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AKT2B_XENLA
ID   AKT2B_XENLA             Reviewed;         485 AA.
AC   Q6IP76;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=RAC-beta serine/threonine-protein kinase B;
DE            EC=2.7.11.1;
DE   AltName: Full=Protein kinase Akt-2-B;
DE   AltName: Full=Protein kinase B, beta-B;
DE            Short=PKB beta-B;
DE   AltName: Full=RAC-PK-beta-B;
GN   Name=akt2-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000312|EMBL:AAH72041.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen {ECO:0000312|EMBL:AAH72041.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Akt2-b is one of several closely related serine/threonine-
CC       protein kinases known as the AKT kinase, and which regulate many
CC       processes including metabolism, proliferation, cell survival, growth
CC       and angiogenesis. This is mediated through serine and/or threonine
CC       phosphorylation of a range of downstream substrates. Over 100 substrate
CC       candidates have been reported so far, but for most of them, no isoform
CC       specificity has been reported (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000250|UniProtKB:Q60823};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q60823};
CC   -!- ACTIVITY REGULATION: Two specific sites, one in the kinase domain (Thr-
CC       313) and the other in the C-terminal regulatory region (Ser-478), need
CC       to be phosphorylated for its full activation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. RAC subfamily. {ECO:0000305}.
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DR   EMBL; BC072041; AAH72041.1; -; mRNA.
DR   RefSeq; NP_001085101.1; NM_001091632.1.
DR   AlphaFoldDB; Q6IP76; -.
DR   SMR; Q6IP76; -.
DR   DNASU; 432172; -.
DR   GeneID; 432172; -.
DR   KEGG; xla:432172; -.
DR   CTD; 432172; -.
DR   Xenbase; XB-GENE-17345542; akt2.S.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 432172; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR   GO; GO:0031340; P:positive regulation of vesicle fusion; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   CDD; cd01241; PH_PKB; 1.
DR   CDD; cd05595; STKc_PKB_beta; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR034677; Akt2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR039026; PH_PKB.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Glycoprotein; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..485
FT                   /note="RAC-beta serine/threonine-protein kinase B"
FT                   /id="PRO_0000223509"
FT   DOMAIN          5..109
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          156..413
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          414..485
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   REGION          454..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        279
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         162..170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         313
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         478
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        132
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        135
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        310
FT                   /note="O-linked (GlcNAc) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        317
FT                   /note="O-linked (GlcNAc) threonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   485 AA;  56024 MW;  27D584109098CC56 CRC64;
     MNEVMVIKEG WLQKRGEYIK TWRPRYFLLK SDGSFIGYKE KPDSTEHSLL PPLNNFSVAE
     CQLMKTERPR PNTFVIRCLQ WTTVIERTFH VDTPEEREEW IIAIQTVANG LKNQVPEDEE
     EEAMEVKYGS PSDVSSAEQM DVAMSKGRPK VTMNDFDYLK LLGKGTFGKV ILVREKATGL
     YYAMKILRKE VIIAKDEVAH TLTESRVLQN TKHPFLTGLK YAFQTSDRLC FVMEYANGGE
     LFFHLSRERV FTEDRARFYG AEIVSALEYL HSRNVVYRDI KLENLMLDKD GHVKITDFGL
     CKEGITDGAT MRTFCGTPEY LAPEVLEDND YGRAVDWWGL GVVMYEMMCG RLPFYNQDHE
     RLFELILMEE TRFPRTLSPE AKSLLAGLLK KDPKQRLGGG PDDAQEVMSH GFFASINWQD
     VTERKLSPPF KPQVTSEIDT RYFDDEFTAQ SITLTPPDRY DNLDALESEQ RPHFPQFSYS
     SSIRE
 
 
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