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Reviewed, UniProtKB/Swiss-Prot Q9BZL6 (KPCD2_HUMAN)

Last modified October 13, 2009. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Serine/threonine-protein kinase D2
    EC=2.7.11.13
Alternative name(s):
    nPKC-D2
Gene names
Name: PRKD2
Synonyms: PKD2
ORF Names: HSPC187
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length878 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 bind DAG, mediating translocation to membranes. Autophosphorylation of Ser-710 and phosphorylation of Ser-706 by PKC relieves auto-inhibition by the PH domain By similarity.

Subcellular location

Cytoplasm By similarity. Membrane By similarity. Note: Translocation to the cell membrane is required for kinase activation By similarity.

Tissue specificity

Widely expressed.

Post-translational modification

Phosphorylation of Ser-876 correlates with the activation status of the kinase.

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.

Sequence caution

The sequence AAF36107.1 differs from that shown. Reason: Frameshift at positions 604, 606, 738, 744, 755, 758, 833 and 854.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 878878Serine/threonine-protein kinase D2
PRO_0000055716

Regions

Domain397 – 509113PH
Domain551 – 807257Protein kinase
Zinc finger138 – 18851Phorbol-ester/DAG-type 1
Zinc finger264 – 31451Phorbol-ester/DAG-type 2
Nucleotide binding557 – 5659ATP By similarity

Sites

Active site6741Proton acceptor By similarity
Binding site5801ATP By similarity

Amino acid modifications

Modified residue1971Phosphoserine Ref.4 Ref.5 Ref.6 Ref.8 Ref.10 Ref.11
Modified residue1981Phosphoserine Ref.4
Modified residue2001Phosphoserine Ref.11 Ref.9
Modified residue2031Phosphoserine Ref.11
Modified residue2061Phosphoserine Ref.11
Modified residue2121Phosphoserine By similarity
Modified residue2141Phosphoserine Ref.6 Ref.10 Ref.11
Modified residue3751Phosphoserine Ref.10
Modified residue3961Phosphoserine Ref.10
Modified residue5181Phosphoserine Ref.10
Modified residue7061Phosphoserine; by PKC By similarity
Modified residue7101Phosphoserine; by autocatalysis By similarity
Modified residue8761Phosphoserine; by autocatalysis Ref.10 Ref.1

Natural variations

Natural variant3241V → M
VAR_042330
Natural variant4961A → V
VAR_042331
Natural variant6041S → G
VAR_042332
Natural variant7731W → R
VAR_042333
Natural variant8481G → E in a lung adenocarcinoma sample; somatic mutation. Ref.14
VAR_042334
Natural variant8701G → E in a gastric adenocarcinoma sample; somatic mutation. Ref.14
VAR_042335

Experimental info

Mutagenesis2751P → G: Increase in ability to bind phorbol ester, slight increase in ability to bind DAG. Ref.7
Sequence conflict7901V → L in AAF36107. Ref.3

Secondary structure

...................... 878
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BZL6-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 8BAB45E8F99D23E7

FASTA87896,722
        10         20         30         40         50         60 
MATAPSYPAG LPGSPGPGSP PPPGGLELQS PPPLLPQIPA PGSGVSFHIQ IGLTREFVLL 

        70         80         90        100        110        120 
PAASELAHVK QLACSIVDQK FPECGFYGLY DKILLFKHDP TSANLLQLVR SSGDIQEGDL 

       130        140        150        160        170        180 
VEVVLSASAT FEDFQIRPHA LTVHSYRAPA FCDHCGEMLF GLVRQGLKCD GCGLNYHKRC 

       190        200        210        220        230        240 
AFSIPNNCSG ARKRRLSSTS LASGHSVRLG TSESLPCTAE ELSRSTTELL PRRPPSSSSS 

       250        260        270        280        290        300 
SSASSYTGRP IELDKMLLSK VKVPHTFLIH SYTRPTVCQA CKKLLKGLFR QGLQCKDCKF 

       310        320        330        340        350        360 
NCHKRCATRV PNDCLGEALI NGDVPMEEAT DFSEADKSAL MDESEDSGVI PGSHSENALH 

       370        380        390        400        410        420 
ASEEEEGEGG KAQSSLGYIP LMRVVQSVRH TTRKSSTTLR EGWVVHYSNK DTLRKRHYWR 

       430        440        450        460        470        480 
LDCKCITLFQ NNTTNRYYKE IPLSEILTVE SAQNFSLVPP GTNPHCFEIV TANATYFVGE 

       490        500        510        520        530        540 
MPGGTPGGPS GQGAEAARGW ETAIRQALMP VILQDAPSAP GHAPHRQASL SISVSNSQIQ 

       550        560        570        580        590        600 
ENVDIATVYQ IFPDEVLGSG QFGVVYGGKH RKTGRDVAVK VIDKLRFPTK QESQLRNEVA 

       610        620        630        640        650        660 
ILQSLRHPGI VNLECMFETP EKVFVVMEKL HGDMLEMILS SEKGRLPERL TKFLITQILV 

       670        680        690        700        710        720 
ALRHLHFKNI VHCDLKPENV LLASADPFPQ VKLCDFGFAR IIGEKSFRRS VVGTPAYLAP 

       730        740        750        760        770        780 
EVLLNQGYNR SLDMWSVGVI MYVSLSGTFP FNEDEDINDQ IQNAAFMYPA SPWSHISAGA 

       790        800        810        820        830        840 
IDLINNLLQV KMRKRYSVDK SLSHPWLQEY QTWLDLRELE GKMGERYITH ESDDARWEQF 

       850        860        870 
AAEHPLPGSG LPTDRDLGGA CPPQDHDMQG LAERISVL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of the human protein kinase D2. A novel member of the protein kinase d family of serine threonine kinases."
Sturany S., Van Lint J., Mueller F., Wilda M., Hameister H., Hoecker M., Brey A., Gern U., Vandenheede J., Gress T., Adler G., Seufferlein T.
J. Biol. Chem. 276:3310-3318(2001) [PubMed: 11062248] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-876.
Tissue: Pancreas.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-878.
Tissue: Uterus.
[3]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 574-878.
Tissue: Umbilical cord blood.
[4]"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."
Kim J.-E., Tannenbaum S.R., White F.M.
J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-198, MASS SPECTROMETRY.
[5]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, MASS SPECTROMETRY.
Tissue: Epithelium.
[6]"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.
Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-214 AND SER-710, MASS SPECTROMETRY.
[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: 18076381] [Abstract]
Cited for: PHORBOL-ESTER BINDING, MUTAGENESIS OF PRO-275.
[8]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, MASS SPECTROMETRY.
[9]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, MASS SPECTROMETRY.
Tissue: T-cell.
[10]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-214; SER-375; SER-396; SER-518; SER-706; SER-710 AND SER-876, MASS SPECTROMETRY.
[11]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-200; SER-203; SER-206; SER-214 AND SER-710, MASS SPECTROMETRY.
[12]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]"Solution structure of the PH domain of protein kinase C, D2 type from human."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 395-509.
[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. expand/collapse author list , 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: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-324; VAL-496; GLY-604; ARG-773; GLU-848 AND GLU-870.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF309082 mRNA. Translation: AAK01149.1.
AL050147 mRNA. Translation: CAB43292.1.
AF151021 mRNA. Translation: AAF36107.1. Frameshift.
IPIIPI00941257.
PIRT08777.
RefSeqNP_001073349.1.
NP_001073350.1.
NP_001073351.1.
NP_057541.2.
UniGeneHs.466987

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2COANMR-A398-509[»]
3BGMX-ray1.60C526-534[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9BZL6.

PTM databases

PhosphoSiteQ9BZL6.

Proteomic databases

PRIDEQ9BZL6.

Genome annotation databases

EnsemblENST00000291281; ENSP00000291281; ENSG00000105287; Homo sapiens. [Genome view]
ENST00000433867; ENSP00000393978; ENSG00000105287; Homo sapiens. [Genome view]
ENST00000449438; ENSP00000408285; ENSG00000105287; Homo sapiens. [Genome view]
ENST00000454760; ENSP00000414761; ENSG00000105287; Homo sapiens. [Genome view]
GeneID25865.
KEGGhsa:25865.
UCSCuc002pfh.1. human.

Organism-specific databases

CTD25865.
GeneCardsGC19M051869.
H-InvDBHIX0015258.
HGNCHGNC:17293. PRKD2.
HPAHPA021490.
MIM607074. gene.
PharmGKBPA134903505.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9BZL6.
HOVERGENQ9BZL6.

Enzyme and pathway databases

BRENDA2.7.11.13. 247.

Gene expression databases

ArrayExpressQ9BZL6.
BgeeQ9BZL6.
CleanExHS_PKD2.
HS_PRKD2.
GenevestigatorQ9BZL6.
GermOnlineENSG00000105287. Homo sapiens.

Family and domain databases

InterProIPR020454. DAG/PE_bd.
IPR011993. PH_type.
IPR001849. Pleckstrin_homology.
IPR002219. Prot_Kinase_C-like_PE/DAG_bd.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR015727. Protein_Kinase_C_mu-related.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 1 hit.
PANTHERPTHR22968. PKC_mu_like. 1 hit.
PfamPF00130. C1_1. 2 hits.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR00008. DAGPEDOMAIN.
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00109. C1. 2 hits.
SM00233. PH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS50003. 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]
ProtoNetSearch...

Other Resources

NextBio47239.
SOURCESearch...

Entry information

Entry nameKPCD2_HUMAN
AccessionPrimary (citable) accession number: Q9BZL6
Secondary accession number(s): Q8TB08, Q9P0T6, Q9Y3X8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: June 1, 2001
Last modified: October 13, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents