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Q96GX5

- GWL_HUMAN

UniProt

Q96GX5 - GWL_HUMAN

Protein

Serine/threonine-protein kinase greatwall

Gene

MASTL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and ENSA at 'Ser-62' and 'Ser-67', respectively. ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited. Phosphorylates histone protein in vitro; however such activity is unsure in vivo. May be involved in megakaryocyte differentiation.5 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei62 – 621ATPPROSITE-ProRule annotation
    Active sitei156 – 1561Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi41 – 499ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. G2/M transition of mitotic cell cycle Source: UniProtKB
    3. mitotic cell cycle Source: Reactome
    4. mitotic nuclear division Source: UniProtKB
    5. negative regulation of protein phosphatase type 2A activity Source: UniProtKB
    6. regulation of cell cycle Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_150182. MASTL Facilitates Mitotic Progression.
    SignaLinkiQ96GX5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase greatwall (EC:2.7.11.1)
    Short name:
    GW
    Short name:
    GWL
    Short name:
    hGWL
    Alternative name(s):
    Microtubule-associated serine/threonine-protein kinase-like
    Short name:
    MAST-L
    Gene namesi
    Name:MASTL
    Synonyms:GW, GWL, THC2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:19042. MASTL.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Nucleus. Cleavage furrow
    Note: During interphase is mainly nuclear, upon nuclear envelope breakdown localizes at the cytoplasm and during mitosis at the centrosomes. Upon mitotic exit moves to the cleavage furrow.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cleavage furrow Source: UniProtKB
    3. cytoplasm Source: UniProtKB-KW
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Thrombocytopenia 2 (THC2) [MIM:188000]: Thrombocytopenia is defined by a decrease in the number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti167 – 1671E → D in THC2. 1 Publication
    Corresponds to variant rs28941470 [ dbSNP | Ensembl ].
    VAR_022838

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi72 – 721K → M: Hyperactive form. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi188000. phenotype.
    Orphaneti168629. Autosomal thrombocytopenia with normal platelets.
    PharmGKBiPA134943781.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 879879Serine/threonine-protein kinase greatwallPRO_0000086315Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei207 – 2071Phosphothreonine1 Publication
    Modified residuei222 – 2221Phosphothreonine1 Publication
    Modified residuei293 – 2931Phosphoserine1 Publication
    Modified residuei370 – 3701Phosphoserine4 Publications
    Modified residuei552 – 5521Phosphoserine1 Publication
    Modified residuei556 – 5561Phosphoserine1 Publication
    Modified residuei631 – 6311Phosphoserine2 Publications
    Modified residuei657 – 6571Phosphoserine1 Publication
    Modified residuei668 – 6681Phosphoserine1 Publication
    Modified residuei722 – 7221Phosphothreonine1 Publication
    Modified residuei725 – 7251Phosphoserine1 Publication
    Modified residuei741 – 7411Phosphothreonine1 Publication
    Modified residuei875 – 8751Phosphoserine2 Publications
    Modified residuei878 – 8781Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylation at Thr-741 by CDK1 during M phase activates its kinase activity By similarity. Maximum phosphorylation occurs in prometaphase.By similarity7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96GX5.
    PaxDbiQ96GX5.
    PRIDEiQ96GX5.

    PTM databases

    PhosphoSiteiQ96GX5.

    Expressioni

    Gene expression databases

    BgeeiQ96GX5.
    CleanExiHS_MASTL.
    GenevestigatoriQ96GX5.

    Organism-specific databases

    HPAiHPA027175.

    Interactioni

    Protein-protein interaction databases

    BioGridi124364. 5 interactions.
    IntActiQ96GX5. 2 interactions.
    STRINGi9606.ENSP00000365113.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96GX5.
    SMRiQ96GX5. Positions 33-291, 676-873.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 835801Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini836 – 87944AGC-kinase C-terminalAdd
    BLAST

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG074267.
    InParanoidiQ96GX5.
    KOiK16309.
    OMAiILLTIDD.
    OrthoDBiEOG73RB9T.
    PhylomeDBiQ96GX5.
    TreeFamiTF313149.

    Family and domain databases

    InterProiIPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 2 hits.
    [Graphical view]
    SMARTiSM00133. S_TK_X. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96GX5-1) [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

    MDPTAGSKKE PGGGAATEEG VNRIAVPKPP SIEEFSIVKP ISRGAFGKVY    50
    LGQKGGKLYA VKVVKKADMI NKNMTHQVQA ERDALALSKS PFIVHLYYSL 100
    QSANNVYLVM EYLIGGDVKS LLHIYGYFDE EMAVKYISEV ALALDYLHRH 150
    GIIHRDLKPD NMLISNEGHI KLTDFGLSKV TLNRDINMMD ILTTPSMAKP 200
    RQDYSRTPGQ VLSLISSLGF NTPIAEKNQD PANILSACLS ETSQLSQGLV 250
    CPMSVDQKDT TPYSSKLLKS CLETVASNPG MPVKCLTSNL LQSRKRLATS 300
    SASSQSHTFI SSVESECHSS PKWEKDCQES DEALGPTMMS WNAVEKLCAK 350
    SANAIETKGF NKKDLELALS PIHNSSALPT TGRSCVNLAK KCFSGEVSWE 400
    AVELDVNNIN MDTDTSQLGF HQSNQWAVDS GGISEEHLGK RSLKRNFELV 450
    DSSPCKKIIQ NKKTCVEYKH NEMTNCYTNQ NTGLTVEVQD LKLSVHKSQQ 500
    NDCANKENIV NSFTDKQQTP EKLPIPMIAK NLMCELDEDC EKNSKRDYLS 550
    SSFLCSDDDR ASKNISMNSD SSFPGISIME SPLESQPLDS DRSIKESSFE 600
    ESNIEDPLIV TPDCQEKTSP KGVENPAVQE SNQKMLGPPL EVLKTLASKR 650
    NAVAFRSFNS HINASNNSEP SRMNMTSLDA MDISCAYSGS YPMAITPTQK 700
    RRSCMPHQQT PNQIKSGTPY RTPKSVRRGV APVDDGRILG TPDYLAPELL 750
    LGRAHGPAVD WWALGVCLFE FLTGIPPFND ETPQQVFQNI LKRDIPWPEG 800
    EEKLSDNAQS AVEILLTIDD TKRAGMKELK RHPLFSDVDW ENLQHQTMPF 850
    IPQPDDETDT SYFEARNTAQ HLTVSGFSL 879
    Length:879
    Mass (Da):97,319
    Last modified:December 1, 2001 - v1
    Checksum:iE6533029D1CE58B4
    GO
    Isoform 2 (identifier: Q96GX5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         708-708: Missing.
         756-793: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:840
    Mass (Da):92,861
    Checksum:i72CD7A9036188FE1
    GO
    Isoform 3 (identifier: Q96GX5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         708-708: Missing.

    Show »
    Length:878
    Mass (Da):97,191
    Checksum:iD04E9C47F8615FCE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti634 – 6341K → E in BAC11218. (PubMed:14702039)Curated
    Sequence conflicti685 – 6851C → R in BAB55321. (PubMed:14702039)Curated
    Sequence conflicti731 – 7311A → P in BAC11218. (PubMed:14702039)Curated
    Sequence conflicti865 – 8651A → T in BAB55321. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti167 – 1671E → D in THC2. 1 Publication
    Corresponds to variant rs28941470 [ dbSNP | Ensembl ].
    VAR_022838
    Natural varianti337 – 3371T → K.1 Publication
    Corresponds to variant rs36121140 [ dbSNP | Ensembl ].
    VAR_040792
    Natural varianti606 – 6061D → Y.
    Corresponds to variant rs35413630 [ dbSNP | Ensembl ].
    VAR_057103
    Natural varianti610 – 6101V → I.1 Publication
    Corresponds to variant rs35571315 [ dbSNP | Ensembl ].
    VAR_040793
    Natural varianti620 – 6201P → A.1 Publication
    Corresponds to variant rs3802526 [ dbSNP | Ensembl ].
    VAR_022839

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei708 – 7081Missing in isoform 2 and isoform 3. 1 PublicationVSP_014574
    Alternative sequencei756 – 79338Missing in isoform 2. 1 PublicationVSP_014575Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK027719 mRNA. Translation: BAB55321.1.
    AK074804 mRNA. Translation: BAC11218.1.
    AL160291 Genomic DNA. Translation: CAI16908.1.
    AL160291 Genomic DNA. Translation: CAI16909.1.
    AL160291 Genomic DNA. Translation: CAI16910.1.
    BC009107 mRNA. Translation: AAH09107.1.
    CCDSiCCDS53502.1. [Q96GX5-1]
    CCDS53503.1. [Q96GX5-2]
    CCDS7153.1. [Q96GX5-3]
    RefSeqiNP_001165774.1. NM_001172303.1. [Q96GX5-1]
    NP_001165775.1. NM_001172304.1. [Q96GX5-2]
    NP_116233.2. NM_032844.3. [Q96GX5-3]
    UniGeneiHs.276905.

    Genome annotation databases

    EnsembliENST00000342386; ENSP00000343446; ENSG00000120539. [Q96GX5-2]
    ENST00000375940; ENSP00000365107; ENSG00000120539. [Q96GX5-1]
    ENST00000375946; ENSP00000365113; ENSG00000120539. [Q96GX5-3]
    GeneIDi84930.
    KEGGihsa:84930.
    UCSCiuc001itl.3. human. [Q96GX5-3]
    uc001itm.3. human. [Q96GX5-1]
    uc009xkw.2. human. [Q96GX5-2]

    Polymorphism databases

    DMDMi68565604.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK027719 mRNA. Translation: BAB55321.1 .
    AK074804 mRNA. Translation: BAC11218.1 .
    AL160291 Genomic DNA. Translation: CAI16908.1 .
    AL160291 Genomic DNA. Translation: CAI16909.1 .
    AL160291 Genomic DNA. Translation: CAI16910.1 .
    BC009107 mRNA. Translation: AAH09107.1 .
    CCDSi CCDS53502.1. [Q96GX5-1 ]
    CCDS53503.1. [Q96GX5-2 ]
    CCDS7153.1. [Q96GX5-3 ]
    RefSeqi NP_001165774.1. NM_001172303.1. [Q96GX5-1 ]
    NP_001165775.1. NM_001172304.1. [Q96GX5-2 ]
    NP_116233.2. NM_032844.3. [Q96GX5-3 ]
    UniGenei Hs.276905.

    3D structure databases

    ProteinModelPortali Q96GX5.
    SMRi Q96GX5. Positions 33-291, 676-873.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124364. 5 interactions.
    IntActi Q96GX5. 2 interactions.
    STRINGi 9606.ENSP00000365113.

    PTM databases

    PhosphoSitei Q96GX5.

    Polymorphism databases

    DMDMi 68565604.

    Proteomic databases

    MaxQBi Q96GX5.
    PaxDbi Q96GX5.
    PRIDEi Q96GX5.

    Protocols and materials databases

    DNASUi 84930.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000342386 ; ENSP00000343446 ; ENSG00000120539 . [Q96GX5-2 ]
    ENST00000375940 ; ENSP00000365107 ; ENSG00000120539 . [Q96GX5-1 ]
    ENST00000375946 ; ENSP00000365113 ; ENSG00000120539 . [Q96GX5-3 ]
    GeneIDi 84930.
    KEGGi hsa:84930.
    UCSCi uc001itl.3. human. [Q96GX5-3 ]
    uc001itm.3. human. [Q96GX5-1 ]
    uc009xkw.2. human. [Q96GX5-2 ]

    Organism-specific databases

    CTDi 84930.
    GeneCardsi GC10P027484.
    HGNCi HGNC:19042. MASTL.
    HPAi HPA027175.
    MIMi 188000. phenotype.
    608221. gene.
    neXtProti NX_Q96GX5.
    Orphaneti 168629. Autosomal thrombocytopenia with normal platelets.
    PharmGKBi PA134943781.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG074267.
    InParanoidi Q96GX5.
    KOi K16309.
    OMAi ILLTIDD.
    OrthoDBi EOG73RB9T.
    PhylomeDBi Q96GX5.
    TreeFami TF313149.

    Enzyme and pathway databases

    Reactomei REACT_150182. MASTL Facilitates Mitotic Progression.
    SignaLinki Q96GX5.

    Miscellaneous databases

    GeneWikii MASTL.
    GenomeRNAii 84930.
    NextBioi 75361.
    PROi Q96GX5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q96GX5.
    CleanExi HS_MASTL.
    Genevestigatori Q96GX5.

    Family and domain databases

    InterProi IPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 2 hits.
    [Graphical view ]
    SMARTi SM00133. S_TK_X. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    2. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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).
      Tissue: Placenta.
    4. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-657 AND SER-878, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-370; SER-552; SER-556; THR-722; SER-725; THR-741; SER-875 AND SER-878, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Greatwall maintains mitosis through regulation of PP2A."
      Vigneron S., Brioudes E., Burgess A., Labbe J.C., Lorca T., Castro A.
      EMBO J. 28:2786-2793(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "The M phase kinase Greatwall (Gwl) promotes inactivation of PP2A/B55delta, a phosphatase directed against CDK phosphosites."
      Castilho P.V., Williams B.C., Mochida S., Zhao Y., Goldberg M.L.
      Mol. Biol. Cell 20:4777-4789(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "MASTL is the human orthologue of Greatwall kinase that facilitates mitotic entry, anaphase and cytokinesis."
      Voets E., Wolthuis R.M.F.
      Cell Cycle 9:3591-3601(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    12. "Loss of human Greatwall results in G2 arrest and multiple mitotic defects due to deregulation of the cyclin B-Cdc2/PP2A balance."
      Burgess A., Vigneron S., Brioudes E., Labbe J.-C., Lorca T., Castro A.
      Proc. Natl. Acad. Sci. U.S.A. 107:12564-12569(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    13. "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 THR-207; THR-222; SER-370; SER-631; SER-668; SER-875 AND SER-878, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "The substrate of Greatwall kinase, Arpp19, controls mitosis by inhibiting protein phosphatase 2A."
      Gharbi-Ayachi A., Labbe J.C., Burgess A., Vigneron S., Strub J.M., Brioudes E., Van-Dorsselaer A., Castro A., Lorca T.
      Science 330:1673-1677(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-72.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "FLJ14813 missense mutation: a candidate for autosomal dominant thrombocytopenia on human chromosome 10."
      Gandhi M.J., Cummings C.L., Drachman J.G.
      Hum. Hered. 55:66-70(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT THC2 ASP-167, FUNCTION.
    18. "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] LYS-337; ILE-610 AND ALA-620.

    Entry informationi

    Entry nameiGWL_HUMAN
    AccessioniPrimary (citable) accession number: Q96GX5
    Secondary accession number(s): Q5T8D5
    , Q5T8D7, Q8NCD6, Q96SJ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 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

    Miscellaneous

    Reduced levels of MASTL by RNAi causes mitotic abnormalities that consist of delay in G2 phase and slow chromosome condensation. Cells that enter and progress through mitosis often fail to completely separate their sister chromatids in anaphase leading to the formation of 4N G1 cells subsequent to failure of cytokinesis (PubMed:20818157 and PubMed:20538976).

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3