O94806 (KPCD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PRKD3
Synonyms:	EPK2, PRKCN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	890 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Enzyme regulation	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. Ref.7
Subcellular location	Cytoplasm. Membrane. Note: Translocation to the cell membrane is required for kinase activation. Ref.7
Tissue specificity	Ubiquitous.
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PKD subfamily. Contains 1 PH domain. Contains 2 phorbol-ester/DAG-type zinc fingers. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	intracellular signal transduction Inferred from electronic annotation. Source: InterPro protein kinase C-activating G-protein coupled receptor signaling pathway Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipid binding Inferred from electronic annotation. Source: InterPro protein kinase C activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-1255366,EBI-1255366
VAMP2	P63027	7	EBI-1255366,EBI-520113

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O94806-1)

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.

Isoform 2 (identifier: O94806-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 890

890

Serine/threonine-protein kinase D3

PRO_0000055717

Regions

Domain

416 – 532

117

PH

Domain

576 – 832

257

Protein kinase

Zinc finger

154 – 204

51

Phorbol-ester/DAG-type 1

Zinc finger

271 – 321

51

Phorbol-ester/DAG-type 2

Nucleotide binding

582 – 590

9

ATP By similarity

Sites

Active site

699

1

Proton acceptor By similarity

Binding site

605

1

ATP By similarity

Amino acid modifications

Modified residue

6

1

Phosphoserine Ref.8

Modified residue

27

1

Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11

Modified residue

37

1

Phosphoserine Ref.8

Modified residue

41

1

Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11

Modified residue

44

1

Phosphoserine Ref.9 Ref.11

Modified residue

213

1

Phosphoserine Ref.8 Ref.10

Modified residue

216

1

Phosphoserine Ref.8 Ref.10

Modified residue

364

1

Phosphoserine Ref.6 Ref.8 Ref.9 Ref.10

Modified residue

535

1

Phosphothreonine Ref.8 Ref.10

Modified residue

731

1

Phosphoserine; by PKC

Modified residue

735

1

Phosphoserine; by autocatalysis

Natural variations

Alternative sequence

595 – 611

17

HRKTG…IDKMR → QLQPFAYCTHYFKNWKM in isoform 2.

VSP_029405

Alternative sequence

612 – 890

279

Missing in isoform 2.

VSP_029406

Natural variant

42

1

N → D.
Corresponds to variant rs11896614 [ dbSNP | Ensembl ].

VAR_037147

Natural variant

128

1

A → T. Ref.5
Corresponds to variant rs17852819 [ dbSNP | Ensembl ].

VAR_037148

Natural variant

225

1

P → S.
Corresponds to variant rs34280934 [ dbSNP | Ensembl ].

VAR_050561

Natural variant

445

1

L → I.
Corresponds to variant rs55912911 [ dbSNP | Ensembl ].

VAR_061532

Natural variant

546

1

Q → R. Ref.5
Corresponds to variant rs17856887 [ dbSNP | Ensembl ].

VAR_037149

Natural variant

716

1

V → M in a glioblastoma multiforme sample; somatic mutation. Ref.13

VAR_042336

Experimental info

Mutagenesis

156

1

T → A: Slight loss in ability to bind DAG and phorbol-ester; when associated with F-158. Ref.7

Mutagenesis

158

1

Y → F: Slight loss in ability to bind DAG and phorbol-ester; when associated with A-156. Ref.7

Mutagenesis

165

1

P → G: No effect on ability to bind phorbol ester, loss of ability to bind DAG, reduced DAG-induced membrane translocation. Ref.7

Mutagenesis

166

1

T → A: Slight loss in ability to bind DAG and phorbol-ester. Ref.7

Mutagenesis

170

1

Y → F: Slight loss in ability to bind DAG and phorbol-ester. Ref.7

Mutagenesis

282

1

P → G: No effect on ability to bind phorbol ester, increase in ability to bind DAG. Ref.7

Mutagenesis

284

1

I → V: Slight increase in ability to bind DAG, no effect on phorbol-ester binding.

Mutagenesis

293

1

K → W: Increased ability to bind DAG, no effect on phorbol-ester binding. Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

890

Helix Strand Turn

Details...

Beta strand

417 – 429

13

Beta strand

434 – 443

10

Beta strand

445 – 449

5

Turn

462 – 464

3

Beta strand

477 – 479

3

Beta strand

485 – 489

5

Beta strand

494 – 497

4

Turn

508 – 514

7

Helix

517 – 532

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 66D5E7E7235064F5	FASTA	890	100,471
	10 20 30 40 50 60 MSANNSPPSA QKSVLPTAIP AVLPAASPCS SPKTGLSARL SNGSFSAPSL TNSRGSVHTV 70 80 90 100 110 120 SFLLQIGLTR ESVTIEAQEL SLSAVKDLVC SIVYQKFPEC GFFGMYDKIL LFRHDMNSEN 130 140 150 160 170 180 ILQLITSADE IHEGDLVEVV LSALATVEDF QIRPHTLYVH SYKAPTFCDY CGEMLWGLVR 190 200 210 220 230 240 QGLKCEGCGL NYHKRCAFKI PNNCSGVRKR RLSNVSLPGP GLSVPRPLQP EYVALPSEES 250 260 270 280 290 300 HVHQEPSKRI PSWSGRPIWM EKMVMCRVKV PHTFAVHSYT RPTICQYCKR LLKGLFRQGM 310 320 330 340 350 360 QCKDCKFNCH KRCASKVPRD CLGEVTFNGE PSSLGTDTDI PMDIDNNDIN SDSSRGLDDT 370 380 390 400 410 420 EEPSPPEDKM FFLDPSDLDV ERDEEAVKTI SPSTSNNIPL MRVVQSIKHT KRKSSTMVKE 430 440 450 460 470 480 GWMVHYTSRD NLRKRHYWRL DSKCLTLFQN ESGSKYYKEI PLSEILRISS PRDFTNISQG 490 500 510 520 530 540 SNPHCFEIIT DTMVYFVGEN NGDSSHNPVL AATGVGLDVA QSWEKAIRQA LMPVTPQASV 550 560 570 580 590 600 CTSPGQGKDH KDLSTSISVS NCQIQENVDI STVYQIFADE VLGSGQFGIV YGGKHRKTGR 610 620 630 640 650 660 DVAIKVIDKM RFPTKQESQL RNEVAILQNL HHPGIVNLEC MFETPERVFV VMEKLHGDML 670 680 690 700 710 720 EMILSSEKSR LPERITKFMV TQILVALRNL HFKNIVHCDL KPENVLLASA EPFPQVKLCD 730 740 750 760 770 780 FGFARIIGEK SFRRSVVGTP AYLAPEVLRS KGYNRSLDMW SVGVIIYVSL SGTFPFNEDE 790 800 810 820 830 840 DINDQIQNAA FMYPPNPWRE ISGEAIDLIN NLLQVKMRKR YSVDKSLSHP WLQDYQTWLD 850 860 870 880 890 LREFETRIGE RYITHESDDA RWEIHAYTHN LVYPKHFIMA PNPDDMEEDP
	Isoform 2 [UniParc]. Checksum: 1714FAD7DA82C942	FASTA	611	68,123
	10 20 30 40 50 60 MSANNSPPSA QKSVLPTAIP AVLPAASPCS SPKTGLSARL SNGSFSAPSL TNSRGSVHTV 70 80 90 100 110 120 SFLLQIGLTR ESVTIEAQEL SLSAVKDLVC SIVYQKFPEC GFFGMYDKIL LFRHDMNSEN 130 140 150 160 170 180 ILQLITSADE IHEGDLVEVV LSALATVEDF QIRPHTLYVH SYKAPTFCDY CGEMLWGLVR 190 200 210 220 230 240 QGLKCEGCGL NYHKRCAFKI PNNCSGVRKR RLSNVSLPGP GLSVPRPLQP EYVALPSEES 250 260 270 280 290 300 HVHQEPSKRI PSWSGRPIWM EKMVMCRVKV PHTFAVHSYT RPTICQYCKR LLKGLFRQGM 310 320 330 340 350 360 QCKDCKFNCH KRCASKVPRD CLGEVTFNGE PSSLGTDTDI PMDIDNNDIN SDSSRGLDDT 370 380 390 400 410 420 EEPSPPEDKM FFLDPSDLDV ERDEEAVKTI SPSTSNNIPL MRVVQSIKHT KRKSSTMVKE 430 440 450 460 470 480 GWMVHYTSRD NLRKRHYWRL DSKCLTLFQN ESGSKYYKEI PLSEILRISS PRDFTNISQG 490 500 510 520 530 540 SNPHCFEIIT DTMVYFVGEN NGDSSHNPVL AATGVGLDVA QSWEKAIRQA LMPVTPQASV 550 560 570 580 590 600 CTSPGQGKDH KDLSTSISVS NCQIQENVDI STVYQIFADE VLGSGQFGIV YGGKQLQPFA 610 YCTHYFKNWK M

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41; SER-44 AND SER-364, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41; SER-213; SER-216; SER-364 AND THR-535, MASS SPECTROMETRY.
[11]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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.
[13]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00015538.
IPI00871931.

RefSeq

NP_005804.1. NM_005813.3.

UniGene

Hs.660757.
Hs.716034.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D9Z	NMR	-	A	417-532	[»]

ProteinModelPortal

O94806.

ModBase

Search...

Protein-protein interaction databases

IntAct

O94806. 8 interactions.

STRING

9606.ENSP00000234179.

PTM databases

PhosphoSite

O94806.

Proteomic databases

PaxDb

O94806.

PRIDE

O94806.

Protocols and materials databases

DNASU

23683.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000234179; ENSP00000234179; ENSG00000115825.
ENST00000379066; ENSP00000368356; ENSG00000115825.

GeneID

23683.

KEGG

hsa:23683.

UCSC

uc002rqd.3. human.
uc002rqf.1. human.

Organism-specific databases

CTD

23683.

GeneCards

GC02M037477.

H-InvDB

HIX0030377.

HGNC

HGNC:9408. PRKD3.

HPA

HPA029529.

MIM

607077. gene.

neXtProt

NX_O94806.

PharmGKB

PA33772.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000015135.

HOVERGEN

HBG003564.

InParanoid

O94806.

KO

K06070.

OMA

ISSPQDF.

OrthoDB

EOG4548XW.

PhylomeDB

O94806.

Enzyme and pathway databases

BRENDA

2.7.11.13. 2681.

Gene expression databases

ArrayExpress

O94806.

Bgee

O94806.

CleanEx

HS_PRKD3.

Genevestigator

O94806.

GermOnline

ENSG00000115825. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_cat_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]

PANTHER

PTHR22968. PTHR22968. 1 hit.

Pfam

PF00130. C1_1. 2 hits.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

PIRSF

PIRSF000552. PKC_mu_nu_D2. 1 hit.

PRINTS

PR00008. DAGPEDOMAIN.

SMART

SM00109. C1. 2 hits.
SM00233. PH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

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.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

O94806.

ChEMBL

CHEMBL2595.

EvolutionaryTrace

O94806.

GenomeRNAi

23683.

NextBio

46561.

SOURCE

Search...

Entry information

Entry name

KPCD3_HUMAN

Accession

Primary (citable) accession number: O94806
Secondary accession number(s): D6W587, Q53TR7, Q8NEL8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.