HUNK_HUMAN
ID HUNK_HUMAN Reviewed; 714 AA.
AC P57058;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Hormonally up-regulated neu tumor-associated kinase;
DE EC=2.7.11.1;
DE AltName: Full=B19;
DE AltName: Full=Serine/threonine-protein kinase MAK-V;
GN Name=HUNK; Synonyms=MAKV;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Scott H.S., Antonarakis S.E., Papasavvas M.P., Michaud J.;
RT "A putative serine/threonine protein kinase MAK-V on human chromosome
RT 21q22.1.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP VARIANTS [LARGE SCALE ANALYSIS] TRP-157; CYS-591; LYS-625 AND THR-648.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
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 -!- INTERACTION:
CC P57058; P23528: CFL1; NbExp=2; IntAct=EBI-3959804, EBI-352733;
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; AJ271722; CAB71146.1; -; mRNA.
DR CCDS; CCDS13610.1; -.
DR RefSeq; NP_055401.1; NM_014586.1.
DR AlphaFoldDB; P57058; -.
DR SMR; P57058; -.
DR BioGRID; 119035; 42.
DR DIP; DIP-58064N; -.
DR IntAct; P57058; 7.
DR MINT; P57058; -.
DR STRING; 9606.ENSP00000270112; -.
DR BindingDB; P57058; -.
DR ChEMBL; CHEMBL1795165; -.
DR DrugCentral; P57058; -.
DR iPTMnet; P57058; -.
DR PhosphoSitePlus; P57058; -.
DR BioMuta; HUNK; -.
DR DMDM; 9973393; -.
DR MassIVE; P57058; -.
DR PaxDb; P57058; -.
DR PeptideAtlas; P57058; -.
DR PRIDE; P57058; -.
DR ProteomicsDB; 56977; -.
DR TopDownProteomics; P57058; -.
DR Antibodypedia; 6820; 350 antibodies from 31 providers.
DR DNASU; 30811; -.
DR Ensembl; ENST00000270112.7; ENSP00000270112.2; ENSG00000142149.9.
DR GeneID; 30811; -.
DR KEGG; hsa:30811; -.
DR MANE-Select; ENST00000270112.7; ENSP00000270112.2; NM_014586.2; NP_055401.1.
DR UCSC; uc002yph.3; human.
DR CTD; 30811; -.
DR DisGeNET; 30811; -.
DR GeneCards; HUNK; -.
DR HGNC; HGNC:13326; HUNK.
DR HPA; ENSG00000142149; Tissue enhanced (pancreas).
DR MIM; 606532; gene.
DR neXtProt; NX_P57058; -.
DR OpenTargets; ENSG00000142149; -.
DR PharmGKB; PA29563; -.
DR VEuPathDB; HostDB:ENSG00000142149; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000161070; -.
DR HOGENOM; CLU_017161_0_0_1; -.
DR InParanoid; P57058; -.
DR OMA; CLISQIQ; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; P57058; -.
DR TreeFam; TF352373; -.
DR PathwayCommons; P57058; -.
DR SignaLink; P57058; -.
DR BioGRID-ORCS; 30811; 10 hits in 1103 CRISPR screens.
DR ChiTaRS; HUNK; human.
DR GenomeRNAi; 30811; -.
DR Pharos; P57058; Tchem.
DR PRO; PR:P57058; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P57058; protein.
DR Bgee; ENSG00000142149; Expressed in ganglionic eminence and 135 other tissues.
DR ExpressionAtlas; P57058; baseline and differential.
DR Genevisible; P57058; HS.
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 GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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 1: Evidence at protein 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_0000086004"
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..615
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 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 VARIANT 157
FT /note="R -> W (in dbSNP:rs35133981)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040561"
FT VARIANT 591
FT /note="R -> C (in dbSNP:rs10775648)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040562"
FT VARIANT 625
FT /note="E -> K (in dbSNP:rs56021554)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040563"
FT VARIANT 648
FT /note="M -> T (in dbSNP:rs56240027)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040564"
SQ SEQUENCE 714 AA; 79686 MW; 87FC85C67D838AA7 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 VEVLSPSHHY RILNSPVSLA RRNSSERTLS
PGLPSGSMSP LHTPLHPTLV SFAHEDKNSP PKEEGLCCPP PVPSNGPMQP LGSPNCVKSR
GRFPMMGIGQ MLRKRHQSLQ PSADRPLEAS LPPLQPLAPV NLAFDMADGV KTQC