P20793 (MAK_RAT) 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

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	622 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. 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. Cytoplasm › cytoskeleton › centrosome By similarity. Cytoplasm › cytoskeleton › spindle By similarity. Midbody By similarity. Cell projection › cilium › photoreceptor 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 process	Differentiation Spermatogenesis Transcription Transcription regulation
Cellular component	Cell projection Cilium Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing
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 cycle Inferred from electronic annotation. Source: GOC 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 sequence or structural similarity. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW spermatogenesis Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	centrosome 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_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cyclin-dependent protein serine/threonine kinase activity Inferred from electronic annotation. Source: 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 622	622	Serine/threonine-protein kinase MAK		PRO_0000086286
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 By similarity
	Modified residue	159	1	Phosphotyrosine; by autocatalysis By similarity
Natural variations
	Alternative sequence	531 – 571	41	Missing in isoform 2.		VSP_042475
Experimental info
	Sequence conflict	581	1	Q → R in AAA41562. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 21, 2012. Version 2. Checksum: 7C2056E1D116D3BF	FASTA	622	69,897
	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
	Isoform 2 [UniParc]. Checksum: 8F4911C903FF3B3D	FASTA	581	65,849
	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 DYTWSTKTGQ 550 560 570 580 GQFSGRTYNP TAKNLNIVNR TQPVPSVHGR TDWVAKYGGH R

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00202523. IPI00464818.
PIR	A34711.
RefSeq	NP_037268.1. NM_013136.1.
UniGene	Rn.9670.
3D structure databases
ProteinModelPortal	P20793.
ModBase	Search...
Proteomic databases
PaxDb	P20793.
PRIDE	P20793.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000020672; ENSRNOP00000020672; ENSRNOG00000015101. ENSRNOT00000040707; ENSRNOP00000050970; ENSRNOG00000015101.
GeneID	25677.
KEGG	rno:25677.
UCSC	RGD:3036. rat.
Organism-specific databases
CTD	4117.
RGD	3036. Mak.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00650000093283.
HOGENOM	HOG000233024.
HOVERGEN	HBG014652.
InParanoid	P20793.
KO	K08829.
OMA	NLGSYAT.
Enzyme and pathway databases
BRENDA	2.7.11.22. 5301.
Gene expression databases
ArrayExpress	P20793.
Genevestigator	P20793.
GermOnline	ENSRNOG00000015101. Rattus norvegicus.
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
NextBio	607631.

Entry information

Entry name

MAK_RAT

Accession

Primary (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:	May 1, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program