTF314320.

Enzyme and pathway databases

BRENDAi2.7.11.13. 2681.
SignaLinkiO94806.

Miscellaneous databases

ChiTaRSiPRKD3. human.
EvolutionaryTraceiO94806.
GeneWikiiPRKD3.
GenomeRNAii23683.
NextBioi46561.
PROiO94806.
SOURCEiSearch...

Gene expression databases

BgeeiO94806.
CleanExiHS_PRKD3.
ExpressionAtlasiO94806. baseline and differential.
GenevestigatoriO94806.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015727. Protein_Kinase_C_mu-related.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR22968. PTHR22968. 1 hit.
PfamiPF00130. C1_1. 2 hits.
PF00169. PH. 1 hit.
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]
SUPFAMiSSF56112. 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...

Publicationsi

« Hide 'large scale' publications
  1. "PKCnu, a new member of the protein kinase C family, composes a fourth subfamily with PKCmu."
    Hayashi A., Seki N., Hattori A., Kozuma S., Saito T.
    Biochim. Biophys. Acta 1450:99-106(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Embryo.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 2), VARIANTS THR-128 AND ARG-546.
    Tissue: Testis.
  6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Selective binding of phorbol esters and diacylglycerol by individual C1 domains of the PKD family."
    Chen J., Deng F., Li J., Wang Q.J.
    Biochem. J. 411:333-342(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION, PHORBOL-ESTER BINDING, MUTAGENESIS OF THR-156; TYR-158; PRO-165; THR-166; TYR-170; PRO-282 AND LYS-293.
  8. "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-6; SER-27; SER-37; SER-41; SER-213; SER-216; SER-364 AND THR-535, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41; SER-44 AND SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41; SER-213; SER-216; SER-364 AND THR-535, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-27; SER-41 AND SER-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Solution structure of the PH domain of protein kinase C, nu type from human."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JAN-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 414-532.
  14. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-716.

Entry informationi

Entry nameiKPCD3_HUMAN
AccessioniPrimary (citable) accession number: O94806
Secondary accession number(s): D6W587, Q53TR7, Q8NEL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 1999
Last modified: May 27, 2015
This is version 147 of the entry and version 1 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 2
    Human chromosome 2: 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

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 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.