ID MAK_HUMAN Reviewed; 623 AA. AC P20794; F1T0K6; G1FL29; Q547D0; Q9NUH7; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 2. DT 02-SEP-2026, entry version 212. DE RecName: Full=Serine/threonine-protein kinase MAK; DE EC=2.7.11.1 {ECO:0000269|PubMed:12084720, ECO:0000269|PubMed:21986944}; DE AltName: Full=Male germ cell-associated kinase; GN Name=MAK; 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] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, INDUCTION, AUTOPHOSPHORYLATION, PHOSPHORYLATION, AND RP MUTAGENESIS OF LYS-33. RC TISSUE=Testis; RX PubMed=12084720; DOI=10.1074/jbc.m203940200; RA Xia L., Robinson D., Ma A.H., Chen H.C., Wu F., Qiu Y., Kung H.J.; RT "Identification of human male germ cell-associated kinase, a kinase RT transcriptionally activated by androgen in prostate cancer cells."; RL J. Biol. Chem. 277:35422-35433(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORM 2), RP VARIANTS RP62 SER-13; ARG-27; HIS-130; HIS-166 AND THR-181, RP CHARACTERIZATION OF VARIANTS RP62 SER-13 AND HIS-130, AND VARIANT LEU-325. RC TISSUE=Retina; RX PubMed=21835304; DOI=10.1016/j.ajhg.2011.07.005; RA Ozgul R.K., Siemiatkowska A.M., Yucel D., Myers C.A., Collin R.W., RA Zonneveld M.N., Beryozkin A., Banin E., Hoyng C.B., van den Born L.I., RA Bose R., Shen W., Sharon D., Cremers F.P., Klevering B.J., RA den Hollander A.I., Corbo J.C.; RT "Exome sequencing and cis-regulatory mapping identify mutations in MAK, a RT gene encoding a regulator of ciliary length, as a cause of retinitis RT pigmentosa."; RL Am. J. Hum. Genet. 89:253-264(2011). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORM 2), RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INVOLVEMENT IN RP62. RC TISSUE=Retina; RX PubMed=21825139; DOI=10.1073/pnas.1108918108; RA Tucker B.A., Scheetz T.E., Mullins R.F., DeLuca A.P., Hoffmann J.M., RA Johnston R.M., Jacobson S.G., Sheffield V.C., Stone E.M.; RT "Exome sequencing and analysis of induced pluripotent stem cells identify RT the cilia-related gene male germ cell-associated kinase (MAK) as a cause of RT retinitis pigmentosa."; RL Proc. Natl. Acad. Sci. U.S.A. 108:E569-E576(2011). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Retinoblastoma; RX PubMed=21697133; DOI=10.1167/iovs.11-7479; RA Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S., RA Usami R., Ohtoko K., Kato S.; RT "Full-length transcriptome analysis of human retina-derived cell lines RT ARPE-19 and Y79 using the vector-capping method."; RL Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 121-163. RX PubMed=2183027; DOI=10.1128/mcb.10.5.2261-2268.1990; RA Matsushime H., Jinno A., Takagi N., Shibuya M.; RT "A novel mammalian protein kinase gene (mak) is highly expressed in RT testicular germ cells at and after meiosis."; RL Mol. Cell. Biol. 10:2261-2268(1990). RN [8] RP FUNCTION, INTERACTION WITH AR, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=16951154; DOI=10.1158/0008-5472.can-06-1636; RA Ma A.H., Xia L., Desai S.J., Boucher D.L., Guan Y., Shih H.M., Shi X.B., RA deVere White R.W., Chen H.W., Tepper C.G., Kung H.J.; RT "Male germ cell-associated kinase, a male-specific kinase regulated by RT androgen, is a coactivator of androgen receptor in prostate cancer cells."; RL Cancer Res. 66:8439-8447(2006). RN [9] RP FUNCTION, INTERACTION WITH CDK20 AND FZR1, CATALYTIC ACTIVITY, COFACTOR, RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-157 AND TYR-159, AND RP MUTAGENESIS OF THR-157 AND TYR-159. RX PubMed=21986944; DOI=10.1038/onc.2011.464; RA Wang L.Y., Kung H.J.; RT "Male germ cell-associated kinase is overexpressed in prostate cancer cells RT and causes mitotic defects via deregulation of APC/C(CDH1)."; RL Oncogene 31:2907-2918(2012). RN [10] RP VARIANTS [LARGE SCALE ANALYSIS] VAL-189; PRO-272; SER-384; SER-520 AND RP LEU-550. 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 -!- FUNCTION: Essential for the regulation of ciliary length and required CC for the long-term survival of photoreceptors (By similarity). CC Phosphorylates FZR1 in a cell cycle-dependent manner. Plays a role in CC the transcriptional coactivation of AR. Could play an important CC function in spermatogenesis. May play a role in chromosomal stability CC in prostate cancer cells. {ECO:0000250, ECO:0000269|PubMed:12084720, CC ECO:0000269|PubMed:16951154, ECO:0000269|PubMed:21986944}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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:12084720, ECO:0000269|PubMed:21986944}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000269|PubMed:12084720, ECO:0000269|PubMed:21986944}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:12084720, ECO:0000269|PubMed:21986944}; CC -!- SUBUNIT: Interacts with RP1 (By similarity). Interacts with AR and CC CDK20. Found in a complex containing MAK, AR and NCOA3. Interacts with CC FZR1 (via WD repeats). {ECO:0000250, ECO:0000269|PubMed:16951154, CC ECO:0000269|PubMed:21986944}. CC -!- INTERACTION: CC P20794; P10275: AR; NbExp=5; IntAct=EBI-3911321, EBI-608057; CC P20794; Q9UM11: FZR1; NbExp=7; IntAct=EBI-3911321, EBI-724997; CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. CC Midbody. Cell projection, cilium, photoreceptor outer segment CC {ECO:0000250}. Photoreceptor inner segment. Note=Localized in both the CC connecting cilia and the outer segment axonemes (By similarity). CC Localized uniformly in nuclei during interphase, to the mitotic spindle CC and centrosomes during metaphase and anaphase, and also to midbody at CC anaphase until telophase. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P20794-1; Sequence=Displayed; CC Name=2; CC IsoId=P20794-2; Sequence=VSP_042470; CC Name=3; CC IsoId=P20794-3; Sequence=VSP_042471; CC -!- TISSUE SPECIFICITY: Expressed in prostate cancer cell lines at CC generally higher levels than in normal prostate epithelial cell lines. CC Isoform 1 is expressed in kidney, testis, lung, trachea, and retina. CC Isoform 2 is retina-specific where it is expressed in rod and cone CC photoreceptors. {ECO:0000269|PubMed:12084720, CC ECO:0000269|PubMed:21825139}. CC -!- INDUCTION: Up-regulated by dihydrotestosterone (DHT) in androgen- CC sensitive LNCaP prostate cancer cells in a dose-dependent manner. Up- CC regulation by DHT is transient, reaching maximum levels after 24 hours CC and decreases slightly after 48 hours. {ECO:0000269|PubMed:12084720}. CC -!- PTM: Autophosphorylated. Phosphorylated on serine and threonine CC residues. {ECO:0000269|PubMed:12084720, ECO:0000269|PubMed:21986944}. CC -!- DISEASE: Retinitis pigmentosa 62 (RP62) [MIM:614181]: A retinal CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis CC pigmentosa is characterized by retinal pigment deposits visible on CC fundus examination and primary loss of rod photoreceptor cells followed CC by secondary loss of cone photoreceptors. Patients typically have night CC vision blindness and loss of midperipheral visual field. As their CC condition progresses, they lose their far peripheral visual field and CC eventually central vision as well. {ECO:0000269|PubMed:21825139, CC ECO:0000269|PubMed:21835304}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF505623; AAN16405.1; -; mRNA. DR EMBL; JN226411; AEL29206.1; -; mRNA. DR EMBL; AB593146; BAJ84080.1; -; mRNA. DR EMBL; AL024498; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471087; EAW55283.1; -; Genomic_DNA. DR EMBL; M35863; AAA36195.1; -; Genomic_DNA. DR CCDS; CCDS4516.1; -. [P20794-1] DR CCDS; CCDS75398.1; -. [P20794-3] DR CCDS; CCDS75399.1; -. [P20794-2] DR PIR; B34711; B34711. DR RefSeq; NP_001229314.1; NM_001242385.2. [P20794-3] DR RefSeq; NP_001229886.1; NM_001242957.3. [P20794-2] DR RefSeq; NP_005897.1; NM_005906.6. [P20794-1] DR RefSeq; XP_011512921.1; XM_011514619.3. [P20794-2] DR RefSeq; XP_011512922.1; XM_011514620.3. [P20794-2] DR RefSeq; XP_011512924.1; XM_011514622.4. [P20794-3] DR RefSeq; XP_054211408.1; XM_054355433.1. [P20794-2] DR RefSeq; XP_054211409.1; XM_054355434.1. [P20794-2] DR RefSeq; XP_054211410.1; XM_054355435.1. [P20794-3] DR AlphaFoldDB; P20794; -. DR SMR; P20794; -. DR BioGRID; 110291; 63. DR CORUM; P20794; -. DR FunCoup; P20794; 867. DR IntAct; P20794; 35. DR NDEx; IQUERY-CP-MAK; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000346484; -. DR BindingDB; P20794; -. DR ChEMBL; CHEMBL1163106; -. DR iPTMnet; P20794; -. DR PhosphoSitePlus; P20794; -. DR BioMuta; MAK; -. DR DMDM; 13432166; -. DR jPOST; P20794; -. DR MassIVE; P20794; -. DR PaxDb; 9606-ENSP00000346484; -. DR PeptideAtlas; P20794; -. DR ProteomicsDB; 53787; -. [P20794-1] DR ProteomicsDB; 53788; -. [P20794-2] DR ProteomicsDB; 53789; -. [P20794-3] DR Antibodypedia; 24855; 446 antibodies from 31 providers. DR DNASU; 4117; -. DR Ensembl; ENST00000313243.6; ENSP00000313021.2; ENSG00000111837.12. [P20794-1] DR Ensembl; ENST00000354489.7; ENSP00000346484.3; ENSG00000111837.12. [P20794-2] DR Ensembl; ENST00000474039.5; ENSP00000476067.1; ENSG00000111837.12. [P20794-1] DR Ensembl; ENST00000536370.6; ENSP00000442221.2; ENSG00000111837.12. [P20794-3] DR GeneID; 4117; -. DR KEGG; hsa:4117; -. DR MANE-Select; ENST00000354489.7; ENSP00000346484.3; NM_001242957.3; NP_001229886.1. [P20794-2] DR UCSC; uc003mzm.4; human. [P20794-1] DR AGR; HGNC:6816; -. DR ClinPGx; PA30564; -. DR CTD; 4117; -. DR DisGeNET; 4117; -. DR GeneCards; MAK; -. DR GeneReviews; MAK; -. DR HGNC; HGNC:6816; MAK. DR HPA; ENSG00000111837; Tissue enriched (retina). DR MalaCards; MAK; -. DR MIM; 154235; gene. DR MIM; 614181; phenotype. DR OpenTargets; ENSG00000111837; -. DR Orphanet; 791; Retinitis pigmentosa. DR VEuPathDB; HostDB:ENSG00000111837; -. DR eggNOG; KOG0661; Eukaryota. DR GeneTree; ENSGT00940000156581; -. DR InParanoid; P20794; -. DR OMA; MASEYTW; -. DR OrthoDB; 2158884at2759; -. DR PAN-GO; P20794; 7 GO annotations based on evolutionary models. DR PhylomeDB; P20794; -. DR BRENDA; 2.7.11.22; 2681. DR PathwayCommons; P20794; -. DR SignaLink; P20794; -. DR SIGNOR; P20794; -. DR Agora; ENSG00000111837; -. DR BioGRID-ORCS; 4117; 19 hits in 1184 CRISPR screens. DR ChiTaRS; MAK; human. DR GeneWiki; MAK_(gene); -. DR GenomeRNAi; 4117; -. DR Pharos; P20794; Tchem. DR PRO; PR:P20794; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P20794; protein. DR Bgee; ENSG00000111837; Expressed in sperm and 117 other cell types or tissues. DR ExpressionAtlas; P20794; baseline and differential. DR GO; GO:0005930; C:axoneme; IEA:Ensembl. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005929; C:cilium; IBA:GO_Central. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB. DR GO; GO:0031514; C:motile cilium; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl. DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB. DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004672; F:protein kinase activity; NAS:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; EXP:UniProtKB. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0042073; P:intraciliary transport; IBA:GO_Central. DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:UniProtKB. DR GO; GO:0046777; P:protein autophosphorylation; IMP:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; NAS:UniProtKB. DR CDD; cd07830; STKc_MAK_like; 1. DR FunFam; 1.10.510.10:FF:000104; serine/threonine-protein kinase MAK isoform X1; 1. DR FunFam; 3.30.200.20:FF:000071; serine/threonine-protein kinase MAK isoform X1; 1. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR050117; MAPK. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; Cilium; Cytoplasm; KW Cytoskeleton; Developmental protein; Differentiation; Disease variant; KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus; KW Phosphoprotein; Proteomics identification; Reference proteome; KW Retinitis pigmentosa; Serine/threonine-protein kinase; Spermatogenesis; KW Transcription; Transcription regulation; Transferase. FT CHAIN 1..623 FT /note="Serine/threonine-protein kinase MAK" FT /id="PRO_0000086284" FT DOMAIN 4..284 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 328..396 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 416..469 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 356..369 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 446..455 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 125 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 MOD_RES 157 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:21986944" FT MOD_RES 159 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:21986944" FT VAR_SEQ 532 FT /note="A -> AEESIIKPIEKLSCNETFPEKLEDPQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:21825139, FT ECO:0000303|PubMed:21835304" FT /id="VSP_042470" FT VAR_SEQ 533..572 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:21697133" FT /id="VSP_042471" FT VARIANT 13 FT /note="G -> S (in RP62; results in a complete loss of FT kinase activity compared to wild-type; dbSNP:rs387906647)" FT /evidence="ECO:0000269|PubMed:21835304" FT /id="VAR_066988" FT VARIANT 27 FT /note="G -> R (in RP62; dbSNP:rs754916169)" FT /evidence="ECO:0000269|PubMed:21835304" FT /id="VAR_066989" FT VARIANT 130 FT /note="N -> H (in RP62; results in a complete loss of FT kinase activity compared to wild-type; dbSNP:rs387906646)" FT /evidence="ECO:0000269|PubMed:21835304" FT /id="VAR_066990" FT VARIANT 166 FT /note="R -> H (in RP62; dbSNP:rs387906648)" FT /evidence="ECO:0000269|PubMed:21835304" FT /id="VAR_066991" FT VARIANT 181 FT /note="I -> T (in RP62; dbSNP:rs750559316)" FT /evidence="ECO:0000269|PubMed:21835304" FT /id="VAR_066992" FT VARIANT 189 FT /note="I -> V (in dbSNP:rs56215624)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042006" FT VARIANT 272 FT /note="R -> P (in a breast infiltrating ductal carcinoma FT sample; somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042007" FT VARIANT 325 FT /note="P -> L (in dbSNP:rs371971492)" FT /evidence="ECO:0000269|PubMed:21835304" FT /id="VAR_066993" FT VARIANT 329 FT /note="D -> E (in dbSNP:rs17579447)" FT /id="VAR_053932" FT VARIANT 384 FT /note="N -> S (in dbSNP:rs55773478)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042008" FT VARIANT 520 FT /note="P -> S (in dbSNP:rs567083)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042009" FT VARIANT 550 FT /note="F -> L (in dbSNP:rs56217305)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042010" FT MUTAGEN 33 FT /note="K->R: Abolishes autophosphorylation." FT /evidence="ECO:0000269|PubMed:12084720" FT MUTAGEN 157 FT /note="T->A: Abolishes autophosphorylation and impairs FT kinase activity." FT /evidence="ECO:0000269|PubMed:21986944" FT MUTAGEN 159 FT /note="Y->F: Abolishes autophosphorylation and impairs FT kinase activity." FT /evidence="ECO:0000269|PubMed:21986944" SQ SEQUENCE 623 AA; 70581 MW; 67F540266F370285 CRC64; MNRYTTMRQL GDGTYGSVLM GKSNESGELV AIKRMKRKFY SWDECMNLRE VKSLKKLNHA NVIKLKEVIR ENDHLYFIFE YMKENLYQLM KDRNKLFPES VIRNIMYQIL QGLAFIHKHG FFHRDMKPEN LLCMGPELVK IADFGLAREL RSQPPYTDYV STRWYRAPEV LLRSSVYSSP IDVWAVGSIM AELYMLRPLF PGTSEVDEIF KICQVLGTPK KSDWPEGYQL ASSMNFRFPQ CVPINLKTLI PNASNEAIQL MTEMLNWDPK KRPTASQALK HPYFQVGQVL GPSSNHLESK QSLNKQLQPL ESKPSLVEVE PKPLPDIIDQ VVGQPQPKTS QQPLQPIQPP QNLSVQQPPK QQSQEKPPQT LFPSIVKNMP TKPNGTLSHK SGRRRWGQTI FKSGDSWEEL EDYDFGASHS KKPSMGVFKE KRKKDSPFRL PEPVPSGSNH STGENKSLPA VTSLKSDSEL STAPTSKQYY LKQSRYLPGV NPKKVSLIAS GKEINPHTWS NQLFPKSLGP VGAELAFKRS NAGNLGSYAT YNQSGYIPSF LKKEVQSAGQ RIHLAPLNAT ASEYTWNTKT GRGQFSGRTY NPTAKNLNIV NRAQPIPSVH GRTDWVAKYG GHR //