MINK1_HUMAN
ID MINK1_HUMAN Reviewed; 1332 AA.
AC Q8N4C8; D3DTK3; D3DTK4; Q5U8Z0; Q9P1X1; Q9P2R8;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Misshapen-like kinase 1;
DE EC=2.7.11.1;
DE AltName: Full=GCK family kinase MiNK;
DE AltName: Full=MAPK/ERK kinase kinase kinase 6;
DE Short=MEK kinase kinase 6;
DE Short=MEKKK 6;
DE AltName: Full=Misshapen/NIK-related kinase;
DE AltName: Full=Mitogen-activated protein kinase kinase kinase kinase 6;
GN Name=MINK1 {ECO:0000312|HGNC:HGNC:17565};
GN Synonyms=B55, MAP4K6 {ECO:0000250|UniProtKB:Q9JM52},
GN MINK {ECO:0000312|EMBL:BAA94838.1}, YSK2, ZC3;
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 {ECO:0000312|EMBL:AAH34673.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=10708748; DOI=10.1016/s0014-5793(00)01247-3;
RA Dan I., Watanabe N.M., Kobayashi T., Yamashita-Suzuki K., Fukagaya Y.,
RA Kajikawa E., Kimura W.K., Nakashima T.M., Matsumoto K., Ninomiya-Tsuji J.,
RA Kusumi A.;
RT "Molecular cloning of MINK, a novel member of mammalian GCK family kinases,
RT which is up-regulated during postnatal mouse cerebral development.";
RL FEBS Lett. 469:19-23(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH NCK1, TISSUE SPECIFICITY, ALTERNATIVE SPLICING,
RP AUTOPHOSPHORYLATION, AND VARIANTS ALA-771 AND LEU-775.
RX PubMed=15469942; DOI=10.1074/jbc.m404497200;
RA Hu Y., Leo C., Yu S., Huang B.C., Wang H., Shen M., Luo Y.,
RA Daniel-Issakani S., Payan D.G., Xu X.;
RT "Identification and functional characterization of a novel human
RT misshapen/Nck interacting kinase-related kinase, hMINK beta.";
RL J. Biol. Chem. 279:54387-54397(2004).
RN [3]
RP ERRATUM OF PUBMED:15469942.
RA Hu Y., Leo C., Yu S., Huang B.C., Wang H., Shen M., Luo Y.,
RA Daniel-Issakani S., Payan D.G., Xu X.;
RL J. Biol. Chem. 280:5128-5128(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5] {ECO:0000305}
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS ALA-771
RP AND LEU-775.
RC TISSUE=Lymph;
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 [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=16337592; DOI=10.1016/j.molcel.2005.10.038;
RA Nicke B., Bastien J., Khanna S.J., Warne P.H., Cowling V., Cook S.J.,
RA Peters G., Delpuech O., Schulze A., Berns K., Mullenders J.,
RA Beijersbergen R.L., Bernards R., Ganesan T.S., Downward J., Hancock D.C.;
RT "Involvement of MINK, a Ste20 family kinase, in Ras oncogene-induced growth
RT arrest in human ovarian surface epithelial cells.";
RL Mol. Cell 20:673-685(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP FUNCTION, INTERACTION WITH RAP2A, AND SUBCELLULAR LOCATION.
RX PubMed=18930710; DOI=10.1016/j.bbrc.2008.10.038;
RA Nonaka H., Takei K., Umikawa M., Oshiro M., Kuninaka K., Bayarjargal M.,
RA Asato T., Yamashiro Y., Uechi Y., Endo S., Suzuki T., Kariya K.;
RT "MINK is a Rap2 effector for phosphorylation of the postsynaptic scaffold
RT protein TANC1.";
RL Biochem. Biophys. Res. Commun. 377:573-578(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-763 AND SER-782,
RP VARIANT [LARGE SCALE ANALYSIS] LEU-775, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763; SER-777; SER-778 AND
RP SER-782, VARIANT [LARGE SCALE ANALYSIS] LEU-775, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, VARIANT [LARGE SCALE
RP ANALYSIS] LEU-775, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-778, VARIANT [LARGE SCALE
RP ANALYSIS] LEU-775, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP FUNCTION.
RX PubMed=21690388; DOI=10.1073/pnas.1104128108;
RA Kaneko S., Chen X., Lu P., Yao X., Wright T.G., Rajurkar M., Kariya K.,
RA Mao J., Ip Y.T., Xu L.;
RT "Smad inhibition by the Ste20 kinase Misshapen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:11127-11132(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-701; SER-754;
RP SER-763 AND SER-778, VARIANT [LARGE SCALE ANALYSIS] LEU-775, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-509, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [23]
RP VARIANTS [LARGE SCALE ANALYSIS] THR-514; ILE-863; VAL-1010 AND VAL-1200.
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).
RN [24]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-775, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
CC -!- FUNCTION: Serine/threonine kinase which acts as a negative regulator of
CC Ras-related Rap2-mediated signal transduction to control neuronal
CC structure and AMPA receptor trafficking. Required for normal synaptic
CC density, dendrite complexity, as well as surface AMPA receptor
CC expression in hippocampal neurons. Can activate the JNK and MAPK14/p38
CC pathways and mediates stimulation of the stress-activated protein
CC kinase MAPK14/p38 MAPK downstream of the Raf/ERK pathway.
CC Phosphorylates: TANC1 upon stimulation by RAP2A, MBP and SMAD1. Has an
CC essential function in negative selection of thymocytes, perhaps by
CC coupling NCK1 to activation of JNK1.
CC -!- FUNCTION: Isoform 4 can activate the JNK pathway. Involved in the
CC regulation of actin cytoskeleton reorganization, cell-matrix adhesion,
CC cell-cell adhesion and cell migration.
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:Q9JM52};
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:Q9JM52};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9JM52};
CC -!- SUBUNIT: Interacts with TANC1 (By similarity). Interacts with RAP2A.
CC Isoform 4 interacts with NCK1. {ECO:0000250,
CC ECO:0000269|PubMed:15469942, ECO:0000269|PubMed:18930710}.
CC -!- INTERACTION:
CC Q8N4C8; Q00613: HSF1; NbExp=2; IntAct=EBI-2133481, EBI-719620;
CC Q8N4C8; O95819: MAP4K4; NbExp=2; IntAct=EBI-2133481, EBI-2511133;
CC Q8N4C8-4; Q5VY09: IER5; NbExp=2; IntAct=EBI-11475194, EBI-1774000;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15469942,
CC ECO:0000269|PubMed:18930710}. Postsynaptic density {ECO:0000250}. Cell
CC projection, axon {ECO:0000250}. Cell projection, dendrite
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Golgi apparatus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=3 {ECO:0000269|PubMed:10708748}; Synonyms=MINK-alpha;
CC IsoId=Q8N4C8-1; Sequence=Displayed;
CC Name=1 {ECO:0000269|PubMed:10708748}; Synonyms=MiNK-1, MINK-delta;
CC IsoId=Q8N4C8-2; Sequence=VSP_007059;
CC Name=2 {ECO:0000269|PubMed:10708748}; Synonyms=MiNK-2, MINK-gamma;
CC IsoId=Q8N4C8-3; Sequence=VSP_007059, VSP_007060;
CC Name=4; Synonyms=MINK-beta;
CC IsoId=Q8N4C8-4; Sequence=VSP_041871;
CC Name=5; Synonyms=MINK-eta;
CC IsoId=Q8N4C8-5; Sequence=VSP_041871, VSP_007059;
CC -!- TISSUE SPECIFICITY: Expressed in the brain, isoform 2 is more abundant
CC than isoform 1. Isoform 3 is ubiquitously expressed. Isoform 1 is most
CC abundant in the skeletal muscle. Isoform 4 is ubiquitously expressed
CC with relative high levels in brain, skeletal muscle, pancreas and
CC testis. {ECO:0000269|PubMed:15469942}.
CC -!- INDUCTION: Activated after Ras induction via a mechanism involving
CC reactive oxygen species. {ECO:0000269|PubMed:16337592}.
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; AB041926; BAA94838.1; -; mRNA.
DR EMBL; AB035698; BAA90753.1; -; mRNA.
DR EMBL; AY775058; AAV41830.1; -; mRNA.
DR EMBL; AC233723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90401.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90403.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90399.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90400.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90402.1; -; Genomic_DNA.
DR EMBL; BC034673; AAH34673.1; -; mRNA.
DR CCDS; CCDS45588.1; -. [Q8N4C8-1]
DR CCDS; CCDS45589.1; -. [Q8N4C8-3]
DR CCDS; CCDS45590.1; -. [Q8N4C8-4]
DR RefSeq; NP_001020108.1; NM_001024937.3. [Q8N4C8-4]
DR RefSeq; NP_001308165.1; NM_001321236.1.
DR RefSeq; NP_056531.1; NM_015716.4. [Q8N4C8-2]
DR RefSeq; NP_722549.2; NM_153827.4. [Q8N4C8-1]
DR RefSeq; NP_733763.1; NM_170663.4. [Q8N4C8-3]
DR AlphaFoldDB; Q8N4C8; -.
DR SMR; Q8N4C8; -.
DR BioGRID; 119075; 125.
DR IntAct; Q8N4C8; 55.
DR MINT; Q8N4C8; -.
DR STRING; 9606.ENSP00000347427; -.
DR BindingDB; Q8N4C8; -.
DR ChEMBL; CHEMBL5518; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q8N4C8; -.
DR GuidetoPHARMACOLOGY; 2103; -.
DR GlyGen; Q8N4C8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N4C8; -.
DR PhosphoSitePlus; Q8N4C8; -.
DR BioMuta; MINK1; -.
DR DMDM; 296437370; -.
DR EPD; Q8N4C8; -.
DR jPOST; Q8N4C8; -.
DR MassIVE; Q8N4C8; -.
DR MaxQB; Q8N4C8; -.
DR PaxDb; Q8N4C8; -.
DR PeptideAtlas; Q8N4C8; -.
DR PRIDE; Q8N4C8; -.
DR ProteomicsDB; 71917; -. [Q8N4C8-1]
DR ProteomicsDB; 71918; -. [Q8N4C8-2]
DR ProteomicsDB; 71919; -. [Q8N4C8-3]
DR ProteomicsDB; 71920; -. [Q8N4C8-4]
DR ProteomicsDB; 71921; -. [Q8N4C8-5]
DR Antibodypedia; 5678; 240 antibodies from 32 providers.
DR DNASU; 50488; -.
DR Ensembl; ENST00000347992.11; ENSP00000269296.7; ENSG00000141503.17. [Q8N4C8-3]
DR Ensembl; ENST00000355280.11; ENSP00000347427.6; ENSG00000141503.17. [Q8N4C8-1]
DR Ensembl; ENST00000453408.7; ENSP00000406487.3; ENSG00000141503.17. [Q8N4C8-4]
DR GeneID; 50488; -.
DR KEGG; hsa:50488; -.
DR MANE-Select; ENST00000355280.11; ENSP00000347427.6; NM_153827.5; NP_722549.2.
DR UCSC; uc010vsl.3; human. [Q8N4C8-1]
DR CTD; 50488; -.
DR DisGeNET; 50488; -.
DR GeneCards; MINK1; -.
DR HGNC; HGNC:17565; MINK1.
DR HPA; ENSG00000141503; Low tissue specificity.
DR MIM; 609426; gene.
DR neXtProt; NX_Q8N4C8; -.
DR OpenTargets; ENSG00000141503; -.
DR PharmGKB; PA134910641; -.
DR VEuPathDB; HostDB:ENSG00000141503; -.
DR eggNOG; KOG0587; Eukaryota.
DR GeneTree; ENSGT00950000183196; -.
DR InParanoid; Q8N4C8; -.
DR OMA; WAQEYKR; -.
DR OrthoDB; 669799at2759; -.
DR PhylomeDB; Q8N4C8; -.
DR TreeFam; TF105138; -.
DR PathwayCommons; Q8N4C8; -.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR SignaLink; Q8N4C8; -.
DR SIGNOR; Q8N4C8; -.
DR BioGRID-ORCS; 50488; 15 hits in 1112 CRISPR screens.
DR ChiTaRS; MINK1; human.
DR GeneWiki; MINK1; -.
DR GenomeRNAi; 50488; -.
DR Pharos; Q8N4C8; Tchem.
DR PRO; PR:Q8N4C8; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8N4C8; protein.
DR Bgee; ENSG00000141503; Expressed in CA1 field of hippocampus and 206 other tissues.
DR ExpressionAtlas; Q8N4C8; baseline and differential.
DR Genevisible; Q8N4C8; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
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:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; ISS:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0007254; P:JNK cascade; TAS:ProtInc.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:UniProtKB.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IMP:CACAO.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0001952; P:regulation of cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
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 Alternative splicing; ATP-binding; Cell projection; Cytoplasm;
KW Golgi apparatus; Kinase; Methylation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Synapse; Transferase.
FT CHAIN 1..1332
FT /note="Misshapen-like kinase 1"
FT /id="PRO_0000086329"
FT DOMAIN 25..289
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1019..1306
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT REGION 300..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..1332
FT /note="Mediates interaction with RAP2A"
FT /evidence="ECO:0000269|PubMed:18930710"
FT REGION 902..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..335
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..573
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..662
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..732
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..843
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
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 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM52"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM52"
FT MOD_RES 501
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM52"
FT MOD_RES 509
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976"
FT MOD_RES 891
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM52"
FT VAR_SEQ 581..600
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15469942"
FT /id="VSP_041871"
FT VAR_SEQ 696..732
FT /note="Missing (in isoform 1, isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10708748"
FT /id="VSP_007059"
FT VAR_SEQ 800
FT /note="A -> ASYKRAIGE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10708748"
FT /id="VSP_007060"
FT VARIANT 514
FT /note="A -> T (in dbSNP:rs56131206)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040799"
FT VARIANT 771
FT /note="V -> A (in dbSNP:rs11556634)"
FT /evidence="ECO:0000269|PubMed:15469942,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_046058"
FT VARIANT 775
FT /note="P -> L (in dbSNP:rs11556635)"
FT /evidence="ECO:0000269|PubMed:15469942,
FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT /id="VAR_046059"
FT VARIANT 863
FT /note="V -> I (in dbSNP:rs2302319)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_046060"
FT VARIANT 1010
FT /note="E -> V (in a gastric adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_046061"
FT VARIANT 1200
FT /note="I -> V"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040800"
SQ SEQUENCE 1332 AA; 149822 MW; 3E3B182CDDB3659C CRC64;
MGDPAPARSL DDIDLSALRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL AAIKVMDVTE
DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKSPPGNDDQ LWLVMEFCGA GSVTDLVKNT
KGNALKEDCI AYICREILRG LAHLHAHKVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR
TVGRRNTFIG TPYWMAPEVI ACDENPDATY DYRSDIWSLG ITAIEMAEGA PPLCDMHPMR
ALFLIPRNPP PRLKSKKWSK KFIDFIDTCL IKTYLSRPPT EQLLKFPFIR DQPTERQVRI
QLKDHIDRSR KKRGEKEETE YEYSGSEEED DSHGEEGEPS SIMNVPGEST LRREFLRLQQ
ENKSNSEALK QQQQLQQQQQ RDPEAHIKHL LHQRQRRIEE QKEERRRVEE QQRREREQRK
LQEKEQQRRL EDMQALRREE ERRQAEREQE YKRKQLEEQR QSERLQRQLQ QEHAYLKSLQ
QQQQQQQLQK QQQQQLLPGD RKPLYHYGRG MNPADKPAWA REVEERTRMN KQQNSPLAKS
KPGSTGPEPP IPQASPGPPG PLSQTPPMQR PVEPQEGPHK SLVAHRVPLK PYAAPVPRSQ
SLQDQPTRNL AAFPASHDPD PAIPAPTATP SARGAVIRQN SDPTSEGPGP SPNPPAWVRP
DNEAPPKVPQ RTSSIATALN TSGAGGSRPA QAVRARPRSN SAWQIYLQRR AERGTPKPPG
PPAQPPGPPN ASSNPDLRRS DPGWERSDSV LPASHGHLPQ AGSLERNRVG VSSKPDSSPV
LSPGNKAKPD DHRSRPGRPA DFVLLKERTL DEAPRPPKKA MDYSSSSEEV ESSEDDEEEG
EGGPAEGSRD TPGGRSDGDT DSVSTMVVHD VEEITGTQPP YGGGTMVVQR TPEEERNLLH
ADSNGYTNLP DVVQPSHSPT ENSKGQSPPS KDGSGDYQSR GLVKAPGKSS FTMFVDLGIY
QPGGSGDSIP ITALVGGEGT RLDQLQYDVR KGSVVNVNPT NTRAHSETPE IRKYKKRFNS
EILCAALWGV NLLVGTENGL MLLDRSGQGK VYGLIGRRRF QQMDVLEGLN LLITISGKRN
KLRVYYLSWL RNKILHNDPE VEKKQGWTTV GDMEGCGHYR VVKYERIKFL VIALKSSVEV
YAWAPKPYHK FMAFKSFADL PHRPLLVDLT VEEGQRLKVI YGSSAGFHAV DVDSGNSYDI
YIPVHIQSQI TPHAIIFLPN TDGMEMLLCY EDEGVYVNTY GRIIKDVVLQ WGEMPTSVAY
ICSNQIMGWG EKAIEIRSVE TGHLDGVFMH KRAQRLKFLC ERNDKVFFAS VRSGGSSQVY
FMTLNRNCIM NW
