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O94806

- KPCD3_HUMAN

UniProt

O94806 - KPCD3_HUMAN

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Protein
Serine/threonine-protein kinase D3
Gene
PRKD3, EPK2, PRKCN
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium 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 – 6051ATP By similarity
Active sitei699 – 6991Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri154 – 20451Phorbol-ester/DAG-type 1
Add
BLAST
Zinc fingeri271 – 32151Phorbol-ester/DAG-type 2
Add
BLAST
Nucleotide bindingi582 – 5909ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: IntAct
  4. protein kinase C activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. intracellular signal transduction Source: InterPro
  2. protein kinase C-activating G-protein coupled receptor signaling pathway Source: ProtInc
  3. 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: Chromosome 2

Organism-specific databases

HGNCiHGNC:9408. PRKD3.

Subcellular locationi

Cytoplasm. Membrane
Note: Translocation to the cell membrane is required for kinase activation.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. membrane Source: UniProtKB-SubCell
  3. nucleus Source: HPA
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 890890Serine/threonine-protein kinase D3
PRO_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 residuei535 – 5351Phosphothreonine2 Publications
Modified residuei731 – 7311Phosphoserine; by PKC
Modified residuei735 – 7351Phosphoserine; by autocatalysis

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO94806.
PaxDbiO94806.
PRIDEiO94806.

PTM databases

PhosphoSiteiO94806.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiO94806.
BgeeiO94806.
CleanExiHS_PRKD3.
GenevestigatoriO94806.

Organism-specific databases

HPAiHPA029529.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi117199. 8 interactions.
IntActiO94806. 9 interactions.
MINTiMINT-5003932.
STRINGi9606.ENSP00000234179.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9ZNMR-A417-532[»]
ProteinModelPortaliO94806.
SMRiO94806. Positions 155-204, 241-321, 414-532, 537-859.

Miscellaneous databases

EvolutionaryTraceiO94806.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini416 – 532117PH
Add
BLAST
Domaini576 – 832257Protein kinase
Add
BLAST

Sequence similaritiesi

Contains 1 PH domain.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000015135.
HOVERGENiHBG003564.
InParanoidiO94806.
KOiK06070.
OMAiFRHDLNS.
OrthoDBiEOG75B84N.
PhylomeDBiO94806.
TreeFamiTF314320.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015727. Protein_Kinase_C_mu-related.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
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. Align

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

MSANNSPPSA QKSVLPTAIP AVLPAASPCS SPKTGLSARL SNGSFSAPSL    50
TNSRGSVHTV SFLLQIGLTR ESVTIEAQEL SLSAVKDLVC SIVYQKFPEC 100
GFFGMYDKIL LFRHDMNSEN ILQLITSADE IHEGDLVEVV LSALATVEDF 150
QIRPHTLYVH SYKAPTFCDY CGEMLWGLVR QGLKCEGCGL NYHKRCAFKI 200
PNNCSGVRKR RLSNVSLPGP GLSVPRPLQP EYVALPSEES HVHQEPSKRI 250
PSWSGRPIWM EKMVMCRVKV PHTFAVHSYT RPTICQYCKR LLKGLFRQGM 300
QCKDCKFNCH KRCASKVPRD CLGEVTFNGE PSSLGTDTDI PMDIDNNDIN 350
SDSSRGLDDT EEPSPPEDKM FFLDPSDLDV ERDEEAVKTI SPSTSNNIPL 400
MRVVQSIKHT KRKSSTMVKE GWMVHYTSRD NLRKRHYWRL DSKCLTLFQN 450
ESGSKYYKEI PLSEILRISS PRDFTNISQG SNPHCFEIIT DTMVYFVGEN 500
NGDSSHNPVL AATGVGLDVA QSWEKAIRQA LMPVTPQASV CTSPGQGKDH 550
KDLSTSISVS NCQIQENVDI STVYQIFADE VLGSGQFGIV YGGKHRKTGR 600
DVAIKVIDKM RFPTKQESQL RNEVAILQNL HHPGIVNLEC MFETPERVFV 650
VMEKLHGDML EMILSSEKSR LPERITKFMV TQILVALRNL HFKNIVHCDL 700
KPENVLLASA EPFPQVKLCD FGFARIIGEK SFRRSVVGTP AYLAPEVLRS 750
KGYNRSLDMW SVGVIIYVSL SGTFPFNEDE DINDQIQNAA FMYPPNPWRE 800
ISGEAIDLIN NLLQVKMRKR YSVDKSLSHP WLQDYQTWLD LREFETRIGE 850
RYITHESDDA RWEIHAYTHN LVYPKHFIMA PNPDDMEEDP 890
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.
VSP_029405Add
BLAST
Alternative sequencei612 – 890279Missing in isoform 2.
VSP_029406Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_005813.3. [O94806-1]
XP_005264294.1. XM_005264237.1. [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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS1789.1. [O94806-1 ]
RefSeqi NP_005804.1. NM_005813.3. [O94806-1 ]
XP_005264294.1. XM_005264237.1. [O94806-1 ]
UniGenei Hs.660757.
Hs.716034.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2D9Z NMR - A 417-532 [» ]
ProteinModelPortali O94806.
SMRi O94806. Positions 155-204, 241-321, 414-532, 537-859.
ModBasei Search...

Protein-protein interaction databases

BioGridi 117199. 8 interactions.
IntActi O94806. 9 interactions.
MINTi MINT-5003932.
STRINGi 9606.ENSP00000234179.

Chemistry

BindingDBi O94806.
ChEMBLi CHEMBL2595.
GuidetoPHARMACOLOGYi 2174.

PTM databases

PhosphoSitei O94806.

Proteomic databases

MaxQBi O94806.
PaxDbi O94806.
PRIDEi O94806.

Protocols and materials databases

DNASUi 23683.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000234179 ; ENSP00000234179 ; ENSG00000115825 . [O94806-1 ]
ENST00000379066 ; ENSP00000368356 ; ENSG00000115825 . [O94806-1 ]
GeneIDi 23683.
KEGGi hsa:23683.
UCSCi uc002rqd.3. human. [O94806-1 ]
uc002rqf.1. human. [O94806-2 ]

Organism-specific databases

CTDi 23683.
GeneCardsi GC02M037477.
H-InvDBi HIX0030377.
HGNCi HGNC:9408. PRKD3.
HPAi HPA029529.
MIMi 607077. gene.
neXtProti NX_O94806.
PharmGKBi PA33772.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000015135.
HOVERGENi HBG003564.
InParanoidi O94806.
KOi K06070.
OMAi FRHDLNS.
OrthoDBi EOG75B84N.
PhylomeDBi O94806.
TreeFami TF314320.

Enzyme and pathway databases

BRENDAi 2.7.11.13. 2681.
SignaLinki O94806.

Miscellaneous databases

EvolutionaryTracei O94806.
GeneWikii PRKD3.
GenomeRNAii 23683.
NextBioi 46561.
PROi O94806.
SOURCEi Search...

Gene expression databases

ArrayExpressi O94806.
Bgeei O94806.
CleanExi HS_PRKD3.
Genevestigatori O94806.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015727. Protein_Kinase_C_mu-related.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
PANTHERi PTHR22968. PTHR22968. 1 hit.
Pfami PF00130. C1_1. 2 hits.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000552. PKC_mu_nu_D2. 1 hit.
PRINTSi PR00008. DAGPEDOMAIN.
SMARTi SM00109. C1. 2 hits.
SM00233. PH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 138 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

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