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Q6P0Q8

- MAST2_HUMAN

UniProt

Q6P0Q8 - MAST2_HUMAN

Protein

Microtubule-associated serine/threonine-protein kinase 2

Gene

MAST2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (29 Mar 2005)
      Previous versions | rss
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    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 By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.By similarity

    Cofactori

    Magnesium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei541 – 5411ATPBy similarityPROSITE-ProRule annotation
    Active sitei635 – 6351Proton acceptorBy similarityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi518 – 5269ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. phosphatase binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

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

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    SignaLinkiQ6P0Q8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Microtubule-associated serine/threonine-protein kinase 2 (EC:2.7.11.1)
    Gene namesi
    Name:MAST2Imported
    Synonyms:KIAA0807Imported, MAST205Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:19035. MAST2.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication. Cell membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Recruited to the sub-membranous area on interaction with CDHR2.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. microtubule cytoskeleton Source: Ensembl
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134954073.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17981798Microtubule-associated serine/threonine-protein kinase 2PRO_0000086312Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei74 – 741Phosphoserine4 Publications
    Modified residuei148 – 1481Phosphoserine2 Publications
    Modified residuei209 – 2091Phosphoserine1 Publication
    Modified residuei900 – 9001Phosphoserine1 Publication
    Modified residuei1032 – 10321Phosphoserine1 Publication
    Modified residuei1337 – 13371PhosphoserineBy similarity
    Modified residuei1508 – 15081Phosphothreonine1 Publication

    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 By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ6P0Q8.
    PaxDbiQ6P0Q8.
    PRIDEiQ6P0Q8.

    PTM databases

    PhosphoSiteiQ6P0Q8.

    Expressioni

    Tissue specificityi

    Abundant in the testis.1 Publication

    Gene expression databases

    ArrayExpressiQ6P0Q8.
    BgeeiQ6P0Q8.
    CleanExiHS_MAST2.
    GenevestigatoriQ6P0Q8.

    Organism-specific databases

    HPAiHPA039722.
    HPA040155.

    Interactioni

    Subunit structurei

    Interacts with CDHR2.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDHR2Q9BYE94EBI-493777,EBI-493793
    SLC9A3P487642EBI-493777,EBI-7816923
    SLC9A3Q283622EBI-493777,EBI-7817027From a different organism.

    Protein-protein interaction databases

    BioGridi116756. 17 interactions.
    IntActiQ6P0Q8. 18 interactions.
    MINTiMINT-1892333.
    STRINGi9606.ENSP00000354671.

    Structurei

    Secondary structure

    1
    1798
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1104 – 11085
    Beta strandi1116 – 11249
    Beta strandi1126 – 11294
    Beta strandi1131 – 114010
    Beta strandi1142 – 11454
    Helixi1146 – 11494
    Beta strandi1156 – 11649
    Helixi1170 – 118011
    Beta strandi1182 – 11887

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KQFNMR-A1099-1193[»]
    2KYLNMR-A1099-1193[»]
    ProteinModelPortaliQ6P0Q8.
    SMRiQ6P0Q8. Positions 325-849, 1099-1193.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini512 – 785274Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini786 – 85469AGC-kinase C-terminalAdd
    BLAST
    Domaini1104 – 119289PDZPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG052414.
    InParanoidiQ6P0Q8.
    KOiK08789.
    OMAiDMPRFAI.
    OrthoDBiEOG7PK8ZC.
    PhylomeDBiQ6P0Q8.
    TreeFamiTF313149.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q6P0Q8-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MKRSRCRDRP QPPPPDRRED GVQRAAELSQ SLPPRRRAPP GRQRLEERTG     50
    PAGPEGKEQD VVTGVSPLLF RKLSNPDIFS STGKVKLQRQ LSQDDCKLWR 100
    GNLASSLSGK QLLPLSSSVH SSVGQVTWQS SGEASNLVRM RNQSLGQSAP 150
    SLTAGLKELS LPRRGSFCRT SNRKSLIVTS STSPTLPRPH SPLHGHTGNS 200
    PLDSPRNFSP NAPAHFSFVP ARRTDGRRWS LASLPSSGYG TNTPSSTVSS 250
    SCSSQEKLHQ LPFQPTADEL HFLTKHFSTE SVPDEEGRQS PAMRPRSRSL 300
    SPGRSPVSFD SEIIMMNHVY KERFPKATAQ MEERLAEFIS SNTPDSVLPL 350
    ADGALSFIHH QVIEMARDCL DKSRSGLITS QYFYELQDNL EKLLQDAHER 400
    SESSEVAFVM QLVKKLMIII ARPARLLECL EFDPEEFYHL LEAAEGHAKE 450
    GQGIKCDIPR YIVSQLGLTR DPLEEMAQLS SCDSPDTPET DDSIEGHGAS 500
    LPSKKTPSEE DFETIKLISN GAYGAVFLVR HKSTRQRFAM KKINKQNLIL 550
    RNQIQQAFVE RDILTFAENP FVVSMFCSFD TKRHLCMVME YVEGGDCATL 600
    LKNIGALPVD MVRLYFAETV LALEYLHNYG IVHRDLKPDN LLITSMGHIK 650
    LTDFGLSKIG LMSLTTNLYE GHIEKDAREF LDKQVCGTPE YIAPEVILRQ 700
    GYGKPVDWWA MGIILYEFLV GCVPFFGDTP EELFGQVISD EIVWPEGDEA 750
    LPPDAQDLTS KLLHQNPLER LGTGSAYEVK QHPFFTGLDW TGLLRQKAEF 800
    IPQLESEDDT SYFDTRSERY HHMDSEDEEE VSEDGCLEIR QFSSCSPRFN 850
    KVYSSMERLS LLEERRTPPP TKRSLSEEKE DHSDGLAGLK GRDRSWVIGS 900
    PEILRKRLSV SESSHTESDS SPPMTVRRRC SGLLDAPRFP EGPEEASSTL 950
    RRQPQEGIWV LTPPSGEGVS GPVTEHSGEQ RPKLDEEAVG RSSGSSPAME 1000
    TRGRGTSQLA EGATAKAISD LAVRRARHRL LSGDSTEKRT ARPVNKVIKS 1050
    ASATALSLLI PSEHHTCSPL ASPMSPHSQS SNPSSRDSSP SRDFLPALGS 1100
    MRPPIIIHRA GKKYGFTLRA IRVYMGDSDV YTVHHMVWHV EDGGPASEAG 1150
    LRQGDLITHV NGEPVHGLVH TEVVELILKS GNKVAISTTP LENTSIKVGP 1200
    ARKGSYKAKM ARRSKRSRGK DGQESRKRSS LFRKITKQAS LLHTSRSLSS 1250
    LNRSLSSGES GPGSPTHSHS LSPRSPTQGY RVTPDAVHSV GGNSSQSSSP 1300
    SSSVPSSPAG SGHTRPSSLH GLAPKLQRQY RSPRRKSAGS IPLSPLAHTP 1350
    SPPPPTASPQ RSPSPLSGHV AQAFPTKLHL SPPLGRQLSR PKSAEPPRSP 1400
    LLKRVQSAEK LAAALAASEK KLATSRKHSL DLPHSELKKE LPPREVSPLE 1450
    VVGARSVLSG KGALPGKGVL QPAPSRALGT LRQDRAERRE SLQKQEAIRE 1500
    VDSSEDDTEE GPENSQGAQE LSLAPHPEVS QSVAPKGAGE SGEEDPFPSR 1550
    DPRSLGPMVP SLLTGITLGP PRMESPSGPH RRLGSPQAIE EAASSSSAGP 1600
    NLGQSGATDP IPPEGCWKAQ HLHTQALTAL SPSTSGLTPT SSCSPPSSTS 1650
    GKLSMWSWKS LIEGPDRASP SRKATMAGGL ANLQDLENTT PAQPKNLSPR 1700
    EQGKTQPPSA PRLAHPSYED PSQGWLWESE CAQAVKEDPA LSITQVPDAS 1750
    GDRRQDVPCR GCPLTQKSEP SLRRGQEPGG HQKHRDLALV PDELLKQT 1798
    Length:1,798
    Mass (Da):196,436
    Last modified:March 29, 2005 - v2
    Checksum:iDF5C92078A3451AF
    GO
    Isoform 2Curated (identifier: Q6P0Q8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         327-396: Missing.
         1091-1113: Missing.
         1290-1386: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:1,608
    Mass (Da):176,132
    Checksum:iE8E7D89D72A99168
    GO

    Sequence cautioni

    The sequence AAH15816.2 differs from that shown. Reason: Frameshift at positions 1114 and 1387.
    The sequence BAB40778.1 differs from that shown. Reason: Frameshift at position 1688.
    The sequence AAH15816.2 differs from that shown. Reason: Erroneous initiation.
    The sequence CAH73245.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI16563.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI21706.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1225 – 12251Missing in AAH65499. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti69 – 691L → F.1 Publication
    Corresponds to variant rs55914403 [ dbSNP | Ensembl ].
    VAR_040771
    Natural varianti275 – 2751K → E in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
    VAR_040772
    Natural varianti388 – 3881D → E.2 Publications
    Corresponds to variant rs11211247 [ dbSNP | Ensembl ].
    VAR_040773
    Natural varianti655 – 6551G → A in a breast mucinous carcinoma sample; somatic mutation. 1 Publication
    VAR_040774
    Natural varianti659 – 6591I → M.4 Publications
    Corresponds to variant rs1707336 [ dbSNP | Ensembl ].
    VAR_040775
    Natural varianti991 – 9911R → L.1 Publication
    Corresponds to variant rs56114653 [ dbSNP | Ensembl ].
    VAR_040776
    Natural varianti1197 – 11971K → R.1 Publication
    Corresponds to variant rs1052607 [ dbSNP | Ensembl ].
    VAR_040777
    Natural varianti1221 – 12211D → E.1 Publication
    Corresponds to variant rs56060730 [ dbSNP | Ensembl ].
    VAR_040778
    Natural varianti1246 – 12461R → L.1 Publication
    Corresponds to variant rs56309943 [ dbSNP | Ensembl ].
    VAR_040779
    Natural varianti1304 – 13041V → M.1 Publication
    Corresponds to variant rs33931638 [ dbSNP | Ensembl ].
    VAR_040780
    Natural varianti1463 – 14631A → T.1 Publication
    Corresponds to variant rs3737738 [ dbSNP | Ensembl ].
    VAR_040781
    Natural varianti1468 – 14681G → A.1 Publication
    Corresponds to variant rs3737737 [ dbSNP | Ensembl ].
    VAR_040782
    Natural varianti1551 – 15511D → G.3 Publications
    Corresponds to variant rs1052610 [ dbSNP | Ensembl ].
    VAR_040783
    Natural varianti1608 – 16081T → I.
    Corresponds to variant rs35474583 [ dbSNP | Ensembl ].
    VAR_051645
    Natural varianti1673 – 16731K → R.1 Publication
    Corresponds to variant rs34070850 [ dbSNP | Ensembl ].
    VAR_040784
    Natural varianti1703 – 17031G → E.1 Publication
    VAR_040785

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei327 – 39670Missing in isoform 2. 1 PublicationVSP_051698Add
    BLAST
    Alternative sequencei1091 – 111323Missing in isoform 2. 1 PublicationVSP_051699Add
    BLAST
    Alternative sequencei1290 – 138697Missing in isoform 2. 1 PublicationVSP_051700Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB047005 mRNA. Translation: BAB40778.1. Frameshift.
    AL645480
    , AL358075, AL603882, AL603888 Genomic DNA. Translation: CAH73244.1.
    AL645480, AL358075, AL603888 Genomic DNA. Translation: CAH73245.1. Sequence problems.
    AL603882
    , AL358075, AL603888, AL645480 Genomic DNA. Translation: CAI16217.1.
    AL603888
    , AL358075, AL603882, AL645480 Genomic DNA. Translation: CAI16562.1.
    AL603888, AL358075, AL645480 Genomic DNA. Translation: CAI16563.1. Sequence problems.
    AL358075
    , AL603882, AL603888, AL645480 Genomic DNA. Translation: CAI21705.1.
    AL358075, AL603888, AL645480 Genomic DNA. Translation: CAI21706.1. Sequence problems.
    BC015816 mRNA. Translation: AAH15816.2. Different initiation.
    BC065499 mRNA. Translation: AAH65499.1.
    AB018350 mRNA. Translation: BAA34527.2.
    AL833919 mRNA. Translation: CAD38775.1.
    CCDSiCCDS41326.1. [Q6P0Q8-1]
    RefSeqiNP_055927.2. NM_015112.2. [Q6P0Q8-1]
    XP_005270711.1. XM_005270654.1.
    UniGeneiHs.319481.

    Genome annotation databases

    EnsembliENST00000361297; ENSP00000354671; ENSG00000086015. [Q6P0Q8-1]
    GeneIDi23139.
    KEGGihsa:23139.
    UCSCiuc001cov.3. human. [Q6P0Q8-1]

    Polymorphism databases

    DMDMi62287152.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB047005 mRNA. Translation: BAB40778.1 . Frameshift.
    AL645480
    , AL358075 , AL603882 , AL603888 Genomic DNA. Translation: CAH73244.1 .
    AL645480 , AL358075 , AL603888 Genomic DNA. Translation: CAH73245.1 . Sequence problems.
    AL603882
    , AL358075 , AL603888 , AL645480 Genomic DNA. Translation: CAI16217.1 .
    AL603888
    , AL358075 , AL603882 , AL645480 Genomic DNA. Translation: CAI16562.1 .
    AL603888 , AL358075 , AL645480 Genomic DNA. Translation: CAI16563.1 . Sequence problems.
    AL358075
    , AL603882 , AL603888 , AL645480 Genomic DNA. Translation: CAI21705.1 .
    AL358075 , AL603888 , AL645480 Genomic DNA. Translation: CAI21706.1 . Sequence problems.
    BC015816 mRNA. Translation: AAH15816.2 . Different initiation.
    BC065499 mRNA. Translation: AAH65499.1 .
    AB018350 mRNA. Translation: BAA34527.2 .
    AL833919 mRNA. Translation: CAD38775.1 .
    CCDSi CCDS41326.1. [Q6P0Q8-1 ]
    RefSeqi NP_055927.2. NM_015112.2. [Q6P0Q8-1 ]
    XP_005270711.1. XM_005270654.1.
    UniGenei Hs.319481.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KQF NMR - A 1099-1193 [» ]
    2KYL NMR - A 1099-1193 [» ]
    ProteinModelPortali Q6P0Q8.
    SMRi Q6P0Q8. Positions 325-849, 1099-1193.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116756. 17 interactions.
    IntActi Q6P0Q8. 18 interactions.
    MINTi MINT-1892333.
    STRINGi 9606.ENSP00000354671.

    Chemistry

    ChEMBLi CHEMBL3038500.

    PTM databases

    PhosphoSitei Q6P0Q8.

    Polymorphism databases

    DMDMi 62287152.

    Proteomic databases

    MaxQBi Q6P0Q8.
    PaxDbi Q6P0Q8.
    PRIDEi Q6P0Q8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361297 ; ENSP00000354671 ; ENSG00000086015 . [Q6P0Q8-1 ]
    GeneIDi 23139.
    KEGGi hsa:23139.
    UCSCi uc001cov.3. human. [Q6P0Q8-1 ]

    Organism-specific databases

    CTDi 23139.
    GeneCardsi GC01P046252.
    H-InvDB HIX0000540.
    HGNCi HGNC:19035. MAST2.
    HPAi HPA039722.
    HPA040155.
    MIMi 612257. gene.
    neXtProti NX_Q6P0Q8.
    PharmGKBi PA134954073.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG052414.
    InParanoidi Q6P0Q8.
    KOi K08789.
    OMAi DMPRFAI.
    OrthoDBi EOG7PK8ZC.
    PhylomeDBi Q6P0Q8.
    TreeFami TF313149.

    Enzyme and pathway databases

    SignaLinki Q6P0Q8.

    Miscellaneous databases

    ChiTaRSi MAST2. human.
    GeneWikii MAST2.
    GenomeRNAii 23139.
    NextBioi 44410.
    PROi Q6P0Q8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6P0Q8.
    Bgeei Q6P0Q8.
    CleanExi HS_MAST2.
    Genevestigatori Q6P0Q8.

    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

    1. "Protocadherin LKC, a new candidate for a tumor suppressor of colon and liver cancers, its association with contact inhibition of cell proliferation."
      Okazaki N., Takahashi N., Kojima S., Masuho Y., Koga H.
      Carcinogenesis 23:1139-1148(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLU-388; MET-659 AND GLY-1551, SUBCELLULAR LOCATION, INTERACTION WITH CDHR2.
      Tissue: BrainImported.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
    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 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 281-1798 (ISOFORM 2), VARIANT MET-659.
      Tissue: LymphImported and PlacentaImported.
    4. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 470-1797 (ISOFORM 1), VARIANTS MET-659 AND GLY-1551.
      Tissue: BrainImported.
    5. Ohara O., Suyama M., Nagase T., Ishikawa K., Kikuno R.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO C-TERMINUS.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 833-1797 (ISOFORM 1).
      Tissue: Testis.
    7. "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: TISSUE SPECIFICITY.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74 AND SER-900, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74 AND SER-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74 AND SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-1032, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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.
      , 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] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] PHE-69; GLU-275; GLU-388; ALA-655; MET-659; LEU-991; ARG-1197; GLU-1221; LEU-1246; MET-1304; THR-1463; ALA-1468; GLY-1551; ARG-1673 AND GLU-1703.

    Entry informationi

    Entry nameiMAST2_HUMAN
    AccessioniPrimary (citable) accession number: Q6P0Q8
    Secondary accession number(s): O94899
    , Q5VT07, Q5VT08, Q7LGC4, Q8NDG1, Q96B94, Q9BYE8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: March 29, 2005
    Last modified: October 1, 2014
    This is version 111 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3