NRK_MOUSE
ID NRK_MOUSE Reviewed; 1455 AA.
AC Q9R0G8; B2RSW5; Q6NV55; Q8C9S9; Q9R0S4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Nik-related protein kinase;
DE EC=2.7.11.1;
DE AltName: Full=Nck-interacting kinase-like embryo specific kinase;
DE Short=NESK;
DE Short=NIK-like embryo-specific kinase;
GN Name=Nrk; Synonyms=Nesk;
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 [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Embryo;
RX PubMed=10559491; DOI=10.1016/s0925-4773(99)00193-8;
RA Kanai-Azuma M., Kanai Y., Okamoto M., Hayashi Y., Yonekawa H., Yazaki K.;
RT "Nrk: a murine X-linked NIK (Nck-interacting kinase)-related kinase gene
RT expressed in skeletal muscle.";
RL Mech. Dev. 89:155-159(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF LYS-54, FUNCTION, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=10801798; DOI=10.1074/jbc.m001009200;
RA Nakano K., Yamauchi J., Nakagawa K., Itoh H., Kitamura N.;
RT "NESK, a member of the germinal center kinase family that activates the c-
RT Jun N-terminal kinase pathway and is expressed during the late stages of
RT embryogenesis.";
RL J. Biol. Chem. 275:20533-20539(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-334.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [5]
RP FUNCTION, MUTAGENESIS OF LYS-54, AND DEVELOPMENTAL STAGE.
RX PubMed=12837278; DOI=10.1016/s0014-4827(03)00136-8;
RA Nakano K., Kanai-Azuma M., Kanai Y., Moriyama K., Yazaki K., Hayashi Y.,
RA Kitamura N.;
RT "Cofilin phosphorylation and actin polymerization by NRK/NESK, a member of
RT the germinal center kinase family.";
RL Exp. Cell Res. 287:219-227(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-850, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May phosphorylate cofilin-1 and induce actin polymerization
CC through this process, during the late stages of embryogenesis. Involved
CC in the TNF-alpha-induced signaling pathway.
CC {ECO:0000269|PubMed:10801798, ECO:0000269|PubMed:12837278}.
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 -!- DEVELOPMENTAL STAGE: Predominantly expressed in skeletal muscle during
CC embryogenesis. Expression was detected in the myotome at 10.5 dpc and,
CC thereafter, was observed in developing skeletal musculature from 11.5
CC to 13.5 dpc and increased from 15 to 17 dpc. However, expression in
CC skeletal muscle was not observed in adults. Its expression may be down-
CC regulated as development proceeds. {ECO:0000269|PubMed:10559491,
CC ECO:0000269|PubMed:10801798, ECO:0000269|PubMed:12837278}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH68311.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AB020741; BAA84943.1; -; mRNA.
DR EMBL; AB035267; BAA87066.1; -; mRNA.
DR EMBL; BC139029; AAI39030.1; -; mRNA.
DR EMBL; BC139031; AAI39032.1; -; mRNA.
DR EMBL; BC068311; AAH68311.1; ALT_SEQ; mRNA.
DR EMBL; AK041377; BAC30923.1; -; mRNA.
DR CCDS; CCDS41143.1; -.
DR RefSeq; NP_038752.2; NM_013724.2.
DR AlphaFoldDB; Q9R0G8; -.
DR SMR; Q9R0G8; -.
DR BioGRID; 205128; 7.
DR STRING; 10090.ENSMUSP00000108675; -.
DR iPTMnet; Q9R0G8; -.
DR PhosphoSitePlus; Q9R0G8; -.
DR MaxQB; Q9R0G8; -.
DR PaxDb; Q9R0G8; -.
DR PRIDE; Q9R0G8; -.
DR ProteomicsDB; 293896; -.
DR Antibodypedia; 2074; 65 antibodies from 21 providers.
DR DNASU; 27206; -.
DR Ensembl; ENSMUST00000064937; ENSMUSP00000063397; ENSMUSG00000052854.
DR GeneID; 27206; -.
DR KEGG; mmu:27206; -.
DR UCSC; uc009ujx.2; mouse.
DR CTD; 203447; -.
DR MGI; MGI:1351326; Nrk.
DR VEuPathDB; HostDB:ENSMUSG00000052854; -.
DR eggNOG; KOG0587; Eukaryota.
DR GeneTree; ENSGT00940000161533; -.
DR HOGENOM; CLU_001831_2_0_1; -.
DR InParanoid; Q9R0G8; -.
DR OMA; EDTYDHD; -.
DR OrthoDB; 533537at2759; -.
DR TreeFam; TF105138; -.
DR BioGRID-ORCS; 27206; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Nrk; mouse.
DR PRO; PR:Q9R0G8; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9R0G8; protein.
DR Bgee; ENSMUSG00000052854; Expressed in late embryo and 157 other tissues.
DR ExpressionAtlas; Q9R0G8; baseline and differential.
DR Genevisible; Q9R0G8; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP 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; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0007567; P:parturition; IMP:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0060721; P:regulation of spongiotrophoblast cell proliferation; IMP:MGI.
DR InterPro; IPR001180; CNH_dom.
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; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50219; CNH; 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; Coiled coil; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1455
FT /note="Nik-related protein kinase"
FT /id="PRO_0000250512"
FT DOMAIN 25..313
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1138..1425
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT REGION 385..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 716..750
FT /evidence="ECO:0000255"
FT COMPBIAS 471..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..559
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1079
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 31..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2Y5"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 54
FT /note="K->E: Kinase inactivation."
FT /evidence="ECO:0000269|PubMed:10801798,
FT ECO:0000269|PubMed:12837278"
FT CONFLICT 274
FT /note="A -> V (in Ref. 1; BAA84943)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="D -> N (in Ref. 1; BAA84943)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="K -> R (in Ref. 2; BAA87066)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="I -> T (in Ref. 3; AAH68311)"
FT /evidence="ECO:0000305"
FT CONFLICT 1008
FT /note="F -> S (in Ref. 3; AAH68311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1455 AA; 163647 MW; 7588DBE31B15ED91 CRC64;
MAGPGSWRDK EVTDLGQLPD PTGIFSLDKA IGLGTYGRIF LGIHEKTGSL VAVKVMSARK
TPLPEIGRRV RVNKYQKSVG WRYSDEEEDL RTELNLLRKY SFHKNIVTFY GAFFKLNPPG
HQHQLWMVME LCAAGSVTDV VRMTRNQSLK EDWIAYICRE ILQGLAHLHA HQVIHRDIKG
QNVLLTHDAE VKIVDFGVSA QVSRTNGRRN SFIGTPYWMA PEVIHCDEDP RCSYDYRSDV
WSVGITAIEM AEGAPPLCKL QPLEALCVIL REAAPKVKSS GWSRKFQNFM ENCMIKNFLF
RPTSGNMLLH PFVHDIKNER RVVESLTKHL TGIIQKREKK GIPVAFEGEE AAKEQYITRR
FRGPSCTPEL LRVPTSSRCR PLRVLHGEPP QPRWLPDQED PQDQELQQLQ KAAGVFMPLH
SQDNTSKLFP KQVEVAPYLR GAAQVVMPVL VQVEAPPQVS KAAQMLKSLP TQDNKATSPE
VQAPVAEGQQ AQHEALETEQ PKDLDQVPEE FQGQDRAPEQ PRQGQAAEQQ QIHNPVPEQP
PEEDREPEQA EVQEEAVEPP QAEIEDKEPE VVQVHAQVLL PLLSQNRHVL LPLHLDRQLL
IPVGEQNEEV PRAQAWDLEA SRAVGAVQAL IEGLSRDLLR APNAFVTKPL GPLQIFLENL
STDGFYTEPE PTQKKKSKVA SLRKAIAKRL RPKRFRAKAL WRLEDFEFSD VETSRRRRHR
RWEDIFNQHE EQLRRVENDR EDDSSDNDEV FHSIQAEVQI EPHAANPAGN EVHERSAPMP
CNRNRTHRVK FSPSVGEEEP SLEEAQPQQQ QQQPMNIRPR NCLNPQNFQA QSDSSSEEDS
PVTRRKSQSS PPYSTIDQKL LIDIHVPDGF KVGKISPPVY LTNEWVGYNA LSEIFWDDWI
MPTRPARPPE EDGDYVELYD ADANANGDEE VANGAYEDPR DGANGHDDMN NQLDQANGYE
GHGAAGYNGG DVGGNHGAAF NGPRANYPRA GILKNGHNDG RALNRGAFGV FGDNAARAFH
GAAGEAGAAF GNHGANRGNG RGNRNREANG RNEENGAFGR DQHVFPEFEH EESDRGTETS
DSIALEITSF DGEQNSGRPV SSTTMGFPIG RSSPRGSDFG SDISYNSPIL HVYEKDFSSE
VYCGSLWGVN LLLGTQSHLY LMDRSGKAEI VKLIKRRPFR QIQVVEQLNL LITISGKKNR
LRVYHLSWLR NKILNNDPKS KKRQKAMRKK EEACKAIDKL IGCEHFSVLQ HEETTYIAVA
VKSSIHLFAW APKSFDENTA IKVFPTRDLK PLTVDLAVGS EKTLKIFFSS ANGYHIIDAE
SEVMSEVTLP NNNVVILPDC LGLGVMLSLN AEAASEEANE QLLKKILDVW KDIPSSVAFE
CTKRITGWDQ KAIEVRSLQS TILENELKRR SIKKLRFLCA RGDKMFFAST LSNDHSRVYL
MSLGKLEELH RSYAV
