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P20794 (MAK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase MAK

EC=2.7.11.22
Alternative name(s):
Male germ cell-associated kinase
Gene names
Name:MAK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length623 AA.
Sequence statusComplete.
Protein existenceEvidence 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. 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. 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 processDifferentiation
Spermatogenesis
Transcription
Transcription regulation
   Cellular componentCell projection
Cilium
Cytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Retinitis pigmentosa
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell 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

protein phosphorylation

Inferred from direct assay Ref.9. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

spermatogenesis

Non-traceable author statement Ref.7. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentrosome

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_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cyclin-dependent protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein binding

Inferred from physical interaction Ref.8Ref.9. Source: UniProtKB

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

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 623623Serine/threonine-protein kinase MAK
PRO_0000086284

Regions

Domain4 – 284281Protein kinase
Nucleotide binding10 – 189ATP By similarity
Compositional bias309 – 36860Glu/Pro-rich

Sites

Active site1251Proton acceptor By similarity
Binding site331ATP By similarity

Amino acid modifications

Modified residue1571Phosphothreonine; by autocatalysis Ref.9
Modified residue1591Phosphotyrosine; by autocatalysis Ref.9

Natural variations

Alternative sequence5321A → AEESIIKPIEKLSCNETFPE KLEDPQ in isoform 2.
VSP_042470
Alternative sequence533 – 57240Missing in isoform 3.
VSP_042471
Natural variant131G → S in RP62; results in a complete loss of kinase activity compared to wild-type. Ref.2
VAR_066988
Natural variant271G → R in RP62. Ref.2
VAR_066989
Natural variant1301N → H in RP62; results in a complete loss of kinase activity compared to wild-type. Ref.2
VAR_066990
Natural variant1661R → H in RP62. Ref.2
VAR_066991
Natural variant1811I → T in RP62. Ref.2
VAR_066992
Natural variant1891I → V. Ref.10
Corresponds to variant rs56215624 [ dbSNP | Ensembl ].
VAR_042006
Natural variant2721R → P in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.10
VAR_042007
Natural variant3251P → L. Ref.2
VAR_066993
Natural variant3291D → E.
Corresponds to variant rs17579447 [ dbSNP | Ensembl ].
VAR_053932
Natural variant3841N → S. Ref.10
Corresponds to variant rs55773478 [ dbSNP | Ensembl ].
VAR_042008
Natural variant5201P → S. Ref.10
Corresponds to variant rs567083 [ dbSNP | Ensembl ].
VAR_042009
Natural variant5501F → L. Ref.10
Corresponds to variant rs56217305 [ dbSNP | Ensembl ].
VAR_042010

Experimental info

Mutagenesis331K → R: Abolishes autophosphorylation. Ref.1
Mutagenesis1571T → A: Abolishes autophosphorylation and impairs kinase activity. Ref.9
Mutagenesis1591Y → F: Abolishes autophosphorylation and impairs kinase activity. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: 67F540266F370285

FASTA62370,581
        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 

« Hide

Isoform 2 [UniParc].

Checksum: FDF1DD3370B51062
Show »

FASTA64873,480
Isoform 3 [UniParc].

Checksum: 683A5629058D81D2
Show »

FASTA58366,345

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, 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. expand/collapse author list , 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.
CCDSCCDS4516.1. [P20794-1]
PIRB34711.
RefSeqNP_001229314.1. NM_001242385.1. [P20794-3]
NP_001229886.1. NM_001242957.1. [P20794-2]
NP_005897.1. NM_005906.4. [P20794-1]
UniGeneHs.446125.

3D structure databases

ProteinModelPortalP20794.
SMRP20794. Positions 1-285.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110291. 10 interactions.
IntActP20794. 10 interactions.
STRING9606.ENSP00000313021.

Chemistry

BindingDBP20794.
ChEMBLCHEMBL1163106.
GuidetoPHARMACOLOGY2061.

PTM databases

PhosphoSiteP20794.

Polymorphism databases

DMDM13432166.

Proteomic databases

PaxDbP20794.
PRIDEP20794.

Protocols and materials databases

DNASU4117.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313243; ENSP00000313021; ENSG00000111837. [P20794-1]
ENST00000354489; ENSP00000346484; ENSG00000111837. [P20794-1]
ENST00000474039; ENSP00000476067; ENSG00000111837. [P20794-1]
GeneID4117.
KEGGhsa:4117.
UCSCuc003mzm.3. human. [P20794-1]
uc021ylk.1. human. [P20794-2]
uc021yll.1. human. [P20794-3]

Organism-specific databases

CTD4117.
GeneCardsGC06M010820.
GeneReviewsMAK.
HGNCHGNC:6816. MAK.
HPAHPA039092.
MIM154235. gene.
614181. phenotype.
neXtProtNX_P20794.
Orphanet791. Retinitis pigmentosa.
PharmGKBPA30564.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
HOVERGENHBG014652.
InParanoidP20794.
KOK08829.
OMAYATYNQS.
OrthoDBEOG7NCV37.
PhylomeDBP20794.
TreeFamTF328769.

Enzyme and pathway databases

BRENDA2.7.11.22. 2681.
SignaLinkP20794.

Gene expression databases

ArrayExpressP20794.
BgeeP20794.
CleanExHS_MAK.
GenevestigatorP20794.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMAK_(gene).
GenomeRNAi4117.
NextBio16166.
PROP20794.
SOURCESearch...

Entry information

Entry nameMAK_HUMAN
AccessionPrimary (citable) accession number: P20794
Secondary accession number(s): F1T0K6 expand/collapse secondary AC list , G1FL29, Q547D0, Q9NUH7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: April 27, 2001
Last modified: July 9, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM