GTSE1_MOUSE
ID GTSE1_MOUSE Reviewed; 741 AA.
AC Q8R080; O89015; Q9CSG9;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=G2 and S phase-expressed protein 1;
DE Short=GTSE-1;
DE AltName: Full=Protein B99;
GN Name=Gtse1; Synonyms=B99;
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 [MRNA].
RX PubMed=9724637; DOI=10.1093/emboj/17.17.5015;
RA Utrera R., Collavin L., Lazarevic D., Delia D., Schneider C.;
RT "A novel p53-inducible gene coding for a microtubule-localized protein with
RT G2-phase-specific expression.";
RL EMBO J. 17:5015-5025(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-130.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [4]
RP DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
RX PubMed=10984615; DOI=10.1016/s0014-5793(00)01969-4;
RA Collavin L., Monte M., Verardo R., Pfleger C., Schneider C.;
RT "Cell-cycle regulation of the p53-inducible gene B99.";
RL FEBS Lett. 481:57-62(2000).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND THR-465, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May be involved in p53-induced cell cycle arrest in G2/M
CC phase by interfering with microtubule rearrangements that are required
CC to enter mitosis. Overexpression delays G2/M phase progression.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Associated with
CC microtubules.
CC -!- DEVELOPMENTAL STAGE: Expression begins at S phase, accumulates in late
CC S/G2 phase and disappears in G1 phase. {ECO:0000269|PubMed:10984615}.
CC -!- INDUCTION: By p53 when exposed to different DNA damaging agents,
CC including gamma irradiation and chemotherapeutic drugs.
CC -!- PTM: Phosphorylated in mitosis. {ECO:0000269|PubMed:10984615}.
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DR EMBL; AJ222580; CAA10848.1; -; mRNA.
DR EMBL; BC027213; AAH27213.1; -; mRNA.
DR EMBL; AK012870; BAB28524.1; -; mRNA.
DR CCDS; CCDS27725.1; -.
DR RefSeq; NP_001162143.1; NM_001168672.1.
DR RefSeq; NP_038910.1; NM_013882.2.
DR AlphaFoldDB; Q8R080; -.
DR BioGRID; 205935; 4.
DR IntAct; Q8R080; 1.
DR MINT; Q8R080; -.
DR STRING; 10090.ENSMUSP00000128759; -.
DR iPTMnet; Q8R080; -.
DR PhosphoSitePlus; Q8R080; -.
DR EPD; Q8R080; -.
DR jPOST; Q8R080; -.
DR MaxQB; Q8R080; -.
DR PaxDb; Q8R080; -.
DR PRIDE; Q8R080; -.
DR ProteomicsDB; 271351; -.
DR Antibodypedia; 28047; 270 antibodies from 30 providers.
DR DNASU; 29870; -.
DR Ensembl; ENSMUST00000170629; ENSMUSP00000128759; ENSMUSG00000022385.
DR Ensembl; ENSMUST00000231074; ENSMUSP00000155552; ENSMUSG00000022385.
DR GeneID; 29870; -.
DR KEGG; mmu:29870; -.
DR UCSC; uc007xdp.1; mouse.
DR CTD; 51512; -.
DR MGI; MGI:1352755; Gtse1.
DR VEuPathDB; HostDB:ENSMUSG00000022385; -.
DR eggNOG; ENOG502QW86; Eukaryota.
DR GeneTree; ENSGT00940000154189; -.
DR HOGENOM; CLU_023558_0_0_1; -.
DR InParanoid; Q8R080; -.
DR OMA; PSRTKIP; -.
DR OrthoDB; 1407808at2759; -.
DR PhylomeDB; Q8R080; -.
DR TreeFam; TF332555; -.
DR Reactome; R-MMU-69481; G2/M Checkpoints.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR BioGRID-ORCS; 29870; 10 hits in 77 CRISPR screens.
DR ChiTaRS; Gtse1; mouse.
DR PRO; PR:Q8R080; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8R080; protein.
DR Bgee; ENSMUSG00000022385; Expressed in animal zygote and 103 other tissues.
DR ExpressionAtlas; Q8R080; baseline and differential.
DR Genevisible; Q8R080; MM.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR InterPro; IPR026657; DDA3/GTSE-1.
DR InterPro; IPR026659; GTSE1.
DR InterPro; IPR032768; GTSE1_N.
DR PANTHER; PTHR21584; PTHR21584; 1.
DR PANTHER; PTHR21584:SF10; PTHR21584:SF10; 1.
DR Pfam; PF15259; GTSE1_N; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..741
FT /note="G2 and S phase-expressed protein 1"
FT /id="PRO_0000083876"
FT REGION 101..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYZ3"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYZ3"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYZ3"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYZ3"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYZ3"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYZ3"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 465
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYZ3"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYZ3"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYZ3"
FT MOD_RES 518
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYZ3"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYZ3"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYZ3"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYZ3"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYZ3"
FT MOD_RES 696
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYZ3"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYZ3"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYZ3"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYZ3"
FT CONFLICT 153
FT /note="S -> P (in Ref. 2; AAH27213)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="I -> L (in Ref. 2; AAH27213)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="V -> M (in Ref. 2; AAH27213)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="S -> G (in Ref. 2; AAH27213)"
FT /evidence="ECO:0000305"
FT CONFLICT 398..399
FT /note="SP -> IL (in Ref. 2; AAH27213)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 741 AA; 78751 MW; 1C684D06EE9B7ACB CRC64;
MDAGSKKEDF LLLEDEKFDF DLSLSSSSTN EDDEVFFGPV GHKERCIAAS LDLNRRVPGQ
PLAPGSGSPC TLSPLTGEKF VEVYKEAHLL ALQIESHSRR EVAQAATPQN PVNQGKETFV
QDSQLKVSLF EKEQKRDRSP MSLKRETFCL PSSRVQPPMG EPQLLASPGL LSSPVSAGPA
QTQSNQGLPC SSQPLPRESS TSQPPSQAGP QKRITSKLQP PRALPVRGRN LHLATEKLKK
EVPASIQRTK LVNEKGSQSD VLQDKPSTAP DAASREGHPG KRSLPIPGKL GLKKTLLKPP
GYTGNLTRKS STSGSASSLE SGVYRSSVAG KAKSSEQRSS IPASGSQRRT STSKSGRIGP
AASRQALPAA PARVFGRQAN KADAAQTVAE QPKVPTLSPL TQQPQTPEQR GPRLDPDTET
PQLNKTVSIK RRDSYLSCKT EAVSTTTNPF KVPQFSVGES PGGVTPKFSR THRLQSWTPA
SRVVSSTPVR RSSGTTPQGL PGSMRTPLST RRMSVLPTPA SRRLSSLPLM APQSMPRALV
SPLCVPARRL SSEPRRRSTV RAELTQESSG SGSGGQAQGL SSDESSSPPS SVPQALNFSP
EKSASPPPQG SSTGAAQGEA EPPEDTLPSE VHGGGCSHTP SEGLLLDLKL DQLTITPEAG
GRDLADCPLI DFSNTPESNT ALGPSSWPLI DLIMNTPDMG RNDVGKPAKA ELGQLIDLGS
PLIQLSPEAD KENVDSPLLK F
