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Protein

Serine/threonine-protein kinase greatwall

Gene

Mastl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei61 – 611ATPPROSITE-ProRule annotation
Active sitei155 – 1551Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi40 – 489ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

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

ReactomeiR-MMU-2465910. MASTL Facilitates Mitotic Progression.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase greatwall (EC:2.7.11.1)
Short name:
GW
Short name:
GWL
Alternative name(s):
Microtubule-associated serine/threonine-protein kinase-like
Short name:
MAST-L
Gene namesi
Name:Mastl
Synonyms:Gw, Gwl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1914371. Mastl.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 865865Serine/threonine-protein kinase greatwallPRO_0000086316Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei206 – 2061PhosphothreonineBy similarity
Modified residuei221 – 2211PhosphothreonineBy similarity
Modified residuei362 – 3621PhosphoserineBy similarity
Modified residuei545 – 5451PhosphoserineBy similarity
Modified residuei619 – 6191PhosphoserineBy similarity
Modified residuei644 – 6441PhosphoserineBy similarity
Modified residuei655 – 6551PhosphoserineBy similarity
Modified residuei708 – 7081PhosphothreonineBy similarity
Modified residuei711 – 7111PhosphoserineBy similarity
Modified residuei727 – 7271Phosphothreonine; by CDK1By similarity
Modified residuei861 – 8611PhosphoserineBy similarity
Modified residuei864 – 8641PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation at Thr-727 by CDK1 during M phase activates its kinase activity. Maximum phosphorylation occurs in prometaphase (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8C0P0.
MaxQBiQ8C0P0.
PaxDbiQ8C0P0.
PRIDEiQ8C0P0.

PTM databases

iPTMnetiQ8C0P0.
PhosphoSiteiQ8C0P0.

Expressioni

Gene expression databases

BgeeiQ8C0P0.
GenevisibleiQ8C0P0. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028119.

Structurei

3D structure databases

ProteinModelPortaliQ8C0P0.
SMRiQ8C0P0. Positions 32-309, 726-861.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 821788Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini822 – 86544AGC-kinase C-terminalAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IUCW. Eukaryota.
ENOG410ZHM9. LUCA.
GeneTreeiENSGT00830000128396.
HOVERGENiHBG074267.
InParanoidiQ8C0P0.
KOiK16309.
OMAiCAYSGSY.
OrthoDBiEOG73RB9T.
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]
SMARTiSM00220. S_TKc. 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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8C0P0-1) [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

        10         20         30         40         50
MESASASEEN EGGAAIEECV SRIPVPRPPS IEEFTIVKPI SRGAFGKVYL
60 70 80 90 100
GQKGGKLYAV KVVKKADMIN KNMTHQVQAE RDALALSKSP FVVHLYYSLQ
110 120 130 140 150
SASNIYLIME YLIGGDVKSL LHIYGYFDEE MAIKYISEVA LALDYLHRHG
160 170 180 190 200
IIHRDLKPDN MLISNEGHIK LTDFGLSKVT LNRDINMMDI LTTPSMSKPK
210 220 230 240 250
QDYSRTPGQV LSLISSLGFF TPVGEKDQDS ANMFSAPKSA AQLSRGFICP
260 270 280 290 300
MSVDQKEPTS YSSKLLKSCF ETLSSNPEIP VKCLTSNLLQ CRKRLGTSST
310 320 330 340 350
SSQSHTFVSS VESECHSNPK WERDCQSTES SGCAMSWNAV EMLYAKSTSA
360 370 380 390 400
IKTKTELELA LSPIHDSSAI PAAGSNQVTL PRKCFREISW EARDPDNENM
410 420 430 440 450
TIDKGQSGFC QSSQRSVNSS ATSEEHLGKR NYKRNFHLVD SSPCQEIMQS
460 470 480 490 500
KKNCTEYEAN KERQGCRANQ STGLTTEVQN LKLSGCESQQ LDYANKENIV
510 520 530 540 550
TYLTDRQTPE KLHIPTIAKN LMSELDEDCE LSSKKDCLSS NSVCSDEDRA
560 570 580 590 600
LKTTCVDSDS SFPGVSMMES SLEIQALEPD KSIRDYSFEE PNTEDLFVLP
610 620 630 640 650
KCQENSLPQD DCHACIQDSS QVSAHPSKAP KALTSKINVV AFRSFNSHIN
660 670 680 690 700
ASTNSEPSKI SITSLDAMDI SCDYSGSYPM AVSPTEKGRH YTSHQTPNQV
710 720 730 740 750
KLGTSYRTPK SVRRGAAPVD DGRILGTPDY LAPELLLGTA HGPAVDWWAL
760 770 780 790 800
GVCLFEFLTG IPPFNDETPQ QVFQNILKRD IPWPEGEEKL SDNAQSAMDM
810 820 830 840 850
LLTIDDSKRA GMRELKQHPL FSEVDWENLQ HQTMPFVPQP DDETDTSYFE
860
ARNNAQHLTI SGFSL
Length:865
Mass (Da):95,975
Last modified:May 3, 2011 - v2
Checksum:i59C228B1E1D5CDC4
GO
Isoform 2 (identifier: Q8C0P0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     327-348: STESSGCAMSWNAVEMLYAKST → VSSKYSSLKLIYTRNQ
     349-865: Missing.

Show »
Length:342
Mass (Da):38,030
Checksum:i897F8D0E323D1FEE
GO

Sequence cautioni

The sequence AAH86483.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB24595.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC37239.1 differs from that shown. Reason: Erroneous termination at positions 12 and 56. Translated as Gly, Lys.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371V → E in BAC37239 (PubMed:16141072).Curated
Sequence conflicti62 – 621V → G in BAC37239 (PubMed:16141072).Curated
Sequence conflicti69 – 691I → V in BAC26804 (PubMed:16141072).Curated
Sequence conflicti79 – 791A → S in BAC37239 (PubMed:16141072).Curated
Sequence conflicti104 – 1041N → I in BAC37239 (PubMed:16141072).Curated
Sequence conflicti118 – 1181K → Q in BAC37239 (PubMed:16141072).Curated
Sequence conflicti222 – 2221P → S in AAI03780 (PubMed:15489334).Curated
Sequence conflicti247 – 2471F → L in BAB24595 (PubMed:16141072).Curated
Sequence conflicti314 – 3141E → G in AAI03780 (PubMed:15489334).Curated
Sequence conflicti323 – 3231R → T in BAC37239 (PubMed:16141072).Curated
Sequence conflicti376 – 3761N → D in BAB28343 (PubMed:16141072).Curated
Sequence conflicti455 – 4551T → S in AAI03780 (PubMed:15489334).Curated
Sequence conflicti529 – 5291C → R in AAH66834 (PubMed:19468303).Curated
Sequence conflicti529 – 5291C → R in AAH86483 (PubMed:19468303).Curated
Sequence conflicti672 – 6721C → Y in AAH66834 (PubMed:19468303).Curated
Sequence conflicti672 – 6721C → Y in AAH86483 (PubMed:19468303).Curated
Sequence conflicti699 – 6991Q → R in AAI03780 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei327 – 34822STESS…YAKST → VSSKYSSLKLIYTRNQ in isoform 2. 1 PublicationVSP_014576Add
BLAST
Alternative sequencei349 – 865517Missing in isoform 2. 1 PublicationVSP_014577Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK006448 mRNA. Translation: BAB24595.1. Different initiation.
AK012597 mRNA. Translation: BAB28343.2.
AK030140 mRNA. Translation: BAC26804.1.
AK078365 mRNA. Translation: BAC37239.1. Sequence problems.
AL845257 Genomic DNA. Translation: CAM19537.1.
CH466542 Genomic DNA. Translation: EDL08150.1.
BC066834 mRNA. Translation: AAH66834.1.
BC086483 mRNA. Translation: AAH86483.1. Different initiation.
BC103779 mRNA. Translation: AAI03780.1.
CCDSiCCDS15727.1. [Q8C0P0-1]
RefSeqiNP_080255.3. NM_025979.4. [Q8C0P0-1]
UniGeneiMm.253721.

Genome annotation databases

EnsembliENSMUST00000028119; ENSMUSP00000028119; ENSMUSG00000026779. [Q8C0P0-1]
GeneIDi67121.
KEGGimmu:67121.
UCSCiuc008iob.2. mouse. [Q8C0P0-1]
uc008ioc.1. mouse. [Q8C0P0-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK006448 mRNA. Translation: BAB24595.1. Different initiation.
AK012597 mRNA. Translation: BAB28343.2.
AK030140 mRNA. Translation: BAC26804.1.
AK078365 mRNA. Translation: BAC37239.1. Sequence problems.
AL845257 Genomic DNA. Translation: CAM19537.1.
CH466542 Genomic DNA. Translation: EDL08150.1.
BC066834 mRNA. Translation: AAH66834.1.
BC086483 mRNA. Translation: AAH86483.1. Different initiation.
BC103779 mRNA. Translation: AAI03780.1.
CCDSiCCDS15727.1. [Q8C0P0-1]
RefSeqiNP_080255.3. NM_025979.4. [Q8C0P0-1]
UniGeneiMm.253721.

3D structure databases

ProteinModelPortaliQ8C0P0.
SMRiQ8C0P0. Positions 32-309, 726-861.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028119.

PTM databases

iPTMnetiQ8C0P0.
PhosphoSiteiQ8C0P0.

Proteomic databases

EPDiQ8C0P0.
MaxQBiQ8C0P0.
PaxDbiQ8C0P0.
PRIDEiQ8C0P0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028119; ENSMUSP00000028119; ENSMUSG00000026779. [Q8C0P0-1]
GeneIDi67121.
KEGGimmu:67121.
UCSCiuc008iob.2. mouse. [Q8C0P0-1]
uc008ioc.1. mouse. [Q8C0P0-2]

Organism-specific databases

CTDi84930.
MGIiMGI:1914371. Mastl.

Phylogenomic databases

eggNOGiENOG410IUCW. Eukaryota.
ENOG410ZHM9. LUCA.
GeneTreeiENSGT00830000128396.
HOVERGENiHBG074267.
InParanoidiQ8C0P0.
KOiK16309.
OMAiCAYSGSY.
OrthoDBiEOG73RB9T.
TreeFamiTF313149.

Enzyme and pathway databases

ReactomeiR-MMU-2465910. MASTL Facilitates Mitotic Progression.

Miscellaneous databases

PROiQ8C0P0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C0P0.
GenevisibleiQ8C0P0. MM.

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]
SMARTiSM00220. S_TKc. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Cerebellum, Embryo and Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] OF 194-865 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Egg and Embryonic germ cell.
  5. "Targeting mitotic exit leads to tumor regression in vivo: Modulation by Cdk1, Mastl, and the PP2A/B55alpha,delta phosphatase."
    Manchado E., Guillamot M., de Carcer G., Eguren M., Trickey M., Garcia-Higuera I., Moreno S., Yamano H., Canamero M., Malumbres M.
    Cancer Cell 18:641-654(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiGWL_MOUSE
AccessioniPrimary (citable) accession number: Q8C0P0
Secondary accession number(s): A2AQY2
, Q3MIA9, Q5RJW0, Q6NXX9, Q8BVF3, Q9CZH9, Q9D9V0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: May 3, 2011
Last modified: June 8, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.