Microtubule-associated serine/threonine-protein kinase 2

Preferred order of sections

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) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1734 AA.
Sequence status	Complete.
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. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.1
Cofactor	Magnesium. Ref.1
Subunit structure	Interacts with CDHR2 By similarity. Ref.5 Ref.7
Subcellular location	Membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cytoskeleton. Cell junction. Note: Colocalizes with beta 2-syntrophin and utrophin at neuromuscular junctions. Ref.5
Tissue specificity	Detected in round spermatids and residual bodies but not epididymal spermatozoa (at 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. Ref.1 Ref.4 Ref.5 Ref.7
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. Ref.6 Ref.7
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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of interleukin-12 biosynthetic process Inferred from direct assay Ref.6. Source: UniProtKB spermatid differentiation Inferred from direct assay Ref.4. Source: UniProtKB
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule cytoskeleton Inferred from direct assay Ref.1. Source: MGI
Molecular_function	ATP binding Inferred from direct assay Ref.1. Source: UniProtKB magnesium ion binding Inferred from direct assay Ref.1. Source: UniProtKB microtubule binding Inferred from direct assay Ref.1. Source: MGI protein serine/threonine kinase activity Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PTEN	P60484	4	EBI-493888,EBI-696162	From a different organism.
Sntb2	Q61235	4	EBI-493888,EBI-295974
UBB	P0CG47	2	EBI-493888,EBI-413034	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1734

1734

Microtubule-associated serine/threonine-protein kinase 2

PRO_0000086313

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 UniProtKB Q9BXM7

Sites

Active site

576

1

Proton acceptor By similarity UniProtKB Q9BXM7

Binding site

482

1

ATP By similarity UniProtKB Q9BXM7

Amino acid modifications

Modified residue

14

1

Phosphoserine Ref.9

Modified residue

42

1

Phosphoserine Ref.9

Modified residue

88

1

Phosphoserine By similarity

Modified residue

91

1

Phosphoserine Ref.8

Modified residue

149

1

Phosphoserine By similarity

Modified residue

841

1

Phosphoserine By similarity

Modified residue

970

1

Phosphoserine By similarity

Modified residue

1446

1

Phosphothreonine By similarity

Modified residue

1462

1

Phosphoserine Ref.9

Experimental info

Mutagenesis

482 – 483

2

KK → RA: Abolishes LPS-stimulated IL12B synthesis. Ref.6

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

Sequence conflict

1228

1

Missing Ref.3

Sequence conflict

1502

1

T → S Ref.3

Sequence conflict

1521

1

V → L Ref.2

Sequence conflict

1521

1

V → L Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q60592 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 97292FACD85F12E3
Show »

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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, MASS SPECTROMETRY. Tissue: Liver.
[9]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-42 AND SER-1462, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U02313 mRNA. Translation: AAC04312.1. BC060703 mRNA. Translation: AAH60703.1. AB093264 mRNA. Translation: BAC41448.1.
IPI	IPI00622008.
PIR	A54602.
RefSeq	NP_001036208.1. NM_001042743.1. NP_032667.2. NM_008641.2.
UniGene	Mm.9287.
3D structure databases
ProteinModelPortal	Q60592.
SMR	Q60592. Positions 265-366, 398-759, 1037-1131.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q60592. 5 interactions.
MINT	MINT-152278.
STRING	10090.ENSMUSP00000102095.
PTM databases
PhosphoSite	Q60592.
Proteomic databases
PaxDb	Q60592.
PRIDE	Q60592.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	17776.
KEGG	mmu:17776.
Organism-specific databases
CTD	23139.
MGI	MGI:894676. Mast2.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000046662.
HOVERGEN	HBG052414.
KO	K08789.
OrthoDB	EOG44F68B.
Gene expression databases
CleanEx	MM_MAST2.
Genevestigator	Q60592.
GermOnline	ENSMUSG00000003810. Mus musculus.
Family and domain databases
Gene3D	1.20.1480.20. 1 hit.
InterPro	IPR000961. AGC-kinase_C. IPR011009. Kinase-like_dom. IPR015022. MA_Ser/Thr_Kinase_dom. IPR023142. MAST_pre-PK_dom. IPR001478. PDZ. IPR000719. Prot_kinase_cat_dom. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF08926. DUF1908. 1 hit. PF00595. PDZ. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00228. PDZ. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit. SSF50156. PDZ. 1 hit. SSF140482. SSF140482. 1 hit.
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]
ProtoNet	Search...
Other
ChiTaRS	MAST2. mouse.
NextBio	292503.
SOURCE	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:	May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents