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P20794

- MAK_HUMAN

UniProt

P20794 - MAK_HUMAN

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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

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 kinase activity Source: UniProtKB
  4. 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
Complete GO annotation...

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
Complete GO annotation...

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 autocatalysis1 Publication
Modified residuei159 – 1591Phosphotyrosine; by autocatalysis1 Publication

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

BgeeiP20794.
CleanExiHS_MAK.
ExpressionAtlasiP20794. baseline and differential.
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. 11 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.
GeneTreeiENSGT00650000093283.
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.
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

        10         20         30         40         50
MNRYTTMRQL GDGTYGSVLM GKSNESGELV AIKRMKRKFY SWDECMNLRE
60 70 80 90 100
VKSLKKLNHA NVIKLKEVIR ENDHLYFIFE YMKENLYQLM KDRNKLFPES
110 120 130 140 150
VIRNIMYQIL QGLAFIHKHG FFHRDMKPEN LLCMGPELVK IADFGLAREL
160 170 180 190 200
RSQPPYTDYV STRWYRAPEV LLRSSVYSSP IDVWAVGSIM AELYMLRPLF
210 220 230 240 250
PGTSEVDEIF KICQVLGTPK KSDWPEGYQL ASSMNFRFPQ CVPINLKTLI
260 270 280 290 300
PNASNEAIQL MTEMLNWDPK KRPTASQALK HPYFQVGQVL GPSSNHLESK
310 320 330 340 350
QSLNKQLQPL ESKPSLVEVE PKPLPDIIDQ VVGQPQPKTS QQPLQPIQPP
360 370 380 390 400
QNLSVQQPPK QQSQEKPPQT LFPSIVKNMP TKPNGTLSHK SGRRRWGQTI
410 420 430 440 450
FKSGDSWEEL EDYDFGASHS KKPSMGVFKE KRKKDSPFRL PEPVPSGSNH
460 470 480 490 500
STGENKSLPA VTSLKSDSEL STAPTSKQYY LKQSRYLPGV NPKKVSLIAS
510 520 530 540 550
GKEINPHTWS NQLFPKSLGP VGAELAFKRS NAGNLGSYAT YNQSGYIPSF
560 570 580 590 600
LKKEVQSAGQ RIHLAPLNAT ASEYTWNTKT GRGQFSGRTY NPTAKNLNIV
610 620
NRAQPIPSVH GRTDWVAKYG GHR
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]
CCDS75398.1. [P20794-3]
CCDS75399.1. [P20794-2]
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. [P20794-2]
ENST00000474039; ENSP00000476067; ENSG00000111837. [P20794-1]
ENST00000536370; ENSP00000442221; ENSG00000111837. [P20794-3]
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 ]
CCDS75398.1. [P20794-3 ]
CCDS75399.1. [P20794-2 ]
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. 11 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 . [P20794-2 ]
ENST00000474039 ; ENSP00000476067 ; ENSG00000111837 . [P20794-1 ]
ENST00000536370 ; ENSP00000442221 ; ENSG00000111837 . [P20794-3 ]
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.
GeneTreei ENSGT00650000093283.
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

Bgeei P20794.
CleanExi HS_MAK.
ExpressionAtlasi P20794. baseline and differential.
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.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 135 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