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Protein

cAMP-dependent protein kinase catalytic subunit PRKX

Gene

Prkx

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine/threonine protein kinase regulated by and mediating cAMP signaling in cells. Acts through phosphorylation of downstream targets that may include CREB, SMAD6 and PKD1 and has multiple functions in cellular differentiation and epithelial morphogenesis. Regulates myeloid cell differentiation through SMAD6 phosphorylation. Involved in nephrogenesis by stimulating renal epithelial cell migration and tubulogenesis. Also involved in angiogenesis through stimulation of endothelial cell proliferation, migration and vascular-like structure formation.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Binding of cAMP to the PRKAR1A or PRKAR1B regulatory subunits induces dissociation of the holoenzyme heterotetramer. The released monomeric PRKX is then active and able to phosphorylate its substrates (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei75 – 751ATPPROSITE-ProRule annotation
Active sitei169 – 1691Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi52 – 609ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cAMP-dependent protein kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: MGI

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • cell adhesion Source: UniProtKB
  • cell-substrate adhesion Source: UniProtKB
  • endothelial cell migration Source: UniProtKB
  • endothelial cell proliferation Source: UniProtKB
  • epithelial tube morphogenesis Source: UniProtKB
  • kidney morphogenesis Source: UniProtKB
  • myeloid cell differentiation Source: UniProtKB
  • peptidyl-serine phosphorylation Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • regulation of cell adhesion Source: MGI
  • regulation of cell migration Source: UniProtKB
  • regulation of epithelial cell differentiation involved in kidney development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Angiogenesis, Differentiation

Keywords - Ligandi

ATP-binding, cAMP, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase catalytic subunit PRKX (EC:2.7.11.1)
Short name:
PrKX
Short name:
Protein kinase X
Short name:
Protein kinase X-linked
Short name:
Serine/threonine-protein kinase PRKX
Alternative name(s):
PKA-related protein kinase
Gene namesi
Name:Prkx
Synonyms:Pkare
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1309999. Prkx.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: cAMP induces nuclear translocation.By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 355355cAMP-dependent protein kinase catalytic subunit PRKXPRO_0000086583Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei200 – 2001PhosphothreonineCombined sources

Post-translational modificationi

Phosphorylated; autophosphorylates in vitro.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ922R0.
MaxQBiQ922R0.
PaxDbiQ922R0.
PRIDEiQ922R0.

PTM databases

iPTMnetiQ922R0.
PhosphoSiteiQ922R0.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Developmental stagei

Expressed in central nervous system and heart tissues in early development stages and in most organs at later stages (at protein level). Detected in embryos from 9 dpc onward with higher expression in differentiating neuronal tissues at 11.5 dpc.2 Publications

Gene expression databases

BgeeiQ922R0.
CleanExiMM_PRKX.
ExpressionAtlasiQ922R0. baseline and differential.
GenevisibleiQ922R0. MM.

Interactioni

Subunit structurei

Like other cAMP-dependent protein kinases, the inactive holoenzyme is probably composed of 2 PRKX catalytic subunits and a dimer of regulatory subunits. Interacts (cAMP-dependent) specifically with the regulatory subunits PRKAR1A and PRKAR1B. Compared to other cAMP-dependent serine/threonine protein kinases, does not interact with the 2 other PKA regulatory subunits PRKAR2A and PRKAR2B. Interacts with PIN1 (via WW domain). Interacts with cAMP-dependent protein kinase inhibitor/PKI proteins; inhibits PRKX (By similarity). Interacts with GPKOW (By similarity). Interacts with SMAD6 (By similarity). Interacts with PKD1; involved in differentiation and controlled morphogenesis of the kidney (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000045304.

Structurei

3D structure databases

ProteinModelPortaliQ922R0.
SMRiQ922R0. Positions 12-355.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 300255Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini301 – 35555AGC-kinase C-terminalAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0616. Eukaryota.
ENOG410XPQQ. LUCA.
GeneTreeiENSGT00810000125385.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiQ922R0.
KOiK19584.
OMAiQKILACK.
OrthoDBiEOG7VX8WD.
PhylomeDBiQ922R0.
TreeFamiTF313399.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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.

Q922R0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPPAGAAAT VKDPDHDPVK TKVSAPAADP KPRTSSQKAG HSLQDWDTIA
60 70 80 90 100
TVGTGTFGRV NLVKEKTGRQ YCALKIMSIP DVIRLKQEQH VQNEKAVLKE
110 120 130 140 150
INHPFLIKLL WTGHDNRFLY MLMEFVPGGE LFTYLRNRGR FSSVASVFYA
160 170 180 190 200
TEIVCAIEYL HSKEIVYRDL KPENILLDRE GHIKLTDFGF AKKLVDRTWT
210 220 230 240 250
LCGTPEYLAP EVIQSKGHGR AVDWWALGIL IFEMLSGFPP FFDDNPFGIY
260 270 280 290 300
QKILACKIDF PRQLDFTSKD LIKKLLVVDR TRRLGNMKNG AEDIKRHRWF
310 320 330 340 350
RGVEWESVPQ RKLKPPIVPK LSGDGDISNF ETYPESELDK TPSVSDKDLE

TFKNF
Length:355
Mass (Da):40,467
Last modified:December 1, 2001 - v1
Checksum:iAD6E682BE9DCBE46
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711Y → C in CAB57279 (PubMed:10729225).Curated
Sequence conflicti88 – 881E → G in CAB57279 (PubMed:10729225).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK034681 mRNA. Translation: BAC28796.1.
AK036432 mRNA. Translation: BAC29427.1.
AK037141 mRNA. Translation: BAC29717.1.
AK039088 mRNA. Translation: BAC30234.1.
AK081548 mRNA. Translation: BAC38254.1.
AK139510 mRNA. Translation: BAE24043.1.
AK150588 mRNA. Translation: BAE29682.1.
AK154447 mRNA. Translation: BAE32592.1.
AK169322 mRNA. Translation: BAE41076.1.
AJ238004 mRNA. Translation: CAB57279.1.
AL714017 Genomic DNA. Translation: CAM27303.1.
BC006875 mRNA. Translation: AAH06875.1.
CCDSiCCDS30248.1.
RefSeqiNP_058675.1. NM_016979.1.
UniGeneiMm.290338.

Genome annotation databases

EnsembliENSMUST00000036333; ENSMUSP00000045304; ENSMUSG00000035725.
GeneIDi19108.
KEGGimmu:19108.
UCSCiuc009tqp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK034681 mRNA. Translation: BAC28796.1.
AK036432 mRNA. Translation: BAC29427.1.
AK037141 mRNA. Translation: BAC29717.1.
AK039088 mRNA. Translation: BAC30234.1.
AK081548 mRNA. Translation: BAC38254.1.
AK139510 mRNA. Translation: BAE24043.1.
AK150588 mRNA. Translation: BAE29682.1.
AK154447 mRNA. Translation: BAE32592.1.
AK169322 mRNA. Translation: BAE41076.1.
AJ238004 mRNA. Translation: CAB57279.1.
AL714017 Genomic DNA. Translation: CAM27303.1.
BC006875 mRNA. Translation: AAH06875.1.
CCDSiCCDS30248.1.
RefSeqiNP_058675.1. NM_016979.1.
UniGeneiMm.290338.

3D structure databases

ProteinModelPortaliQ922R0.
SMRiQ922R0. Positions 12-355.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000045304.

PTM databases

iPTMnetiQ922R0.
PhosphoSiteiQ922R0.

Proteomic databases

EPDiQ922R0.
MaxQBiQ922R0.
PaxDbiQ922R0.
PRIDEiQ922R0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000036333; ENSMUSP00000045304; ENSMUSG00000035725.
GeneIDi19108.
KEGGimmu:19108.
UCSCiuc009tqp.2. mouse.

Organism-specific databases

CTDi5613.
MGIiMGI:1309999. Prkx.

Phylogenomic databases

eggNOGiKOG0616. Eukaryota.
ENOG410XPQQ. LUCA.
GeneTreeiENSGT00810000125385.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiQ922R0.
KOiK19584.
OMAiQKILACK.
OrthoDBiEOG7VX8WD.
PhylomeDBiQ922R0.
TreeFamiTF313399.

Miscellaneous databases

PROiQ922R0.
SOURCEiSearch...

Gene expression databases

BgeeiQ922R0.
CleanExiMM_PRKX.
ExpressionAtlasiQ922R0. baseline and differential.
GenevisibleiQ922R0. MM.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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. "A novel murine PKA-related protein kinase involved in neuronal differentiation."
    Blaschke R.J., Monaghan P.A., Bock D., Rappold G.A.
    Genomics 64:187-194(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone, Bone marrow, Egg, Embryo, Head, Hypothalamus and Vagina.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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].
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  6. "Protein kinase X activates ureteric bud branching morphogenesis in developing mouse metanephric kidney."
    Li X., Hyink D.P., Polgar K., Gusella G.L., Wilson P.D., Burrow C.R.
    J. Am. Soc. Nephrol. 16:3543-3552(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEPHROGENESIS.
  7. "Profiles of PrKX expression in developmental mouse embryo and human tissues."
    Li W., Yu Z.X., Kotin R.M.
    J. Histochem. Cytochem. 53:1003-1009(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  8. "Protein kinase-X interacts with Pin-1 and Polycystin-1 during mouse kidney development."
    Li X., Hyink D.P., Radbill B., Sudol M., Zhang H., Zheleznova N.N., Wilson P.D.
    Kidney Int. 76:54-62(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEPHROGENESIS, INTERACTION WITH PIN1.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung and Testis.
  10. "Regulation of cAMP-dependent protein kinases: the human protein kinase X (PrKX) reveals the role of the catalytic subunit alphaH-alphaI loop."
    Diskar M., Zenn H.M., Kaupisch A., Kaufholz M., Brockmeyer S., Sohmen D., Berrera M., Zaccolo M., Boshart M., Herberg F.W., Prinz A.
    J. Biol. Chem. 285:35910-35918(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKAR1A AND PRKAR1B.
  11. "PRKX critically regulates endothelial cell proliferation, migration, and vascular-like structure formation."
    Li X., Iomini C., Hyink D., Wilson P.D.
    Dev. Biol. 356:475-485(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANGIOGENESIS.

Entry informationi

Entry nameiPRKX_MOUSE
AccessioniPrimary (citable) accession number: Q922R0
Secondary accession number(s): B1AVU0
, Q3UCD1, Q8BHD6, Q9QZ12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: December 1, 2001
Last modified: June 8, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

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.