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HUNK_MOUSE
ID   HUNK_MOUSE              Reviewed;         714 AA.
AC   O88866;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Hormonally up-regulated neu tumor-associated kinase;
DE            EC=2.7.11.1;
DE   AltName: Full=Serine/threonine-protein kinase MAK-V;
GN   Name=Hunk; Synonyms=Makv;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=A/Sn; TISSUE=Mammary gland;
RX   PubMed=9273061;
RA   Korobko I.V., Kabishev A.A., Kiselev S.L.;
RT   "Identification of the new protein kinase specifically transcribed in mouse
RT   tumors with high metastatic potential.";
RL   Dokl. Akad. Nauk 354:554-556(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=FVB/NJ; TISSUE=Mammary gland;
RX   PubMed=10662544; DOI=10.1006/geno.1999.6078;
RA   Gardner H.P., Wertheim G.B.W., Ha S.I., Copeland N.G., Gilbert D.J.,
RA   Jenkins N.A., Marquis S.T., Chodosh L.A.;
RT   "Cloning and characterization of Hunk, a novel mammalian SNF1-related
RT   protein kinase.";
RL   Genomics 63:46-59(2000).
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   -!- 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;
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; AF055919; AAC61489.1; -; mRNA.
DR   EMBL; AF167987; AAF35282.1; -; mRNA.
DR   CCDS; CCDS28315.1; -.
DR   RefSeq; NP_056570.1; NM_015755.2.
DR   AlphaFoldDB; O88866; -.
DR   SMR; O88866; -.
DR   BioGRID; 205017; 1.
DR   STRING; 10090.ENSMUSP00000068007; -.
DR   iPTMnet; O88866; -.
DR   PhosphoSitePlus; O88866; -.
DR   MaxQB; O88866; -.
DR   PaxDb; O88866; -.
DR   PRIDE; O88866; -.
DR   ProteomicsDB; 273203; -.
DR   Antibodypedia; 6820; 350 antibodies from 31 providers.
DR   DNASU; 26559; -.
DR   Ensembl; ENSMUST00000065856; ENSMUSP00000068007; ENSMUSG00000053414.
DR   GeneID; 26559; -.
DR   KEGG; mmu:26559; -.
DR   UCSC; uc007zwi.1; mouse.
DR   CTD; 30811; -.
DR   MGI; MGI:1347352; Hunk.
DR   VEuPathDB; HostDB:ENSMUSG00000053414; -.
DR   eggNOG; KOG0583; Eukaryota.
DR   GeneTree; ENSGT00940000161070; -.
DR   HOGENOM; CLU_017161_0_0_1; -.
DR   InParanoid; O88866; -.
DR   OMA; CLISQIQ; -.
DR   OrthoDB; 1127668at2759; -.
DR   PhylomeDB; O88866; -.
DR   TreeFam; TF352373; -.
DR   BRENDA; 2.7.11.1; 3474.
DR   BioGRID-ORCS; 26559; 3 hits in 74 CRISPR screens.
DR   ChiTaRS; Hunk; mouse.
DR   PRO; PR:O88866; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; O88866; protein.
DR   Bgee; ENSMUSG00000053414; Expressed in epithelium of cochlear duct and 222 other tissues.
DR   ExpressionAtlas; O88866; baseline and differential.
DR   Genevisible; O88866; MM.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR   CDD; cd14070; STKc_HUNK; 1.
DR   InterPro; IPR034671; Hunk.
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   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..714
FT                   /note="Hormonally up-regulated neu tumor-associated kinase"
FT                   /id="PRO_0000086005"
FT   DOMAIN          62..320
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          624..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        186
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         68..76
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        697
FT                   /note="T -> I (in Ref. 2; AAF35282)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   714 AA;  79603 MW;  D35A53E7A8D9BD1F CRC64;
     MPAAAGDGLL GEPAAPGGDG GAEDTTRPAA ACEGSFLPAW VSGVSRERLR DFQHHKRVGN
     YLIGSRKLGE GSFAKVREGL HVLTGEKVAI KVIDKKRAKK DTYVTKNLRR EGQIQQMIRH
     PNITQLLDIL ETENSYYLVM ELCPGGNLMH KIYEKKRLDE AEARRYIRQL ISAVEHLHRA
     GVVHRDLKIE NLLLDEDNNI KLIDFGLSNC AGILGYSDPF STQCGSPAYA APELLARKKY
     GPKIDVWSIG VNMYAMLTGT LPFTVEPFSL RALYQKMVDK AMNPLPTQLS TGAVNFLRSL
     LEPDPVKRPN IQQALANRWL NENYTGKVPC NVTYPNRISL EDLSPSVVLH MTEKLGYKNS
     DVINTVLSNR ACHILAIYFL LNKKLERYLS GKSDIQDSIC YKTQLYQIEK CRATKEPYEA
     SLDTWTRDFE FHAVQDKKPK EQEKRGDFLH RPFSKKLDKN LPSHKQPSPS LITQLQSTKA
     LLKDRKASKS GFPDKDSFVC RNLFRKTSDS NCVASSSMEF IPVPPPRTPR IVKKLEPHQP
     GPGSASILPK EEPLLLDMVR SFESVDREDH IELLSPSHHY RILSSPVSLA RRNSSERTLS
     QGLLSGSTSP LQTPLHSTLV SFAHEEKNSP PKEEGVCSPP PVPSNGLLQP LGSPNCVKSR
     GRFPMMGIGQ MLRKRHQSLQ PSSERSLDAS MSPLQPTAPS SLSFDMADGV KGQC
 
 
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