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Protein

G2 and S phase-expressed protein 1

Gene

Gtse1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in p53-induced cell cycle arrest in G2/M phase by interfering with microtubule rearrangements that are required to enter mitosis. Overexpression delays G2/M phase progression.

Enzyme and pathway databases

ReactomeiR-MMU-69481. G2/M Checkpoints.
R-MMU-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.

Names & Taxonomyi

Protein namesi
Recommended name:
G2 and S phase-expressed protein 1
Short name:
GTSE-1
Alternative name(s):
Protein B99
Gene namesi
Name:Gtse1
Synonyms:B99
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1352755. Gtse1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 741741G2 and S phase-expressed protein 1PRO_0000083876Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei73 – 731PhosphoserineBy similarity
Modified residuei139 – 1391PhosphoserineBy similarity
Modified residuei153 – 1531PhosphoserineBy similarity
Modified residuei191 – 1911PhosphoserineBy similarity
Modified residuei460 – 4601PhosphoserineCombined sources
Modified residuei465 – 4651PhosphothreonineCombined sources
Modified residuei476 – 4761PhosphoserineCombined sources
Modified residuei493 – 4931PhosphoserineBy similarity
Modified residuei509 – 5091PhosphoserineBy similarity
Modified residuei514 – 5141PhosphoserineBy similarity
Modified residuei518 – 5181PhosphothreonineBy similarity
Modified residuei521 – 5211PhosphoserineBy similarity
Modified residuei541 – 5411PhosphoserineBy similarity
Modified residuei582 – 5821PhosphoserineBy similarity
Modified residuei599 – 5991PhosphoserineBy similarity
Modified residuei696 – 6961PhosphothreonineBy similarity
Modified residuei720 – 7201PhosphoserineBy similarity
Modified residuei726 – 7261PhosphoserineBy similarity
Modified residuei736 – 7361PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated in mitosis.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8R080.
MaxQBiQ8R080.
PaxDbiQ8R080.
PRIDEiQ8R080.

PTM databases

iPTMnetiQ8R080.
PhosphoSiteiQ8R080.

Expressioni

Developmental stagei

Expression begins at S phase, accumulates in late S/G2 phase and disappears in G1 phase.1 Publication

Inductioni

By p53 when exposed to different DNA damaging agents, including gamma irradiation and chemotherapeutic drugs.

Gene expression databases

BgeeiQ8R080.
CleanExiMM_GTSE1.
ExpressionAtlasiQ8R080. baseline and differential.
GenevisibleiQ8R080. MM.

Interactioni

Protein-protein interaction databases

BioGridi205935. 4 interactions.
IntActiQ8R080. 1 interaction.
STRINGi10090.ENSMUSP00000128759.

Structurei

3D structure databases

ProteinModelPortaliQ8R080.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi23 – 286Poly-Ser

Phylogenomic databases

eggNOGiENOG410IHTJ. Eukaryota.
ENOG410ZUTK. LUCA.
GeneTreeiENSGT00510000049189.
HOGENOMiHOG000294205.
HOVERGENiHBG103867.
InParanoidiQ8R080.
KOiK10129.
OMAiKRETYYL.
OrthoDBiEOG7288RK.
PhylomeDBiQ8R080.
TreeFamiTF332555.

Family and domain databases

InterProiIPR026657. DDA3/GTSE-1.
IPR026659. GTSE1.
IPR032768. GTSE1_N.
[Graphical view]
PANTHERiPTHR21584. PTHR21584. 1 hit.
PTHR21584:SF10. PTHR21584:SF10. 1 hit.
PfamiPF15259. GTSE1_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8R080-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDAGSKKEDF LLLEDEKFDF DLSLSSSSTN EDDEVFFGPV GHKERCIAAS
60 70 80 90 100
LDLNRRVPGQ PLAPGSGSPC TLSPLTGEKF VEVYKEAHLL ALQIESHSRR
110 120 130 140 150
EVAQAATPQN PVNQGKETFV QDSQLKVSLF EKEQKRDRSP MSLKRETFCL
160 170 180 190 200
PSSRVQPPMG EPQLLASPGL LSSPVSAGPA QTQSNQGLPC SSQPLPRESS
210 220 230 240 250
TSQPPSQAGP QKRITSKLQP PRALPVRGRN LHLATEKLKK EVPASIQRTK
260 270 280 290 300
LVNEKGSQSD VLQDKPSTAP DAASREGHPG KRSLPIPGKL GLKKTLLKPP
310 320 330 340 350
GYTGNLTRKS STSGSASSLE SGVYRSSVAG KAKSSEQRSS IPASGSQRRT
360 370 380 390 400
STSKSGRIGP AASRQALPAA PARVFGRQAN KADAAQTVAE QPKVPTLSPL
410 420 430 440 450
TQQPQTPEQR GPRLDPDTET PQLNKTVSIK RRDSYLSCKT EAVSTTTNPF
460 470 480 490 500
KVPQFSVGES PGGVTPKFSR THRLQSWTPA SRVVSSTPVR RSSGTTPQGL
510 520 530 540 550
PGSMRTPLST RRMSVLPTPA SRRLSSLPLM APQSMPRALV SPLCVPARRL
560 570 580 590 600
SSEPRRRSTV RAELTQESSG SGSGGQAQGL SSDESSSPPS SVPQALNFSP
610 620 630 640 650
EKSASPPPQG SSTGAAQGEA EPPEDTLPSE VHGGGCSHTP SEGLLLDLKL
660 670 680 690 700
DQLTITPEAG GRDLADCPLI DFSNTPESNT ALGPSSWPLI DLIMNTPDMG
710 720 730 740
RNDVGKPAKA ELGQLIDLGS PLIQLSPEAD KENVDSPLLK F
Length:741
Mass (Da):78,751
Last modified:July 26, 2002 - v2
Checksum:i1C684D06EE9B7ACB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531S → P in AAH27213 (PubMed:15489334).Curated
Sequence conflicti246 – 2461I → L in AAH27213 (PubMed:15489334).Curated
Sequence conflicti252 – 2521V → M in AAH27213 (PubMed:15489334).Curated
Sequence conflicti274 – 2741S → G in AAH27213 (PubMed:15489334).Curated
Sequence conflicti398 – 3992SP → IL in AAH27213 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ222580 mRNA. Translation: CAA10848.1.
BC027213 mRNA. Translation: AAH27213.1.
AK012870 mRNA. Translation: BAB28524.1.
CCDSiCCDS27725.1.
RefSeqiNP_001162143.1. NM_001168672.1.
NP_038910.1. NM_013882.2.
UniGeneiMm.20858.

Genome annotation databases

EnsembliENSMUST00000170629; ENSMUSP00000128759; ENSMUSG00000022385.
GeneIDi29870.
KEGGimmu:29870.
UCSCiuc007xdp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ222580 mRNA. Translation: CAA10848.1.
BC027213 mRNA. Translation: AAH27213.1.
AK012870 mRNA. Translation: BAB28524.1.
CCDSiCCDS27725.1.
RefSeqiNP_001162143.1. NM_001168672.1.
NP_038910.1. NM_013882.2.
UniGeneiMm.20858.

3D structure databases

ProteinModelPortaliQ8R080.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205935. 4 interactions.
IntActiQ8R080. 1 interaction.
STRINGi10090.ENSMUSP00000128759.

PTM databases

iPTMnetiQ8R080.
PhosphoSiteiQ8R080.

Proteomic databases

EPDiQ8R080.
MaxQBiQ8R080.
PaxDbiQ8R080.
PRIDEiQ8R080.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000170629; ENSMUSP00000128759; ENSMUSG00000022385.
GeneIDi29870.
KEGGimmu:29870.
UCSCiuc007xdp.1. mouse.

Organism-specific databases

CTDi51512.
MGIiMGI:1352755. Gtse1.

Phylogenomic databases

eggNOGiENOG410IHTJ. Eukaryota.
ENOG410ZUTK. LUCA.
GeneTreeiENSGT00510000049189.
HOGENOMiHOG000294205.
HOVERGENiHBG103867.
InParanoidiQ8R080.
KOiK10129.
OMAiKRETYYL.
OrthoDBiEOG7288RK.
PhylomeDBiQ8R080.
TreeFamiTF332555.

Enzyme and pathway databases

ReactomeiR-MMU-69481. G2/M Checkpoints.
R-MMU-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.

Miscellaneous databases

PROiQ8R080.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R080.
CleanExiMM_GTSE1.
ExpressionAtlasiQ8R080. baseline and differential.
GenevisibleiQ8R080. MM.

Family and domain databases

InterProiIPR026657. DDA3/GTSE-1.
IPR026659. GTSE1.
IPR032768. GTSE1_N.
[Graphical view]
PANTHERiPTHR21584. PTHR21584. 1 hit.
PTHR21584:SF10. PTHR21584:SF10. 1 hit.
PfamiPF15259. GTSE1_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel p53-inducible gene coding for a microtubule-localized protein with G2-phase-specific expression."
    Utrera R., Collavin L., Lazarevic D., Delia D., Schneider C.
    EMBO J. 17:5015-5025(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
    Tissue: Mammary gland.
  3. "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] OF 1-130.
    Strain: C57BL/6J.
    Tissue: Embryo.
  4. "Cell-cycle regulation of the p53-inducible gene B99."
    Collavin L., Monte M., Verardo R., Pfleger C., Schneider C.
    FEBS Lett. 481:57-62(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE, PHOSPHORYLATION.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND THR-465, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.

Entry informationi

Entry nameiGTSE1_MOUSE
AccessioniPrimary (citable) accession number: Q8R080
Secondary accession number(s): O89015, Q9CSG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: July 26, 2002
Last modified: June 8, 2016
This is version 106 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

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.