NIM1_MOUSE
ID NIM1_MOUSE Reviewed; 436 AA.
AC Q8BHI9; Q148V1; Q80XC1; Q8BXQ9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Serine/threonine-protein kinase NIM1;
DE EC=2.7.11.1;
DE AltName: Full=NIM1 serine/threonine-protein kinase;
GN Name=Nim1k; Synonyms=Nim1;
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] {ECO:0000312|EMBL:BAC33424.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC33424.1};
RC TISSUE=Cerebellum {ECO:0000312|EMBL:BAC33424.1},
RC Eye {ECO:0000312|EMBL:BAC35497.1}, and
RC Retina {ECO:0000312|EMBL:BAC31934.1};
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] {ECO:0000312|EMBL:AAI06123.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye {ECO:0000312|EMBL:AAI06123.1};
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 Evidence={ECO:0000250|UniProtKB:Q8IY84};
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; Evidence={ECO:0000250|UniProtKB:Q8IY84};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8IY84};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation at Thr-229, probably
CC by autophosphorylation. {ECO:0000250|UniProtKB:Q8IY84}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AK044462; BAC31934.1; -; mRNA.
DR EMBL; AK048694; BAC33424.1; -; mRNA.
DR EMBL; AK053734; BAC35497.1; -; mRNA.
DR EMBL; BC051189; AAH51189.2; -; mRNA.
DR EMBL; BC106122; AAI06123.1; -; mRNA.
DR EMBL; BC117955; AAI17956.1; -; mRNA.
DR EMBL; BC117956; AAI17957.1; -; mRNA.
DR CCDS; CCDS56902.1; -.
DR RefSeq; NP_780747.1; NM_175538.3.
DR AlphaFoldDB; Q8BHI9; -.
DR SMR; Q8BHI9; -.
DR STRING; 10090.ENSMUSP00000136377; -.
DR iPTMnet; Q8BHI9; -.
DR PhosphoSitePlus; Q8BHI9; -.
DR PaxDb; Q8BHI9; -.
DR PRIDE; Q8BHI9; -.
DR ProteomicsDB; 293849; -.
DR Antibodypedia; 23239; 158 antibodies from 24 providers.
DR DNASU; 245269; -.
DR Ensembl; ENSMUST00000178142; ENSMUSP00000136377; ENSMUSG00000095930.
DR GeneID; 245269; -.
DR KEGG; mmu:245269; -.
DR UCSC; uc007rzu.1; mouse.
DR CTD; 167359; -.
DR MGI; MGI:2442399; Nim1k.
DR VEuPathDB; HostDB:ENSMUSG00000095930; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000160020; -.
DR HOGENOM; CLU_000288_63_1_1; -.
DR InParanoid; Q8BHI9; -.
DR OMA; IMSNEWM; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q8BHI9; -.
DR TreeFam; TF320558; -.
DR BioGRID-ORCS; 245269; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8BHI9; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8BHI9; protein.
DR Bgee; ENSMUSG00000095930; Expressed in retinal neural layer and 119 other tissues.
DR Genevisible; Q8BHI9; MM.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
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 Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..436
FT /note="Serine/threonine-protein kinase NIM1"
FT /id="PRO_0000247667"
FT DOMAIN 74..325
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 80..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 229
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8IY84"
FT CONFLICT 295
FT /note="S -> F (in Ref. 1; BAC31934)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 49777 MW; 15EF3210F49B2EC6 CRC64;
MTAVFVNGGG LVNTHCDRWE RRDSVESSCQ TEGGKDSEED QQRQLTPFEK LTQDMCQDEK
VVREITLGKR IGFYRIRGEI GSGNFSQVKL GIHSLTKEKV AIKILDKTKL DQKTQRLLSR
EISSMEKLHH PNIVRLYEVV ETLSKLHLVM EYAGGGELFG KISTEGKLSE PESKLIFSQI
LSAVKHMHEN QIIHRDLKAE NVFYTSRTCV KVGDFGFSTV SKKGEMLNTF CGSPPYAAPE
LFRDQHYVGV YVDIWALGVL LYFMVTGTMP FRAETVAKLK KSILEGTYTI PQHVSEPCHR
LIRGVLQPTP TERYGINYIM SNEWMRGVPY PTPLEPFQLD PKHLSETSTL KEEENEVKST
LEHLGITDEH IRNNQGRDAR SSITGVYRII LHRVQRRKAL ESVPIMILPE PKERDLKKGS
RIYRGIRHTS KFCSIL
