Q96GX5 (GWL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	879 AA.
Sequence status	Complete.
Protein existence	Evidence 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.16
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.14
Subcellular location	Cytoplasm › cytoskeleton › centrosome. 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.16
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 process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Inferred from mutant phenotype Ref.12Ref.11. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from mutant phenotype Ref.12. Source: UniProtKB 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 response to DNA damage stimulus Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	centrosome 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 nucleus Inferred from direct assay Ref.12Ref.11. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 879	879	Serine/threonine-protein kinase greatwall		PRO_0000086315
Regions
	Domain	35 – 835	801	Protein kinase
	Domain	836 – 879	44	AGC-kinase C-terminal
	Nucleotide binding	41 – 49	9	ATP By similarity
Sites
	Active site	156	1	Proton acceptor By similarity
	Binding site	62	1	ATP By similarity
Amino acid modifications
	Modified residue	207	1	Phosphothreonine Ref.13
	Modified residue	222	1	Phosphothreonine Ref.13
	Modified residue	293	1	Phosphoserine Ref.7
	Modified residue	370	1	Phosphoserine Ref.5 Ref.6 Ref.7 Ref.13
	Modified residue	552	1	Phosphoserine Ref.7
	Modified residue	556	1	Phosphoserine Ref.7
	Modified residue	631	1	Phosphoserine Ref.4 Ref.13
	Modified residue	657	1	Phosphoserine Ref.6
	Modified residue	668	1	Phosphoserine Ref.13
	Modified residue	722	1	Phosphothreonine Ref.7
	Modified residue	725	1	Phosphoserine Ref.7
	Modified residue	741	1	Phosphothreonine Ref.7
	Modified residue	875	1	Phosphoserine Ref.7 Ref.13
	Modified residue	878	1	Phosphoserine Ref.6 Ref.7 Ref.13
Natural variations
	Alternative sequence	708	1	Missing in isoform 2 and isoform 3.		VSP_014574
	Alternative sequence	756 – 793	38	Missing in isoform 2.		VSP_014575
	Natural variant	167	1	E → D in THC2. Ref.16 Corresponds to variant rs28941470 [ dbSNP | Ensembl ].		VAR_022838
	Natural variant	337	1	T → K. Ref.17 Corresponds to variant rs36121140 [ dbSNP | Ensembl ].		VAR_040792
	Natural variant	606	1	D → Y. Corresponds to variant rs35413630 [ dbSNP | Ensembl ].		VAR_057103
	Natural variant	610	1	V → I. Ref.17 Corresponds to variant rs35571315 [ dbSNP | Ensembl ].		VAR_040793
	Natural variant	620	1	P → A. Ref.17 Corresponds to variant rs3802526 [ dbSNP | Ensembl ].		VAR_022839
Experimental info
	Mutagenesis	72	1	K → M: Hyperactive form. Ref.14
	Sequence conflict	634	1	K → E in BAC11218. Ref.1
	Sequence conflict	685	1	C → R in BAB55321. Ref.1
	Sequence conflict	731	1	A → P in BAC11218. Ref.1
	Sequence conflict	865	1	A → T in BAB55321. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: E6533029D1CE58B4	FASTA	879	97,319
	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
	Isoform 2 [UniParc]. Checksum: 72CD7A9036188FE1	FASTA	840	92,861
	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 RRSCMPHQTP NQIKSGTPYR 730 740 750 760 770 780 TPKSVRRGVA PVDDGRILGT PDYLAPELLL GRAHDIPWPE GEEKLSDNAQ SAVEILLTID 790 800 810 820 830 840 DTKRAGMKEL KRHPLFSDVD WENLQHQTMP FIPQPDDETD TSYFEARNTA QHLTVSGFSL
	Isoform 3 [UniParc]. Checksum: D04E9C47F8615FCE	FASTA	878	97,191
	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 RRSCMPHQTP NQIKSGTPYR 730 740 750 760 770 780 TPKSVRRGVA PVDDGRILGT PDYLAPELLL GRAHGPAVDW WALGVCLFEF LTGIPPFNDE 790 800 810 820 830 840 TPQQVFQNIL KRDIPWPEGE EKLSDNAQSA VEILLTIDDT KRAGMKELKR HPLFSDVDWE 850 860 870 NLQHQTMPFI PQPDDETDTS YFEARNTAQH LTVSGFSL

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"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.
[17]	"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.
+	Additional computationally mapped references.

Web resources

GeneReviews

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.
IPI	IPI00074258. IPI00396230. IPI00550863.
RefSeq	NP_001165774.1. NM_001172303.1. NP_001165775.1. NM_001172304.1. NP_116233.2. NM_032844.3.
UniGene	Hs.276905.
3D structure databases
ProteinModelPortal	Q96GX5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96GX5. 2 interactions.
STRING	9606.ENSP00000365113.
PTM databases
PhosphoSite	Q96GX5.
Polymorphism databases
DMDM	68565604.
Proteomic databases
PaxDb	Q96GX5.
PRIDE	Q96GX5.
Protocols and materials databases
DNASU	84930.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000342386; ENSP00000343446; ENSG00000120539. ENST00000375940; ENSP00000365107; ENSG00000120539. ENST00000375946; ENSP00000365113; ENSG00000120539.
GeneID	84930.
KEGG	hsa:84930.
UCSC	uc001itl.3. human. uc001itm.3. human. uc009xkw.2. human.
Organism-specific databases
CTD	84930.
GeneCards	GC10P027484.
HGNC	HGNC:19042. MASTL.
HPA	HPA027175.
MIM	188000. phenotype. 608221. gene.
neXtProt	NX_Q96GX5.
Orphanet	168629. Autosomal thrombocytopenia with normal platelets.
PharmGKB	PA134943781.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOVERGEN	HBG074267.
InParanoid	Q96GX5.
KO	K16309.
OMA	GTPYRTP.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases.
Gene expression databases
Bgee	Q96GX5.
CleanEx	HS_MASTL.
Genevestigator	Q96GX5.
GermOnline	ENSG00000120539. Homo sapiens.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 2 hits. [Graphical view]
SMART	SM00133. S_TK_X. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	84930.
NextBio	75361.
SOURCE	Search...

Entry information

Entry name

GWL_HUMAN

Accession

Primary (citable) accession number: Q96GX5
Secondary accession number(s): Q5T8D5 , Q5T8D7, Q8NCD6, Q96SJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.