Reviewed, UniProtKB/Swiss-Prot Q60592 (MAST2_MOUSE)

Names and origin

Protein names

Recommended name:
    Microtubule-associated serine/threonine-protein kinase 2
    EC=2.7.11.1

Gene names

Name:	Mast2
Synonyms:	Mast205

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	1734 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Appears to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Phosphorylation of DMD or UTRN may modulate their affinities for associated proteins. Functions in a multi-protein complex in spermatid maturation. Regulates lipopolysaccharide-induced IL-12 synthesis in macrophages by forming a complex with TRAF6, resulting in the inhibition of TRAF6 NF-kappa-B activation.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Subcellular location	Membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cytoskeleton. Cell junction. Note= Colocalizes with beta 2-syntrophin and utrophin at neuromuscular junctions.
Tissue specificity	Detected in round spermatids and residual bodies but not epididymal spermatozoa (at the protein level). Expressed in adult but not fetal testis with levels increasing in parallel with testicular development. Also expressed at high levels in heart, lower levels in all other tissues tested.
Post-translational modification	Phosphorylated and ubiquitinated. N-terminal ubiquitination leads to degradation of MAST2 by proteasome-mediated proteolysis. N-terminal phosphorylation appears to be a prerequisite for ubiquitination.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. Contains 1 AGC-kinase C-terminal domain. Contains 1 PDZ (DHR) domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cell junction Cytoplasm Cytoskeleton Membrane
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Ref.1 Inferred from direct assay. Source: UniProtKB regulation of interleukin-12 biosynthetic process Ref.6 Inferred from direct assay. Source: UniProtKB spermatid differentiation Ref.4 Inferred from direct assay. Source: UniProtKB
Cellular component	microtubule cytoskeleton Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Ref.1 Inferred from direct assay. Source: UniProtKB magnesium ion binding Ref.1 Inferred from direct assay. Source: UniProtKB microtubule binding Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB protein serine/threonine kinase activity Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PTEN	P60484	2	EBI-493888,EBI-696162	From a different organism.
RPS27A	P62988	2	EBI-493888,EBI-413034	From a different organism.
Sntb2	Q61235	1	EBI-493888,EBI-295974

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 1734	1734	Microtubule-associated serine/threonine-protein kinase 2
Regions
	Domain	453 – 726	274	Protein kinase
	Domain	727 – 795	69	AGC-kinase C-terminal
	Domain	1042 – 1130	89	PDZ
	Nucleotide binding	459 – 467	9	ATP By similarity
Sites
	Active site	576	1	Proton acceptor By similarity
	Binding site	482	1	ATP By similarity
Amino acid modifications
	Modified residue	91	1	Phosphoserine
	Modified residue	1441	1	Phosphoserine By similarity
	Modified residue	1446	1	Phosphothreonine By similarity
Experimental info
	Mutagenesis	482 – 483	2	KK → RA: Abolishes LPS-stimulated IL12B synthesis
	Sequence conflict	162	1	R → RSHGHRTD in AAH60703. Ref.2
	Sequence conflict	232	1	R → A in AAH60703. Ref.2
	Sequence conflict	275 – 278	4	PSLT → LAD in AAH60703. Ref.2
	Sequence conflict	478	1	R → C Ref.3
	Sequence conflict	1228	1	Missing Ref.2 Ref.3
	Sequence conflict	1502	1	T → S Ref.3
	Sequence conflict	1521	1	V → L Ref.2 Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q60592-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 97292FACD85F12E3	FASTA	1,734	190,534
	10 20 30 40 50 60 MVTGLSPLLF RKLSNPDIFA PTGKVKLQRQ LSQDDCKLRR GSLASSLSGK QLLPLSSSVH 70 80 90 100 110 120 SSVGQVTWQS TGEASNLVRM RNQSLGQSAP SLTAGLKELS LPRRGSFCRT SNRKSLIVTS 130 140 150 160 170 180 STSPTLPRPH SPLHGHTGNS PLDSPRNFSP NAPAHFSFVP ARRTDGRRWS LASLPSSGYG 190 200 210 220 230 240 TNTPSSTVSS SCSSQEKLHQ LPFQPTADEL HFLTKHFSTE NVPDEEGRRS PRMRPRSRSL 250 260 270 280 290 300 SPGRSPVSFD SEIIMMNHVY KERFPKATAQ MEERPSLTFI SSNTPDSVLP LADGALSFIH 310 320 330 340 350 360 HQVIEMARDC LDKSRSGLIT SHYFYELQEN LEKLLQDAHE RSESSDVAFV IQLVKKLMII 370 380 390 400 410 420 IARPARLLEC LEFDPEEFYH LLEAAEGHAK EGHGIKCDIP RYIVSQLGLT RDPLEEMAQL 430 440 450 460 470 480 SSYDSPDTPE TDDSVEGRGV SQPSQKTPSE EDFETIKLIS NGAYGAVFLV RHKSTRQRFA 490 500 510 520 530 540 MKKINKQNLI LRNQIQQAFV ERDILTFAEN PFVVSMFCSF ETKRHLCMVM EYVEGGDCAT 550 560 570 580 590 600 LLKNIGALPV DMVRLYFAET VLALEYLHNY GIVHRDLKPD NLLITSMGHI KLTDFGLSKI 610 620 630 640 650 660 GLMSLTTNLY EGHIEKDARE FLDKQVCGTP EYIAPEVILR QGYGKPVDWW AMGIILYEFL 670 680 690 700 710 720 VGCVPFFGDT PEELFGQVIS DEIVWPEGDD ALPPDAQDLT SKLLHQNPLE RLGTSSAYEV 730 740 750 760 770 780 KQHPFFMGLD WTGLLRQKAE FIPQLESEDD TSYFDTRSER YHHVDSEDEE EVSEDGCLEI 790 800 810 820 830 840 RQFSSCSPRF SKVYSSMERL SLLEERRTPP PTKRSLSEEK EDHSDGLAGL KGRDRSWVIG 850 860 870 880 890 900 SPEILRKRLS VSESSHTESD SSPPMTVRHR CSGLPDGPHC PEETSSTPRK QQQEGIWVLI 910 920 930 940 950 960 PPSGEGSSRP VPERPLERQL KLDEEPPGQS SRCCPALETR GRGTPQLAEE ATAKAISDLA 970 980 990 1000 1010 1020 VRRARHRLLS GDSIEKRTTR PVNKVIKSAS ATALSLLIPS EHHACSPLAS PMSPHSQSSN 1030 1040 1050 1060 1070 1080 PSSRDSSPSR DFLPALGSLR PPIIIHRAGK KYGFTLRAIR VYMGDTDVYT VHHMVWHVED 1090 1100 1110 1120 1130 1140 GGPASEAGLR QGDLITHVNG EPVHGLVHTE VVELVLKSGN KVSISTTPLE NTSIKVGPAR 1150 1160 1170 1180 1190 1200 KGSYKAKMAR RSKRSKGKDG QESRKRSSLF RKITKQASLL HTSRSLSSLN RSLSSGESGP 1210 1220 1230 1240 1250 1260 GSPTHSHSLS PRSPPQGYRV APDAVHSVGG NSSQSSSPSS SVPSSPAGSG HTRPSSLHGL 1270 1280 1290 1300 1310 1320 APKLQRQYRS PRRKSAGSIP LSPLAHTPSP PATAASPQRS PSPLSGHGSQ SFPTKLHLSP 1330 1340 1350 1360 1370 1380 PLGRQLSRPK SAEPPRSPLL KRVQSAEKLA AALAAAEKKL APSRKHSLDL PHGELKKELT 1390 1400 1410 1420 1430 1440 PREASPLEVV GTRSVLSGKG PLPGKGVLQP APSRALGTLR QDRAERRESL QKQEAIREVD 1450 1460 1470 1480 1490 1500 SSEDDTDEEP ENSQATQEPR LSPHPEASHN LLPKGSGEGT EEDTFLHRDL KKQGPVLSGL 1510 1520 1530 1540 1550 1560 VTGATLGSPR VDVPGLSPRK VSRPQAFEEA TNPLQVPSLS RSGPTSPTPS EGCWKAQHLH 1570 1580 1590 1600 1610 1620 TQALTALCPS FSELTPTGCS AATSTSGKPG TWSWKFLIEG PDRASTNKTI TRKGEPANSQ 1630 1640 1650 1660 1670 1680 DTNTTVPNLL KNLSPEEEKP QPPSVPGLTH PLLEVPSQNW PWESECEQME KEEPSLSITE 1690 1700 1710 1720 1730 VPDSSGDRRQ DIPCRAHPLS PETRPSLLWK SQELGGQQDH QDLALTSDEL LKQT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel 205-kDa testis-specific serine/threonine protein kinase associated with microtubules of the spermatid manchette." Walden P.D., Cowan N.J. Mol. Cell. Biol. 13:7625-7635(1993) [PubMed: 8246979] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Strain: Swiss Webster. Tissue: Testis.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 302-1734. Tissue: Brain.
[4]	"Increased activity associated with the MAST205 protein kinase complex during mammalian spermiogenesis." Walden P.D., Millette C.F. Biol. Reprod. 55:1039-1044(1996) [PubMed: 8902215] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[5]	"Interactions between beta 2-syntrophin and a family of microtubule-associated serine/threonine kinases." Lumeng C., Phelps S., Crawford G.E., Walden P.D., Barald K., Chamberlain J.S. Nat. Neurosci. 2:611-617(1999) [PubMed: 10404183] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH SNTB2.
[6]	"Microtubule-associated serine/threonine kinase-205 kDa and Fc gamma receptor control IL-12 p40 synthesis and NF-kappa B activation." Zhou H., Xiong H., Li H., Plevy S.E., Walden P.D., Sassaroli M., Prestwich G.D., Unkeless J.C. J. Immunol. 172:2559-2568(2004) [PubMed: 14764729] [Abstract] Cited for: FUNCTION, UBIQUITINATION, MUTAGENESIS OF 482-LYS-LYS-483.
[7]	"Interaction of TRAF6 with MAST205 regulates NF-kappaB activation and MAST205 stability." Xiong H., Li H., Chen Y., Zhao J., Unkeless J.C. J. Biol. Chem. 279:43675-43683(2004) [PubMed: 15308666] [Abstract] Cited for: FUNCTION, UBIQUITINATION, PHOSPHORYLATION, INTERACTION WITH TRAF6.
[8]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U02313 mRNA. Translation: AAC04312.1. BC060703 mRNA. Translation: AAH60703.1. AB093264 mRNA. Translation: BAC41448.1.
PIR	A54602.
RefSeq	NP_001036208.1. NP_032667.2.
UniGene	Mm.9287
3D structure databases
HSSP	HSSP built from PDB template 1MRY based on UniProtKB P31751.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q60592.
PTM databases
PhosphoSite	Q60592.
Genome annotation databases
Ensembl	ENSMUSG00000003810. Mus musculus. [Contig view]
GeneID	17776.
KEGG	mmu:17776.
Organism-specific databases
MGI	MGI:894676. Mast2.
Phylogenomic databases
HOGENOM	Q60592.
HOVERGEN	Q60592.
Gene expression databases
ArrayExpress	Q60592.
CleanEx	MM_MAST2.
GermOnline	ENSMUSG00000003810. Mus musculus.
Family and domain databases
InterPro	IPR015022. DUF1908. IPR001478. PDZ. IPR000961. Pkinase_C. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_bd_CS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF08926. DUF1908. 1 hit. PF00595. PDZ. 1 hit. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00228. PDZ. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS50106. PDZ. 1 hit. PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

Entry information

Entry name

MAST2_MOUSE

Accession

Primary (citable) accession number: Q60592
Secondary accession number(s): Q6P9M1, Q8CHD1

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	November 1, 1996
Last modified:	July 22, 2008
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)