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Reviewed, UniProtKB/Swiss-Prot O60307 (MAST3_HUMAN)

Last modified July 22, 2008. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Microtubule-associated serine/threonine-protein kinase 3
    EC=2.7.11.1
Gene names
Name: MAST3
Synonyms: KIAA0561
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1309 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Subunit structure

Interacts with PTEN.

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.

Caution

It is uncertain whether Met-1, Met-171 or Met-172 is the initiator.

Ontologies

Keywords

   Coding sequence diversityPolymorphism
   LigandATP-binding
Magnesium
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Molecular functionprotein binding Ref.3

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PTENP604842EBI-311420,EBI-696162

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 13091309Microtubule-associated serine/threonine-protein kinase 3

Regions

Domain367 – 640274Protein kinase
Domain641 – 71272AGC-kinase C-terminal
Domain950 – 103889PDZ
Nucleotide binding373 – 3819ATP By similarity
Compositional bias104 – 1096Poly-Ser
Compositional bias764 – 7674Poly-Ser
Compositional bias877 – 94165Ser-rich
Compositional bias1080 – 114970Ser-rich

Sites

Active site4901Proton acceptor By similarity
Binding site3961ATP By similarity

Amino acid modifications

Modified residue12231Phosphoserine By similarity
Modified residue12731Phosphoserine By similarity

Natural variations

Natural variant8831G → S

Secondary structure

........... 1309
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O60307-1 [UniParc].

Last modified November 22, 2005. Version 2.
Checksum: 87E82F2D032ED122

FASTA1,309143,137
        10         20         30         40         50         60 
MDESSLLRRR GLQKELSLPR RGRGCRSGNR KSLVVGTPSP TLSRPLSPLS VPTAGSSPLD 

        70         80         90        100        110        120 
SPRNFSAASA LNFPFARRAD GRRWSLASLP SSGYGTNTPS STLSSSSSSR ERLHQLPFQP 

       130        140        150        160        170        180 
TPDELHFLSK HFRSSENVLD EEGGRSPRLR PRSRSLSPGR ATGTFDNEIV MMNHVYRERF 

       190        200        210        220        230        240 
PKATAQMEGR LQEFLTAYAP GARLALADGV LGFIHHQIVE LARDCLAKSG ENLVTSRYFL 

       250        260        270        280        290        300 
EMQEKLERLL QDAHERSDSE EVSFIVQLVR KLLIIISRPA RLLECLEFDP EEFYHLLEAA 

       310        320        330        340        350        360 
EGHAREGQGI KTDLPQYIIG QLGLAKDPLE EMVPLSHLEE EQPPAPESPE SRALVGQSRR 

       370        380        390        400        410        420 
KPCESDFETI KLISNGAYGA VYLVRHRDTR QRFAIKKINK QNLILRNQIQ QVFVERDILT 

       430        440        450        460        470        480 
FAENPFVVSM FCSFETRRHL CMVMEYVEGG DCATLLKNMG PLPVDMARLY FAETVLALEY 

       490        500        510        520        530        540 
LHNYGIVHRD LKPDNLLITS LGHIKLTDFG LSKIGLMSMA TNLYEGHIEK DAREFIDKQV 

       550        560        570        580        590        600 
CGTPEYIAPE VIFRQGYGKP VDWWAMGVVL YEFLVGCVPF FGDTPEELFG QVVSDEIMWP 

       610        620        630        640        650        660 
EGDEALPADA QDLITRLLRQ SPLDRLGTGG THEVKQHPFF LALDWAGLLR HKAEFVPQLE 

       670        680        690        700        710        720 
AEDDTSYFDT RSERYRHLGS EDDETNDEES STEIPQFSSC SHRFSKVYSS SEFLAVQPTP 

       730        740        750        760        770        780 
TFAERSFSED REEGWERSEV DYGRRLSADI RLRSWTSSGS SCQSSSSQPE RGPSPSLLNT 

       790        800        810        820        830        840 
ISLDTMPKFA FSSEDEGVGP GPAGPKRPVF ILGEPDPPPA ATPVMPKPSS LSADTAALSH 

       850        860        870        880        890        900 
ARLRSNSIGA RHSTPRPLDA GRGRRLGGPR DPAPEKSRAS SSGGSGGGSG GRVPKSASVS 

       910        920        930        940        950        960 
ALSLIITADD GSGGPLMSPL SPRSLSSNPS SRDSSPSRDP SPVCGSLRPP IVIHSSGKKY 

       970        980        990       1000       1010       1020 
GFSLRAIRVY MGDSDVYTVH HVVWSVEDGS PAQEAGLRAG DLITHINGES VLGLVHMDVV 

      1030       1040       1050       1060       1070       1080 
ELLLKSGNKI SLRTTALENT SIKVGPARKN VAKGRMARRS KRSRRRETQD RRKSLFKKIS 

      1090       1100       1110       1120       1130       1140 
KQTSVLHTSR SFSSGLHHSL SSSESLPGSP THSLSPSPTT PCRSPAPDVP ADTTASPPSA 

      1150       1160       1170       1180       1190       1200 
SPSSSSPASP AAAGHTRPSS LHGLAAKLGP PRPKTGRRKS TSSIPPSPLA CPPISAPPPR 

      1210       1220       1230       1240       1250       1260 
SPSPLPGHPP APARSPRLRR GQSADKLGTG ERLDGEAGRR TRGPEAELVV MRRLHLSERR 

      1270       1280       1290       1300 
DSFKKQEAVQ EVSFDEPQEE ATGLPTSVPQ IAVEGEEAVP VALGPTGRD 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed: 15057824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed: 9628581] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1309.
Tissue: Brain.
[3]"Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-associated serine/threonine kinases."
Valiente M., Andres-Pons A., Gomar B., Torres J., Gil A., Tapparel C., Antonarakis S.E., Pulido R.
J. Biol. Chem. 280:28936-28943(2005) [PubMed: 15951562] [Abstract]
Cited for: INTERACTION WITH PTEN.
[4]"Solution structure of putative domain of human KIAA0561 protein."
RIKEN structural genomics initiative (RSGI)
Submitted (MAR-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 181-281.
[5]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-883.

Cross-references

Sequence databases

AC005793 Genomic DNA. Translation: AAC62830.1. Different initiation.
AC007192 Genomic DNA. Translation: AAD22670.1.
AC093054 Genomic DNA. No translation available.
AB011133 mRNA. Translation: BAA25487.1.
RefSeqNP_055831.1.
UniGeneHs.466184

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1V9VNMR-A181-281[»]
ModBaseSearch...

Protein-protein interaction databases

IntActO60307.

PTM databases

PhosphoSiteO60307.

Genome annotation databases

EnsemblENSG00000099308. Homo sapiens. [Contig view]
GeneID23031.
KEGGhsa:23031.

Organism-specific databases

H-InvDBHIX0014904.
HGNCHGNC:19036. MAST3.
PharmGKBPA134877725.
HUGESearch...
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMO60307.
HOVERGENO60307.

Gene expression databases

ArrayExpressO60307.
CleanExHS_MAST3.
GermOnlineENSG00000099308. Homo sapiens.

Family and domain databases

InterProIPR015022. 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]
PfamPF08926. DUF1908. 1 hit.
PF00595. PDZ. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00228. PDZ. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS51285. 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]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

Entry information

Entry nameMAST3_HUMAN
AccessionPrimary (citable) accession number: O60307
Secondary accession number(s): Q7LDZ8, Q9UPI0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: July 22, 2008
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents