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   27-MAR-2024, entry version 180.
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       P57058; P53667: LIMK1; NbExp=2; IntAct=EBI-3959804, EBI-444403;
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; 96.
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; 9606-ENSP00000270112; -.
DR   PeptideAtlas; P57058; -.
DR   ProteomicsDB; 56977; -.
DR   TopDownProteomics; P57058; -.
DR   Antibodypedia; 6820; 378 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   AGR; HGNC:13326; -.
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; PMMGVGQ; -.
DR   OrthoDB; 5475340at2759; -.
DR   PhylomeDB; P57058; -.
DR   TreeFam; TF352373; -.
DR   PathwayCommons; P57058; -.
DR   SignaLink; P57058; -.
DR   SIGNOR; P57058; -.
DR   BioGRID-ORCS; 30811; 10 hits in 1178 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 137 other cell types or tissues.
DR   ExpressionAtlas; P57058; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   CDD; cd14070; STKc_HUNK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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   PANTHER; PTHR24346:SF80; HORMONALLY UP-REGULATED NEU TUMOR-ASSOCIATED KINASE; 1.
DR   PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; P57058; HS.
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
//