P20794 (MAK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase MAK
EC=2.7.11.22

Alternative name(s):
Male germ cell-associated kinase

Gene names

Name:

MAK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	623 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.8 Ref.9
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	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). Ref.8 Ref.9
Subcellular location	Nucleus. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle. Midbody. Cell projection › cilium › photoreceptor 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. Ref.1 Ref.3 Ref.8 Ref.9
Tissue specificity	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. Ref.1 Ref.3
Induction	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. Ref.1
Post-translational modification	Autophosphorylated. Phosphorylated on serine and threonine residues. Ref.1 Ref.9
Involvement in disease	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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.3
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Differentiation Spermatogenesis Transcription Transcription regulation
Cellular component	Cell projection Cilium Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Retinitis pigmentosa
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW photoreceptor cell maintenance Inferred from sequence or structural similarity. Source: UniProtKB protein autophosphorylation Inferred from mutant phenotype Ref.9. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW spermatogenesis Non-traceable author statement Ref.7. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	centrosome Inferred from direct assay Ref.9. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW midbody Inferred from direct assay Ref.9. Source: UniProtKB mitotic spindle Inferred from direct assay Ref.9. Source: UniProtKB nucleus Inferred from direct assay Ref.1. Source: UniProtKB photoreceptor inner segment Inferred from direct assay Ref.3. Source: UniProtKB photoreceptor outer segment Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Non-traceable author statement. Source: UniProtKB cyclin-dependent protein serine/threonine kinase activity Inferred from electronic annotation. Source: EC protein kinase activity Non-traceable author statement Ref.7. Source: UniProtKB transcription coactivator activity Inferred from direct assay Ref.8. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AR	P10275	5	EBI-3911321,EBI-608057
FZR1	Q9UM11	7	EBI-3911321,EBI-724997

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P20794-1)

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.

Isoform 2 (identifier: P20794-2)

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

Isoform 3 (identifier: P20794-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 623	623	Serine/threonine-protein kinase MAK		PRO_0000086284
Regions
	Domain	4 – 284	281	Protein kinase
	Nucleotide binding	10 – 18	9	ATP By similarity
	Compositional bias	309 – 368	60	Glu/Pro-rich
Sites
	Active site	125	1	Proton acceptor By similarity
	Binding site	33	1	ATP By similarity
Amino acid modifications
	Modified residue	157	1	Phosphothreonine; by autocatalysis Ref.9
	Modified residue	159	1	Phosphotyrosine; by autocatalysis Ref.9
Natural variations
	Alternative sequence	532	1	A → AEESIIKPIEKLSCNETFPE KLEDPQ in isoform 2.		VSP_042470
	Alternative sequence	533 – 572	40	Missing in isoform 3.		VSP_042471
	Natural variant	13	1	G → S in RP62; results in a complete loss of kinase activity compared to wild-type. Ref.2		VAR_066988
	Natural variant	27	1	G → R in RP62. Ref.2		VAR_066989
	Natural variant	130	1	N → H in RP62; results in a complete loss of kinase activity compared to wild-type. Ref.2		VAR_066990
	Natural variant	166	1	R → H in RP62. Ref.2		VAR_066991
	Natural variant	181	1	I → T in RP62. Ref.2		VAR_066992
	Natural variant	189	1	I → V. Ref.10 Corresponds to variant rs56215624 [ dbSNP | Ensembl ].		VAR_042006
	Natural variant	272	1	R → P in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.10		VAR_042007
	Natural variant	325	1	P → L. Ref.2		VAR_066993
	Natural variant	329	1	D → E. Corresponds to variant rs17579447 [ dbSNP | Ensembl ].		VAR_053932
	Natural variant	384	1	N → S. Ref.10 Corresponds to variant rs55773478 [ dbSNP | Ensembl ].		VAR_042008
	Natural variant	520	1	P → S. Ref.10 Corresponds to variant rs567083 [ dbSNP | Ensembl ].		VAR_042009
	Natural variant	550	1	F → L. Ref.10 Corresponds to variant rs56217305 [ dbSNP | Ensembl ].		VAR_042010
Experimental info
	Mutagenesis	33	1	K → R: Abolishes autophosphorylation. Ref.1
	Mutagenesis	157	1	T → A: Abolishes autophosphorylation and impairs kinase activity. Ref.9
	Mutagenesis	159	1	Y → F: Abolishes autophosphorylation and impairs kinase activity. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 27, 2001. Version 2. Checksum: 67F540266F370285	FASTA	623	70,581
	10 20 30 40 50 60 MNRYTTMRQL GDGTYGSVLM GKSNESGELV AIKRMKRKFY SWDECMNLRE VKSLKKLNHA 70 80 90 100 110 120 NVIKLKEVIR ENDHLYFIFE YMKENLYQLM KDRNKLFPES VIRNIMYQIL QGLAFIHKHG 130 140 150 160 170 180 FFHRDMKPEN LLCMGPELVK IADFGLAREL RSQPPYTDYV STRWYRAPEV LLRSSVYSSP 190 200 210 220 230 240 IDVWAVGSIM AELYMLRPLF PGTSEVDEIF KICQVLGTPK KSDWPEGYQL ASSMNFRFPQ 250 260 270 280 290 300 CVPINLKTLI PNASNEAIQL MTEMLNWDPK KRPTASQALK HPYFQVGQVL GPSSNHLESK 310 320 330 340 350 360 QSLNKQLQPL ESKPSLVEVE PKPLPDIIDQ VVGQPQPKTS QQPLQPIQPP QNLSVQQPPK 370 380 390 400 410 420 QQSQEKPPQT LFPSIVKNMP TKPNGTLSHK SGRRRWGQTI FKSGDSWEEL EDYDFGASHS 430 440 450 460 470 480 KKPSMGVFKE KRKKDSPFRL PEPVPSGSNH STGENKSLPA VTSLKSDSEL STAPTSKQYY 490 500 510 520 530 540 LKQSRYLPGV NPKKVSLIAS GKEINPHTWS NQLFPKSLGP VGAELAFKRS NAGNLGSYAT 550 560 570 580 590 600 YNQSGYIPSF LKKEVQSAGQ RIHLAPLNAT ASEYTWNTKT GRGQFSGRTY NPTAKNLNIV 610 620 NRAQPIPSVH GRTDWVAKYG GHR
	Isoform 2 [UniParc]. Checksum: FDF1DD3370B51062	FASTA	648	73,480
	10 20 30 40 50 60 MNRYTTMRQL GDGTYGSVLM GKSNESGELV AIKRMKRKFY SWDECMNLRE VKSLKKLNHA 70 80 90 100 110 120 NVIKLKEVIR ENDHLYFIFE YMKENLYQLM KDRNKLFPES VIRNIMYQIL QGLAFIHKHG 130 140 150 160 170 180 FFHRDMKPEN LLCMGPELVK IADFGLAREL RSQPPYTDYV STRWYRAPEV LLRSSVYSSP 190 200 210 220 230 240 IDVWAVGSIM AELYMLRPLF PGTSEVDEIF KICQVLGTPK KSDWPEGYQL ASSMNFRFPQ 250 260 270 280 290 300 CVPINLKTLI PNASNEAIQL MTEMLNWDPK KRPTASQALK HPYFQVGQVL GPSSNHLESK 310 320 330 340 350 360 QSLNKQLQPL ESKPSLVEVE PKPLPDIIDQ VVGQPQPKTS QQPLQPIQPP QNLSVQQPPK 370 380 390 400 410 420 QQSQEKPPQT LFPSIVKNMP TKPNGTLSHK SGRRRWGQTI FKSGDSWEEL EDYDFGASHS 430 440 450 460 470 480 KKPSMGVFKE KRKKDSPFRL PEPVPSGSNH STGENKSLPA VTSLKSDSEL STAPTSKQYY 490 500 510 520 530 540 LKQSRYLPGV NPKKVSLIAS GKEINPHTWS NQLFPKSLGP VGAELAFKRS NAEESIIKPI 550 560 570 580 590 600 EKLSCNETFP EKLEDPQGNL GSYATYNQSG YIPSFLKKEV QSAGQRIHLA PLNATASEYT 610 620 630 640 WNTKTGRGQF SGRTYNPTAK NLNIVNRAQP IPSVHGRTDW VAKYGGHR
	Isoform 3 [UniParc]. Checksum: 683A5629058D81D2	FASTA	583	66,345
	10 20 30 40 50 60 MNRYTTMRQL GDGTYGSVLM GKSNESGELV AIKRMKRKFY SWDECMNLRE VKSLKKLNHA 70 80 90 100 110 120 NVIKLKEVIR ENDHLYFIFE YMKENLYQLM KDRNKLFPES VIRNIMYQIL QGLAFIHKHG 130 140 150 160 170 180 FFHRDMKPEN LLCMGPELVK IADFGLAREL RSQPPYTDYV STRWYRAPEV LLRSSVYSSP 190 200 210 220 230 240 IDVWAVGSIM AELYMLRPLF PGTSEVDEIF KICQVLGTPK KSDWPEGYQL ASSMNFRFPQ 250 260 270 280 290 300 CVPINLKTLI PNASNEAIQL MTEMLNWDPK KRPTASQALK HPYFQVGQVL GPSSNHLESK 310 320 330 340 350 360 QSLNKQLQPL ESKPSLVEVE PKPLPDIIDQ VVGQPQPKTS QQPLQPIQPP QNLSVQQPPK 370 380 390 400 410 420 QQSQEKPPQT LFPSIVKNMP TKPNGTLSHK SGRRRWGQTI FKSGDSWEEL EDYDFGASHS 430 440 450 460 470 480 KKPSMGVFKE KRKKDSPFRL PEPVPSGSNH STGENKSLPA VTSLKSDSEL STAPTSKQYY 490 500 510 520 530 540 LKQSRYLPGV NPKKVSLIAS GKEINPHTWS NQLFPKSLGP VGAELAFKRS NAEYTWNTKT 550 560 570 580 GRGQFSGRTY NPTAKNLNIV NRAQPIPSVH GRTDWVAKYG GHR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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, AUTOPHOSPHORYLATION 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00025489. IPI01011223.
PIR	B34711.
RefSeq	NP_001229314.1. NM_001242385.1. NP_001229886.1. NM_001242957.1. NP_005897.1. NM_005906.4.
UniGene	Hs.446125.
3D structure databases
ProteinModelPortal	P20794.
ModBase	Search...
Protein-protein interaction databases
IntAct	P20794. 10 interactions.
STRING	9606.ENSP00000313021.
PTM databases
PhosphoSite	P20794.
Polymorphism databases
DMDM	13432166.
Proteomic databases
PaxDb	P20794.
PRIDE	P20794.
Protocols and materials databases
DNASU	4117.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000313243; ENSP00000313021; ENSG00000111837. ENST00000354489; ENSP00000346484; ENSG00000111837.
GeneID	4117.
KEGG	hsa:4117.
UCSC	uc003mzm.3. human. uc021yll.1. human.
Organism-specific databases
CTD	4117.
GeneCards	GC06M010820.
HGNC	HGNC:6816. MAK.
HPA	HPA039092.
MIM	154235. gene. 614181. phenotype.
neXtProt	NX_P20794.
Orphanet	791. Retinitis pigmentosa.
PharmGKB	PA30564.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233024.
HOVERGEN	HBG014652.
InParanoid	P20794.
KO	K08829.
OMA	NLGSYAT.
OrthoDB	EOG41RPTH.
PhylomeDB	P20794.
Enzyme and pathway databases
BRENDA	2.7.11.22. 2681.
SignaLink	P20794.
Gene expression databases
ArrayExpress	P20794.
Bgee	P20794.
CleanEx	HS_MAK.
Genevestigator	P20794.
GermOnline	ENSG00000111837. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P20794.
ChEMBL	CHEMBL1163106.
GenomeRNAi	4117.
NextBio	16166.
SOURCE	Search...

Entry information

Entry name

MAK_HUMAN

Accession

Primary (citable) accession number: P20794
Secondary accession number(s): F1T0K6 , G1FL29, Q547D0, Q9NUH7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	April 27, 2001
Last modified:	May 29, 2013
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.