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Protein

5'-AMP-activated protein kinase catalytic subunit alpha-1

Gene

PRKAA1

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

Functioni

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. 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. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. 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. 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. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. 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. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1. In response to nutrient limitation, phosphorylates transcription factor FOXO3 promoting FOXO3 mitochondrial import (By similarity). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. 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. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1.By similarity12 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.By similarity
ATP + [acetyl-CoA carboxylase] = ADP + [acetyl-CoA carboxylase] phosphate.By similarity
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate.By similarity
ATP + [tau protein] = ADP + [tau protein] phosphate.

Cofactori

Activity regulationi

Activated by phosphorylation on Thr-183. Binding of AMP to non-catalytic gamma subunit (PRKAG1, PRKAG2 or PRKAG3) results in allosteric activation, inducing phosphorylation on Thr-183. AMP-binding to gamma subunit also sustains activity by preventing dephosphorylation of Thr-183. ADP also stimulates Thr-183 phosphorylation, without stimulating already phosphorylated AMPK. ATP promotes dephosphorylation of Thr-183, rendering the enzyme inactive. Under physiological conditions AMPK mainly exists in its inactive form in complex with ATP, which is much more abundant than AMP. AMPK is activated by antihyperglycemic drug metformin, a drug prescribed to patients with type 2 diabetes: in vivo, metformin seems to mainly inhibit liver gluconeogenesis. However, metformin can be used to activate AMPK in muscle and other cells in culture or ex vivo (PubMed:11602624). Selectively inhibited by compound C (6-[4-(2-Piperidin-1-yl-ethoxy)-phenyl)]-3-pyridin-4-yl-pyyrazolo[1,5-a] pyrimidine. Activated by resveratrol, a natural polyphenol present in red wine, and S17834, a synthetic polyphenol.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei56ATPPROSITE-ProRule annotation1
Active sitei150Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi33 – 41ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase
Biological processAutophagy, Biological rhythms, Cholesterol biosynthesis, Cholesterol metabolism, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism, Transcription, Transcription regulation, Wnt signaling pathway
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-1632852 Macroautophagy
R-HSA-380972 Energy dependent regulation of mTOR by LKB1-AMPK
R-HSA-5628897 TP53 Regulates Metabolic Genes
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
SignaLinkiQ13131
SIGNORiQ13131

Names & Taxonomyi

Protein namesi
Recommended name:
5'-AMP-activated protein kinase catalytic subunit alpha-1 (EC:2.7.11.1By similarity)
Short name:
AMPK subunit alpha-1
Alternative name(s):
Acetyl-CoA carboxylase kinase (EC:2.7.11.27By similarity)
Short name:
ACACA kinase
Hydroxymethylglutaryl-CoA reductase kinase (EC:2.7.11.31By similarity)
Short name:
HMGCR kinase
Tau-protein kinase PRKAA1 (EC:2.7.11.26)
Gene namesi
Name:PRKAA1
Synonyms:AMPK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiHostDB:ENSG00000132356.11
HGNCiHGNC:9376 PRKAA1
MIMi602739 gene
neXtProtiNX_Q13131

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi307V → G or Q: Activates the kinase activity. 1 Publication1

Organism-specific databases

DisGeNETi5562
OpenTargetsiENSG00000132356
PharmGKBiPA33744

Chemistry databases

ChEMBLiCHEMBL4045
DrugBankiDB00945 Acetylsalicylic acid
DB00131 Adenosine monophosphate
DB00171 Adenosine triphosphate
DB00914 Phenformin

Polymorphism and mutation databases

BioMutaiPRKAA1
DMDMi254763436

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000855891 – 5595'-AMP-activated protein kinase catalytic subunit alpha-1Add BLAST559

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei32PhosphothreonineCombined sources1
Modified residuei183Phosphothreonine; by LKB1 and CaMKK2By similarity1
Modified residuei269PhosphothreonineBy similarity1
Modified residuei355PhosphothreonineCombined sources1
Modified residuei356PhosphoserineCombined sources1
Modified residuei360Phosphoserine; by ULK1By similarity1
Modified residuei368Phosphothreonine; by ULK1By similarity1
Modified residuei382PhosphothreonineCombined sources1
Modified residuei397PhosphoserineBy similarity1
Modified residuei467PhosphoserineCombined sources1
Modified residuei486PhosphoserineCombined sources1
Modified residuei488PhosphothreonineBy similarity1
Modified residuei490PhosphothreonineCombined sources1
Modified residuei496PhosphoserineCombined sources1
Modified residuei508PhosphoserineCombined sources1
Modified residuei524PhosphoserineCombined sources1
Modified residuei527PhosphoserineCombined sources1

Post-translational modificationi

Ubiquitinated.By similarity
Phosphorylated at Thr-183 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Also phosphorylated at Thr-183 by CAMKK2; triggered by a rise in intracellular calcium ions, without detectable changes in the AMP/ATP ratio. CAMKK1 can also phosphorylate Thr-183, but at a much lower level. Dephosphorylated by protein phosphatase 2A and 2C (PP2A and PP2C). 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. Dephosphorylated by PPM1A and PPM1B.4 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ13131
MaxQBiQ13131
PaxDbiQ13131
PeptideAtlasiQ13131
PRIDEiQ13131
ProteomicsDBi59180
59181 [Q13131-2]

PTM databases

iPTMnetiQ13131
PhosphoSitePlusiQ13131

Expressioni

Gene expression databases

BgeeiENSG00000132356 Expressed in 215 organ(s), highest expression level in intestine
CleanExiHS_PRKAA1
ExpressionAtlasiQ13131 baseline and differential
GenevisibleiQ13131 HS

Organism-specific databases

HPAiCAB005050
HPA035409
HPA064946

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). Interacts with FNIP1 and FNIP2.4 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi111549, 161 interactors
CORUMiQ13131
DIPiDIP-39973N
IntActiQ13131, 105 interactors
MINTiQ13131
STRINGi9606.ENSP00000346148

Chemistry databases

BindingDBiQ13131

Structurei

Secondary structure

1559
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ13131
SMRiQ13131
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 279Protein kinasePROSITE-ProRule annotationAdd BLAST253

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni302 – 381AISAdd BLAST80

Domaini

The AIS (autoinhibitory sequence) region shows some sequence similarity with the ubiquitin-associated domains and represses kinase activity.2 Publications

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0586 Eukaryota
ENOG410XNQ0 LUCA
GeneTreeiENSGT00930000150880
HOGENOMiHOG000233016
HOVERGENiHBG050432
KOiK07198
OMAiQGVRRAK
OrthoDBiEOG091G03TG
PhylomeDBiQ13131
TreeFamiTF314032

Family and domain databases

CDDicd12199 AMPKA1_C, 1 hit
InterProiView protein in InterPro
IPR032270 AMPK_C
IPR039137 AMPKA1_C
IPR028375 KA1/Ssp2_C
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF16579 AdenylateSensor, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF103243 SSF103243, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

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

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q13131-1) [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
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
VTSTYSKMSL QLYQVDSRTY LLDFRSIDDE ITEAKSGTAT PQRSGSVSNY
510 520 530 540 550
RSCQRSDSDA EAQGKSSEVS LTSSVTSLDS SPVDLTPRPG SHTIEFFEMC

ANLIKILAQ
Length:559
Mass (Da):64,009
Last modified:July 28, 2009 - v4
Checksum:iABAE71FBF912947A
GO
Isoform 2 (identifier: Q13131-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     121-121: R → RKSDVPGVVKTGSTKE

Show »
Length:574
Mass (Da):65,523
Checksum:i8EA8B85393F48DAA
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q96E92Q96E92_HUMAN
5'-AMP-activated protein kinase cat...
PRKAA1 hCG_37338
207Annotation score:

Sequence cautioni

The sequence AAA64850 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAD43027 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH37303 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA36547 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG35788 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5S → C in BAG35788 (PubMed:14702039).Curated1
Sequence conflicti9K → S in AAD43027 (PubMed:11042152).Curated1
Sequence conflicti37T → A in AAA64850 (Ref. 6) Curated1
Sequence conflicti202A → V in AAA64850 (Ref. 6) Curated1
Sequence conflicti208I → L in AAA64850 (Ref. 6) Curated1
Sequence conflicti269T → S in BAA36547 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05840110M → L1 PublicationCorresponds to variant dbSNP:rs17855679Ensembl.1
Natural variantiVAR_03562216Q → R in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs928784854Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_035431121R → RKSDVPGVVKTGSTKE in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC008810 Genomic DNA No translation available.
BC048980 mRNA Translation: AAH48980.1
AB022017 mRNA Translation: BAA36547.1 Different initiation.
AK312947 mRNA Translation: BAG35788.1 Different initiation.
BC037303 mRNA Translation: AAH37303.1 Different initiation.
AF100763 mRNA Translation: AAD43027.1 Different initiation.
U22456 mRNA Translation: AAA64850.1 Different initiation.
Y12856 mRNA Translation: CAA73361.1
CCDSiCCDS3932.2 [Q13131-1]
CCDS3933.2 [Q13131-2]
PIRiG01743
RefSeqiNP_006242.5, NM_006251.5 [Q13131-1]
NP_996790.3, NM_206907.3 [Q13131-2]
UniGeneiHs.43322

Genome annotation databases

EnsembliENST00000354209; ENSP00000346148; ENSG00000132356 [Q13131-2]
ENST00000397128; ENSP00000380317; ENSG00000132356 [Q13131-1]
GeneIDi5562
KEGGihsa:5562
UCSCiuc003jmb.4 human [Q13131-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC008810 Genomic DNA No translation available.
BC048980 mRNA Translation: AAH48980.1
AB022017 mRNA Translation: BAA36547.1 Different initiation.
AK312947 mRNA Translation: BAG35788.1 Different initiation.
BC037303 mRNA Translation: AAH37303.1 Different initiation.
AF100763 mRNA Translation: AAD43027.1 Different initiation.
U22456 mRNA Translation: AAA64850.1 Different initiation.
Y12856 mRNA Translation: CAA73361.1
CCDSiCCDS3932.2 [Q13131-1]
CCDS3933.2 [Q13131-2]
PIRiG01743
RefSeqiNP_006242.5, NM_006251.5 [Q13131-1]
NP_996790.3, NM_206907.3 [Q13131-2]
UniGeneiHs.43322

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4REDX-ray2.95A/B22-362[»]
4RERX-ray4.05A20-559[»]
4REWX-ray4.58A20-559[»]
5EZVX-ray2.99A/C359-401[»]
ProteinModelPortaliQ13131
SMRiQ13131
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111549, 161 interactors
CORUMiQ13131
DIPiDIP-39973N
IntActiQ13131, 105 interactors
MINTiQ13131
STRINGi9606.ENSP00000346148

Chemistry databases

BindingDBiQ13131
ChEMBLiCHEMBL4045
DrugBankiDB00945 Acetylsalicylic acid
DB00131 Adenosine monophosphate
DB00171 Adenosine triphosphate
DB00914 Phenformin

PTM databases

iPTMnetiQ13131
PhosphoSitePlusiQ13131

Polymorphism and mutation databases

BioMutaiPRKAA1
DMDMi254763436

Proteomic databases

EPDiQ13131
MaxQBiQ13131
PaxDbiQ13131
PeptideAtlasiQ13131
PRIDEiQ13131
ProteomicsDBi59180
59181 [Q13131-2]

Protocols and materials databases

DNASUi5562
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354209; ENSP00000346148; ENSG00000132356 [Q13131-2]
ENST00000397128; ENSP00000380317; ENSG00000132356 [Q13131-1]
GeneIDi5562
KEGGihsa:5562
UCSCiuc003jmb.4 human [Q13131-1]

Organism-specific databases

CTDi5562
DisGeNETi5562
EuPathDBiHostDB:ENSG00000132356.11
GeneCardsiPRKAA1
H-InvDBiHIX0004832
HGNCiHGNC:9376 PRKAA1
HPAiCAB005050
HPA035409
HPA064946
MIMi602739 gene
neXtProtiNX_Q13131
OpenTargetsiENSG00000132356
PharmGKBiPA33744
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0586 Eukaryota
ENOG410XNQ0 LUCA
GeneTreeiENSGT00930000150880
HOGENOMiHOG000233016
HOVERGENiHBG050432
KOiK07198
OMAiQGVRRAK
OrthoDBiEOG091G03TG
PhylomeDBiQ13131
TreeFamiTF314032

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-1632852 Macroautophagy
R-HSA-380972 Energy dependent regulation of mTOR by LKB1-AMPK
R-HSA-5628897 TP53 Regulates Metabolic Genes
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
SignaLinkiQ13131
SIGNORiQ13131

Miscellaneous databases

ChiTaRSiPRKAA1 human
GeneWikiiProtein_kinase,_AMP-activated,_alpha_1
GenomeRNAii5562
PROiPR:Q13131
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000132356 Expressed in 215 organ(s), highest expression level in intestine
CleanExiHS_PRKAA1
ExpressionAtlasiQ13131 baseline and differential
GenevisibleiQ13131 HS

Family and domain databases

CDDicd12199 AMPKA1_C, 1 hit
InterProiView protein in InterPro
IPR032270 AMPK_C
IPR039137 AMPKA1_C
IPR028375 KA1/Ssp2_C
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF16579 AdenylateSensor, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF103243 SSF103243, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiAAPK1_HUMAN
AccessioniPrimary (citable) accession number: Q13131
Secondary accession number(s): A8MTQ6
, B2R7E1, O00286, Q5D0E1, Q86VS1, Q9UNQ4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 28, 2009
Last modified: November 7, 2018
This is version 204 of the entry and version 4 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  7. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
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