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P20794

- MAK_HUMAN

UniProt

P20794 - MAK_HUMAN

Protein

Serine/threonine-protein kinase MAK

Gene

MAK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (27 Apr 2001)
      Previous versions | rss
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    Functioni

    Essential for the regulation of ciliary length and required for the long-term survival of photoreceptors By similarity. Phosphorylates FZR1 in a cell cycle-dependent manner. Plays a role in the transcriptional coactivation of AR. Could play an important function in spermatogenesis. May play a role in chromosomal stability in prostate cancer cells.By similarity3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei33 – 331ATPPROSITE-ProRule annotation
    Active sitei125 – 1251Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 189ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
    3. protein binding Source: UniProtKB
    4. protein kinase activity Source: UniProtKB
    5. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. multicellular organismal development Source: UniProtKB-KW
    3. photoreceptor cell maintenance Source: UniProtKB
    4. protein autophosphorylation Source: UniProtKB
    5. protein phosphorylation Source: UniProtKB
    6. regulation of transcription, DNA-templated Source: UniProtKB-KW
    7. spermatogenesis Source: UniProtKB
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Differentiation, Spermatogenesis, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.22. 2681.
    SignaLinkiP20794.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase MAK (EC:2.7.11.22)
    Alternative name(s):
    Male germ cell-associated kinase
    Gene namesi
    Name:MAK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:6816. MAK.

    Subcellular locationi

    Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle. Midbody. Cell projectionciliumphotoreceptor outer segment By similarity. Photoreceptor inner segment
    Note: Localized in both the connecting cilia and the outer segment axonemes By similarity. Localized uniformly in nuclei during interphase, to the mitotic spindle and centrosomes during metaphase and anaphase, and also to midbody at anaphase until telophase.By similarity

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB-KW
    3. midbody Source: UniProtKB
    4. mitotic spindle Source: UniProtKB
    5. nucleus Source: UniProtKB
    6. photoreceptor inner segment Source: UniProtKB
    7. photoreceptor outer segment Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cilium, Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Retinitis pigmentosa 62 (RP62) [MIM:614181]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti13 – 131G → S in RP62; results in a complete loss of kinase activity compared to wild-type. 1 Publication
    VAR_066988
    Natural varianti27 – 271G → R in RP62. 1 Publication
    VAR_066989
    Natural varianti130 – 1301N → H in RP62; results in a complete loss of kinase activity compared to wild-type. 1 Publication
    VAR_066990
    Natural varianti166 – 1661R → H in RP62. 1 Publication
    VAR_066991
    Natural varianti181 – 1811I → T in RP62. 1 Publication
    VAR_066992

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi33 – 331K → R: Abolishes autophosphorylation. 1 Publication
    Mutagenesisi157 – 1571T → A: Abolishes autophosphorylation and impairs kinase activity. 1 Publication
    Mutagenesisi159 – 1591Y → F: Abolishes autophosphorylation and impairs kinase activity. 1 Publication

    Keywords - Diseasei

    Disease mutation, Retinitis pigmentosa

    Organism-specific databases

    MIMi614181. phenotype.
    Orphaneti791. Retinitis pigmentosa.
    PharmGKBiPA30564.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 623623Serine/threonine-protein kinase MAKPRO_0000086284Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei157 – 1571Phosphothreonine; by autocatalysis2 Publications
    Modified residuei159 – 1591Phosphotyrosine; by autocatalysis2 Publications

    Post-translational modificationi

    Autophosphorylated. Phosphorylated on serine and threonine residues.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP20794.
    PRIDEiP20794.

    PTM databases

    PhosphoSiteiP20794.

    Expressioni

    Tissue specificityi

    Expressed in prostate cancer cell lines at generally higher levels than in normal prostate epithelial cell lines. Isoform 1 is expressed in kidney, testis, lung, trachea, and retina. Isoform 2 is retina-specific where it is expressed in rod and cone photoreceptors.2 Publications

    Inductioni

    Up-regulated by dihydrotestosterone (DHT) in androgen-sensitive LNCaP prostate cancer cells in a dose-dependent manner. Up-regulation by DHT is transient, reaching maximum levels after 24 hours and decreases slightly after 48 hours.1 Publication

    Gene expression databases

    ArrayExpressiP20794.
    BgeeiP20794.
    CleanExiHS_MAK.
    GenevestigatoriP20794.

    Organism-specific databases

    HPAiHPA039092.

    Interactioni

    Subunit structurei

    Interacts with RP1 By similarity. Interacts with AR and CDK20. Found in a complex containing MAK, AR and NCOA3. Interacts with FZR1 (via WD repeats).By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARP102755EBI-3911321,EBI-608057
    FZR1Q9UM117EBI-3911321,EBI-724997

    Protein-protein interaction databases

    BioGridi110291. 10 interactions.
    IntActiP20794. 11 interactions.
    STRINGi9606.ENSP00000313021.

    Structurei

    3D structure databases

    ProteinModelPortaliP20794.
    SMRiP20794. Positions 1-285.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 284281Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi309 – 36860Glu/Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233024.
    HOVERGENiHBG014652.
    InParanoidiP20794.
    KOiK08829.
    OMAiYATYNQS.
    OrthoDBiEOG7NCV37.
    PhylomeDBiP20794.
    TreeFamiTF328769.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P20794-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNRYTTMRQL GDGTYGSVLM GKSNESGELV AIKRMKRKFY SWDECMNLRE    50
    VKSLKKLNHA NVIKLKEVIR ENDHLYFIFE YMKENLYQLM KDRNKLFPES 100
    VIRNIMYQIL QGLAFIHKHG FFHRDMKPEN LLCMGPELVK IADFGLAREL 150
    RSQPPYTDYV STRWYRAPEV LLRSSVYSSP IDVWAVGSIM AELYMLRPLF 200
    PGTSEVDEIF KICQVLGTPK KSDWPEGYQL ASSMNFRFPQ CVPINLKTLI 250
    PNASNEAIQL MTEMLNWDPK KRPTASQALK HPYFQVGQVL GPSSNHLESK 300
    QSLNKQLQPL ESKPSLVEVE PKPLPDIIDQ VVGQPQPKTS QQPLQPIQPP 350
    QNLSVQQPPK QQSQEKPPQT LFPSIVKNMP TKPNGTLSHK SGRRRWGQTI 400
    FKSGDSWEEL EDYDFGASHS KKPSMGVFKE KRKKDSPFRL PEPVPSGSNH 450
    STGENKSLPA VTSLKSDSEL STAPTSKQYY LKQSRYLPGV NPKKVSLIAS 500
    GKEINPHTWS NQLFPKSLGP VGAELAFKRS NAGNLGSYAT YNQSGYIPSF 550
    LKKEVQSAGQ RIHLAPLNAT ASEYTWNTKT GRGQFSGRTY NPTAKNLNIV 600
    NRAQPIPSVH GRTDWVAKYG GHR 623
    Length:623
    Mass (Da):70,581
    Last modified:April 27, 2001 - v2
    Checksum:i67F540266F370285
    GO
    Isoform 2 (identifier: P20794-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         532-532: A → AEESIIKPIEKLSCNETFPEKLEDPQ

    Show »
    Length:648
    Mass (Da):73,480
    Checksum:iFDF1DD3370B51062
    GO
    Isoform 3 (identifier: P20794-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         533-572: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:583
    Mass (Da):66,345
    Checksum:i683A5629058D81D2
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti13 – 131G → S in RP62; results in a complete loss of kinase activity compared to wild-type. 1 Publication
    VAR_066988
    Natural varianti27 – 271G → R in RP62. 1 Publication
    VAR_066989
    Natural varianti130 – 1301N → H in RP62; results in a complete loss of kinase activity compared to wild-type. 1 Publication
    VAR_066990
    Natural varianti166 – 1661R → H in RP62. 1 Publication
    VAR_066991
    Natural varianti181 – 1811I → T in RP62. 1 Publication
    VAR_066992
    Natural varianti189 – 1891I → V.1 Publication
    Corresponds to variant rs56215624 [ dbSNP | Ensembl ].
    VAR_042006
    Natural varianti272 – 2721R → P in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication
    VAR_042007
    Natural varianti325 – 3251P → L.1 Publication
    VAR_066993
    Natural varianti329 – 3291D → E.
    Corresponds to variant rs17579447 [ dbSNP | Ensembl ].
    VAR_053932
    Natural varianti384 – 3841N → S.1 Publication
    Corresponds to variant rs55773478 [ dbSNP | Ensembl ].
    VAR_042008
    Natural varianti520 – 5201P → S.1 Publication
    Corresponds to variant rs567083 [ dbSNP | Ensembl ].
    VAR_042009
    Natural varianti550 – 5501F → L.1 Publication
    Corresponds to variant rs56217305 [ dbSNP | Ensembl ].
    VAR_042010

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei532 – 5321A → AEESIIKPIEKLSCNETFPE KLEDPQ in isoform 2. 2 PublicationsVSP_042470
    Alternative sequencei533 – 57240Missing in isoform 3. 1 PublicationVSP_042471Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF505623 mRNA. Translation: AAN16405.1.
    JN226411 mRNA. Translation: AEL29206.1.
    AB593146 mRNA. Translation: BAJ84080.1.
    AL024498 Genomic DNA. Translation: CAB75823.1.
    CH471087 Genomic DNA. Translation: EAW55283.1.
    M35863 Genomic DNA. Translation: AAA36195.1.
    CCDSiCCDS4516.1. [P20794-1]
    PIRiB34711.
    RefSeqiNP_001229314.1. NM_001242385.1. [P20794-3]
    NP_001229886.1. NM_001242957.1. [P20794-2]
    NP_005897.1. NM_005906.4. [P20794-1]
    UniGeneiHs.446125.

    Genome annotation databases

    EnsembliENST00000313243; ENSP00000313021; ENSG00000111837. [P20794-1]
    ENST00000354489; ENSP00000346484; ENSG00000111837. [P20794-1]
    ENST00000474039; ENSP00000476067; ENSG00000111837. [P20794-1]
    GeneIDi4117.
    KEGGihsa:4117.
    UCSCiuc003mzm.3. human. [P20794-1]
    uc021ylk.1. human. [P20794-2]
    uc021yll.1. human. [P20794-3]

    Polymorphism databases

    DMDMi13432166.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF505623 mRNA. Translation: AAN16405.1 .
    JN226411 mRNA. Translation: AEL29206.1 .
    AB593146 mRNA. Translation: BAJ84080.1 .
    AL024498 Genomic DNA. Translation: CAB75823.1 .
    CH471087 Genomic DNA. Translation: EAW55283.1 .
    M35863 Genomic DNA. Translation: AAA36195.1 .
    CCDSi CCDS4516.1. [P20794-1 ]
    PIRi B34711.
    RefSeqi NP_001229314.1. NM_001242385.1. [P20794-3 ]
    NP_001229886.1. NM_001242957.1. [P20794-2 ]
    NP_005897.1. NM_005906.4. [P20794-1 ]
    UniGenei Hs.446125.

    3D structure databases

    ProteinModelPortali P20794.
    SMRi P20794. Positions 1-285.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110291. 10 interactions.
    IntActi P20794. 11 interactions.
    STRINGi 9606.ENSP00000313021.

    Chemistry

    BindingDBi P20794.
    ChEMBLi CHEMBL1163106.
    GuidetoPHARMACOLOGYi 2061.

    PTM databases

    PhosphoSitei P20794.

    Polymorphism databases

    DMDMi 13432166.

    Proteomic databases

    PaxDbi P20794.
    PRIDEi P20794.

    Protocols and materials databases

    DNASUi 4117.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313243 ; ENSP00000313021 ; ENSG00000111837 . [P20794-1 ]
    ENST00000354489 ; ENSP00000346484 ; ENSG00000111837 . [P20794-1 ]
    ENST00000474039 ; ENSP00000476067 ; ENSG00000111837 . [P20794-1 ]
    GeneIDi 4117.
    KEGGi hsa:4117.
    UCSCi uc003mzm.3. human. [P20794-1 ]
    uc021ylk.1. human. [P20794-2 ]
    uc021yll.1. human. [P20794-3 ]

    Organism-specific databases

    CTDi 4117.
    GeneCardsi GC06M010820.
    GeneReviewsi MAK.
    HGNCi HGNC:6816. MAK.
    HPAi HPA039092.
    MIMi 154235. gene.
    614181. phenotype.
    neXtProti NX_P20794.
    Orphaneti 791. Retinitis pigmentosa.
    PharmGKBi PA30564.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233024.
    HOVERGENi HBG014652.
    InParanoidi P20794.
    KOi K08829.
    OMAi YATYNQS.
    OrthoDBi EOG7NCV37.
    PhylomeDBi P20794.
    TreeFami TF328769.

    Enzyme and pathway databases

    BRENDAi 2.7.11.22. 2681.
    SignaLinki P20794.

    Miscellaneous databases

    GeneWikii MAK_(gene).
    GenomeRNAii 4117.
    NextBioi 16166.
    PROi P20794.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20794.
    Bgeei P20794.
    CleanExi HS_MAK.
    Genevestigatori P20794.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of human male germ cell-associated kinase, a kinase transcriptionally activated by androgen in prostate cancer cells."
      Xia L., Robinson D., Ma A.H., Chen H.C., Wu F., Qiu Y., Kung H.J.
      J. Biol. Chem. 277:35422-35433(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AUTOPHOSPHORYLATION, PHOSPHORYLATION, MUTAGENESIS OF LYS-33.
      Tissue: Testis.
    2. "Exome sequencing and cis-regulatory mapping identify mutations in MAK, a gene encoding a regulator of ciliary length, as a cause of retinitis pigmentosa."
      Ozgul R.K., Siemiatkowska A.M., Yucel D., Myers C.A., Collin R.W., Zonneveld M.N., Beryozkin A., Banin E., Hoyng C.B., van den Born L.I., Bose R., Shen W., Sharon D., Cremers F.P., Klevering B.J., den Hollander A.I., Corbo J.C.
      Am. J. Hum. Genet. 89:253-264(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORM 2), VARIANTS RP62 SER-13; ARG-27; HIS-130; HIS-166 AND THR-181, CHARACTERIZATION OF VARIANTS RP62 SER-13 AND HIS-130, VARIANT LEU-325.
      Tissue: Retina.
    3. "Exome sequencing and analysis of induced pluripotent stem cells identify the cilia-related gene male germ cell-associated kinase (MAK) as a cause of retinitis pigmentosa."
      Tucker B.A., Scheetz T.E., Mullins R.F., DeLuca A.P., Hoffmann J.M., Johnston R.M., Jacobson S.G., Sheffield V.C., Stone E.M.
      Proc. Natl. Acad. Sci. U.S.A. 108:E569-E576(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN RP62.
      Tissue: Retina.
    4. "Full-length transcriptome analysis of human retina-derived cell lines ARPE-19 and Y79 using the vector-capping method."
      Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S., Usami R., Ohtoko K., Kato S.
      Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Retinoblastoma.
    5. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "A novel mammalian protein kinase gene (mak) is highly expressed in testicular germ cells at and after meiosis."
      Matsushime H., Jinno A., Takagi N., Shibuya M.
      Mol. Cell. Biol. 10:2261-2268(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 121-163.
    8. "Male germ cell-associated kinase, a male-specific kinase regulated by androgen, is a coactivator of androgen receptor in prostate cancer cells."
      Ma A.H., Xia L., Desai S.J., Boucher D.L., Guan Y., Shih H.M., Shi X.B., deVere White R.W., Chen H.W., Tepper C.G., Kung H.J.
      Cancer Res. 66:8439-8447(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AR, SUBUNIT, SUBCELLULAR LOCATION.
    9. "Male germ cell-associated kinase is overexpressed in prostate cancer cells and causes mitotic defects via deregulation of APC/C(CDH1)."
      Wang L.Y., Kung H.J.
      Oncogene 31:2907-2918(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CDK20 AND FZR1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-157 AND TYR-159, MUTAGENESIS OF THR-157 AND TYR-159.
    10. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-189; PRO-272; SER-384; SER-520 AND LEU-550.

    Entry informationi

    Entry nameiMAK_HUMAN
    AccessioniPrimary (citable) accession number: P20794
    Secondary accession number(s): F1T0K6
    , G1FL29, Q547D0, Q9NUH7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: April 27, 2001
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3