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Q96GX5 (GWL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase greatwall

Short name=GW
Short name=GWL
Short name=hGWL
EC=2.7.11.1
Alternative name(s):
Microtubule-associated serine/threonine-protein kinase-like
Short name=MAST-L
Gene names
Name:MASTL
Synonyms:GW, GWL, THC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length879 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9 Ref.11 Ref.12 Ref.17

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.14

Subcellular location

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. Ref.11 Ref.12

Post-translational modification

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

Involvement in disease

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. Ref.17

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 (Ref.11 and Ref.12).

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Inferred from mutant phenotype Ref.12Ref.11. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

mitosis

Inferred from mutant phenotype Ref.12. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of protein phosphatase type 2A activity

Inferred from mutant phenotype Ref.12. Source: UniProtKB

regulation of cell cycle

Inferred from mutant phenotype Ref.11. Source: UniProtKB

   Cellular_componentcentrosome

Inferred from direct assay Ref.12. Source: UniProtKB

cleavage furrow

Inferred from direct assay Ref.12Ref.11. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.12Ref.11. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

kinase activity

Inferred from direct assay Ref.11. Source: UniProtKB

protein phosphatase 2A binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.12. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96GX5-1)

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.
Isoform 2 (identifier: Q96GX5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     708-708: Missing.
     756-793: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q96GX5-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 879879Serine/threonine-protein kinase greatwall
PRO_0000086315

Regions

Domain35 – 835801Protein kinase
Domain836 – 87944AGC-kinase C-terminal
Nucleotide binding41 – 499ATP By similarity

Sites

Active site1561Proton acceptor By similarity
Binding site621ATP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.16
Modified residue2071Phosphothreonine Ref.13
Modified residue2221Phosphothreonine Ref.13
Modified residue2931Phosphoserine Ref.7
Modified residue3701Phosphoserine Ref.5 Ref.6 Ref.7 Ref.13
Modified residue5521Phosphoserine Ref.7
Modified residue5561Phosphoserine Ref.7
Modified residue6311Phosphoserine Ref.4 Ref.13
Modified residue6571Phosphoserine Ref.6
Modified residue6681Phosphoserine Ref.13
Modified residue7221Phosphothreonine Ref.7
Modified residue7251Phosphoserine Ref.7
Modified residue7411Phosphothreonine Ref.7
Modified residue8751Phosphoserine Ref.7 Ref.13
Modified residue8781Phosphoserine Ref.6 Ref.7 Ref.13

Natural variations

Alternative sequence7081Missing in isoform 2 and isoform 3.
VSP_014574
Alternative sequence756 – 79338Missing in isoform 2.
VSP_014575
Natural variant1671E → D in THC2. Ref.17
Corresponds to variant rs28941470 [ dbSNP | Ensembl ].
VAR_022838
Natural variant3371T → K. Ref.18
Corresponds to variant rs36121140 [ dbSNP | Ensembl ].
VAR_040792
Natural variant6061D → Y.
Corresponds to variant rs35413630 [ dbSNP | Ensembl ].
VAR_057103
Natural variant6101V → I. Ref.18
Corresponds to variant rs35571315 [ dbSNP | Ensembl ].
VAR_040793
Natural variant6201P → A. Ref.18
Corresponds to variant rs3802526 [ dbSNP | Ensembl ].
VAR_022839

Experimental info

Mutagenesis721K → M: Hyperactive form. Ref.14
Sequence conflict6341K → E in BAC11218. Ref.1
Sequence conflict6851C → R in BAB55321. Ref.1
Sequence conflict7311A → P in BAC11218. Ref.1
Sequence conflict8651A → T in BAB55321. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: E6533029D1CE58B4

FASTA87997,319
        10         20         30         40         50         60 
MDPTAGSKKE PGGGAATEEG VNRIAVPKPP SIEEFSIVKP ISRGAFGKVY LGQKGGKLYA 

        70         80         90        100        110        120 
VKVVKKADMI NKNMTHQVQA ERDALALSKS PFIVHLYYSL QSANNVYLVM EYLIGGDVKS 

       130        140        150        160        170        180 
LLHIYGYFDE EMAVKYISEV ALALDYLHRH GIIHRDLKPD NMLISNEGHI KLTDFGLSKV 

       190        200        210        220        230        240 
TLNRDINMMD ILTTPSMAKP RQDYSRTPGQ VLSLISSLGF NTPIAEKNQD PANILSACLS 

       250        260        270        280        290        300 
ETSQLSQGLV CPMSVDQKDT TPYSSKLLKS CLETVASNPG MPVKCLTSNL LQSRKRLATS 

       310        320        330        340        350        360 
SASSQSHTFI SSVESECHSS PKWEKDCQES DEALGPTMMS WNAVEKLCAK SANAIETKGF 

       370        380        390        400        410        420 
NKKDLELALS PIHNSSALPT TGRSCVNLAK KCFSGEVSWE AVELDVNNIN MDTDTSQLGF 

       430        440        450        460        470        480 
HQSNQWAVDS GGISEEHLGK RSLKRNFELV DSSPCKKIIQ NKKTCVEYKH NEMTNCYTNQ 

       490        500        510        520        530        540 
NTGLTVEVQD LKLSVHKSQQ NDCANKENIV NSFTDKQQTP EKLPIPMIAK NLMCELDEDC 

       550        560        570        580        590        600 
EKNSKRDYLS SSFLCSDDDR ASKNISMNSD SSFPGISIME SPLESQPLDS DRSIKESSFE 

       610        620        630        640        650        660 
ESNIEDPLIV TPDCQEKTSP KGVENPAVQE SNQKMLGPPL EVLKTLASKR NAVAFRSFNS 

       670        680        690        700        710        720 
HINASNNSEP SRMNMTSLDA MDISCAYSGS YPMAITPTQK RRSCMPHQQT PNQIKSGTPY 

       730        740        750        760        770        780 
RTPKSVRRGV APVDDGRILG TPDYLAPELL LGRAHGPAVD WWALGVCLFE FLTGIPPFND 

       790        800        810        820        830        840 
ETPQQVFQNI LKRDIPWPEG EEKLSDNAQS AVEILLTIDD TKRAGMKELK RHPLFSDVDW 

       850        860        870 
ENLQHQTMPF IPQPDDETDT SYFEARNTAQ HLTVSGFSL 

« Hide

Isoform 2 [UniParc].

Checksum: 72CD7A9036188FE1
Show »

FASTA84092,861
Isoform 3 [UniParc].

Checksum: D04E9C47F8615FCE
Show »

FASTA87897,191

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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. 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] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-337; ILE-610 AND ALA-620.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001165774.1. NM_001172303.1.
NP_001165775.1. NM_001172304.1.
NP_116233.2. NM_032844.3.
UniGeneHs.276905.

3D structure databases

ProteinModelPortalQ96GX5.
SMRQ96GX5. Positions 33-291, 740-870.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124364. 5 interactions.
IntActQ96GX5. 2 interactions.
STRING9606.ENSP00000365113.

PTM databases

PhosphoSiteQ96GX5.

Polymorphism databases

DMDM68565604.

Proteomic databases

PaxDbQ96GX5.
PRIDEQ96GX5.

Protocols and materials databases

DNASU84930.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342386; ENSP00000343446; ENSG00000120539. [Q96GX5-2]
ENST00000375940; ENSP00000365107; ENSG00000120539. [Q96GX5-1]
ENST00000375946; ENSP00000365113; ENSG00000120539. [Q96GX5-3]
GeneID84930.
KEGGhsa:84930.
UCSCuc001itl.3. human. [Q96GX5-3]
uc001itm.3. human. [Q96GX5-1]
uc009xkw.2. human. [Q96GX5-2]

Organism-specific databases

CTD84930.
GeneCardsGC10P027484.
HGNCHGNC:19042. MASTL.
HPAHPA027175.
MIM188000. phenotype.
608221. gene.
neXtProtNX_Q96GX5.
Orphanet168629. Autosomal thrombocytopenia with normal platelets.
PharmGKBPA134943781.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG074267.
InParanoidQ96GX5.
KOK16309.
OMAILLTIDD.
OrthoDBEOG73RB9T.
PhylomeDBQ96GX5.
TreeFamTF313149.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
SignaLinkQ96GX5.

Gene expression databases

BgeeQ96GX5.
CleanExHS_MASTL.
GenevestigatorQ96GX5.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 2 hits.
[Graphical view]
SMARTSM00133. S_TK_X. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
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Other

GeneWikiMASTL.
GenomeRNAi84930.
NextBio75361.
PROQ96GX5.
SOURCESearch...

Entry information

Entry nameGWL_HUMAN
AccessionPrimary (citable) accession number: Q96GX5
Secondary accession number(s): Q5T8D5 expand/collapse secondary AC list , Q5T8D7, Q8NCD6, Q96SJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM