NEK5_MOUSE
ID NEK5_MOUSE Reviewed; 627 AA.
AC Q7TSC3; Q8C6N6; Q8CCJ0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
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 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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Oviduct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Olfactory epithelium;
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7TSC3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TSC3-2; Sequence=VSP_021531, VSP_021532;
CC Name=3;
CC IsoId=Q7TSC3-3; Sequence=VSP_021533;
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; AK032672; BAC27980.1; -; mRNA.
DR EMBL; AK054168; BAC35677.1; -; mRNA.
DR EMBL; BC053516; AAH53516.1; -; mRNA.
DR CCDS; CCDS52518.1; -. [Q7TSC3-3]
DR CCDS; CCDS85511.1; -. [Q7TSC3-1]
DR RefSeq; NP_001334247.1; NM_001347318.1. [Q7TSC3-1]
DR RefSeq; NP_808566.2; NM_177898.4. [Q7TSC3-3]
DR AlphaFoldDB; Q7TSC3; -.
DR SMR; Q7TSC3; -.
DR STRING; 10090.ENSMUSP00000126705; -.
DR iPTMnet; Q7TSC3; -.
DR PhosphoSitePlus; Q7TSC3; -.
DR PaxDb; Q7TSC3; -.
DR PRIDE; Q7TSC3; -.
DR ProteomicsDB; 287364; -. [Q7TSC3-1]
DR ProteomicsDB; 287365; -. [Q7TSC3-2]
DR ProteomicsDB; 287366; -. [Q7TSC3-3]
DR Antibodypedia; 35078; 166 antibodies from 25 providers.
DR DNASU; 330721; -.
DR Ensembl; ENSMUST00000169834; ENSMUSP00000126705; ENSMUSG00000037738. [Q7TSC3-3]
DR Ensembl; ENSMUST00000209656; ENSMUSP00000148211; ENSMUSG00000037738. [Q7TSC3-1]
DR GeneID; 330721; -.
DR KEGG; mmu:330721; -.
DR UCSC; uc009lco.1; mouse. [Q7TSC3-3]
DR UCSC; uc009lcp.1; mouse. [Q7TSC3-1]
DR UCSC; uc009lcq.1; mouse. [Q7TSC3-2]
DR CTD; 341676; -.
DR MGI; MGI:2142824; Nek5.
DR VEuPathDB; HostDB:ENSMUSG00000037738; -.
DR eggNOG; KOG0589; Eukaryota.
DR GeneTree; ENSGT00940000160136; -.
DR HOGENOM; CLU_000288_63_39_1; -.
DR InParanoid; Q7TSC3; -.
DR OMA; QTEFCSC; -.
DR OrthoDB; 70360at2759; -.
DR PhylomeDB; Q7TSC3; -.
DR TreeFam; TF106472; -.
DR BioGRID-ORCS; 330721; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q7TSC3; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q7TSC3; protein.
DR Bgee; ENSMUSG00000037738; Expressed in choroid plexus epithelium and 54 other tissues.
DR ExpressionAtlas; Q7TSC3; baseline and differential.
DR Genevisible; Q7TSC3; MM.
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; IDA:MGI.
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:2001056; P:positive regulation of cysteine-type endopeptidase activity; IMP:MGI.
DR GO; GO:0051155; P:positive regulation of striated muscle cell differentiation; IDA:MGI.
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 Alternative splicing; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..627
FT /note="Serine/threonine-protein kinase Nek5"
FT /id="PRO_0000259766"
FT DOMAIN 4..255
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 563..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..578
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 124
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 VAR_SEQ 295..336
FT /note="SAAYLQRKFEAQQYKLKVERQLGLRPSSVEPHPNEGEKLQSH -> WDHVTM
FT SLKSMRGWLGVVAYRLPSLHKILPEFHPQCHKNEKF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021531"
FT VAR_SEQ 337..627
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021532"
FT VAR_SEQ 573..627
FT /note="IKFEESEDELRSEIIESLEKLAASTEEAEQAPSSSKNAEEPGEKEKTNLPVK
FT KLQ -> MQEGRGIKNSMPSSATSKIKASPGCMASCPNSVTPPPLQRKI (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021533"
SQ SEQUENCE 627 AA; 71790 MW; AD5789B6621ACA2F CRC64;
MDNFHLIKII GEGTFGKVYL AKDKSESSHC VIKEISLTKE KEASKNEVIL LARMEHPNIV
TFFSSFQENG RLFIVMEYCD GGDLMQRIQR QRGVMFSEDQ ILCWFVQISL GLKHIHDRKI
LHRDIKSQNI FLSKNGMVAK LGDFGTARTL NDSMELAQTC AGTPYYLSPE ICQNRPYNNK
TDIWSLGCVL YELCTLKHPF ESNNFHHLVL KICQGRVAPI SPHFSRDLQS LIPQLFRVSP
QDRPSVTSLL KRPFLETLIA RSLYPEVCSR RIQSHAHMEN MAIGPTACWR VSPWSAAYLQ
RKFEAQQYKL KVERQLGLRP SSVEPHPNEG EKLQSHWEET KFQELQYRKN KMKDQEYWKQ
LEEIRQQYHN DMKEIKKKMG RELKRVVKFE ISLDKCISEE DTVQENEAVD KLNATLSFED
GTKFQEHRCK EEHEDYTDRA FEELCGPEAE GFFQDVIAAE NRRQWDAGAP HTLLRIMAMA
DVTSTCPTMP DDGQVIVMEG SVENGKQWWL DVPGTPCALA AECACSGSLS ASKGETVMIK
PQLPKEDQEK VEIATGIMVD DEQLEPGSDE DDIKFEESED ELRSEIIESL EKLAASTEEA
EQAPSSSKNA EEPGEKEKTN LPVKKLQ
