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Protein

Protein kinase C

Gene

Prkcd

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.UniRule annotationSAAS annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinaseUniRule annotationSAAS annotation, Transferase

Keywords - Ligandi

ATP-bindingUniRule annotationSAAS annotation, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-111465. Apoptotic cleavage of cellular proteins.
R-RNO-111933. Calmodulin induced events.
R-RNO-114508. Effects of PIP2 hydrolysis.
R-RNO-1489509. DAG and IP3 signaling.
R-RNO-2029485. Role of phospholipids in phagocytosis.
R-RNO-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-RNO-5218921. VEGFR2 mediated cell proliferation.
R-RNO-5607764. CLEC7A (Dectin-1) signaling.
R-RNO-877300. Interferon gamma signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase CUniRule annotationSAAS annotation (EC:2.7.11.13UniRule annotationSAAS annotation)
Gene namesi
Name:PrkcdImported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi67383. Prkcd.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025858.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini158 – 20851Phorbol-ester/DAG-typeInterPro annotationAdd
BLAST
Domaini230 – 28051Phorbol-ester/DAG-typeInterPro annotationAdd
BLAST
Domaini347 – 600254Protein kinaseInterPro annotationAdd
BLAST
Domaini601 – 67272AGC-kinase C-terminalInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.UniRule annotation
Contains AGC-kinase C-terminal domain.SAAS annotation
Contains protein kinase domain.SAAS annotation

Keywords - Domaini

Zinc-fingerSAAS annotation

Phylogenomic databases

eggNOGiENOG410XNPH. LUCA.
KOG0694. Eukaryota.
GeneTreeiENSGT00820000126964.
OMAiGEDEAKF.
OrthoDBiEOG77M8QM.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR027436. PKC_delta.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000551. PKC_delta. 1 hit.
PIRSF501104. Protein_kin_C_delta. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 2 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 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]

Sequencei

Sequence statusi: Complete.

D4A0U0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPFLRISFN SYELGSLQAE DDASQPFCAV KMKEALTTDR GKTLVQKKPT
60 70 80 90 100
MYPEWKSTFD AHIYEGRVIQ IVLMRAAEDP MSEVTVGVSV LAERCKKNNG
110 120 130 140 150
KAEFWLDLQP QAKVLMCVQY FLEDGDCKQS MRSEEEAMFP TMNRRGAIKQ
160 170 180 190 200
AKIHYIKNHE FIATFFGQPT FCSVCKEFVW GLNKQGYKCR QCNAAIHKKC
210 220 230 240 250
IDKIIGRCTG TATNSRDTIF QKERFNIDMP HRFKVYNYMS PTFCDHCGSL
260 270 280 290 300
LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQKASR
310 320 330 340 350
KPETPETVGI YQGFEKKTAV SGNDIPDNNG TYGKIWEGSN RCRLENFTFQ
360 370 380 390 400
KVLGKGSFGK VLLAELKGKE RYFAIKYLKK DVVLIDDDVE CTMVEKRVLA
410 420 430 440 450
LAWENPFLTH LICTFQTKDH LFFVMEFLNG GDLMFHIQDK GRFELYRATF
460 470 480 490 500
YAAEIICGLQ FLHGKGIIYR DLKLDNVMLD KDGHIKIADF GMCKENIFGE
510 520 530 540 550
NRASTFCGTP DYIAPEILQG LKYSFSVDWW SFGVLLYEML IGQSPFHGDD
560 570 580 590 600
EDELFESIRV DTPHYPRWIT KDTAPVDQLF ERDPAKRLGV TGNIRLHPFF
610 620 630 640 650
KTINWNLLEK RKVEPPFKPK VKSPSDYSNF DPEFLNEKPQ LSFSDKNLID
660 670
SMDQTAFKGF SFVNPKYEQF LE
Length:672
Mass (Da):77,272
Last modified:July 22, 2015 - v3
Checksum:i9C788EFCC9228D53
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06086358 Genomic DNA. No translation available.
AABR06086359 Genomic DNA. No translation available.
AABR07024579 Genomic DNA. No translation available.
AABR07024580 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENSRNOT00000025858; ENSRNOP00000025858; ENSRNOG00000016346.
ENSRNOT00000067639; ENSRNOP00000061108; ENSRNOG00000016346.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06086358 Genomic DNA. No translation available.
AABR06086359 Genomic DNA. No translation available.
AABR07024579 Genomic DNA. No translation available.
AABR07024580 Genomic DNA. No translation available.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025858.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000025858; ENSRNOP00000025858; ENSRNOG00000016346.
ENSRNOT00000067639; ENSRNOP00000061108; ENSRNOG00000016346.

Organism-specific databases

RGDi67383. Prkcd.

Phylogenomic databases

eggNOGiENOG410XNPH. LUCA.
KOG0694. Eukaryota.
GeneTreeiENSGT00820000126964.
OMAiGEDEAKF.
OrthoDBiEOG77M8QM.

Enzyme and pathway databases

ReactomeiR-RNO-111465. Apoptotic cleavage of cellular proteins.
R-RNO-111933. Calmodulin induced events.
R-RNO-114508. Effects of PIP2 hydrolysis.
R-RNO-1489509. DAG and IP3 signaling.
R-RNO-2029485. Role of phospholipids in phagocytosis.
R-RNO-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-RNO-5218921. VEGFR2 mediated cell proliferation.
R-RNO-5607764. CLEC7A (Dectin-1) signaling.
R-RNO-877300. Interferon gamma signaling.

Miscellaneous databases

NextBioi35571647.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR027436. PKC_delta.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000551. PKC_delta. 1 hit.
PIRSF501104. Protein_kin_C_delta. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 2 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 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. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  2. "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."
    Moser K., White F.M.
    J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Ensembl
    Submitted (APR-2014) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiD4A0U0_RAT
AccessioniPrimary (citable) accession number: D4A0U0
Secondary accession number(s): Z4YNR1
Entry historyi
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: July 22, 2015
Last modified: January 20, 2016
This is version 54 of the entry and version 3 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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 one 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.