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Protein
Submitted name:

5'-AMP-activated protein kinase subunit beta-2

Gene

Prkab2

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

Functioni

GO - Molecular functioni

  • kinase activity Source: UniProtKB-KW
  • protein kinase binding Source: RGD

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_271537. Regulation of Rheb GTPase activity by AMPK.
REACT_277707. Regulation of AMPK activity via LKB1.
REACT_284928. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_314418. AMPK inhibits chREBP transcriptional activation activity.
REACT_324879. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_347820. Translocation of GLUT4 to the plasma membrane.
REACT_358301. TP53 Regulates Metabolic Genes.

Names & Taxonomyi

Protein namesi
Submitted name:
5'-AMP-activated protein kinase subunit beta-2Imported
Submitted name:
Prkab2 proteinImported
Gene namesi
Name:Prkab2Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi620905. Prkab2.

Subcellular locationi

GO - Cellular componenti

  • AMP-activated protein kinase complex Source: RGD Source: InterPro
  • cAMP-dependent protein kinase complex Source: RGD
Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000062137.

Family & Domainsi

Phylogenomic databases

GeneTreeiENSGT00390000001416.
HOGENOMiHOG000230597.
HOVERGENiHBG050430.
OMAiGERHGTK.
OrthoDBiEOG7SXW3Z.
TreeFamiTF313827.

Family and domain databases

InterProiIPR030081. AMPK_beta-2.
IPR006828. ASC_dom.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10343:SF43. PTHR10343:SF43. 1 hit.
PfamiPF04739. AMPKBI. 1 hit.
[Graphical view]
SMARTiSM01010. AMPKBI. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

G3V9X3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNTTSERVS GERHGAKAAR AEGGGHGPGK EHKIMVGSTD DPSVFSLPDS
60 70 80 90 100
KLPGDKEFVP WQQDLDDSVK PTQQARPTVI RWSEGGKEVF ISGSFNNWST
110 120 130 140 150
KIPLIKSHND FVAILDLPEG EHQYKFFVDG QWVHDPSEPV VTSQLGTINN
160 170
LIHVKKSDFE VFDALKLDSM ESSETSCRV
Length:179
Mass (Da):19,749
Last modified:July 22, 2015 - v2
Checksum:i56EF351AC35416D2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC121381 Genomic DNA. No translation available.
BC078821 mRNA. Translation: AAH78821.1.
RefSeqiXP_006233073.1. XM_006233011.2.
XP_006233074.1. XM_006233012.2.
UniGeneiRn.207202.

Genome annotation databases

EnsembliENSRNOT00000063783; ENSRNOP00000062137; ENSRNOG00000018166.
GeneIDi64562.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC121381 Genomic DNA. No translation available.
BC078821 mRNA. Translation: AAH78821.1.
RefSeqiXP_006233073.1. XM_006233011.2.
XP_006233074.1. XM_006233012.2.
UniGeneiRn.207202.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000062137.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000063783; ENSRNOP00000062137; ENSRNOG00000018166.
GeneIDi64562.

Organism-specific databases

CTDi5565.
RGDi620905. Prkab2.

Phylogenomic databases

GeneTreeiENSGT00390000001416.
HOGENOMiHOG000230597.
HOVERGENiHBG050430.
OMAiGERHGTK.
OrthoDBiEOG7SXW3Z.
TreeFamiTF313827.

Enzyme and pathway databases

ReactomeiREACT_271537. Regulation of Rheb GTPase activity by AMPK.
REACT_277707. Regulation of AMPK activity via LKB1.
REACT_284928. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_314418. AMPK inhibits chREBP transcriptional activation activity.
REACT_324879. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_347820. Translocation of GLUT4 to the plasma membrane.
REACT_358301. TP53 Regulates Metabolic Genes.

Miscellaneous databases

NextBioi35584432.

Family and domain databases

InterProiIPR030081. AMPK_beta-2.
IPR006828. ASC_dom.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10343:SF43. PTHR10343:SF43. 1 hit.
PfamiPF04739. AMPKBI. 1 hit.
[Graphical view]
SMARTiSM01010. AMPKBI. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.
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: TestisImported.
  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. Ensembl
    Submitted (SEP-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].

Entry informationi

Entry nameiG3V9X3_RAT
AccessioniPrimary (citable) accession number: G3V9X3
Secondary accession number(s): Q6AYZ8
Entry historyi
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: July 22, 2015
Last modified: July 22, 2015
This is version 30 of the entry and version 2 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.