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NUAK2_RAT
ID   NUAK2_RAT               Reviewed;         630 AA.
AC   Q66HE5;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=NUAK family SNF1-like kinase 2;
DE            EC=2.7.11.1;
DE   AltName: Full=SNF1/AMP kinase-related kinase;
DE            Short=SNARK;
GN   Name=Nuak2 {ECO:0000312|EMBL:AAH81899.1};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ALTERNATIVE SPLICING,
RP   AUTOPHOSPHORYLATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Keratinocyte {ECO:0000269|PubMed:11284715},
RC   Kidney {ECO:0000269|PubMed:11284715}, and
RC   Lung {ECO:0000269|PubMed:11284715};
RX   PubMed=11284715; DOI=10.1042/0264-6021:3550297;
RA   Lefebvre D.L., Bai Y., Shahmolky N., Sharma M., Poon R., Drucker D.J.,
RA   Rosen C.F.;
RT   "Identification and characterization of a novel sucrose-non-fermenting
RT   protein kinase/AMP-activated protein kinase-related protein kinase,
RT   SNARK.";
RL   Biochem. J. 355:297-305(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3] {ECO:0000305}
RP   FUNCTION, ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RX   PubMed=15893879; DOI=10.1016/j.bbagen.2005.03.015;
RA   Lefebvre D.L., Rosen C.F.;
RT   "Regulation of SNARK activity in response to cellular stresses.";
RL   Biochim. Biophys. Acta 1724:71-85(2005).
CC   -!- FUNCTION: Stress-activated kinase involved in tolerance to glucose
CC       starvation. Induces cell-cell detachment by increasing F-actin
CC       conversion to G-actin. Expression is induced by CD95 or TNF-alpha, via
CC       NF-kappa-B. Protects cells from CD95-mediated apoptosis and is required
CC       for the increased motility and invasiveness of CD95-activated tumor
CC       cells. Phosphorylates LATS1 and LATS2. Plays a key role in neural tube
CC       closure during embryonic development through LATS2 phosphorylation and
CC       regulation of the nuclear localization of YAP1 a critical downstream
CC       regulatory target in the Hippo signaling pathway.
CC       {ECO:0000250|UniProtKB:Q9H093}.
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:0000269|PubMed:11284715, ECO:0000269|PubMed:15893879};
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:0000269|PubMed:11284715,
CC         ECO:0000269|PubMed:15893879};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:11284715};
CC   -!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-212 by STK11
CC       in complex with STE20-related adapter-alpha (STRAD alpha) pseudo kinase
CC       and CAB39. {ECO:0000250, ECO:0000269|PubMed:11284715,
CC       ECO:0000269|PubMed:15893879}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=Additional isoforms seem to exist. At least one
CC         kinase-inactive isoform is believed to be expressed.
CC         {ECO:0000269|PubMed:11284715};
CC       Name=1;
CC         IsoId=Q66HE5-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in liver, skin, testis, uterus, ovary,
CC       adrenal gland and brain (at protein level). Expressed in kidney, heart,
CC       skin, spleen, lung, uterus, liver and the exocrine and endocrine
CC       compartments of the human pancreas. A kinase-inactive isoform also
CC       appears to be expressed in the skin, spleen, lung, uterus, liver and
CC       testis. {ECO:0000269|PubMed:11284715, ECO:0000269|PubMed:15893879}.
CC   -!- PTM: Phosphorylated at Thr-212 by STK11/LKB1 in complex with STE20-
CC       related adapter-alpha (STRADA) pseudo kinase and CAB39.
CC       Autophosphorylation is also possible at Thr-212.
CC       {ECO:0000250|UniProtKB:Q9H093}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR   EMBL; BC081899; AAH81899.1; -; mRNA.
DR   RefSeq; NP_001007618.1; NM_001007617.1. [Q66HE5-1]
DR   AlphaFoldDB; Q66HE5; -.
DR   SMR; Q66HE5; -.
DR   STRING; 10116.ENSRNOP00000000039; -.
DR   PhosphoSitePlus; Q66HE5; -.
DR   PaxDb; Q66HE5; -.
DR   Ensembl; ENSRNOT00000000039; ENSRNOP00000000039; ENSRNOG00000000034. [Q66HE5-1]
DR   GeneID; 289419; -.
DR   KEGG; rno:289419; -.
DR   UCSC; RGD:1359167; rat. [Q66HE5-1]
DR   CTD; 81788; -.
DR   RGD; 1359167; Nuak2.
DR   eggNOG; KOG0611; Eukaryota.
DR   GeneTree; ENSGT00940000158422; -.
DR   HOGENOM; CLU_000288_63_42_1; -.
DR   InParanoid; Q66HE5; -.
DR   OMA; NWGYKVP; -.
DR   OrthoDB; 1127668at2759; -.
DR   PRO; PR:Q66HE5; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000000034; Expressed in kidney and 19 other tissues.
DR   Genevisible; Q66HE5; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0035330; P:regulation of hippo signaling; ISS:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Apoptosis; ATP-binding; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..630
FT                   /note="NUAK family SNF1-like kinase 2"
FT                   /id="PRO_0000247759"
FT   DOMAIN          57..307
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          361..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        179
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O60285,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT                   ProRule:PRU10027"
FT   BINDING         63..71
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H093,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         85
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H093,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H093"
FT   MOD_RES         212
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H093"
FT   MOD_RES         529
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H093"
FT   MOD_RES         550
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H093"
FT   MOD_RES         553
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H093"
FT   MOD_RES         579
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BZN4"
SQ   SEQUENCE   630 AA;  69953 MW;  1626427ABCD5F66E CRC64;
     MESVALHRRG NLAPSASALA TESARPLADR LIKSPKPLMK KQAVKRHHHK HNLRHRYEFL
     ETLGKGTYGK VKKARESSGR LVAIKSIRKD KIKDEQDLLH IRREIEIMSS LNHPHIIAIH
     EVFENSSKIV IVMEYASRGD LYDYISERPR LNERDARHFF RQIVSALHYC HQNGIVHRDL
     KLENILLDAS GNIKIADFGL SNLYHKGKFL QTFCGSPLYA SPEIVNGKPY VGPEVDSWSL
     GVLLYILVHG TMPFDGQDHK TLVKQISSGA YREPCKPSDA CGLIRWLLMV NPIRRATLED
     VASHWWVNWG YSTRIGEQEA LREGGHPSGD SGRASMADWL RRSSRPLLEN GAKVCSFFKQ
     HVPGGGSTGP GLERQHSLKK SRKENDMAQT LQNDPAEDTS SRPGKNSLKL PKGILKKKAS
     PSSGEVQEGP QELRPVSNTP GQPVPAIPLL PRKGILKKSR QRESGYYSSP EPSESGELLD
     AGDVFVSGDP MEQKSPQASG RLHRKGILKL NGKFSRTALE GTAPSTFGSL DQLASPHPTA
     RASRPSGAVS EDSILSSESF DQLDLPERLP ETPLRGCVSV DNLRRLEQPP SEGLKRWWQE
     SLGDSCFSLT DCQEVTAAYR QALGICSKLS
 
 
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