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Q96GX5

- GWL_HUMAN

UniProt

Q96GX5 - GWL_HUMAN

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Protein
Serine/threonine-protein kinase greatwall
Gene
MASTL, GW, GWL, THC2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 621ATP By similarity
Active sitei156 – 1561Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi41 – 499ATP By similarity

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. G2/M transition of mitotic cell cycle Source: UniProtKB
  2. cellular response to DNA damage stimulus 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
Complete GO annotation...

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.2 Publications

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 greatwall
PRO_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.

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 835801Protein kinase
Add
BLAST
Domaini836 – 87944AGC-kinase C-terminal
Add
BLAST

Sequence similaritiesi

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

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.
VSP_014574
Alternative sequencei756 – 79338Missing in isoform 2.
VSP_014575Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti634 – 6341K → E in BAC11218. 1 Publication
Sequence conflicti685 – 6851C → R in BAB55321. 1 Publication
Sequence conflicti731 – 7311A → P in BAC11218. 1 Publication
Sequence conflicti865 – 8651A → T in BAB55321. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 122 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 (1 Publication and 1 Publication).

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

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