TASP1_MOUSE
ID TASP1_MOUSE Reviewed; 420 AA.
AC Q8R1G1; Q99JP3;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Threonine aspartase 1;
DE Short=Taspase-1;
DE EC=3.4.25.-;
DE Contains:
DE RecName: Full=Threonine aspartase subunit alpha;
DE Contains:
DE RecName: Full=Threonine aspartase subunit beta;
GN Name=Tasp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16951254; DOI=10.1101/gad.1449406;
RA Takeda S., Chen D.Y., Westergard T.D., Fisher J.K., Rubens J.A.,
RA Sasagawa S., Kan J.T., Korsmeyer S.J., Cheng E.H., Hsieh J.J.;
RT "Proteolysis of MLL family proteins is essential for taspase1-orchestrated
RT cell cycle progression.";
RL Genes Dev. 20:2397-2409(2006).
CC -!- FUNCTION: Protease responsible for KMT2A/MLL1 and KMT2D/MLL2 processing
CC and activation (PubMed:16951254). Through substrate activation, it
CC controls the expression of HOXA genes, and the expression of key cell
CC cycle regulators including CCNA1, CCNB1, CCNE1 and CDKN2A
CC (PubMed:16951254). {ECO:0000250|UniProtKB:Q9H6P5,
CC ECO:0000269|PubMed:16951254}.
CC -!- SUBUNIT: Intramolecular proteolysis generates 2 subunits, alpha and
CC beta, which reassemble through a non-covalent association to form the
CC fully active enzyme. {ECO:0000250|UniProtKB:Q9H6P5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist. Experimental confirmation
CC may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q8R1G1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R1G1-2; Sequence=VSP_000334, VSP_000335;
CC -!- DISRUPTION PHENOTYPE: Tasp1-null mice are born with no apparent
CC respiratory distress, but the majority dies at postpartum day 1 or 2
CC with no obvious milk spots, suggesting a feeding defect. Newborns are
CC smaller in size compared to their wild-type littermates. This phenotype
CC appears in utero. Animals that survive the newborn period are markedly
CC smaller through adulthood, and display skeletal abnormalities.
CC {ECO:0000269|PubMed:16951254}.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05776.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK036512; BAC29457.1; -; mRNA.
DR EMBL; AK050603; BAC34335.1; -; mRNA.
DR EMBL; BC005776; AAH05776.1; ALT_INIT; mRNA.
DR EMBL; BC024597; AAH24597.1; -; mRNA.
DR CCDS; CCDS16802.1; -. [Q8R1G1-1]
DR RefSeq; NP_001153112.1; NM_001159640.2. [Q8R1G1-1]
DR RefSeq; NP_001153113.1; NM_001159641.2.
DR RefSeq; NP_001276540.1; NM_001289611.1.
DR RefSeq; NP_780434.1; NM_175225.5. [Q8R1G1-1]
DR AlphaFoldDB; Q8R1G1; -.
DR SMR; Q8R1G1; -.
DR STRING; 10090.ENSMUSP00000039546; -.
DR MEROPS; T02.004; -.
DR iPTMnet; Q8R1G1; -.
DR PhosphoSitePlus; Q8R1G1; -.
DR EPD; Q8R1G1; -.
DR MaxQB; Q8R1G1; -.
DR PaxDb; Q8R1G1; -.
DR PeptideAtlas; Q8R1G1; -.
DR PRIDE; Q8R1G1; -.
DR ProteomicsDB; 263208; -. [Q8R1G1-1]
DR ProteomicsDB; 263209; -. [Q8R1G1-2]
DR Antibodypedia; 24250; 197 antibodies from 26 providers.
DR DNASU; 75812; -.
DR Ensembl; ENSMUST00000046656; ENSMUSP00000039546; ENSMUSG00000039033. [Q8R1G1-1]
DR Ensembl; ENSMUST00000110079; ENSMUSP00000105706; ENSMUSG00000039033. [Q8R1G1-1]
DR GeneID; 75812; -.
DR KEGG; mmu:75812; -.
DR UCSC; uc008mpg.3; mouse. [Q8R1G1-1]
DR UCSC; uc008mpm.2; mouse. [Q8R1G1-2]
DR CTD; 55617; -.
DR MGI; MGI:1923062; Tasp1.
DR VEuPathDB; HostDB:ENSMUSG00000039033; -.
DR eggNOG; KOG1592; Eukaryota.
DR GeneTree; ENSGT00950000183045; -.
DR InParanoid; Q8R1G1; -.
DR OMA; RLWCAFT; -.
DR OrthoDB; 1450528at2759; -.
DR PhylomeDB; Q8R1G1; -.
DR TreeFam; TF106358; -.
DR BioGRID-ORCS; 75812; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Tasp1; mouse.
DR PRO; PR:Q8R1G1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8R1G1; protein.
DR Bgee; ENSMUSG00000039033; Expressed in spermatid and 241 other tissues.
DR ExpressionAtlas; Q8R1G1; baseline and differential.
DR Genevisible; Q8R1G1; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0051604; P:protein maturation; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR CDD; cd04514; Taspase1_like; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000246; Peptidase_T2.
DR InterPro; IPR037464; Taspase1.
DR PANTHER; PTHR10188; PTHR10188; 1.
DR Pfam; PF01112; Asparaginase_2; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Protease; Reference proteome;
KW Threonine protease; Zymogen.
FT CHAIN 1..233
FT /note="Threonine aspartase subunit alpha"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002352"
FT CHAIN 234..420
FT /note="Threonine aspartase subunit beta"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002353"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 234
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9H6P5"
FT VAR_SEQ 226..253
FT /note="ENDSGTLDTVGAVVVDHEGNVAAAVSSG -> VRRCLKNWLMHGRDVVDLLL
FT EQYCPFEL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_000334"
FT VAR_SEQ 254..420
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_000335"
SQ SEQUENCE 420 AA; 44360 MW; 13F648362CF617C4 CRC64;
MIMEKGMNSG EGLPSRSSQA SAAKVTVKEL ETQQPCKEKR GGFVLVHAGA GYHSESKAKE
YKHVCKRACQ KAIEKLQAGA LATDAVAAAL VELEDSPFTN AGIGSNLNLL GEIECDASIM
DGKSLNFGAV GALSGIKNPV SVAHRLLCEG QKGKLSAGRI PPCFLVGEGA YRWAVDHGIP
SCPPSTMTTR FSLAAFKRNK RKLELAERVE TDFIQLKRRR QSSAKENDSG TLDTVGAVVV
DHEGNVAAAV SSGGLALKHP GRVGQAALYG CGCWAENTGA QNPYSTAVST SGCGEHLVRT
ILARECSHAL QAEDAHQALL ETMQNKFISS PFLACEDGVL GGVIVLRSCR CSSESDSSQD
KQTLLVEFLW SHTTESMCVG YMSAQDGKAK THISRLPPGA VAGQSVAIEG GVCRLESPVN
