[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N; TISSUE=Mammary tumor; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[2]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1021/pr0604155; PubMed=17203969 [NCBI, ExPASy, EBI, Israel, Japan] Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; "Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."; J. Proteome Res. 6:250-262(2007).
[3]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-44; SER-213 AND SER-216, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1073/pnas.0609836104; PubMed=17242355 [NCBI, ExPASy, EBI, Israel, Japan] Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; "Large-scale phosphorylation analysis of mouse liver."; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).

Comments

FUNCTION: Calcium-independent, phospholipid-dependent, serine- and threonine-specific kinase. Upon diacylglycerol-activation, phosphorylates a range of cellular proteins. Also serves as the receptor for phorbol esters, a class of tumor promoters (By similarity).
CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PKD subfamily.
SIMILARITY: Contains 1 PH domain.
SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers.
SIMILARITY: Contains 1 protein kinase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BC037012; AAH37012.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_083515.2; -.

UniGene

Mm.252776

3D structure databases

HSSP

P28867; 1PTQ. [HSSP ENTRY / PDB]

Q8K1Y2; 414-532.

PTM databases

Q8K1Y2; -.

Organism-specific databases

MGI

MGI:1922542; Prkd3.

Gene expression databases

ArrayExpress

Q8K1Y2; -.

CleanEx

MM_PRKD3; -.

GermOnline

ENSMUSG00000024070; Mus musculus.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0019992;	Molecular function: diacylglycerol binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004697;	Molecular function: protein kinase C activity (inferred from electronic annotation from EC).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0007242;	Biological process: intracellular signaling cascade (inferred from electronic annotation from InterPro).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR002219; DAG_PE_bd.
IPR001849; PH.
IPR011993; PH_type.
IPR015727; PKC_mu_like.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.

Gene3D

G3DSA:2.30.29.30; PH_type; 1.

PANTHER

PTHR22968; PKC_mu_like; 1.

Pfam

PF00130; C1_1; 2.
PF00169; PH; 1.
PF00069; Pkinase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00008; DAGPEDOMAIN.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00109; C1; 2.
SM00233; PH; 1.
SM00220; S_TKc; 1.
SMART graphical view of domain structure.

PROSITE

PS50003; PH_DOMAIN; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PS00479; ZF_DAG_PE_1; 2.
PS50081; ZF_DAG_PE_2; 2.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q8K1Y2.

Genome annotation databases

Ensembl

ENSMUSG00000024070; Mus musculus. [Contig view]

GeneID

75292; -.

KEGG

mmu:75292; -.

Phylogenomic databases

HOVERGEN

Q8K1Y2; -.

Other

NextBio

342658; -.

SOURCE

Prkd3; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Kinase; Metal-binding; Nucleotide-binding; Phorbol-ester binding; Phosphoprotein; Repeat; Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 889`	`889`	`Serine/threonine-protein kinase D3.`	`PRO_0000055718`
`DOMAIN`	`416 532`	`117`	`PH.`
`DOMAIN`	`575 831`	`257`	`Protein kinase.`
`ZN_FING`	`154 204`	`51`	`Phorbol-ester/DAG-type 1.`
`ZN_FING`	`271 321`	`51`	`Phorbol-ester/DAG-type 2.`
`NP_BIND`	`581 589`	`9`	`ATP (By similarity).`
`ACT_SITE`	`698 698`		`Proton acceptor (By similarity).`
`BINDING`	`604 604`		`ATP (By similarity).`
`MOD_RES`	`41 41`		`Phosphoserine.`
`MOD_RES`	`44 44`		`Phosphoserine.`
`MOD_RES`	`213 213`		`Phosphoserine.`
`MOD_RES`	`216 216`		`Phosphoserine.`
`MOD_RES`	`364 364`		`Phosphoserine.`
`MOD_RES`	`391 391`		`Phosphoserine (By similarity).`
`MOD_RES`	`734 734`		`Phosphoserine (By similarity).`

Sequence information

Length: 889 AA [This is the length of the unprocessed precursor]

Molecular weight: 100078 Da [This is the MW of the unprocessed precursor]

CRC64: 7D03938ED4ECC2E4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSANNSPPSA QKSVFPATVS AVLPAPSPCS SPKTGLSARL SNGSFSAPSL TNSRGSVHTV 

        70         80         90        100        110        120 
SFLLQIGLTR ESVTIEAQEL SLSAVKDLVC SIVYQKFPEC GFFGMYDKIL LFRHDMNSEN 

       130        140        150        160        170        180 
ILQLITSADE IHEGDLVEVV LSALATVEDF QIRPHALYVH SYKAPTFCDY CGEMLWGLVR 

       190        200        210        220        230        240 
QGLKCEGCGL NYHKRCAFKI PNNCSGVRKR RLSNVSLPGP GLSVPRPLQP ECVPLLSEES 

       250        260        270        280        290        300 
HTHQEPSKRI PSWSGRPIWM EKMVMCRVKV PHTFAVHSYG RPTICQYCKR LLKGLFRQGM 

       310        320        330        340        350        360 
QCKDCKFNCH KRCASKVPRD CLGEVTFNGE PCSVGTDADM PMDIDSSDVN SDGSRGLDDS 

       370        380        390        400        410        420 
EEPSPPEDKM FFLDPTDLDV ERDEETVKTI SPSTSNNIPL MRVVQSIKHT KRRSSTVVKE 

       430        440        450        460        470        480 
GWMVHYTSRD NLRKRHYWRL DSKCLTLFQN ESGSKYYKEI PLSEILRVSS PQDFTSISQG 

       490        500        510        520        530        540 
SNPHCFEIIT DTVVYFVGEN NGSSSHNPVL AATGVGLDVA QSWEKAIRQA LMPVTPQASV 

       550        560        570        580        590        600 
CTSPGQGKDH NLATSISVSN CQVQENVDIS SVYQIFADEV LGSGQFGIVY GGKHRKTGRD 

       610        620        630        640        650        660 
VAIKVIDKMR FPTKQESQLR NEVAILQNLH HPGIVNLECM FETPERVFVV MEKLHGDMLE 

       670        680        690        700        710        720 
MILSSEKSRL PERITKFMVT QILVALRNLH FKNIVHCDLK PENVLLASAE PFPQVKLCDF 

       730        740        750        760        770        780 
GFARIIGEKS FRRSVVGTPA YLAPEVLRSK GYNRSLDMWS VGVIVYVSLS GTFPFNEDED 

       790        800        810        820        830        840 
INDQIQNAAF MYPPNPWREI SSEAIDLINN LLQVKMRKRY SVDKSLSHPW LQDYQTWLDL 

       850        860        870        880 
REFETRIGER YITHESDDAR WEIHAYTHNL EYPKHFIMAP NPDDMEEDP

Q8K1Y2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools