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Q60592

- MAST2_MOUSE

UniProt

Q60592 - MAST2_MOUSE

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Protein
Microtubule-associated serine/threonine-protein kinase 2
Gene
Mast2, Mast205
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Magnesium.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei482 – 4821ATP By similarityBy similarity
Active sitei576 – 5761Proton acceptor By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi459 – 4679ATP By similarityBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. microtubule binding Source: MGI
  4. protein binding Source: IntAct
  5. protein serine/threonine kinase activity Source: MGI
Complete GO annotation...

GO - Biological processi

  1. protein phosphorylation Source: UniProtKB
  2. regulation of interleukin-12 biosynthetic process Source: UniProtKB
  3. spermatid differentiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated serine/threonine-protein kinase 2 (EC:2.7.11.1)
Gene namesi
Name:Mast2
Synonyms:Mast205
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:894676. Mast2.

Subcellular locationi

Membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. Cell junction
Note: Colocalizes with beta 2-syntrophin and utrophin at neuromuscular junctions.1 Publication

GO - Cellular componenti

  1. cell junction Source: UniProtKB-SubCell
  2. cytoplasm Source: UniProtKB-KW
  3. membrane Source: UniProtKB-SubCell
  4. microtubule cytoskeleton Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi482 – 4832KK → RA: Abolishes LPS-stimulated IL12B synthesis. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17341734Microtubule-associated serine/threonine-protein kinase 2
PRO_0000086313Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141Phosphoserine By similarity
Modified residuei88 – 881Phosphoserine By similarity
Modified residuei149 – 1491Phosphoserine By similarity
Modified residuei841 – 8411Phosphoserine By similarity
Modified residuei970 – 9701Phosphoserine By similarity
Modified residuei1275 – 12751Phosphoserine1 Publication
Modified residuei1446 – 14461Phosphothreonine By similarity

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ60592.
PRIDEiQ60592.

PTM databases

PhosphoSiteiQ60592.

Expressioni

Tissue specificityi

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.4 Publications

Gene expression databases

CleanExiMM_MAST2.
GenevestigatoriQ60592.

Interactioni

Subunit structurei

Interacts with CDHR2 By similarity.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PTENP604844EBI-493888,EBI-696162From a different organism.
UBBP0CG472EBI-493888,EBI-413034From a different organism.

Protein-protein interaction databases

BioGridi201600. 1 interaction.
IntActiQ60592. 7 interactions.
MINTiMINT-152278.
STRINGi10090.ENSMUSP00000102095.

Structurei

3D structure databases

ProteinModelPortaliQ60592.
SMRiQ60592. Positions 265-788, 1037-1131.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini453 – 726274Protein kinase
Add
BLAST
Domaini727 – 79569AGC-kinase C-terminal
Add
BLAST
Domaini1042 – 113089PDZ
Add
BLAST

Sequence similaritiesi

Contains 1 PDZ (DHR) domain.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000046662.
HOVERGENiHBG052414.
KOiK08789.

Family and domain databases

Gene3Di1.20.1480.20. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR015022. MA_Ser/Thr_Kinase_dom.
IPR028779. MAST2.
IPR023142. MAST_pre-PK_dom.
IPR001478. PDZ.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24356:SF136. PTHR24356:SF136. 1 hit.
PfamiPF08926. DUF1908. 1 hit.
PF00595. PDZ. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF140482. SSF140482. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50106. PDZ. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60592-1 [UniParc]FASTAAdd to Basket

« Hide

MVTGLSPLLF RKLSNPDIFA PTGKVKLQRQ LSQDDCKLRR GSLASSLSGK     50
QLLPLSSSVH SSVGQVTWQS TGEASNLVRM RNQSLGQSAP SLTAGLKELS 100
LPRRGSFCRT SNRKSLIVTS STSPTLPRPH SPLHGHTGNS PLDSPRNFSP 150
NAPAHFSFVP ARRTDGRRWS LASLPSSGYG TNTPSSTVSS SCSSQEKLHQ 200
LPFQPTADEL HFLTKHFSTE NVPDEEGRRS PRMRPRSRSL SPGRSPVSFD 250
SEIIMMNHVY KERFPKATAQ MEERPSLTFI SSNTPDSVLP LADGALSFIH 300
HQVIEMARDC LDKSRSGLIT SHYFYELQEN LEKLLQDAHE RSESSDVAFV 350
IQLVKKLMII IARPARLLEC LEFDPEEFYH LLEAAEGHAK EGHGIKCDIP 400
RYIVSQLGLT RDPLEEMAQL SSYDSPDTPE TDDSVEGRGV SQPSQKTPSE 450
EDFETIKLIS NGAYGAVFLV RHKSTRQRFA MKKINKQNLI LRNQIQQAFV 500
ERDILTFAEN PFVVSMFCSF ETKRHLCMVM EYVEGGDCAT LLKNIGALPV 550
DMVRLYFAET VLALEYLHNY GIVHRDLKPD NLLITSMGHI KLTDFGLSKI 600
GLMSLTTNLY EGHIEKDARE FLDKQVCGTP EYIAPEVILR QGYGKPVDWW 650
AMGIILYEFL VGCVPFFGDT PEELFGQVIS DEIVWPEGDD ALPPDAQDLT 700
SKLLHQNPLE RLGTSSAYEV KQHPFFMGLD WTGLLRQKAE FIPQLESEDD 750
TSYFDTRSER YHHVDSEDEE EVSEDGCLEI RQFSSCSPRF SKVYSSMERL 800
SLLEERRTPP PTKRSLSEEK EDHSDGLAGL KGRDRSWVIG SPEILRKRLS 850
VSESSHTESD SSPPMTVRHR CSGLPDGPHC PEETSSTPRK QQQEGIWVLI 900
PPSGEGSSRP VPERPLERQL KLDEEPPGQS SRCCPALETR GRGTPQLAEE 950
ATAKAISDLA VRRARHRLLS GDSIEKRTTR PVNKVIKSAS ATALSLLIPS 1000
EHHACSPLAS PMSPHSQSSN PSSRDSSPSR DFLPALGSLR PPIIIHRAGK 1050
KYGFTLRAIR VYMGDTDVYT VHHMVWHVED GGPASEAGLR QGDLITHVNG 1100
EPVHGLVHTE VVELVLKSGN KVSISTTPLE NTSIKVGPAR KGSYKAKMAR 1150
RSKRSKGKDG QESRKRSSLF RKITKQASLL HTSRSLSSLN RSLSSGESGP 1200
GSPTHSHSLS PRSPPQGYRV APDAVHSVGG NSSQSSSPSS SVPSSPAGSG 1250
HTRPSSLHGL APKLQRQYRS PRRKSAGSIP LSPLAHTPSP PATAASPQRS 1300
PSPLSGHGSQ SFPTKLHLSP PLGRQLSRPK SAEPPRSPLL KRVQSAEKLA 1350
AALAAAEKKL APSRKHSLDL PHGELKKELT PREASPLEVV GTRSVLSGKG 1400
PLPGKGVLQP APSRALGTLR QDRAERRESL QKQEAIREVD SSEDDTDEEP 1450
ENSQATQEPR LSPHPEASHN LLPKGSGEGT EEDTFLHRDL KKQGPVLSGL 1500
VTGATLGSPR VDVPGLSPRK VSRPQAFEEA TNPLQVPSLS RSGPTSPTPS 1550
EGCWKAQHLH TQALTALCPS FSELTPTGCS AATSTSGKPG TWSWKFLIEG 1600
PDRASTNKTI TRKGEPANSQ DTNTTVPNLL KNLSPEEEKP QPPSVPGLTH 1650
PLLEVPSQNW PWESECEQME KEEPSLSITE VPDSSGDRRQ DIPCRAHPLS 1700
PETRPSLLWK SQELGGQQDH QDLALTSDEL LKQT 1734
Length:1,734
Mass (Da):190,534
Last modified:November 1, 1996 - v1
Checksum:i97292FACD85F12E3
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1621R → RSHGHRTD in AAH60703. 1 Publication
Sequence conflicti232 – 2321R → A in AAH60703. 1 Publication
Sequence conflicti275 – 2784PSLT → LAD in AAH60703. 1 Publication
Sequence conflicti478 – 4781R → C1 Publication
Sequence conflicti1228 – 12281Missing1 Publication
Sequence conflicti1228 – 12281Missing1 Publication
Sequence conflicti1502 – 15021T → S1 Publication
Sequence conflicti1521 – 15211V → L1 Publication
Sequence conflicti1521 – 15211V → L1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U02313 mRNA. Translation: AAC04312.1.
BC060703 mRNA. Translation: AAH60703.1.
AB093264 mRNA. Translation: BAC41448.1.
PIRiA54602.
RefSeqiNP_001036208.1. NM_001042743.2.
NP_032667.2. NM_008641.3.
UniGeneiMm.9287.

Genome annotation databases

GeneIDi17776.
KEGGimmu:17776.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U02313 mRNA. Translation: AAC04312.1 .
BC060703 mRNA. Translation: AAH60703.1 .
AB093264 mRNA. Translation: BAC41448.1 .
PIRi A54602.
RefSeqi NP_001036208.1. NM_001042743.2.
NP_032667.2. NM_008641.3.
UniGenei Mm.9287.

3D structure databases

ProteinModelPortali Q60592.
SMRi Q60592. Positions 265-788, 1037-1131.
ModBasei Search...

Protein-protein interaction databases

BioGridi 201600. 1 interaction.
IntActi Q60592. 7 interactions.
MINTi MINT-152278.
STRINGi 10090.ENSMUSP00000102095.

PTM databases

PhosphoSitei Q60592.

Proteomic databases

PaxDbi Q60592.
PRIDEi Q60592.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 17776.
KEGGi mmu:17776.

Organism-specific databases

CTDi 23139.
MGIi MGI:894676. Mast2.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000046662.
HOVERGENi HBG052414.
KOi K08789.

Miscellaneous databases

ChiTaRSi MAST2. mouse.
NextBioi 292503.
PROi Q60592.
SOURCEi Search...

Gene expression databases

CleanExi MM_MAST2.
Genevestigatori Q60592.

Family and domain databases

Gene3Di 1.20.1480.20. 1 hit.
2.30.42.10. 1 hit.
InterProi IPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR015022. MA_Ser/Thr_Kinase_dom.
IPR028779. MAST2.
IPR023142. MAST_pre-PK_dom.
IPR001478. PDZ.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
PANTHERi PTHR24356:SF136. PTHR24356:SF136. 1 hit.
Pfami PF08926. DUF1908. 1 hit.
PF00595. PDZ. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00228. PDZ. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF140482. SSF140482. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
PS50106. PDZ. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMAST2_MOUSE
AccessioniPrimary (citable) accession number: Q60592
Secondary accession number(s): Q6P9M1, Q8CHD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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