AKT1
entrez
207
canonical
uniprot
P31749
canonical
ensembl
ENSG00000142208
resolver
ensp
ENSP00000270202
resolver
ensp
ENSP00000384293
resolver
ensp
ENSP00000385326
resolver
ensp
ENSP00000451166
resolver
ensp
ENSP00000451828
resolver
ensp
ENSP00000497822
resolver
ensp
ENSP00000525655
resolver
ensp
ENSP00000609436
resolver
ensp
ENSP00000609443
resolver
ensp
ENSP00000629710
resolver
ensp
ENSP00000629722
resolver
ensp
ENSP00000629735
resolver
ensp
ENSP00000629736
resolver
genesymbol
AKT1
resolver
genesymbol_syn
PKB
resolver
genesymbol_syn
RAC
resolver
hgnc
HGNC:391
resolver
uniprot
B0LPE5
resolver
uniprot
B2RAM5
resolver
uniprot
B3KVH4
resolver
uniprot
B7Z5R1
resolver
uniprot
Q9BWB6
resolver
uniprot_entry
AKT1_HUMAN
resolver
uniprot_entry
B0LPE5_HUMAN
resolver
uniprot_entry
B3KVH4_HUMAN
resolver
uniprot_sec
B2RAM5
resolver
uniprot_sec
B7Z5R1
resolver
uniprot_sec
Q9BWB6
resolver
activity_regulation
ACTIVITY REGULATION: Three specific sites, one in the kinase domain (Thr-308) and the two other ones in the C-terminal regulatory region (Ser-473 and Tyr-474), need to be phosphorylated for its full activation (PubMed:15262962, PubMed:20481595, PubMed:21392984, PubMed:9512493, PubMed:9736715). Inhibited by pyrrolopyrimidine inhibitors like aniline triazole and spiroindoline (PubMed:18456494, PubMed:20810279). {ECO:0000269|PubMed:15262962, ECO:0000269|PubMed:18456494, ECO:0000269|PubMed:20481595, ECO:0000269|PubMed:20810279, ECO:0000269|PubMed:21392984, ECO:0000269|PubMed:9512493, ECO:0000269|PubMed:9736715, ECO:0000305|PubMed:20810279}.
uniprot
proteins
amino_acid_sequence
MSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA
uniprot
proteins
disease_involvement
DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. {ECO:0000269|PubMed:17611497}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Note=Genetic variations in AKT1 may play a role in susceptibility to ovarian cancer.; DISEASE: Proteus syndrome (PROTEUSS) [MIM:176920]: A highly variable, severe disorder of asymmetric and disproportionate overgrowth of body parts, connective tissue nevi, epidermal nevi, dysregulated adipose tissue, and vascular malformations. Many features of Proteus syndrome overlap with other overgrowth syndromes. {ECO:0000269|PubMed:18954143, ECO:0000269|PubMed:21793738}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cowden syndrome 6 (CWS6) [MIM:615109]: A form of Cowden syndrome, a hamartomatous polyposis syndrome with age-related penetrance. Cowden syndrome is characterized by hamartomatous lesions affecting derivatives of ectodermal, mesodermal and endodermal layers, macrocephaly, facial trichilemmomas (benign tumors of the hair follicle infundibulum), acral keratoses, papillomatous papules, and elevated risk for development of several types of malignancy, particularly breast carcinoma in women and thyroid carcinoma in both men and women. Colon cancer and renal cell carcinoma have also been reported. Hamartomas can be found in virtually every organ, but most commonly in the skin, gastrointestinal tract, breast and thyroid. {ECO:0000269|PubMed:12176338, ECO:0000269|PubMed:23246288}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: AKT1 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 (PubMed:11882383, PubMed:15526160, PubMed:15861136, PubMed:21432781, PubMed:21620960, PubMed:31204173). This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates (PubMed:11882383, PubMed:15526160, PubMed:21432781, PubMed:21620960, PubMed:29343641, PubMed:31204173). Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported (PubMed:11882383, PubMed:15526160, PubMed:21432781, PubMed:21620960). AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface (By similarity). Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling (By similarity). Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport (PubMed:11994271). AKT also regulates 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 (By similarity). Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven (By similarity). AKT also regulates cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase) (PubMed:11154276). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis (PubMed:11154276). AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating the mTORC1 signaling pathway, and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1 (PubMed:12150915, PubMed:12172553). Also regulates the mTORC1 signaling pathway by catalyzing phosphorylation of CASTOR1 and DEPDC5 (PubMed:31548394, PubMed:33594058). 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 (By similarity). Part of a positive feedback loop of mTORC2 signaling by mediating phosphorylation of MAPKAP1/SIN1, promoting mTORC2 activation (By similarity). 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 (PubMed:10358075). In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319' (PubMed:10358075). FOXO3 and FOXO4 are phosphorylated on equivalent sites (PubMed:10358075). 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) (PubMed:9829964). 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 (PubMed:9829964). AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis (By similarity). Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis (By similarity). Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity (By similarity). The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth (By similarity). Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) 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 1 (IGF1) (PubMed:12176338, PubMed:12964941). AKT mediates the antiapoptotic effects of IGF1 (By similarity). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly (PubMed:19934221). May be involved in the regulation of the placental development (By similarity). Phosphorylates STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its: kinase activity, nuclear translocation, autophosphorylation and ability to phosphorylate FOXO3 (PubMed:17726016). Phosphorylates STK3/MST2 at 'Thr-117' and 'Thr-384' leading to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation (PubMed:20086174). Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation (PubMed:19592491). Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity (PubMed:10576742). Phosphorylation of BAD stimulates its pro-apoptotic activity (PubMed:10926925). Phosphorylates KAT6A at 'Thr-369' and this phosphorylation inhibits the interaction of KAT6A with PML and negatively regulates its acetylation activity towards p53/TP53 (PubMed:23431171). Phosphorylates palladin (PALLD), modulating cytoskeletal organization and cell motility (PubMed:20471940). Phosphorylates prohibitin (PHB), playing an important role in cell metabolism and proliferation (PubMed:18507042). Phosphorylates CDKN1A, for which phosphorylation at 'Thr-145' induces its release from CDK2 and cytoplasmic relocalization (PubMed:16982699). These recent findings indicate that the AKT1 isoform has a more specific role in cell motility and proliferation (PubMed:16139227). Phosphorylates CLK2 thereby controlling cell survival to ionizing radiation (PubMed:20682768). Phosphorylates PCK1 at 'Ser-90', reducing the binding affinity of PCK1 to oxaloacetate and changing PCK1 into an atypical protein kinase activity using GTP as donor (PubMed:32322062). Also acts as an activator of TMEM175 potassium channel activity in response to growth factors: forms the lysoK(GF) complex together with TMEM175 and acts by promoting TMEM175 channel activation, independently of its protein kinase activity (PubMed:32228865). Acts as a regulator of mitochondrial calcium uptake by mediating phosphorylation of MICU1 in the mitochondrial intermembrane space, impairing MICU1 maturation (PubMed:30504268). Acts as an inhibitor of tRNA methylation by mediating phosphorylation of the N-terminus of METTL1, thereby inhibiting METTL1 methyltransferase activity (PubMed:15861136). In response to LPAR1 receptor pathway activation, phosphorylates Rabin8/RAB3IP which alters its activity and phosphorylates WDR44 which induces WDR44 binding to Rab11, thereby switching Rab11 vesicular function from preciliary trafficking to endocytic recycling (PubMed:31204173). {ECO:0000250|UniProtKB:P31750, ECO:0000250|UniProtKB:P47196, ECO:0000269|PubMed:10358075, ECO:0000269|PubMed:10576742, ECO:0000269|PubMed:10926925, ECO:0000269|PubMed:11154276, ECO:0000269|PubMed:11994271, ECO:0000269|PubMed:12150915, ECO:0000269|PubMed:12172553, ECO:0000269|PubMed:12176338, ECO:0000269|PubMed:12964941, ECO:0000269|PubMed:15861136, ECO:0000269|PubMed:16139227, ECO:0000269|PubMed:16982699, ECO:0000269|PubMed:17726016, ECO:0000269|PubMed:18507042, ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:19934221, ECO:0000269|PubMed:20086174, ECO:0000269|PubMed:20471940, ECO:0000269|PubMed:20682768, ECO:0000269|PubMed:23431171, ECO:0000269|PubMed:30504268, ECO:0000269|PubMed:31204173, ECO:0000269|PubMed:31548394, ECO:0000269|PubMed:32228865, ECO:0000269|PubMed:32322062, ECO:0000269|PubMed:33594058, ECO:0000269|PubMed:9829964, ECO:0000303|PubMed:11882383, ECO:0000303|PubMed:15526160, ECO:0000303|PubMed:21432781, ECO:0000303|PubMed:21620960}.
uniprot
proteins
mass_dalton
55686
uniprot
proteins
mutagenesis
MUTAGEN 8; /note="K->R: Substantial reduction of ubiquitination, phosphorylation at T-308 and S-473, AKT activation as well as IGF1-induced membrane recruitment. Decrease in ubiquitination and phosphorylation at T-308 as well as impaired association with the membrane; when associated with K-17."; /evidence="ECO:0000269|PubMed:19713527"; MUTAGEN 14; /note="K->A: Impairs interaction with PtdIns(3,4,5)P3 and PtdIns(3,4)P2."; /evidence="ECO:0000269|PubMed:12176338, ECO:0000269|PubMed:19713527, ECO:0000269|PubMed:21775285"; MUTAGEN 14; /note="K->Q: Substantial reduction of phosphorylation at T-308 and S-473, loss of AKT activation, and loss of binding to PIP3 as well as IGF1-induced membrane recruitment."; /evidence="ECO:0000269|PubMed:12176338, ECO:0000269|PubMed:19713527, ECO:0000269|PubMed:21775285"; MUTAGEN 14; /note="K->R: Substantial reduction of ubiquitination, phosphorylation at T-308 and S-473, AKT activation, loss of binding to PIP3 as well as IGF1-induced membrane recruitment."; /evidence="ECO:0000269|PubMed:12176338, ECO:0000269|PubMed:19713527, ECO:0000269|PubMed:21775285"; MUTAGEN 17; /note="E->K: Loss of membrane localization; when associated with Q-20."; /evidence="ECO:0000269|PubMed:21775285"; MUTAGEN 20; /note="K->Q: Substantial reduction of phosphorylation at T-308 and S-473, reduced AKT activation, and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization; when associated with K-17."; /evidence="ECO:0000269|PubMed:21775285"; MUTAGEN 20; /note="K->R: Slight increase of phosphorylation at T-308 and S-473."; /evidence="ECO:0000269|PubMed:21775285"; MUTAGEN 25; /note="R->A: Impairs interaction with PtdIns(3,4,5)P3 and PtdIns(3,4)P2."; /evidence="ECO:0000269|PubMed:12176338"; MUTAGEN 76..78; /note="RCL->ACA: Abolished binding to cyclin-A, preventing phosphorylation by CDK2."; /evidence="ECO:0000269|PubMed:24670654"; MUTAGEN 86; /note="R->A: Impairs interaction with PtdIns(3,4,5)P3 and PtdIns(3,4)P2."; /evidence="ECO:0000269|PubMed:12176338"; MUTAGEN 176; /note="Y->F: Significant loss of interaction with TNK2. Loss of membrane localization. Significant reduction in phosphorylation on Ser-473."; /evidence="ECO:0000269|PubMed:20333297"; MUTAGEN 179; /note="K->M: Abolished serine/threonine-protein kinase activity."; /evidence="ECO:0000269|PubMed:12172553, ECO:0000269|PubMed:33594058"; MUTAGEN 273..275; /note="RDL->ADA: Abolished binding to cyclin-A, preventing phosphorylation by CDK2."; /evidence="ECO:0000269|PubMed:24670654"; MUTAGEN 305; /note="T->A: Reduces O-GlcNAc levels; Reduces O-GlcNAc levels even more; when associated with A-312."; /evidence="ECO:0000269|PubMed:22629392"; MUTAGEN 305; /note="T->Y: Abolishes phosphorylation at Thr-308."; /evidence="ECO:0000269|PubMed:22629392"; MUTAGEN 308; /note="T->D: 5-fold activation and 18-fold activation; when associated with D-473."; /evidence="ECO:0000269|PubMed:12244301, ECO:0000269|PubMed:8978681"; MUTAGEN 312; /note="T->A: Reduces O-GlcNAc levels; Reduces O-GlcNAc levels even more; when associated with A-305."; /evidence="ECO:0000269|PubMed:22629392"; MUTAGEN 312; /note="T->Y: Abolishes phosphorylation at Thr-308."; /evidence="ECO:0000269|PubMed:22629392"; MUTAGEN 473; /note="S->D: 7-fold activation and 25-fold activation; when associated with D-308."; /evidence="ECO:0000269|PubMed:12244301, ECO:0000269|PubMed:8978681"; MUTAGEN 474; /note="Y->F: 55% inhibition of activation."; /evidence="ECO:0000269|PubMed:12149249
uniprot
proteins
post_translational_modification
PTM: O-GlcNAcylation at Thr-305 and Thr-312 inhibits activating phosphorylation at Thr-308 via disrupting the interaction between AKT1 and PDPK1. O-GlcNAcylation at Ser-473 also probably interferes with phosphorylation at this site. {ECO:0000269|PubMed:14761976, ECO:0000269|PubMed:15047712, ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:16266983, ECO:0000269|PubMed:17013611, ECO:0000269|PubMed:18456494, ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:20481595, ECO:0000269|PubMed:20978158, ECO:0000269|PubMed:21464307, ECO:0000269|PubMed:23799035, ECO:0000269|PubMed:8978681, ECO:0000269|PubMed:9512493, ECO:0000269|PubMed:9736715}.; PTM: Phosphorylation on Thr-308, Ser-473 and Tyr-474 is required for full activity (PubMed:12149249, PubMed:15047712, PubMed:15262962, PubMed:16266983, PubMed:18456494, PubMed:20481595, PubMed:20978158, PubMed:8978681, PubMed:9512493, PubMed:9736715). Phosphorylation of the activation loop at Thr-308 by PDPK1/PDK1 is a prerequisite for full activation (PubMed:9512493). Phosphorylation by mTORC2 in response to growth factors plays a key role in AKT1 activation: mTORC2 phosphorylates different sites depending on the context, such as Thr-450, Ser-473, Ser-477 or Thr-479, thereby facilitating subsequent phosphorylation of the activation loop by PDPK1/PDK1 (PubMed:15718470, PubMed:24670654). Phosphorylation at Ser-473 by mTORC2 promotes ubiquitination and degradation by the proteasome (By similarity). Also phosphorylated at Ser-477 and Thr-479 by CDK2, facilitating subsequent phosphorylation of the activation loop by PDPK1/PDK1 (PubMed:24670654). Activated TNK2 phosphorylates it on Tyr-176 resulting in its binding to the anionic plasma membrane phospholipid PA (PubMed:20333297). This phosphorylated form localizes to the cell membrane, where it is targeted by PDPK1 and PDPK2 for further phosphorylations on Thr-308 and Ser-473 leading to its activation (PubMed:20333297). Phosphorylated at Thr-308 and Ser-473 by IKBKE and TBK1 (PubMed:21464307). Ser-473 phosphorylation is enhanced by interaction with AGAP2 isoform 2 (PIKE-A) (PubMed:14761976). Ser-473 phosphorylation is enhanced in focal cortical dysplasias with Taylor-type balloon cells (PubMed:17013611). Ser-473 phosphorylation is enhanced by signaling through activated FLT3 (PubMed:16266983). Ser-473 is dephosphorylated by PHLPP (PubMed:28147277). Dephosphorylated at Thr-308 and Ser-473 by PP2A phosphatase (PubMed:21329884). The phosphorylated form of PPP2R5B is required for bridging AKT1 with PP2A phosphatase (PubMed:21329884). Ser-473 is dephosphorylated by CPPED1, leading to termination of signaling (PubMed:23799035). AIM2 acts as an inhibitor of AKT1 by inhibiting phosphorylation Ser-473: AIM2 acts both by inhibiting the activity of PRKDC/DNA-PK kinase and promoting dephosphorylation by PP2A phosphatase (By similarity). {ECO:0000250|UniProtKB:P31750, ECO:0000269|PubMed:12149249, ECO:0000269|PubMed:14761976, ECO:0000269|PubMed:15047712, ECO:0000269|PubMed:15262962, ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:16266983, ECO:0000269|PubMed:17013611, ECO:0000269|PubMed:18456494, ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:20481595, ECO:0000269|PubMed:20978158, ECO:0000269|PubMed:21329884, ECO:0000269|PubMed:21464307, ECO:0000269|PubMed:23799035, ECO:0000269|PubMed:24670654, ECO:0000269|PubMed:28147277, ECO:0000269|PubMed:8978681, ECO:0000269|PubMed:9512493, ECO:0000269|PubMed:9736715}.; PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination. TRAF6-induced 'Lys-63'-linked AKT1 ubiquitination is critical for phosphorylation and activation (PubMed:19713527). When ubiquitinated, it translocates to the plasma membrane, where it becomes phosphorylated (PubMed:20059950). When fully phosphorylated and translocated into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its degradation by the proteasome (PubMed:20059950). Also ubiquitinated by TRIM13 leading to its proteasomal degradation (PubMed:21333377). Phosphorylated, undergoes 'Lys-48'-linked polyubiquitination preferentially at Lys-284 catalyzed by MUL1, leading to its proteasomal degradation (PubMed:22410793). Ubiquitinated via 'Lys-48'-linked polyubiquitination by ZNRF1, leading to its degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:P31750, ECO:0000269|PubMed:19713527, ECO:0000269|PubMed:20059950, ECO:0000269|PubMed:21333377, ECO:0000269|PubMed:22410793}.; PTM: Acetylated on Lys-14 and Lys-20 by the histone acetyltransferases EP300 and KAT2B. Acetylation results in reduced phosphorylation and inhibition of activity. Deacetylated at Lys-14 and Lys-20 by SIRT1. SIRT1-mediated deacetylation relieves the inhibition. {ECO:0000269|PubMed:21775285}.; PTM: Cleavage by caspase-3/CASP3 (By similarity). Cleaved at the caspase-3 consensus site Asp-462 during apoptosis, resulting in down-regulation of the AKT signaling pathway and decreased cell survival (PubMed:23152800). {ECO:0000250|UniProtKB:P31750, ECO:0000269|PubMed:23152800}.
uniprot
proteins
protein_family
AGC Ser/Thr protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
RAC subfamily
uniprot
proteins
pubmed
10358075
uniprot
proteins
pubmed
10576742
uniprot
proteins
pubmed
10716693
uniprot
proteins
pubmed
10926925
uniprot
proteins
pubmed
10983986
uniprot
proteins
pubmed
11154276
uniprot
proteins
pubmed
11508278
uniprot
proteins
pubmed
11598301
uniprot
proteins
pubmed
11839817
uniprot
proteins
pubmed
11882383
uniprot
proteins
pubmed
11994271
uniprot
proteins
pubmed
12042314
uniprot
proteins
pubmed
12149249
uniprot
proteins
pubmed
12150915
uniprot
proteins
pubmed
12172553
uniprot
proteins
pubmed
12176338
uniprot
proteins
pubmed
12244301
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
12878163
uniprot
proteins
pubmed
12964941
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14749367
uniprot
proteins
pubmed
14761976
uniprot
proteins
pubmed
15047712
uniprot
proteins
pubmed
15118108
uniprot
proteins
pubmed
15262962
uniprot
proteins
pubmed
1533586
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15526160
uniprot
proteins
pubmed
15718470
uniprot
proteins
pubmed
15861136
uniprot
proteins
pubmed
16139227
uniprot
proteins
pubmed
16266983
uniprot
proteins
pubmed
16417524
uniprot
proteins
pubmed
16540465
uniprot
proteins
pubmed
16792529
uniprot
proteins
pubmed
16982699
uniprot
proteins
pubmed
17013611
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
1718748
uniprot
proteins
pubmed
17611497
uniprot
proteins
pubmed
17726016
uniprot
proteins
pubmed
17932490
uniprot
proteins
pubmed
18456494
uniprot
proteins
pubmed
18507042
uniprot
proteins
pubmed
1851997
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18954143
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19592491
uniprot
proteins
pubmed
19713527
uniprot
proteins
pubmed
19934221
uniprot
proteins
pubmed
19940129
uniprot
proteins
pubmed
20059950
uniprot
proteins
pubmed
20086174
uniprot
proteins
pubmed
20231902
uniprot
proteins
pubmed
20333297
uniprot
proteins
pubmed
20471940
uniprot
proteins
pubmed
20481595
uniprot
proteins
pubmed
20682768
uniprot
proteins
pubmed
20810279
uniprot
proteins
pubmed
20886116
uniprot
proteins
pubmed
20978158
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21329884
uniprot
proteins
pubmed
21333377
uniprot
proteins
pubmed
21392984
uniprot
proteins
pubmed
21432781
uniprot
proteins
pubmed
21464307
uniprot
proteins
pubmed
21620960
uniprot
proteins
pubmed
21775285
uniprot
proteins
pubmed
21793738
uniprot
proteins
pubmed
22410793
uniprot
proteins
pubmed
22629392
uniprot
proteins
pubmed
23152800
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23246288
uniprot
proteins
pubmed
23251525
uniprot
proteins
pubmed
23300339
uniprot
proteins
pubmed
23431171
uniprot
proteins
pubmed
23676467
uniprot
proteins
pubmed
23799035
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24670654
uniprot
proteins
pubmed
24784001
uniprot
proteins
pubmed
26440888
uniprot
proteins
pubmed
27825096
uniprot
proteins
pubmed
28147277
uniprot
proteins
pubmed
29343641
uniprot
proteins
pubmed
30504268
uniprot
proteins
pubmed
31204173
uniprot
proteins
pubmed
31548394
uniprot
proteins
pubmed
32228865
uniprot
proteins
pubmed
32322062
uniprot
proteins
pubmed
33594058
uniprot
proteins
pubmed
37490513
uniprot
proteins
pubmed
40285646
uniprot
proteins
pubmed
8978681
uniprot
proteins
pubmed
9512493
uniprot
proteins
pubmed
9736715
uniprot
proteins
pubmed
9829964
uniprot
proteins
sequence_length
480
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P31750}. Nucleus {ECO:0000269|PubMed:20333297}. Cell membrane {ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:40285646}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P31750}. Note=Nucleus after activation by integrin-linked protein kinase 1 (ILK1). Nuclear translocation is enhanced by interaction with TCL1A. Phosphorylation on Tyr-176 by TNK2 results in its localization to the cell membrane where it is targeted for further phosphorylations on Thr-308 and Ser-473 leading to its activation and the activated form translocates to the nucleus. Colocalizes with WDFY2 in intracellular vesicles (PubMed:16792529). Also localizes to mitochondrial intermembrane space in response to rapamycin treatment (By similarity). {ECO:0000250|UniProtKB:P31750, ECO:0000269|PubMed:16792529}.
uniprot
proteins