HUNK_PANTR
ID HUNK_PANTR Reviewed; 714 AA.
AC Q68UT7;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Hormonally up-regulated neu tumor-associated kinase;
DE EC=2.7.11.1;
GN Name=HUNK;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164055; DOI=10.1038/nature02564;
RA Watanabe H., Fujiyama A., Hattori M., Taylor T.D., Toyoda A., Kuroki Y.,
RA Noguchi H., BenKahla A., Lehrach H., Sudbrak R., Kube M., Taenzer S.,
RA Galgoczy P., Platzer M., Scharfe M., Nordsiek G., Bloecker H., Hellmann I.,
RA Khaitovich P., Paeaebo S., Reinhardt R., Zheng H.-J., Zhang X.-L.,
RA Zhu G.-F., Wang B.-F., Fu G., Ren S.-X., Zhao G.-P., Chen Z., Lee Y.-S.,
RA Cheong J.-E., Choi S.-H., Wu K.-M., Liu T.-T., Hsiao K.-J., Tsai S.-F.,
RA Kim C.-G., Oota S., Kitano T., Kohara Y., Saitou N., Park H.-S.,
RA Wang S.-Y., Yaspo M.-L., Sakaki Y.;
RT "DNA sequence and comparative analysis of chimpanzee chromosome 22.";
RL Nature 429:382-388(2004).
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; AL954201; CAH18570.1; -; Genomic_DNA.
DR RefSeq; NP_001065290.1; NM_001071822.1.
DR AlphaFoldDB; Q68UT7; -.
DR SMR; Q68UT7; -.
DR STRING; 9598.ENSPTRP00000023839; -.
DR PaxDb; Q68UT7; -.
DR Ensembl; ENSPTRT00000025828; ENSPTRP00000023839; ENSPTRG00000013849.
DR GeneID; 746122; -.
DR KEGG; ptr:746122; -.
DR CTD; 30811; -.
DR VGNC; VGNC:1149; HUNK.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000161070; -.
DR HOGENOM; CLU_017161_0_0_1; -.
DR InParanoid; Q68UT7; -.
DR OMA; CLISQIQ; -.
DR OrthoDB; 1127668at2759; -.
DR TreeFam; TF352373; -.
DR Proteomes; UP000002277; Chromosome 21.
DR Bgee; ENSPTRG00000013849; Expressed in Brodmann (1909) area 10 and 15 other tissues.
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; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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 3: Inferred from homology;
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_0000086006"
FT DOMAIN 62..320
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..648
FT /note="Pro 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"
SQ SEQUENCE 714 AA; 79683 MW; 5062E91669D1B66D CRC64;
MPAAAGDGLL GEPAAPGGGG GAEDAARPAA ACEGSFLPAW VSGVPRERLR DFQHHKRVGN
YLIGSRKLGE GSFAKVREGL HVLTGEKVAI KVIDKKRAKK DTYVTKNLRR EGQIQQMIRH
PNITQLLDIL ETENSYYLVM ELCPGGNLMH KIYEKKRLEE SEARRYIRQL ISAVEHLHRA
GVVHRDLKIE NLLLDEDNNI KLIDFGLSNC AGILGYSDPF STQCGSPAYA APELLARKKY
GPKIDVWSIG VNMYAMLTGT LPFTVEPFSL RALYQKMVDK EMNPLPTQLS TGAISFLRSL
LEPDPVKRPN IQQALANRWL NENYTGKVPC NVTYPNRISL EDLSPSVVLH MTEKLGYKNS
DVINTVLSNR ACHILAIYFL LNKKLERYLS GKSDIQDSLC YKTRLYQIEK YRAPKESYEA
SLDTWTRDLE FHAVQDKKPK EQEKRGDFLH RPFSKKLDKN LPSHKQPSGS LMTQIQNTKA
LLKDRKASKS SFPDKDSFGC RNIFRKTSDS NCVASSSMEF IPVPPPRTPR IVKKPEPHQP
GPGSTGIPHK EDPLMLDMVR SFESVDRDDH IEVLSPSHHY RILNSPVSLA RRNSSERTLS
PGLPSGSMSP LHTPLHPTLV SFAHEDKNSP PKEEGLCSPP PVPSNGPMQP LGSPNCVKSR
GRFPMMGIGQ MLRKRHQSLQ PSADRPLEAS LPPLQPLAPV NLAFDMADGV KTQC
