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Protein
Submitted name:

Protein kinase, cAMP-dependent, catalytic, alpha

Gene

Prkaca

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

Functioni

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.SAAS annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cAMP-dependent protein kinase activity Source: RGD
  • protein complex binding Source: RGD
  • protein kinase A regulatory subunit binding Source: RGD
  • protein serine/threonine/tyrosine kinase activity Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinaseSAAS annotation, Transferase

Keywords - Ligandi

ATP-bindingUniRule annotationSAAS annotation, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_275619. Factors involved in megakaryocyte development and platelet production.
REACT_280161. Rap1 signalling.
REACT_280715. GLI3 is processed to GLI3R by the proteasome.
REACT_280793. Interleukin-3, 5 and GM-CSF signaling.
REACT_287195. Degradation of GLI2 by the proteasome.
REACT_295737. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_297045. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_302681. PKA activation in glucagon signalling.
REACT_319206. Regulation of PLK1 Activity at G2/M Transition.
REACT_328763. Recruitment of mitotic centrosome proteins and complexes.
REACT_329529. Anchoring of the basal body to the plasma membrane.
REACT_331690. PKA activation.
REACT_333441. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_342405. Hedgehog 'off' state.
REACT_345047. Regulation of insulin secretion.
REACT_348359. DARPP-32 events.
REACT_352967. Loss of Nlp from mitotic centrosomes.
REACT_357442. Degradation of GLI1 by the proteasome.
REACT_359478. CD209 (DC-SIGN) signaling.

Names & Taxonomyi

Protein namesi
Submitted name:
Protein kinase, cAMP-dependent, catalytic, alphaImported
Submitted name:
cAMP-dependent protein kinase catalytic subunit alphaImported
Gene namesi
Name:PrkacaImported
ORF Names:rCG_51506Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi3389. Prkaca.

Subcellular locationi

GO - Cellular componenti

  • AMP-activated protein kinase complex Source: Ensembl
  • cAMP-dependent protein kinase complex Source: RGD
  • centrosome Source: Ensembl
  • ciliary base Source: Ensembl
  • cytoplasm Source: RGD
  • extracellular exosome Source: Ensembl
  • Golgi apparatus Source: RGD
  • membrane Source: RGD
  • mitochondrion Source: Ensembl
  • neuromuscular junction Source: Ensembl
  • neuron projection Source: RGD
  • nucleus Source: RGD
  • perinuclear region of cytoplasm Source: RGD
  • plasma membrane Source: Ensembl
  • protein complex Source: RGD
  • sperm midpiece Source: Ensembl
Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000044732.

Family & Domainsi

Sequence similaritiesi

Contains AGC-kinase C-terminal domain.SAAS annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00790000122941.
HOVERGENiHBG108317.
KOiK04345.
OMAiNAATANK.
OrthoDBiEOG7VX8WD.
TreeFamiTF313399.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A1L1M0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WETPSQNTAQ LDHFDRIKTL
60 70 80 90 100
GTGSFGRVML VKHKESGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN
110 120 130 140 150
FPFLVKLEFS FKDNSNLYMV MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ
160 170 180 190 200
IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY IQVTDFGFAK RVKGRTWTLC
210 220 230 240 250
GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK
260 270 280 290 300
IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT
310 320 330 340 350
TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFTE

F
Length:351
Mass (Da):40,606
Last modified:February 6, 2007 - v1
Checksum:i3065123824A47880
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07043167 Genomic DNA. No translation available.
BC129128 mRNA. Translation: AAI29129.1.
CH473972 Genomic DNA. Translation: EDL92251.1.
RefSeqiNP_001094392.1. NM_001100922.1.
UniGeneiRn.20.

Genome annotation databases

EnsembliENSRNOT00000041717; ENSRNOP00000044732; ENSRNOG00000005257.
GeneIDi25636.
KEGGirno:25636.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07043167 Genomic DNA. No translation available.
BC129128 mRNA. Translation: AAI29129.1.
CH473972 Genomic DNA. Translation: EDL92251.1.
RefSeqiNP_001094392.1. NM_001100922.1.
UniGeneiRn.20.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000044732.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000041717; ENSRNOP00000044732; ENSRNOG00000005257.
GeneIDi25636.
KEGGirno:25636.

Organism-specific databases

CTDi5566.
RGDi3389. Prkaca.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00790000122941.
HOVERGENiHBG108317.
KOiK04345.
OMAiNAATANK.
OrthoDBiEOG7VX8WD.
TreeFamiTF313399.

Enzyme and pathway databases

ReactomeiREACT_275619. Factors involved in megakaryocyte development and platelet production.
REACT_280161. Rap1 signalling.
REACT_280715. GLI3 is processed to GLI3R by the proteasome.
REACT_280793. Interleukin-3, 5 and GM-CSF signaling.
REACT_287195. Degradation of GLI2 by the proteasome.
REACT_295737. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_297045. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_302681. PKA activation in glucagon signalling.
REACT_319206. Regulation of PLK1 Activity at G2/M Transition.
REACT_328763. Recruitment of mitotic centrosome proteins and complexes.
REACT_329529. Anchoring of the basal body to the plasma membrane.
REACT_331690. PKA activation.
REACT_333441. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_342405. Hedgehog 'off' state.
REACT_345047. Regulation of insulin secretion.
REACT_348359. DARPP-32 events.
REACT_352967. Loss of Nlp from mitotic centrosomes.
REACT_357442. Degradation of GLI1 by the proteasome.
REACT_359478. CD209 (DC-SIGN) signaling.

Miscellaneous databases

NextBioi607455.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. 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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: BrainImported.
  2. "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.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  5. "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].
  6. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiA1L1M0_RAT
AccessioniPrimary (citable) accession number: A1L1M0
Entry historyi
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: July 22, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

External Data

Dasty 3

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 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.