UniProtKB - P54645 (AAPK1_RAT)
5'-AMP-activated protein kinase catalytic subunit alpha-1
Prkaa1
Functioni
Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:14511394).
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 (By similarity).
AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (By similarity).
Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively (PubMed:2369897, PubMed:9029219).
Promotes lipolysis of lipid droplets by mediating phosphorylation of isoform 1 of CHKA (CHKalpha2) (By similarity).
Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3 (PubMed:11598104, PubMed:11069105, PubMed:12065600).
AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160 (By similarity).
Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A (PubMed:12740371, PubMed:11724780).
Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm (By similarity).
In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription (By similarity).
Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2 (By similarity).
In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1 (By similarity).
In that process also activates WDR45/WIPI4. Phosphorylates CASP6, thereby preventing its autoprocessing and subsequent activation (By similarity).
In response to nutrient limitation, phosphorylates transcription factor FOXO3 promoting FOXO3 mitochondrial import (By similarity).
Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (By similarity).
AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it (By similarity).
May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it (By similarity).
Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo (PubMed:21204788).
Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1 (PubMed:10025949, PubMed:17341212, PubMed:14709557).
By similarity12 PublicationsCatalytic activityi
- EC:2.7.11.12 Publications
- EC:2.7.11.12 Publications
- ATP + L-seryl-[acetyl-CoA carboxylase] = ADP + H+ + O-phospho-L-seryl-[acetyl-CoA carboxylase]1 PublicationEC:2.7.11.271 Publication
- ATP + L-seryl-[3-hydroxy-3-methylglutaryl-coenzyme A reductase] = ADP + H+ + O-phospho-L-seryl-[3-hydroxy-3-methylglutaryl-coenzyme A reductase]1 PublicationEC:2.7.11.311 Publication
- EC:2.7.11.261 Publication
- EC:2.7.11.261 Publication
Cofactori
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 56 | ATPPROSITE-ProRule annotation | 1 | |
Active sitei | 150 | Proton acceptorPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 33 – 41 | ATPPROSITE-ProRule annotation | 9 |
GO - Molecular functioni
- [acetyl-CoA carboxylase] kinase activity Source: UniProtKB-EC
- [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity Source: UniProtKB-EC
- AMP-activated protein kinase activity Source: UniProtKB
- ATP binding Source: RGD
- chromatin binding Source: UniProtKB
- eukaryotic elongation factor-2 kinase activator activity Source: UniProtKB
- histone serine kinase activity Source: UniProtKB
- metal ion binding Source: UniProtKB-KW
- protein-containing complex binding Source: RGD
- protein C-terminus binding Source: RGD
- protein kinase activity Source: RGD
- protein serine/threonine/tyrosine kinase activity Source: RHEA
- protein serine/threonine kinase activity Source: RGD
- protein serine kinase activity Source: RHEA
- tau-protein kinase activity Source: UniProtKB-EC
GO - Biological processi
- autophagy Source: UniProtKB-KW
- bile acid and bile salt transport Source: RGD
- bile acid signaling pathway Source: RGD
- CAMKK-AMPK signaling cascade Source: RGD
- cellular response to calcium ion Source: ARUK-UCL
- cellular response to ethanol Source: RGD
- cellular response to glucose starvation Source: UniProtKB
- cellular response to glucose stimulus Source: ARUK-UCL
- cellular response to hydrogen peroxide Source: RGD
- cellular response to hypoxia Source: RGD
- cellular response to nutrient levels Source: UniProtKB
- cellular response to organonitrogen compound Source: RGD
- cellular response to oxidative stress Source: RGD
- cellular response to prostaglandin E stimulus Source: RGD
- cellular response to xenobiotic stimulus Source: RGD
- cholesterol biosynthetic process Source: UniProtKB-KW
- chromatin organization Source: UniProtKB-KW
- cold acclimation Source: RGD
- energy homeostasis Source: UniProtKB
- fatty acid biosynthetic process Source: UniProtKB-KW
- fatty acid homeostasis Source: UniProtKB
- fatty acid oxidation Source: RGD
- glucose homeostasis Source: UniProtKB
- glucose metabolic process Source: RGD
- intracellular signal transduction Source: GO_Central
- lipid biosynthetic process Source: UniProtKB
- motor behavior Source: RGD
- negative regulation of apoptotic process Source: UniProtKB
- negative regulation of gene expression Source: RGD
- negative regulation of hepatocyte apoptotic process Source: UniProtKB
- negative regulation of insulin receptor signaling pathway Source: RGD
- negative regulation of lipid catabolic process Source: UniProtKB
- negative regulation of TOR signaling Source: UniProtKB
- negative regulation of translation Source: UniProtKB
- negative regulation of tubulin deacetylation Source: RGD
- neuron cellular homeostasis Source: RGD
- positive regulation of autophagy Source: UniProtKB
- positive regulation of cell population proliferation Source: RGD
- positive regulation of fatty acid oxidation Source: UniProtKB
- positive regulation of gene expression Source: RGD
- positive regulation of gluconeogenesis Source: UniProtKB
- positive regulation of glucose import Source: UniProtKB
- positive regulation of glycolytic process Source: UniProtKB
- positive regulation of mitochondrial transcription Source: RGD
- positive regulation of peptidyl-lysine acetylation Source: RGD
- positive regulation of protein localization Source: RGD
- positive regulation of protein targeting to mitochondrion Source: RGD
- positive regulation of skeletal muscle tissue development Source: RGD
- protein phosphorylation Source: RGD
- regulation of bile acid secretion Source: RGD
- regulation of circadian rhythm Source: UniProtKB
- regulation of gene expression Source: RGD
- regulation of microtubule cytoskeleton organization Source: RGD
- regulation of peptidyl-serine phosphorylation Source: RGD
- regulation of stress granule assembly Source: RGD
- regulation of vesicle-mediated transport Source: RGD
- response to 17alpha-ethynylestradiol Source: RGD
- response to activity Source: RGD
- response to caffeine Source: RGD
- response to camptothecin Source: RGD
- response to gamma radiation Source: UniProtKB
- response to hydrogen peroxide Source: RGD
- response to UV Source: RGD
- response to xenobiotic stimulus Source: RGD
- rhythmic process Source: UniProtKB-KW
- Wnt signaling pathway Source: UniProtKB-KW
Keywordsi
Enzyme and pathway databases
BRENDAi | 2.7.11.1, 5301 2.7.11.31, 5301 |
Reactomei | R-RNO-1632852, Macroautophagy R-RNO-380972, Energy dependent regulation of mTOR by LKB1-AMPK R-RNO-5628897, TP53 Regulates Metabolic Genes R-RNO-6804756, Regulation of TP53 Activity through Phosphorylation |
SABIO-RKi | P54645 |
Names & Taxonomyi
Protein namesi | Recommended name: 5'-AMP-activated protein kinase catalytic subunit alpha-1 (EC:2.7.11.12 Publications)Short name: AMPK subunit alpha-1 Alternative name(s): |
Gene namesi | Name:Prkaa1 Synonyms:Ampk1 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 3387, Prkaa1 |
Subcellular locationi
Cytosol
- cytosol Source: Reactome
Nucleus
- nuclear speck Source: Ensembl
- nucleus Source: RGD
Plasma Membrane
- apical plasma membrane Source: UniProtKB
Other locations
- axon Source: ARUK-UCL
- cytoplasm Source: UniProtKB
- dendrite Source: ARUK-UCL
- neuronal cell body Source: ARUK-UCL
- nucleotide-activated protein kinase complex Source: UniProtKB
- protein-containing complex Source: RGD
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 183 | T → E: Hinders activation. 1 Publication | 1 | |
Mutagenesisi | 269 | T → A: Hinders activation. 1 Publication | 1 | |
Mutagenesisi | 269 | T → D: Retains activation ability. 1 Publication | 1 | |
Mutagenesisi | 386 – 391 | RHTLDE → AHALAA: Allosterically activated by AMP but is not protected against dephosphorylation by AMP or ADP. 1 Publication | 6 | |
Mutagenesisi | 496 | S → A: Hinders activation. 1 Publication | 1 | |
Mutagenesisi | 496 | S → D: Retains activation ability. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL4533 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000085593 | 1 – 559 | 5'-AMP-activated protein kinase catalytic subunit alpha-1Add BLAST | 559 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 32 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 183 | Phosphothreonine; by LKB1 and CaMKK25 Publications | 1 | |
Modified residuei | 269 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 355 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 356 | PhosphoserineBy similarity | 1 | |
Modified residuei | 360 | Phosphoserine; by ULK11 Publication | 1 | |
Modified residuei | 368 | Phosphothreonine; by ULK11 Publication | 1 | |
Modified residuei | 382 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 397 | Phosphoserine; by ULK11 Publication | 1 | |
Modified residuei | 467 | PhosphoserineBy similarity | 1 | |
Modified residuei | 486 | PhosphoserineCombined sources | 1 | |
Modified residuei | 486 | Phosphoserine; by ULK1Combined sources1 Publication | 1 | |
Modified residuei | 488 | Phosphothreonine; by ULK11 Publication | 1 | |
Modified residuei | 490 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 496 | PhosphoserineCombined sources1 Publication | 1 | |
Modified residuei | 508 | PhosphoserineBy similarity | 1 | |
Modified residuei | 524 | PhosphoserineBy similarity | 1 | |
Modified residuei | 527 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Phosphoprotein, Ubl conjugationProteomic databases
jPOSTi | P54645 |
PaxDbi | P54645 |
PRIDEi | P54645 |
PTM databases
iPTMneti | P54645 |
PhosphoSitePlusi | P54645 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSRNOG00000012799, Expressed in ileum and 21 other tissues |
Genevisiblei | P54645, RN |
Interactioni
Subunit structurei
Binary interactionsi
P54645
With | #Exp. | IntAct |
---|---|---|
Flcn [Q76JQ2] | 2 | EBI-7596967,EBI-7596839 |
GO - Molecular functioni
- protein C-terminus binding Source: RGD
Protein-protein interaction databases
BioGRIDi | 249325, 368 interactors |
CORUMi | P54645 |
DIPi | DIP-57168N |
IntActi | P54645, 315 interactors |
MINTi | P54645 |
STRINGi | 10116.ENSRNOP00000017626 |
Chemistry databases
BindingDBi | P54645 |
Structurei
Secondary structure
3D structure databases
SMRi | P54645 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P54645 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 27 – 279 | Protein kinasePROSITE-ProRule annotationAdd BLAST | 253 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 302 – 381 | AISBy similarityAdd BLAST | 80 | |
Regioni | 484 – 536 | DisorderedSequence analysisAdd BLAST | 53 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 484 – 531 | Polar residuesSequence analysisAdd BLAST | 48 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0583, Eukaryota |
GeneTreei | ENSGT00940000158865 |
HOGENOMi | CLU_000288_59_3_1 |
InParanoidi | P54645 |
OMAi | YRSCQKD |
OrthoDBi | 1127668at2759 |
PhylomeDBi | P54645 |
TreeFami | TF314032 |
Family and domain databases
CDDi | cd12199, AMPKA1_C, 1 hit cd14403, UBA_AID_AAPK1, 1 hit |
InterProi | View protein in InterPro IPR032270, AMPK_C IPR039137, AMPKA1_C IPR028375, KA1/Ssp2_C IPR011009, Kinase-like_dom_sf IPR028797, PRKAA1_UBA IPR000719, Prot_kinase_dom IPR017441, Protein_kinase_ATP_BS IPR008271, Ser/Thr_kinase_AS |
Pfami | View protein in Pfam PF16579, AdenylateSensor, 1 hit PF00069, Pkinase, 1 hit |
SMARTi | View protein in SMART SM00220, S_TKc, 1 hit |
SUPFAMi | SSF103243, SSF103243, 1 hit SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in PROSITE PS00107, PROTEIN_KINASE_ATP, 1 hit PS50011, PROTEIN_KINASE_DOM, 1 hit PS00108, PROTEIN_KINASE_ST, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MRRLSSWRKM ATAEKQKHDG RVKIGHYILG DTLGVGTFGK VKVGKHELTG
60 70 80 90 100
HKVAVKILNR QKIRSLDVVG KIRREIQNLK LFRHPHIIKL YQVISTPSDI
110 120 130 140 150
FMVMEYVSGG ELFDYICKNG RLDEKESRRL FQQILSGVDY CHRHMVVHRD
160 170 180 190 200
LKPENVLLDA HMNAKIADFG LSNMMSDGEF LRTSCGSPNY AAPEVISGRL
210 220 230 240 250
YAGPEVDIWS SGVILYALLC GTLPFDDDHV PTLFKKICDG IFYTPQYLNP
260 270 280 290 300
SVISLLKHML QVDPMKRATI KDIREHEWFK QDLPKYLFPE DPSYSSTMID
310 320 330 340 350
DEALKEVCEK FECSEEEVLS CLYNRNHQDP LAVAYHLIID NRRIMNEAKD
360 370 380 390 400
FYLATSPPDS FLDDHHLTRP HPERVPFLVA ETPRARHTLD ELNPQKSKHQ
410 420 430 440 450
GVRKAKWHLG IRSQSRPNDI MAEVCRAIKQ LDYEWKVVNP YYLRVRRKNP
460 470 480 490 500
VTSTFSKMSL QLYQVDSRTY LLDFRSIDDE ITEAKSGTAT PQRSGSISNY
510 520 530 540 550
RSCQRSDSDA EAQGKPSEVS LTSSVTSLDS SPVDVAPRPG SHTIEFFEMC
ANLIKILAQ
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 13 – 14 | Missing in AAC52355 (PubMed:8557660).Curated | 2 | |
Sequence conflicti | 473 | D → L AA sequence (PubMed:8557660).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CH474048 Genomic DNA No translation available. U40819 mRNA Translation: AAC52355.1 |
RefSeqi | NP_062015.2, NM_019142.2 |
Genome annotation databases
Ensembli | ENSRNOT00000017626; ENSRNOP00000017626; ENSRNOG00000012799 |
GeneIDi | 65248 |
KEGGi | rno:65248 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CH474048 Genomic DNA No translation available. U40819 mRNA Translation: AAC52355.1 |
RefSeqi | NP_062015.2, NM_019142.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2V8Q | X-ray | 2.10 | A | 407-559 | [»] | |
2V92 | X-ray | 2.40 | A | 407-559 | [»] | |
2V9J | X-ray | 2.53 | A | 407-559 | [»] | |
2Y8L | X-ray | 2.50 | A | 407-555 | [»] | |
2Y8Q | X-ray | 2.80 | A | 407-555 | [»] | |
2YA3 | X-ray | 2.51 | A | 407-555 | [»] | |
4CFH | X-ray | 3.24 | A | 13-481 | [»] | |
C | 535-559 | [»] | ||||
4EAI | X-ray | 2.28 | A | 405-479 | [»] | |
A | 540-559 | [»] | ||||
4EAJ | X-ray | 2.61 | A | 405-479 | [»] | |
A | 540-559 | [»] | ||||
4EAK | X-ray | 2.50 | A | 405-479 | [»] | |
A | 540-559 | [»] | ||||
4EAL | X-ray | 2.51 | A | 405-479 | [»] | |
A | 540-559 | [»] | ||||
4F2L | X-ray | 1.50 | A | 295-347 | [»] | |
4QFG | X-ray | 3.46 | A | 11-480 | [»] | |
A | 536-559 | [»] | ||||
4QFR | X-ray | 3.34 | A | 11-480 | [»] | |
A | 536-559 | [»] | ||||
4QFS | X-ray | 3.55 | A | 11-479 | [»] | |
A | 536-559 | [»] | ||||
5KQ5 | X-ray | 3.41 | A | 11-480 | [»] | |
A | 536-559 | [»] | ||||
5T5T | X-ray | 3.46 | A | 11-480 | [»] | |
A | 536-559 | [»] | ||||
5UFU | X-ray | 3.45 | A | 269-559 | [»] | |
6E4T | X-ray | 3.40 | A | 11-480 | [»] | |
A | 536-559 | [»] | ||||
6E4U | X-ray | 3.27 | A | 11-480 | [»] | |
A | 536-559 | [»] | ||||
6E4W | X-ray | 3.35 | A | 11-480 | [»] | |
A | 536-559 | [»] | ||||
SMRi | P54645 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 249325, 368 interactors |
CORUMi | P54645 |
DIPi | DIP-57168N |
IntActi | P54645, 315 interactors |
MINTi | P54645 |
STRINGi | 10116.ENSRNOP00000017626 |
Chemistry databases
BindingDBi | P54645 |
ChEMBLi | CHEMBL4533 |
PTM databases
iPTMneti | P54645 |
PhosphoSitePlusi | P54645 |
Proteomic databases
jPOSTi | P54645 |
PaxDbi | P54645 |
PRIDEi | P54645 |
Genome annotation databases
Ensembli | ENSRNOT00000017626; ENSRNOP00000017626; ENSRNOG00000012799 |
GeneIDi | 65248 |
KEGGi | rno:65248 |
Organism-specific databases
CTDi | 5562 |
RGDi | 3387, Prkaa1 |
Phylogenomic databases
eggNOGi | KOG0583, Eukaryota |
GeneTreei | ENSGT00940000158865 |
HOGENOMi | CLU_000288_59_3_1 |
InParanoidi | P54645 |
OMAi | YRSCQKD |
OrthoDBi | 1127668at2759 |
PhylomeDBi | P54645 |
TreeFami | TF314032 |
Enzyme and pathway databases
BRENDAi | 2.7.11.1, 5301 2.7.11.31, 5301 |
Reactomei | R-RNO-1632852, Macroautophagy R-RNO-380972, Energy dependent regulation of mTOR by LKB1-AMPK R-RNO-5628897, TP53 Regulates Metabolic Genes R-RNO-6804756, Regulation of TP53 Activity through Phosphorylation |
SABIO-RKi | P54645 |
Miscellaneous databases
EvolutionaryTracei | P54645 |
PROi | PR:P54645 |
Gene expression databases
Bgeei | ENSRNOG00000012799, Expressed in ileum and 21 other tissues |
Genevisiblei | P54645, RN |
Family and domain databases
CDDi | cd12199, AMPKA1_C, 1 hit cd14403, UBA_AID_AAPK1, 1 hit |
InterProi | View protein in InterPro IPR032270, AMPK_C IPR039137, AMPKA1_C IPR028375, KA1/Ssp2_C IPR011009, Kinase-like_dom_sf IPR028797, PRKAA1_UBA IPR000719, Prot_kinase_dom IPR017441, Protein_kinase_ATP_BS IPR008271, Ser/Thr_kinase_AS |
Pfami | View protein in Pfam PF16579, AdenylateSensor, 1 hit PF00069, Pkinase, 1 hit |
SMARTi | View protein in SMART SM00220, S_TKc, 1 hit |
SUPFAMi | SSF103243, SSF103243, 1 hit SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in PROSITE PS00107, PROTEIN_KINASE_ATP, 1 hit PS50011, PROTEIN_KINASE_DOM, 1 hit PS00108, PROTEIN_KINASE_ST, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | AAPK1_RAT | |
Accessioni | P54645Primary (citable) accession number: P54645 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | July 28, 2009 | |
Last modified: | February 23, 2022 | |
This is version 201 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families