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O43741

- AAKB2_HUMAN

UniProt

O43741 - AAKB2_HUMAN

Protein

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

Gene

PRKAB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. kinase activity Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. carnitine shuttle Source: Reactome
    2. cell cycle arrest Source: Reactome
    3. cellular lipid metabolic process Source: Reactome
    4. energy reserve metabolic process Source: Reactome
    5. fatty acid biosynthetic process Source: UniProtKB-KW
    6. insulin receptor signaling pathway Source: Reactome
    7. membrane organization Source: Reactome
    8. protein phosphorylation Source: GOC
    9. regulation of fatty acid biosynthetic process Source: Reactome
    10. signal transduction Source: ProtInc
    11. small molecule metabolic process Source: Reactome

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Enzyme and pathway databases

    ReactomeiREACT_11082. Import of palmitoyl-CoA into the mitochondrial matrix.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_1988. AMPK inhibits chREBP transcriptional activation activity.
    REACT_200686. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
    REACT_21285. Regulation of AMPK activity via LKB1.
    REACT_21393. Regulation of Rheb GTPase activity by AMPK.
    SignaLinkiO43741.

    Protein family/group databases

    CAZyiCBM48. Carbohydrate-Binding Module Family 48.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5'-AMP-activated protein kinase subunit beta-2
    Short name:
    AMPK subunit beta-2
    Gene namesi
    Name:PRKAB2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9379. PRKAB2.

    Subcellular locationi

    GO - Cellular componenti

    1. AMP-activated protein kinase complex Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi235 – 2351H → A: Results in an AMPK enzyme that is activable by phosphorylation but has significantly increased rate of dephosphorylation in phosphatase assays. 1 Publication

    Organism-specific databases

    PharmGKBiPA33747.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2722725'-AMP-activated protein kinase subunit beta-2PRO_0000204368Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei39 – 391Phosphoserine; by ULK11 Publication
    Modified residuei40 – 401Phosphothreonine; by ULK11 Publication
    Modified residuei69 – 691Phosphoserine; by ULK1By similarity
    Modified residuei108 – 1081Phosphoserine7 Publications
    Modified residuei174 – 1741PhosphoserineBy similarity
    Modified residuei184 – 1841Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated when associated with the catalytic subunit (PRKAA1 or PRKAA2). Phosphorylated by ULK1 and ULK2; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1, ULK2 and AMPK.8 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO43741.
    PaxDbiO43741.
    PeptideAtlasiO43741.
    PRIDEiO43741.

    PTM databases

    PhosphoSiteiO43741.

    Expressioni

    Gene expression databases

    ArrayExpressiO43741.
    BgeeiO43741.
    CleanExiHS_PRKAB2.
    GenevestigatoriO43741.

    Organism-specific databases

    HPAiHPA044342.

    Interactioni

    Subunit structurei

    AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic subunits (PRKAG1, PRKAG2 or PRKAG3).2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-1053424,EBI-1053424
    PRKAA1Q131316EBI-1053424,EBI-1181405
    PRKAG1P546193EBI-1053424,EBI-1181439

    Protein-protein interaction databases

    BioGridi111552. 40 interactions.
    DIPiDIP-39763N.
    IntActiO43741. 32 interactions.
    STRINGi9606.ENSP00000254101.

    Structurei

    Secondary structure

    1
    272
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi76 – 838
    Beta strandi90 – 945
    Helixi95 – 973
    Beta strandi112 – 12918
    Beta strandi132 – 1343
    Beta strandi141 – 1433
    Beta strandi149 – 1557
    Turni159 – 1624
    Beta strandi201 – 2044
    Helixi210 – 2134
    Beta strandi214 – 2174
    Turni236 – 2394
    Beta strandi242 – 2443
    Beta strandi250 – 25910
    Beta strandi262 – 27110

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2F15X-ray2.00A69-163[»]
    2V8QX-ray2.10B187-272[»]
    2V92X-ray2.40B187-272[»]
    2V9JX-ray2.53B187-272[»]
    2Y8LX-ray2.50B187-272[»]
    2Y8QX-ray2.80B187-270[»]
    2YA3X-ray2.51B187-272[»]
    4CFHX-ray3.24B187-272[»]
    4EAIX-ray2.28B189-272[»]
    4EAJX-ray2.61B189-272[»]
    ProteinModelPortaliO43741.
    SMRiO43741. Positions 68-272.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43741.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG238368.
    HOGENOMiHOG000230597.
    HOVERGENiHBG050430.
    InParanoidiO43741.
    KOiK07199.
    OMAiESKYITV.
    PhylomeDBiO43741.
    TreeFamiTF313827.

    Family and domain databases

    InterProiIPR006828. AMP_prot_kin_bsu_interact-dom.
    IPR014756. Ig_E-set.
    [Graphical view]
    PfamiPF04739. AMPKBI. 1 hit.
    [Graphical view]
    SMARTiSM01010. AMPKBI. 1 hit.
    [Graphical view]
    SUPFAMiSSF81296. SSF81296. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O43741-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGNTTSDRVS GERHGAKAAR SEGAGGHAPG KEHKIMVGST DDPSVFSLPD    50
    SKLPGDKEFV SWQQDLEDSV KPTQQARPTV IRWSEGGKEV FISGSFNNWS 100
    TKIPLIKSHN DFVAILDLPE GEHQYKFFVD GQWVHDPSEP VVTSQLGTIN 150
    NLIHVKKSDF EVFDALKLDS MESSETSCRD LSSSPPGPYG QEMYAFRSEE 200
    RFKSPPILPP HLLQVILNKD TNISCDPALL PEPNHVMLNH LYALSIKDSV 250
    MVLSATHRYK KKYVTTLLYK PI 272
    Length:272
    Mass (Da):30,302
    Last modified:June 1, 1998 - v1
    Checksum:i42B23BD70B92519C
    GO
    Isoform 2 (identifier: O43741-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-25: MGNTTSDRVSGERHGAKAARSEGAG → MPRGRSTRSWWGVRTTPACSASLTP
         26-107: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:190
    Mass (Da):21,485
    Checksum:iBB41913AB4FDEB54
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2525MGNTT…SEGAG → MPRGRSTRSWWGVRTTPACS ASLTP in isoform 2. 1 PublicationVSP_055820Add
    BLAST
    Alternative sequencei26 – 10782Missing in isoform 2. 1 PublicationVSP_055821Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ224538 mRNA. Translation: CAA12030.1.
    AF504543
    , AF504538, AF504539, AF504540, AF504541, AF504542 Genomic DNA. Translation: AAM74153.1.
    AK292820 mRNA. Translation: BAF85509.1.
    AK294863 mRNA. Translation: BAG57967.1.
    AK316005 mRNA. Translation: BAH14376.1.
    AL356378 Genomic DNA. Translation: CAH72644.1.
    CH471223 Genomic DNA. Translation: EAW50945.1.
    BC053610 mRNA. Translation: AAH53610.1.
    CCDSiCCDS925.1.
    RefSeqiNP_005390.1. NM_005399.4.
    UniGeneiHs.50732.

    Genome annotation databases

    EnsembliENST00000254101; ENSP00000254101; ENSG00000131791. [O43741-1]
    GeneIDi5565.
    KEGGihsa:5565.
    UCSCiuc001epe.3. human.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ224538 mRNA. Translation: CAA12030.1 .
    AF504543
    , AF504538 , AF504539 , AF504540 , AF504541 , AF504542 Genomic DNA. Translation: AAM74153.1 .
    AK292820 mRNA. Translation: BAF85509.1 .
    AK294863 mRNA. Translation: BAG57967.1 .
    AK316005 mRNA. Translation: BAH14376.1 .
    AL356378 Genomic DNA. Translation: CAH72644.1 .
    CH471223 Genomic DNA. Translation: EAW50945.1 .
    BC053610 mRNA. Translation: AAH53610.1 .
    CCDSi CCDS925.1.
    RefSeqi NP_005390.1. NM_005399.4.
    UniGenei Hs.50732.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2F15 X-ray 2.00 A 69-163 [» ]
    2V8Q X-ray 2.10 B 187-272 [» ]
    2V92 X-ray 2.40 B 187-272 [» ]
    2V9J X-ray 2.53 B 187-272 [» ]
    2Y8L X-ray 2.50 B 187-272 [» ]
    2Y8Q X-ray 2.80 B 187-270 [» ]
    2YA3 X-ray 2.51 B 187-272 [» ]
    4CFH X-ray 3.24 B 187-272 [» ]
    4EAI X-ray 2.28 B 189-272 [» ]
    4EAJ X-ray 2.61 B 189-272 [» ]
    ProteinModelPortali O43741.
    SMRi O43741. Positions 68-272.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111552. 40 interactions.
    DIPi DIP-39763N.
    IntActi O43741. 32 interactions.
    STRINGi 9606.ENSP00000254101.

    Chemistry

    BindingDBi O43741.
    ChEMBLi CHEMBL3038453.
    DrugBanki DB00945. Acetylsalicylic acid.
    DB00131. Adenosine monophosphate.

    Protein family/group databases

    CAZyi CBM48. Carbohydrate-Binding Module Family 48.

    PTM databases

    PhosphoSitei O43741.

    Proteomic databases

    MaxQBi O43741.
    PaxDbi O43741.
    PeptideAtlasi O43741.
    PRIDEi O43741.

    Protocols and materials databases

    DNASUi 5565.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000254101 ; ENSP00000254101 ; ENSG00000131791 . [O43741-1 ]
    GeneIDi 5565.
    KEGGi hsa:5565.
    UCSCi uc001epe.3. human.

    Organism-specific databases

    CTDi 5565.
    GeneCardsi GC01M146627.
    HGNCi HGNC:9379. PRKAB2.
    HPAi HPA044342.
    MIMi 602741. gene.
    neXtProti NX_O43741.
    PharmGKBi PA33747.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG238368.
    HOGENOMi HOG000230597.
    HOVERGENi HBG050430.
    InParanoidi O43741.
    KOi K07199.
    OMAi ESKYITV.
    PhylomeDBi O43741.
    TreeFami TF313827.

    Enzyme and pathway databases

    Reactomei REACT_11082. Import of palmitoyl-CoA into the mitochondrial matrix.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_1988. AMPK inhibits chREBP transcriptional activation activity.
    REACT_200686. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
    REACT_21285. Regulation of AMPK activity via LKB1.
    REACT_21393. Regulation of Rheb GTPase activity by AMPK.
    SignaLinki O43741.

    Miscellaneous databases

    ChiTaRSi PRKAB2. human.
    EvolutionaryTracei O43741.
    GeneWikii PRKAB2.
    GenomeRNAii 5565.
    NextBioi 21560.
    PROi O43741.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43741.
    Bgeei O43741.
    CleanExi HS_PRKAB2.
    Genevestigatori O43741.

    Family and domain databases

    InterProi IPR006828. AMP_prot_kin_bsu_interact-dom.
    IPR014756. Ig_E-set.
    [Graphical view ]
    Pfami PF04739. AMPKBI. 1 hit.
    [Graphical view ]
    SMARTi SM01010. AMPKBI. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81296. SSF81296. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel AMP-activated protein kinase beta subunit isoform that is highly expressed in skeletal muscle."
      Thornton C., Snowden M.A., Carling D.
      J. Biol. Chem. 273:12443-12450(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Variant screening of PRKAB2, a type 2 diabetes mellitus susceptibility candidate gene on 1q in Pima Indians."
      Prochazka M., Farook V.S., Ossowski V., Wolford J.K., Bogardus C.
      Mol. Cell. Probes 16:421-427(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain and Trachea.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Pancreas.
    7. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop."
      Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M., Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.
      Autophagy 7:696-706(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY ULK1 AND ULK2.
    15. "AMP-activated protein kinase in metabolic control and insulin signaling."
      Towler M.C., Hardie D.G.
      Circ. Res. 100:328-341(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    16. "AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy."
      Hardie D.G.
      Nat. Rev. Mol. Cell Biol. 8:774-785(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 187-272 IN COMPLEX WITH PRKAA1 AND PRKAG1.
    20. Cited for: X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 187-272 IN COMPLEX WITH PRKAA1 AND PRKAG1, MUTAGENESIS OF HIS-235.

    Entry informationi

    Entry nameiAAKB2_HUMAN
    AccessioniPrimary (citable) accession number: O43741
    Secondary accession number(s): A8K9V5, B4DH06, Q5VXY0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 135 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3