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P31751

- AKT2_HUMAN

UniProt

P31751 - AKT2_HUMAN

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Protein

RAC-beta serine/threonine-protein kinase

Gene

AKT2

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

Functioni

AKT2 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI3P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development.
One of the few specific substrates of AKT2 identified recently is PITX2. Phosphorylation of PITX2 impairs its association with the CCND1 mRNA-stabilizing complex thus shortening the half-life of CCND1. AKT2 seems also to be the principal isoform responsible of the regulation of glucose uptake. Phosphorylates C2CD5 on 'Ser-197' during insulin-stimulated adipocytes. AKT2 is also specifically involved in skeletal muscle differentiation, one of its substrates in this process being ANKRD2. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis. Phosphorylates CLK2 on 'Thr-343'.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Two specific sites, one in the kinase domain (Thr-309) and the other in the C-terminal regulatory region (Ser-474), need to be phosphorylated for its full activation. Aminofurazans are potent AKT2 inhibitors.2 Publications

Kineticsi

  1. KM=358.4 µM for ATP (for purified and in vitro activated AKT2)1 Publication
  2. KM=3.4 µM for peptide substrate (for purified and in vitro activated AKT2)1 Publication
  3. KM=564 µM for ATP (for recombinant myristoylated AKT2 expressed and immunoprecipitated from Rat-1 cells)1 Publication
  4. KM=2.3 µM for peptide substrate (for recombinant myristoylated AKT2 expressed and immunoprecipitated from Rat-1 cells)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei181 – 1811ATPPROSITE-ProRule annotation
Binding sitei181 – 1811Inhibitor
Binding sitei200 – 2001Inhibitor
Binding sitei232 – 2321Inhibitor; via amide nitrogen
Binding sitei236 – 2361Inhibitor
Active sitei275 – 2751Proton acceptorPROSITE-ProRule annotation
Binding sitei279 – 2791Inhibitor; via carbonyl oxygen
Binding sitei280 – 2801Manganese1 Publication
Binding sitei293 – 2931Inhibitor
Binding sitei293 – 2931Manganese1 Publication
Binding sitei294 – 2941Inhibitor; via amide nitrogen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi158 – 1669ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. kinase activity Source: Reactome
  3. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. activation of Ral GTPase activity Source: Ensembl
  2. apoptotic process Source: UniProtKB-KW
  3. carbohydrate transport Source: UniProtKB-KW
  4. cellular protein modification process Source: ProtInc
  5. cellular response to insulin stimulus Source: BHF-UCL
  6. fat cell differentiation Source: UniProtKB
  7. glucose metabolic process Source: UniProtKB-KW
  8. glycogen biosynthetic process Source: UniProtKB-KW
  9. insulin receptor signaling pathway Source: UniProtKB
  10. intracellular protein transmembrane transport Source: UniProtKB
  11. mammary gland epithelial cell differentiation Source: UniProtKB
  12. membrane organization Source: Reactome
  13. negative regulation of plasma membrane long-chain fatty acid transport Source: BHF-UCL
  14. peripheral nervous system myelin maintenance Source: Ensembl
  15. positive regulation of cell motility Source: BHF-UCL
  16. positive regulation of fatty acid beta-oxidation Source: BHF-UCL
  17. positive regulation of glucose import Source: BHF-UCL
  18. positive regulation of glucose import in response to insulin stimulus Source: Ensembl
  19. positive regulation of glucose metabolic process Source: BHF-UCL
  20. positive regulation of glycogen biosynthetic process Source: BHF-UCL
  21. positive regulation of protein phosphorylation Source: UniProtKB
  22. positive regulation of protein targeting to membrane Source: UniProtKB
  23. positive regulation of vesicle fusion Source: UniProtKB
  24. protein localization to plasma membrane Source: Ensembl
  25. regulation of cell cycle arrest Source: UniProtKB
  26. regulation of cell migration Source: UniProtKB
  27. regulation of translation Source: UniProtKB-KW
  28. signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Carbohydrate metabolism, Glucose metabolism, Glycogen biosynthesis, Glycogen metabolism, Sugar transport, Translation regulation, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_115662. Downregulation of ERBB2:ERBB3 signaling.
REACT_12442. AKT phosphorylates targets in the nucleus.
REACT_12447. Negative regulation of the PI3K/AKT network.
REACT_12564. AKT phosphorylates targets in the cytosol.
REACT_13655. AKT-mediated inactivation of FOXO1A.
REACT_1451. PDE3B signalling.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_1695. GPVI-mediated activation cascade.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
REACT_19358. CD28 dependent PI3K/Akt signaling.
REACT_19405. CTLA4 inhibitory signaling.
REACT_200731. deactivation of the beta-catenin transactivating complex.
REACT_6743. Inhibition of TSC complex formation by PKB.
REACT_75829. PIP3 activates AKT signaling.
REACT_790. Activation of PKB.
SignaLinkiP31751.

Names & Taxonomyi

Protein namesi
Recommended name:
RAC-beta serine/threonine-protein kinase (EC:2.7.11.1)
Alternative name(s):
Protein kinase Akt-2
Protein kinase B beta
Short name:
PKB beta
RAC-PK-beta
Gene namesi
Name:AKT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:392. AKT2.

Subcellular locationi

Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein
Note: Localizes within both nucleus and cytoplasm of proliferative primary myoblasts and mostly within the nucleus of differentiated primary myoblasts. By virtue of the N-terminal PH domain, is recruited to sites of the plasma membrane containing increased PI(3,4,5)P3 or PI(3,4)P2, cell membrane targeting is also facilitared by interaction with CLIP3.

GO - Cellular componenti

  1. cell cortex Source: UniProtKB
  2. cytosol Source: Reactome
  3. nucleus Source: UniProtKB
  4. plasma membrane Source: UniProtKB
  5. ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Defects in AKT2 are a cause of susceptibility to breast cancer (BC). AKT2 promotes metastasis of tumor cells without affecting the latency of tumor development. With AKT3, plays also a pivotal role in the biology of glioblastoma.
Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti274 – 2741R → H in NIDDM; associated with typical metabolic dyslipidemia with elevated fastin triglyceride, high VLDL triglyceride/cholesterol ratios, low HDL cholesterol levels and high small dense LDL levels; de novo lipogenesis and liver fat are also significantly elevated in this subject. 1 Publication
VAR_067310
Hypoinsulinemic hypoglycemia with hemihypertrophy (HIHGHH) [MIM:240900]: A disorder characterized by hypoglycemia, low insulin levels, low serum levels of ketone bodies and branched-chain amino acids, left-sided hemihypertrophy, neonatal macrosomia, reduced consciousness and hypoglycemic seizures.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171E → K in HIHGHH; exhibits plasma membrane localization in serum-starved cells and produced inappropriate tonic nuclear exclusion of FOXO1 in preadipocytes. 1 Publication
VAR_067309

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi309 – 3091T → A: Impairs interaction with TTC3; when associated with A-474. 2 Publications
Mutagenesisi309 – 3091T → E: Constitutively active; when associated with D-474. 2 Publications
Mutagenesisi474 – 4741S → A: Impairs interaction with TTC3; when associated with A-309. 2 Publications
Mutagenesisi474 – 4741S → D: Constitutively active; when associated with E-309. 2 Publications

Keywords - Diseasei

Diabetes mellitus, Disease mutation, Proto-oncogene

Organism-specific databases

MIMi125853. phenotype.
240900. phenotype.
Orphaneti79085. Familial partial lipodystrophy due to AKT2 mutations.
293964. Hypoinsulinemic hypoglycemia and body hemihypertrophy.
PharmGKBiPA24685.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 481481RAC-beta serine/threonine-protein kinasePRO_0000085608Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Disulfide bondi60 ↔ 77By similarity
Modified residuei126 – 1261Phosphoserine1 Publication
Glycosylationi128 – 1281O-linked (GlcNAc)By similarity
Glycosylationi131 – 1311O-linked (GlcNAc)By similarity
Disulfide bondi297 ↔ 3111 Publication
Glycosylationi306 – 3061O-linked (GlcNAc)By similarity
Modified residuei309 – 3091Phosphothreonine; by PDPK14 Publications
Glycosylationi313 – 3131O-linked (GlcNAc)By similarity
Modified residuei447 – 4471Phosphoserine1 Publication
Modified residuei451 – 4511Phosphothreonine1 Publication
Modified residuei474 – 4741Phosphoserine3 Publications
Modified residuei478 – 4781Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation on Thr-309 and Ser-474 is required for full activity.5 Publications
Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination. TRAF6-induced 'Lys-63'-linked AKT2 ubiquitination. When fully phosphorylated and translocated into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its degradation by the proteasome.2 Publications
O-GlcNAcylation at Thr-306 and Thr-313 inhibits activating phosphorylation at Thr-309 via disrupting the interaction between AKT and PDK1.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP31751.
PaxDbiP31751.
PRIDEiP31751.

PTM databases

PhosphoSiteiP31751.

Expressioni

Tissue specificityi

Expressed in all cell types so far analyzed.

Gene expression databases

BgeeiP31751.
CleanExiHS_AKT2.
ExpressionAtlasiP31751. baseline and differential.
GenevestigatoriP31751.

Organism-specific databases

HPAiCAB004204.

Interactioni

Subunit structurei

Interacts (via PH domain) with MTCP1, TCL1A AND TCL1B. Interacts with CLK2, PBH2 and TRAF6. Interacts (when phosphorylated) with CLIP3, the interaction promotes cell membrane localization.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GSK3BP498412EBI-296058,EBI-373586
HSP90AB1P082382EBI-296058,EBI-352572
VIMP086706EBI-296058,EBI-353844

Protein-protein interaction databases

BioGridi106711. 38 interactions.
DIPiDIP-32583N.
IntActiP31751. 22 interactions.
MINTiMINT-87790.
STRINGi9606.ENSP00000375892.

Structurei

Secondary structure

1
481
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 1510
Beta strandi17 – 204
Beta strandi22 – 309
Turni31 – 333
Beta strandi34 – 407
Beta strandi45 – 473
Beta strandi52 – 565
Beta strandi58 – 603
Beta strandi62 – 654
Beta strandi67 – 759
Beta strandi86 – 927
Helixi93 – 11018
Helixi149 – 1513
Beta strandi152 – 1609
Beta strandi162 – 17110
Turni172 – 1743
Beta strandi177 – 1848
Helixi185 – 1906
Helixi194 – 20512
Beta strandi215 – 2206
Beta strandi222 – 2309
Helixi237 – 2448
Helixi249 – 26820
Beta strandi280 – 2834
Beta strandi289 – 2913
Beta strandi298 – 3003
Beta strandi310 – 3123
Helixi314 – 3163
Helixi319 – 3224
Beta strandi323 – 3253
Helixi331 – 34515
Beta strandi351 – 3533
Helixi355 – 36410
Beta strandi371 – 3733
Helixi375 – 38410
Turni389 – 3913
Turni393 – 3953
Turni397 – 3993
Helixi400 – 4045
Helixi407 – 4093
Helixi414 – 4185
Beta strandi431 – 4344
Beta strandi437 – 4393
Helixi441 – 4444
Beta strandi474 – 4763
Turni477 – 4793

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GZKX-ray2.30A146-460[»]
1GZNX-ray2.50A146-480[»]
1GZOX-ray2.75A146-460[»]
1MRVX-ray2.80A143-481[»]
1MRYX-ray2.80A143-481[»]
1O6KX-ray1.70A146-481[»]
1O6LX-ray1.60A146-467[»]
1P6SNMR-A1-111[»]
2JDOX-ray1.80A146-467[»]
2JDRX-ray2.30A146-467[»]
2UW9X-ray2.10A146-467[»]
2X39X-ray1.93A146-467[»]
2XH5X-ray2.72A146-479[»]
3D0EX-ray2.00A/B146-480[»]
3E87X-ray2.30A/B146-480[»]
3E88X-ray2.50A/B146-480[»]
3E8DX-ray2.70A/B146-480[»]
DisProtiDP00304.
ProteinModelPortaliP31751.
SMRiP31751. Positions 1-480.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31751.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 108104PHPROSITE-ProRule annotationAdd
BLAST
Domaini152 – 409258Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini410 – 48172AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni230 – 2323Inhibitor binding
Regioni277 – 2793Inhibitor binding
Regioni292 – 2932Inhibitor binding

Domaini

Binding of the PH domain to phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) following phosphatidylinositol 3-kinase alpha (PIK3CA) activity results in its targeting to the plasma membrane.

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118793.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiP31751.
KOiK04456.
OMAiAGMEHEQ.
OrthoDBiEOG7Q5HCW.
PhylomeDBiP31751.
TreeFamiTF102004.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P31751) [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
MNEVSVIKEG WLHKRGEYIK TWRPRYFLLK SDGSFIGYKE RPEAPDQTLP
60 70 80 90 100
PLNNFSVAEC QLMKTERPRP NTFVIRCLQW TTVIERTFHV DSPDEREEWM
110 120 130 140 150
RAIQMVANSL KQRAPGEDPM DYKCGSPSDS STTEEMEVAV SKARAKVTMN
160 170 180 190 200
DFDYLKLLGK GTFGKVILVR EKATGRYYAM KILRKEVIIA KDEVAHTVTE
210 220 230 240 250
SRVLQNTRHP FLTALKYAFQ THDRLCFVME YANGGELFFH LSRERVFTEE
260 270 280 290 300
RARFYGAEIV SALEYLHSRD VVYRDIKLEN LMLDKDGHIK ITDFGLCKEG
310 320 330 340 350
ISDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM YEMMCGRLPF
360 370 380 390 400
YNQDHERLFE LILMEEIRFP RTLSPEAKSL LAGLLKKDPK QRLGGGPSDA
410 420 430 440 450
KEVMEHRFFL SINWQDVVQK KLLPPFKPQV TSEVDTRYFD DEFTAQSITI
460 470 480
TPPDRYDSLG LLELDQRTHF PQFSYSASIR E
Length:481
Mass (Da):55,769
Last modified:November 1, 1995 - v2
Checksum:iB18C87A7246BFB24
GO
Isoform 2 (identifier: P31751-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     278-320: Missing.

Note: No experimental confirmation available

Show »
Length:438
Mass (Da):51,083
Checksum:iEEAF3B6E42F6A5C1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti478 – 4814SIRE → FREEKDLLMSLFVSLILFSD FSSLKSHSFSSNFILLSFSS LKK in AAA36585. (PubMed:1801921)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171E → K in HIHGHH; exhibits plasma membrane localization in serum-starved cells and produced inappropriate tonic nuclear exclusion of FOXO1 in preadipocytes. 1 Publication
VAR_067309
Natural varianti188 – 1881I → V.1 Publication
Corresponds to variant rs55859611 [ dbSNP | Ensembl ].
VAR_040356
Natural varianti208 – 2081R → K.1 Publication
Corresponds to variant rs35817154 [ dbSNP | Ensembl ].
VAR_040357
Natural varianti274 – 2741R → H in NIDDM; associated with typical metabolic dyslipidemia with elevated fastin triglyceride, high VLDL triglyceride/cholesterol ratios, low HDL cholesterol levels and high small dense LDL levels; de novo lipogenesis and liver fat are also significantly elevated in this subject. 1 Publication
VAR_067310

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei278 – 32043Missing in isoform 2. 1 PublicationVSP_056930Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M77198 mRNA. Translation: AAA36585.1.
M95936 mRNA. Translation: AAA58364.1.
AK314619 mRNA. Translation: BAG37185.1.
AC118344 Genomic DNA. No translation available.
BC032709 mRNA. Translation: AAH32709.1.
BC120995 mRNA. Translation: AAI20996.1.
BC120994 mRNA. Translation: AAI20995.1.
AY708392 Genomic DNA. Translation: AAT97984.1.
CCDSiCCDS12552.1.
PIRiA46288.
RefSeqiNP_001617.1. NM_001626.5.
UniGeneiHs.631535.

Genome annotation databases

EnsembliENST00000392038; ENSP00000375892; ENSG00000105221.
GeneIDi208.
KEGGihsa:208.
UCSCiuc002one.3. human.

Polymorphism databases

DMDMi1170703.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M77198 mRNA. Translation: AAA36585.1 .
M95936 mRNA. Translation: AAA58364.1 .
AK314619 mRNA. Translation: BAG37185.1 .
AC118344 Genomic DNA. No translation available.
BC032709 mRNA. Translation: AAH32709.1 .
BC120995 mRNA. Translation: AAI20996.1 .
BC120994 mRNA. Translation: AAI20995.1 .
AY708392 Genomic DNA. Translation: AAT97984.1 .
CCDSi CCDS12552.1.
PIRi A46288.
RefSeqi NP_001617.1. NM_001626.5.
UniGenei Hs.631535.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GZK X-ray 2.30 A 146-460 [» ]
1GZN X-ray 2.50 A 146-480 [» ]
1GZO X-ray 2.75 A 146-460 [» ]
1MRV X-ray 2.80 A 143-481 [» ]
1MRY X-ray 2.80 A 143-481 [» ]
1O6K X-ray 1.70 A 146-481 [» ]
1O6L X-ray 1.60 A 146-467 [» ]
1P6S NMR - A 1-111 [» ]
2JDO X-ray 1.80 A 146-467 [» ]
2JDR X-ray 2.30 A 146-467 [» ]
2UW9 X-ray 2.10 A 146-467 [» ]
2X39 X-ray 1.93 A 146-467 [» ]
2XH5 X-ray 2.72 A 146-479 [» ]
3D0E X-ray 2.00 A/B 146-480 [» ]
3E87 X-ray 2.30 A/B 146-480 [» ]
3E88 X-ray 2.50 A/B 146-480 [» ]
3E8D X-ray 2.70 A/B 146-480 [» ]
DisProti DP00304.
ProteinModelPortali P31751.
SMRi P31751. Positions 1-480.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106711. 38 interactions.
DIPi DIP-32583N.
IntActi P31751. 22 interactions.
MINTi MINT-87790.
STRINGi 9606.ENSP00000375892.

Chemistry

BindingDBi P31751.
ChEMBLi CHEMBL2431.
GuidetoPHARMACOLOGYi 1480.

PTM databases

PhosphoSitei P31751.

Polymorphism databases

DMDMi 1170703.

Proteomic databases

MaxQBi P31751.
PaxDbi P31751.
PRIDEi P31751.

Protocols and materials databases

DNASUi 208.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000392038 ; ENSP00000375892 ; ENSG00000105221 .
GeneIDi 208.
KEGGi hsa:208.
UCSCi uc002one.3. human.

Organism-specific databases

CTDi 208.
GeneCardsi GC19M040736.
HGNCi HGNC:392. AKT2.
HPAi CAB004204.
MIMi 125853. phenotype.
164731. gene.
240900. phenotype.
neXtProti NX_P31751.
Orphaneti 79085. Familial partial lipodystrophy due to AKT2 mutations.
293964. Hypoinsulinemic hypoglycemia and body hemihypertrophy.
PharmGKBi PA24685.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118793.
HOGENOMi HOG000233033.
HOVERGENi HBG108317.
InParanoidi P31751.
KOi K04456.
OMAi AGMEHEQ.
OrthoDBi EOG7Q5HCW.
PhylomeDBi P31751.
TreeFami TF102004.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 2681.
Reactomei REACT_115662. Downregulation of ERBB2:ERBB3 signaling.
REACT_12442. AKT phosphorylates targets in the nucleus.
REACT_12447. Negative regulation of the PI3K/AKT network.
REACT_12564. AKT phosphorylates targets in the cytosol.
REACT_13655. AKT-mediated inactivation of FOXO1A.
REACT_1451. PDE3B signalling.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_1695. GPVI-mediated activation cascade.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
REACT_19358. CD28 dependent PI3K/Akt signaling.
REACT_19405. CTLA4 inhibitory signaling.
REACT_200731. deactivation of the beta-catenin transactivating complex.
REACT_6743. Inhibition of TSC complex formation by PKB.
REACT_75829. PIP3 activates AKT signaling.
REACT_790. Activation of PKB.
SignaLinki P31751.

Miscellaneous databases

ChiTaRSi AKT2. human.
EvolutionaryTracei P31751.
GeneWikii AKT2.
GenomeRNAii 208.
NextBioi 836.
PROi P31751.
SOURCEi Search...

Gene expression databases

Bgeei P31751.
CleanExi HS_AKT2.
ExpressionAtlasi P31751. baseline and differential.
Genevestigatori P31751.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a second form of rac protein kinase."
    Jones P.F., Jakubowicz T., Hemmings B.A.
    Cell Regul. 2:1001-1009(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Epithelium.
  2. "AKT2, a putative oncogene encoding a member of a subfamily of protein-serine/threonine kinases, is amplified in human ovarian carcinomas."
    Cheng J.Q., Godwin A.K., Bellacosa A., Taguchi T., Franke T.F., Hamilton T.C., Tsichlis P.N., Testa J.R.
    Proc. Natl. Acad. Sci. U.S.A. 89:9267-9271(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORM 1).
    Tissue: Placenta.
  4. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 1 AND 2).
    Tissue: Lymph.
  6. NIEHS SNPs program
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 237-277.
  7. "Activation of protein kinase B beta and gamma isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: comparison with protein kinase B alpha."
    Walker K.S., Deak M., Paterson A., Hudson K., Cohen P., Alessi D.R.
    Biochem. J. 331:299-308(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, PHOSPHORYLATION AT THR-309 BY PDPK1.
  8. "The protooncogene TCL1 is an Akt kinase coactivator."
    Laine J., Kuenstle G., Obata T., Sha M., Noguchi M.
    Mol. Cell 6:395-407(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MTCP1; TCL1A AND TCL1B.
  9. Cited for: MUTAGENESIS OF THR-309 AND SER-474, PHOSPHORYLATION AT THR-309 AND SER-474.
  10. Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  11. "Akt2 is implicated in skeletal muscle differentiation and specifically binds Prohibitin2/REA."
    Heron-Milhavet L., Mamaeva D., Rochat A., Lamb N.J., Fernandez A.
    J. Cell. Physiol. 214:158-165(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PBH2.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: UBIQUITINATION BY TTC3, PHOSPHORYLATION AT THR-309 AND SER-474, MUTAGENESIS OF THR-309 AND SER-474.
  14. "ClipR-59 interacts with Akt and regulates Akt cellular compartmentalization."
    Ding J., Du K.
    Mol. Cell. Biol. 29:1459-1471(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLIP3, SUBCELLULAR LOCATION.
  15. "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-447; THR-451; SER-474 AND SER-478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. Cited for: UBIQUITINATION, INTERACTION WITH TRAF6.
  17. Cited for: INVOLVEMENT IN CANCER.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: REVIEW ON FUNCTION.
  20. "Akt1 and Akt2: differentiating the aktion."
    Heron-Milhavet L., Khouya N., Fernandez A., Lamb N.J.
    Histol. Histopathol. 26:651-662(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  21. "Ankrd2/ARPP is a novel Akt2 specific substrate and regulates myogenic differentiation upon cellular exposure to H(2)O(2)."
    Cenni V., Bavelloni A., Beretti F., Tagliavini F., Manzoli L., Lattanzi G., Maraldi N.M., Cocco L., Marmiroli S.
    Mol. Biol. Cell 22:2946-2956(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MUSCLE DIFFERENTIATION, INTERACTION WITH ANKRD2.
  22. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation."
    Yang J., Cron P., Thompson V., Good V.M., Hess D., Hemmings B.A., Barford D.
    Mol. Cell 9:1227-1240(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 146-480.
  24. "Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP."
    Yang J., Cron P., Good V.M., Thompson V., Hemmings B.A., Barford D.
    Nat. Struct. Biol. 9:940-944(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 146-467 IN COMPLEX WITH PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER AND MANGANESE, PHOSPHORYLATION AT THR-309.
  25. "Crystal structure of an inactive Akt2 kinase domain."
    Huang X., Begley M., Morgenstern K.A., Gu Y., Rose P., Zhao H., Zhu X.
    Structure 11:21-30(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 143-481, ATP-BINDING, SUBSTRATE-BINDING, DISULFIDE BOND.
  26. "Solution structure and backbone dynamics of the pleckstrin homology domain of the human protein kinase B (PKB/Akt). Interaction with inositol phosphates."
    Auguin D., Barthe P., Auge-Senegas M.T., Stern M.H., Noguchi M., Roumestand C.
    J. Biomol. NMR 28:137-155(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-111.
  27. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 146-467, INHIBITOR-BINDING.
  28. "Identification of 4-(2-(4-amino-1,2,5-oxadiazol-3-yl)-1-ethyl-7-{[(3S)-3-piperidinylmethyl]oxy}-1H-imidazo[4,5-c]pyridin-4-yl)-2-methyl-3-butyn-2-ol (GSK690693), a novel inhibitor of AKT kinase."
    Heerding D.A., Rhodes N., Leber J.D., Clark T.J., Keenan R.M., Lafrance L.V., Li M., Safonov I.G., Takata D.T., Venslavsky J.W., Yamashita D.S., Choudhry A.E., Copeland R.A., Lai Z., Schaber M.D., Tummino P.J., Strum S.L., Wood E.R.
    , Duckett D.R., Eberwein D., Knick V.B., Lansing T.J., McConnell R.T., Zhang S., Minthorn E.A., Concha N.O., Warren G.L., Kumar R.
    J. Med. Chem. 51:5663-5679(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 146-480, ENZYME REGULATION.
  29. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 146-480, ENZYME REGULATION.
  30. Cited for: VARIANT NIDDM HIS-274.
  31. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-188 AND LYS-208.
  32. Cited for: ASSOCIATION OF VARIANT NIDDM HIS-274 WITH TYPICAL METABOLIC DYSLIPIDEMIA.
  33. Cited for: VARIANT HIHGHH LYS-17.

Entry informationi

Entry nameiAKT2_HUMAN
AccessioniPrimary (citable) accession number: P31751
Secondary accession number(s): B2RBD8
, Q05BV0, Q0VAN0, Q0VAN1, Q68GC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 161 of the entry and version 2 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  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 and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3