Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P20793 (MAK_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length622 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. Could play an important function in spermatogenesis. Phosphorylates FZR1 in a cell cycle-dependent manner By similarity. Plays a role in the transcriptional coactivation of AR By similarity. Ref.1

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

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

Subcellular location

Nucleus By similarity. Cytoplasm. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytoskeletonspindle By similarity. Midbody By similarity. Cell projectionciliumphotoreceptor outer segment By similarity. Photoreceptor inner segment By similarity. Note: Localized in both the connecting cilia and the outer segment axonemes By similarity. Ref.4

Tissue specificity

Expressed mainly in testicular cells at and after meiosis. Ref.1 Ref.4

Developmental stage

Expression in testis is detected 16 days after birth and increases gradually to reach a plateau about 4 weeks after birth (at protein level). Ref.4

Post-translational modification

Autophosphorylated By similarity. Phosphorylated on serine and threonine residues. Ref.4

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
   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 sequence or structural similarity. Source: UniProtKB

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

spermatogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentrosome

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic spindle

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

photoreceptor inner segment

Inferred from sequence or structural similarity. 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

transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P20793-1)

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: P20793-2)

The sequence of this isoform differs from the canonical sequence as follows:
     531-571: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 622622Serine/threonine-protein kinase MAK
PRO_0000086286

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 By similarity
Modified residue1591Phosphotyrosine; by autocatalysis By similarity

Natural variations

Alternative sequence531 – 57141Missing in isoform 2.
VSP_042475

Experimental info

Sequence conflict5811Q → R in AAA41562. Ref.1

Sequences

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

Last modified March 21, 2012. Version 2.
Checksum: 7C2056E1D116D3BF

FASTA62269,897
        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 AELYTFRPLF PGTSEVDEIF KICQVLGTPK KSDWPEGYQL ASSMNFRFPQ 

       250        260        270        280        290        300 
CIPINLKTLI PNASSEAIQL MTEMLNWDPK KRPTASQALK HPYFQVGQVL GPSAHHLDAK 

       310        320        330        340        350        360 
QTLHKQLQPP EPKPSSSERD PKPLPNILDQ PAGQPQPKQG HQPLQAIQPP QNTVVQPPPK 

       370        380        390        400        410        420 
QQGHHKQPQT MFPSIVKTIP TNPVSTVGHK GARRRWGQTV FKSGDSCDNI EDCDLGASHS 

       430        440        450        460        470        480 
KKPSMDAFKE KKKKESPFRF PEAGLPVSNH LKGENRNLHA SLKSDTNLST ASTAKQYYLK 

       490        500        510        520        530        540 
QSRYLPGVNP KNVSLVAGGK DINSHSWNNQ LFPKSLGSMG ADLAFKRSNA AGNLGSYSAY 

       550        560        570        580        590        600 
SQTGCVPSFL KKEVGSAGQR IHLAPLGASA ADYTWSTKTG QGQFSGRTYN PTAKNLNIVN 

       610        620 
RTQPVPSVHG RTDWVAKYGG HR 

« Hide

Isoform 2 [UniParc].

Checksum: 8F4911C903FF3B3D
Show »

FASTA58165,849

References

« Hide 'large scale' references
[1]"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 [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
Tissue: Testis.
[2]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: Brown Norway.
Tissue: Testis.
[4]"Testis-specific mak protein kinase is expressed specifically in the meiotic phase in spermatogenesis and is associated with a 210-kilodalton cellular phosphoprotein."
Jinno A., Tanaka K., Matsushime H., Haneji T., Shibuya M.
Mol. Cell. Biol. 13:4146-4156(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION, ALTERNATIVE SPLICING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M35862 mRNA. Translation: AAA41562.1.
CH473977 Genomic DNA. Translation: EDL98222.1.
BC078887 mRNA. Translation: AAH78887.1.
PIRA34711.
RefSeqNP_037268.1. NM_013136.1.
UniGeneRn.9670.

3D structure databases

ProteinModelPortalP20793.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000059085.

Proteomic databases

PaxDbP20793.
PRIDEP20793.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000020672; ENSRNOP00000020672; ENSRNOG00000015101. [P20793-1]
ENSRNOT00000040707; ENSRNOP00000050970; ENSRNOG00000015101. [P20793-2]
GeneID25677.
KEGGrno:25677.
UCSCRGD:3036. rat. [P20793-1]

Organism-specific databases

CTD4117.
RGD3036. Mak.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00650000093283.
HOGENOMHOG000233024.
HOVERGENHBG014652.
InParanoidP20793.
KOK08829.
OMAYATYNQS.
OrthoDBEOG7NCV37.

Enzyme and pathway databases

BRENDA2.7.11.22. 5301.

Gene expression databases

GenevestigatorP20793.

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

NextBio607631.
PROP20793.

Entry information

Entry nameMAK_RAT
AccessionPrimary (citable) accession number: P20793
Secondary accession number(s): G3V7Y4, Q6AYW0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: March 21, 2012
Last modified: April 16, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families