NEK5_HUMAN
ID NEK5_HUMAN Reviewed; 708 AA.
AC Q6P3R8; Q5TAP5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Serine/threonine-protein kinase Nek5;
DE EC=2.7.11.1;
DE AltName: Full=Never in mitosis A-related kinase 5;
DE Short=NimA-related protein kinase 5;
GN Name=NEK5;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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]
RP VARIANTS [LARGE SCALE ANALYSIS] HIS-290 AND ARG-531.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000305}.
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DR EMBL; AL139082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC063885; AAH63885.1; -; mRNA.
DR CCDS; CCDS31979.1; -.
DR RefSeq; NP_954983.1; NM_199289.2.
DR AlphaFoldDB; Q6P3R8; -.
DR SMR; Q6P3R8; -.
DR BioGRID; 131150; 4.
DR IntAct; Q6P3R8; 3.
DR STRING; 9606.ENSP00000347767; -.
DR BindingDB; Q6P3R8; -.
DR ChEMBL; CHEMBL5044; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q6P3R8; -.
DR iPTMnet; Q6P3R8; -.
DR PhosphoSitePlus; Q6P3R8; -.
DR BioMuta; NEK5; -.
DR DMDM; 74758252; -.
DR jPOST; Q6P3R8; -.
DR MassIVE; Q6P3R8; -.
DR PaxDb; Q6P3R8; -.
DR PeptideAtlas; Q6P3R8; -.
DR PRIDE; Q6P3R8; -.
DR ProteomicsDB; 66925; -.
DR Antibodypedia; 35078; 166 antibodies from 25 providers.
DR DNASU; 341676; -.
DR Ensembl; ENST00000355568.8; ENSP00000347767.4; ENSG00000197168.14.
DR Ensembl; ENST00000617045.1; ENSP00000477810.1; ENSG00000197168.14.
DR GeneID; 341676; -.
DR KEGG; hsa:341676; -.
DR UCSC; uc001vge.4; human.
DR CTD; 341676; -.
DR DisGeNET; 341676; -.
DR GeneCards; NEK5; -.
DR HGNC; HGNC:7748; NEK5.
DR HPA; ENSG00000197168; Group enriched (brain, choroid plexus, fallopian tube, testis).
DR neXtProt; NX_Q6P3R8; -.
DR OpenTargets; ENSG00000197168; -.
DR PharmGKB; PA31549; -.
DR VEuPathDB; HostDB:ENSG00000197168; -.
DR eggNOG; KOG0589; Eukaryota.
DR GeneTree; ENSGT00940000160136; -.
DR HOGENOM; CLU_000288_63_39_1; -.
DR InParanoid; Q6P3R8; -.
DR OrthoDB; 70360at2759; -.
DR PhylomeDB; Q6P3R8; -.
DR TreeFam; TF106472; -.
DR PathwayCommons; Q6P3R8; -.
DR SignaLink; Q6P3R8; -.
DR BioGRID-ORCS; 341676; 22 hits in 1110 CRISPR screens.
DR ChiTaRS; NEK5; human.
DR GenomeRNAi; 341676; -.
DR Pharos; Q6P3R8; Tchem.
DR PRO; PR:Q6P3R8; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q6P3R8; protein.
DR Bgee; ENSG00000197168; Expressed in bronchial epithelial cell and 125 other tissues.
DR ExpressionAtlas; Q6P3R8; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..708
FT /note="Serine/threonine-protein kinase Nek5"
FT /id="PRO_0000259765"
FT DOMAIN 4..259
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 376..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VARIANT 255
FT /note="K -> Q (in dbSNP:rs34756139)"
FT /id="VAR_051652"
FT VARIANT 290
FT /note="R -> H"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040922"
FT VARIANT 531
FT /note="C -> R"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040923"
SQ SEQUENCE 708 AA; 81445 MW; D9A5B3606414D128 CRC64;
MDKYDVIKAI GQGAFGKAYL AKGKSDSKHC VIKEINFEKM PIQEKEASKK EVILLEKMKH
PNIVAFFNSF QENGRLFIVM EYCDGGDLMK RINRQRGVLF SEDQILGWFV QISLGLKHIH
DRKILHRDIK AQNIFLSKNG MVAKLGDFGI ARVLNNSMEL ARTCIGTPYY LSPEICQNKP
YNNKTDIWSL GCVLYELCTL KHPFEGNNLQ QLVLKICQAH FAPISPGFSR ELHSLISQLF
QVSPRDRPSI NSILKRPFLE NLIPKYLTPE VIQEEFSHML ICRAGAPASR HAGKVVQKCK
IQKVRFQGKC PPRSRISVPI KRNAILHRNE WRPPAGAQKA RSIKMIERPK IAAVCGHYDY
YYAQLDMLRR RAHKPSYHPI PQENTGVEDY GQETRHGPSP SQWPAEYLQR KFEAQQYKLK
VEKQLGLRPS SAEPNYNQRQ ELRSNGEEPR FQELPFRKNE MKEQEYWKQL EEIRQQYHND
MKEIRKKMGR EPEENSKISH KTYLVKKSNL PVHQDASEGE APVQMEFRSC CPGWSAMARS
WLTATSASQD IEKDLKQMRL QNTKESKNPE QKYKAKKGVK FEINLDKCIS DENILQEEEA
MDIPNETLTF EDGMKFKEYE CVKEHGDYTD KAFEKLHCPE AGFSTQTVAA VGNRRQWDGG
APQTLLQMMA VADITSTCPT GPDSESVLSV SRQEGKTKDP YSPVLILM
