NIM1_HUMAN
ID NIM1_HUMAN Reviewed; 436 AA.
AC Q8IY84; B3KVM1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 152.
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 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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION
RP AT THR-229, AND MUTAGENESIS OF THR-229.
RX PubMed=15733851; DOI=10.1016/j.febslet.2005.01.042;
RA Jaleel M., McBride A., Lizcano J.M., Deak M., Toth R., Morrice N.A.,
RA Alessi D.R.;
RT "Identification of the sucrose non-fermenting related kinase SNRK, as a
RT novel LKB1 substrate.";
RL FEBS Lett. 579:1417-1423(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAH36422.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAH36422.1};
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).
RN [6]
RP VARIANTS [LARGE SCALE ANALYSIS] TRP-21; GLN-64; ILE-260; ILE-320; SER-333
RP AND THR-411.
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 Evidence={ECO:0000269|PubMed:15733851};
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:0000269|PubMed:15733851};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15733851};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation at Thr-229, probably
CC by autophosphorylation. {ECO:0000269|PubMed:15733851}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AK122985; BAG53833.1; -; mRNA.
DR EMBL; AC106800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471119; EAW56053.1; -; Genomic_DNA.
DR EMBL; BC036422; AAH36422.1; -; mRNA.
DR CCDS; CCDS3943.1; -.
DR RefSeq; NP_699192.1; NM_153361.3.
DR RefSeq; XP_006714513.1; XM_006714450.1.
DR AlphaFoldDB; Q8IY84; -.
DR SMR; Q8IY84; -.
DR BioGRID; 127945; 3.
DR IntAct; Q8IY84; 6.
DR STRING; 9606.ENSP00000420849; -.
DR BindingDB; Q8IY84; -.
DR ChEMBL; CHEMBL3542; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q8IY84; -.
DR GuidetoPHARMACOLOGY; 2291; -.
DR iPTMnet; Q8IY84; -.
DR PhosphoSitePlus; Q8IY84; -.
DR BioMuta; NIM1K; -.
DR DMDM; 74759697; -.
DR PaxDb; Q8IY84; -.
DR PeptideAtlas; Q8IY84; -.
DR PRIDE; Q8IY84; -.
DR ProteomicsDB; 71124; -.
DR Antibodypedia; 23239; 158 antibodies from 24 providers.
DR DNASU; 167359; -.
DR Ensembl; ENST00000326035.6; ENSP00000313572.2; ENSG00000177453.7.
DR Ensembl; ENST00000512796.1; ENSP00000420849.1; ENSG00000177453.7.
DR GeneID; 167359; -.
DR KEGG; hsa:167359; -.
DR MANE-Select; ENST00000326035.6; ENSP00000313572.2; NM_153361.4; NP_699192.1.
DR UCSC; uc003jno.5; human.
DR CTD; 167359; -.
DR DisGeNET; 167359; -.
DR GeneCards; NIM1K; -.
DR HGNC; HGNC:28646; NIM1K.
DR HPA; ENSG00000177453; Group enriched (brain, choroid plexus, pituitary gland, retina).
DR neXtProt; NX_Q8IY84; -.
DR OpenTargets; ENSG00000177453; -.
DR VEuPathDB; HostDB:ENSG00000177453; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000160020; -.
DR HOGENOM; CLU_000288_63_1_1; -.
DR InParanoid; Q8IY84; -.
DR OMA; IMSNEWM; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q8IY84; -.
DR PathwayCommons; Q8IY84; -.
DR SignaLink; Q8IY84; -.
DR BioGRID-ORCS; 167359; 9 hits in 1052 CRISPR screens.
DR ChiTaRS; NIM1K; human.
DR GenomeRNAi; 167359; -.
DR Pharos; Q8IY84; Tchem.
DR PRO; PR:Q8IY84; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8IY84; protein.
DR Bgee; ENSG00000177453; Expressed in middle temporal gyrus and 126 other tissues.
DR Genevisible; Q8IY84; HS.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA: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; IDA: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 1: Evidence at protein 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_0000247666"
FT DOMAIN 74..325
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 23..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000269|PubMed:15733851"
FT VARIANT 21
FT /note="R -> W (in dbSNP:rs55664335)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040945"
FT VARIANT 64
FT /note="E -> Q (in dbSNP:rs55663207)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040946"
FT VARIANT 260
FT /note="L -> I (in dbSNP:rs35659008)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040947"
FT VARIANT 320
FT /note="M -> I (in dbSNP:rs55770078)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040948"
FT VARIANT 333
FT /note="P -> S (in a lung neuroendocrine carcinoma sample;
FT somatic mutation; dbSNP:rs866026698)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040949"
FT VARIANT 411
FT /note="P -> T (in a lung large cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040950"
FT MUTAGEN 229
FT /note="T->A: Loss of autophosphorylation and kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:15733851"
FT MUTAGEN 229
FT /note="T->E: Constitutively active."
FT /evidence="ECO:0000269|PubMed:15733851"
SQ SEQUENCE 436 AA; 49606 MW; C183F11F54E3B87C CRC64;
MTAVYMNGGG LVNPHYARWD RRDSVESGCQ TESSKEGEEG QPRQLTPFEK LTQDMSQDEK
VVREITLGKR IGFYRIRGEI GSGNFSQVKL GIHSLTKEKV AIKILDKTKL DQKTQRLLSR
EISSMEKLHH PNIIRLYEVV ETLSKLHLVM EYAGGGELFG KISTEGKLSE PESKLIFSQI
VSAVKHMHEN QIIHRDLKAE NVFYTSNTCV KVGDFGFSTV SKKGEMLNTF CGSPPYAAPE
LFRDEHYIGI YVDIWALGVL LYFMVTGTMP FRAETVAKLK KSILEGTYSV PPHVSEPCHR
LIRGVLQQIP TERYGIDCIM NDEWMQGVPY PTPLEPFQLD PKHLSETSTL KEEENEVKST
LEHLGITEEH IRNNQGRDAR SSITGVYRII LHRVQRKKAL ESVPVMMLPD PKERDLKKGS
RVYRGIRHTS KFCSIL
