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Protein

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

Gene

PRKAB2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • identical protein binding Source: IntAct

GO - Biological processi

Complete GO annotation...

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_21285. Regulation of AMPK activity via LKB1.
REACT_21393. Regulation of Rheb GTPase activity by AMPK.
REACT_264544. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_355377. TP53 Regulates Metabolic Genes.
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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9379. PRKAB2.

Subcellular locationi

GO - Cellular componenti

  • AMP-activated protein kinase complex Source: UniProtKB
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
Complete GO annotation...

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.

Chemistry

DrugBankiDB00945. Acetylsalicylic acid.
DB00131. Adenosine monophosphate.

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 residuei95 – 951Phosphoserine1 Publication
Modified residuei108 – 1081Phosphoserine7 Publications
Modified residuei148 – 1481Phosphothreonine1 Publication
Modified residuei158 – 1581Phosphoserine1 Publication
Modified residuei170 – 1701Phosphoserine1 Publication
Modified residuei174 – 1741PhosphoserineBy similarity
Modified residuei184 – 1841Phosphoserine2 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.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO43741.
PaxDbiO43741.
PeptideAtlasiO43741.
PRIDEiO43741.

PTM databases

PhosphoSiteiO43741.

Expressioni

Gene expression databases

BgeeiO43741.
CleanExiHS_PRKAB2.
GenevisibleiO43741. HS.

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
BANPQ8N9N53EBI-1053424,EBI-744695
BEND5Q7L4P63EBI-1053424,EBI-724373
BLZF1Q9H2G94EBI-1053424,EBI-2548012
CCDC36Q8IYA83EBI-1053424,EBI-8638439
CDX4O146273EBI-1053424,EBI-10181162
CREB3L1Q96BA83EBI-1053424,EBI-6942903
CRXO431863EBI-1053424,EBI-748171
DAOP149204EBI-1053424,EBI-3908043
FAM208BQ5VWN6-23EBI-1053424,EBI-10172380
GATA1P159763EBI-1053424,EBI-3909284
GATAD2BQ8WXI93EBI-1053424,EBI-923440
GET4Q7L5D64EBI-1053424,EBI-711823
GOLGA2Q083793EBI-1053424,EBI-618309
IKZF1Q134223EBI-1053424,EBI-745305
IKZF3Q9UKT94EBI-1053424,EBI-747204
KLF15Q9UIH93EBI-1053424,EBI-2796400
KRT40Q6A1623EBI-1053424,EBI-10171697
KRTAP10-5P603703EBI-1053424,EBI-10172150
KRTAP10-7P604093EBI-1053424,EBI-10172290
KRTAP10-8P604103EBI-1053424,EBI-10171774
KRTAP10-9P604113EBI-1053424,EBI-10172052
KRTAP4-12Q9BQ663EBI-1053424,EBI-739863
KRTAP4-2Q9BYR53EBI-1053424,EBI-10172511
KRTAP5-9P263713EBI-1053424,EBI-3958099
KRTAP9-2Q9BYQ43EBI-1053424,EBI-1044640
KRTAP9-4Q9BYQ23EBI-1053424,EBI-10185730
LZTS2Q9BRK43EBI-1053424,EBI-741037
MAGED1Q9Y5V33EBI-1053424,EBI-716006
MDFIQ997503EBI-1053424,EBI-724076
MEOX2A4D1273EBI-1053424,EBI-10172134
PIAS2O759283EBI-1053424,EBI-348555
PRKAA1Q1313112EBI-1053424,EBI-1181405
PRKAA2P546467EBI-1053424,EBI-1383852
PRKAG1P546196EBI-1053424,EBI-1181439
PSME3P612893EBI-1053424,EBI-355546
PYGMP112173EBI-1053424,EBI-357469
RHEBL1Q8TAI73EBI-1053424,EBI-746555
RIMBP3Q9UFD93EBI-1053424,EBI-10182375
SPRY2O435973EBI-1053424,EBI-742487
STX11O755583EBI-1053424,EBI-714135
STX19Q8N4C73EBI-1053424,EBI-8484990
TRAF2Q129334EBI-1053424,EBI-355744
UBXN11Q5T1243EBI-1053424,EBI-746004

Protein-protein interaction databases

BioGridi111552. 96 interactions.
DIPiDIP-39763N.
IntActiO43741. 68 interactions.
STRINGi9606.ENSP00000254101.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4RERX-ray4.05B76-272[»]
4REWX-ray4.58B76-272[»]
ProteinModelPortaliO43741.
SMRiO43741. Positions 68-272.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43741.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG238368.
GeneTreeiENSGT00390000001416.
HOGENOMiHOG000230597.
HOVERGENiHBG050430.
KOiK07199.
OMAiGERHGTK.
OrthoDBiEOG7SXW3Z.
PhylomeDBiO43741.
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.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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

        10         20         30         40         50
MGNTTSDRVS GERHGAKAAR SEGAGGHAPG KEHKIMVGST DDPSVFSLPD
60 70 80 90 100
SKLPGDKEFV SWQQDLEDSV KPTQQARPTV IRWSEGGKEV FISGSFNNWS
110 120 130 140 150
TKIPLIKSHN DFVAILDLPE GEHQYKFFVD GQWVHDPSEP VVTSQLGTIN
160 170 180 190 200
NLIHVKKSDF EVFDALKLDS MESSETSCRD LSSSPPGPYG QEMYAFRSEE
210 220 230 240 250
RFKSPPILPP HLLQVILNKD TNISCDPALL PEPNHVMLNH LYALSIKDSV
260 270
MVLSATHRYK KKYVTTLLYK PI
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:
EMBLi
GenBanki
DDBJi
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. [O43741-1]
RefSeqiNP_005390.1. NM_005399.4. [O43741-1]
UniGeneiHs.50732.

Genome annotation databases

EnsembliENST00000254101; ENSP00000254101; ENSG00000131791.
GeneIDi5565.
KEGGihsa:5565.
UCSCiuc001epe.3. human. [O43741-1]
uc010ozm.2. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [O43741-1]
RefSeqiNP_005390.1. NM_005399.4. [O43741-1]
UniGeneiHs.50732.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4RERX-ray4.05B76-272[»]
4REWX-ray4.58B76-272[»]
ProteinModelPortaliO43741.
SMRiO43741. Positions 68-272.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111552. 96 interactions.
DIPiDIP-39763N.
IntActiO43741. 68 interactions.
STRINGi9606.ENSP00000254101.

Chemistry

ChEMBLiCHEMBL3038453.
DrugBankiDB00945. Acetylsalicylic acid.
DB00131. Adenosine monophosphate.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.

PTM databases

PhosphoSiteiO43741.

Proteomic databases

MaxQBiO43741.
PaxDbiO43741.
PeptideAtlasiO43741.
PRIDEiO43741.

Protocols and materials databases

DNASUi5565.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254101; ENSP00000254101; ENSG00000131791.
GeneIDi5565.
KEGGihsa:5565.
UCSCiuc001epe.3. human. [O43741-1]
uc010ozm.2. human.

Organism-specific databases

CTDi5565.
GeneCardsiGC01M146627.
HGNCiHGNC:9379. PRKAB2.
HPAiHPA044342.
MIMi602741. gene.
neXtProtiNX_O43741.
PharmGKBiPA33747.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG238368.
GeneTreeiENSGT00390000001416.
HOGENOMiHOG000230597.
HOVERGENiHBG050430.
KOiK07199.
OMAiGERHGTK.
OrthoDBiEOG7SXW3Z.
PhylomeDBiO43741.
TreeFamiTF313827.

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_21285. Regulation of AMPK activity via LKB1.
REACT_21393. Regulation of Rheb GTPase activity by AMPK.
REACT_264544. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_355377. TP53 Regulates Metabolic Genes.
SignaLinkiO43741.

Miscellaneous databases

ChiTaRSiPRKAB2. human.
EvolutionaryTraceiO43741.
GeneWikiiPRKAB2.
GenomeRNAii5565.
NextBioi21560.
PROiO43741.
SOURCEiSearch...

Gene expression databases

BgeeiO43741.
CleanExiHS_PRKAB2.
GenevisibleiO43741. HS.

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. "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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-108; THR-148; SER-158 AND SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 187-272 IN COMPLEX WITH PRKAA1 AND PRKAG1.
  21. 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: July 22, 2015
This is version 145 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

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.