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Protein asunder (Cell cycle regulator Mat89Bb) (Integrator complex subunit 13) (Maternal transcript 89Bb) (Set apart in position or space protein)

 INT13_DROME             Reviewed;         689 AA.
Q9VEX5; Q27924; Q7JP08;
22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
02-JUN-2021, entry version 126.
RecName: Full=Protein asunder {ECO:0000303|PubMed:19357193};
AltName: Full=Cell cycle regulator Mat89Bb {ECO:0000303|PubMed:15737938};
AltName: Full=Integrator complex subunit 13 {ECO:0000303|PubMed:23097424};
AltName: Full=Maternal transcript 89Bb {ECO:0000312|EMBL:AAF55290.1};
AltName: Full=Set apart in position or space protein {ECO:0000303|PubMed:19357193};
Name=Asun {ECO:0000312|FlyBase:FBgn0020407};
Synonyms=IntS13 {ECO:0000303|PubMed:23097424},
Mat89Bb {ECO:0000303|PubMed:15737938},
ovary2 {ECO:0000312|EMBL:AAA90971.1};
ORFNames=CG6814 {ECO:0000312|FlyBase:FBgn0020407};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:AAA90971.1}
NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 413-689,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=9799434; DOI=10.1007/s004270050211;
Stebbings L.A., Grimes B.R., Bownes M.;
"A testis-specifically expressed gene is embedded within a cluster of
maternally expressed genes at 89B in Drosophila melanogaster.";
Dev. Genes Evol. 208:523-530(1998).
[2] {ECO:0000312|EMBL:AAF55290.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3] {ECO:0000305, ECO:0000312|EMBL:AAF55290.1}
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic
review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4] {ECO:0000312|EMBL:AAM49919.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000312|EMBL:AAM49919.1};
TISSUE=Embryo {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5] {ECO:0000305}
FUNCTION, PHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
PubMed=15737938; DOI=10.1016/j.devcel.2004.12.008;
Lee L.A., Lee E., Anderson M.A., Vardy L., Tahinci E., Ali S.M.,
Kashevsky H., Benasutti M., Kirschner M.W., Orr-Weaver T.L.;
"Drosophila genome-scale screen for PAN GU kinase substrates identifies
Mat89Bb as a cell cycle regulator.";
Dev. Cell 8:435-442(2005).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19357193; DOI=10.1091/mbc.e08-12-1165;
Anderson M.A., Jodoin J.N., Lee E., Hales K.G., Hays T.S., Lee L.A.;
"Asunder is a critical regulator of dynein-dynactin localization during
Drosophila spermatogenesis.";
Mol. Biol. Cell 20:2709-2721(2009).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE INTEGRATOR
COMPLEX.
PubMed=23097424; DOI=10.1261/rna.035725.112;
Chen J., Ezzeddine N., Waltenspiel B., Albrecht T.R., Warren W.D.,
Marzluff W.F., Wagner E.J.;
"An RNAi screen identifies additional members of the Drosophila Integrator
complex and a requirement for cyclin C/Cdk8 in snRNA 3'-end formation.";
RNA 18:2148-2156(2012).
[8]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF
617-LYS--ARG-619.
PubMed=23904267; DOI=10.1091/mbc.e13-05-0254;
Jodoin J.N., Sitaram P., Albrecht T.R., May S.B., Shboul M., Lee E.,
Reversade B., Wagner E.J., Lee L.A.;
"Nuclear-localized Asunder regulates cytoplasmic dynein localization via
its role in the integrator complex.";
Mol. Biol. Cell 24:2954-2965(2013).
-!- FUNCTION: Component of the Integrator complex, a complex involved in
the transcription of small nuclear RNAs (snRNA) and their 3'-box-
dependent processing (PubMed:23097424). Involved in the 3'-end
processing of the U7 snRNA, and also the spliceosomal snRNAs U1 and U5
(PubMed:23097424). Plays a role as a regulator of spermatogenesis
(PubMed:19357193). Crucial regulator of the mitotic cell cycle and
development (PubMed:15737938, PubMed:19357193). Required for the
correct dynein-dynactin perinuclear localization important for nucleus-
centrosome coupling that occur upon meiotic progression of primary
spermatocytes (PubMed:19357193,PubMed:23904267). Plays a role in sperm
motility and fertility (PubMed:19357193). May have a role in the
PNG/PLU/GNU pathway (PubMed:15737938). {ECO:0000269|PubMed:15737938,
ECO:0000269|PubMed:19357193, ECO:0000269|PubMed:23097424,
ECO:0000269|PubMed:23904267}.
-!- SUBUNIT: Belongs to the multiprotein complex Integrator, at least
composed of IntS1, IntS2, IntS3, IntS4, omd/IntS5, IntS6, defl/IntS7,
IntS8, IntS9, IntS10, IntS11, IntS12, asun/IntS13 and IntS14.
{ECO:0000305|PubMed:23097424}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19357193,
ECO:0000269|PubMed:23097424}. Cytoplasm {ECO:0000269|PubMed:19357193,
ECO:0000269|PubMed:23097424, ECO:0000269|PubMed:9799434}. Cytoplasm,
perinuclear region {ECO:0000269|PubMed:19357193}. Note=Colocalizes with
dynein-dynactin on the nuclear surface at the meiotic G2/prophase
transition in primary spermatocytes (PubMed:19357193). Nuclear location
is required for recruitment of dynein motors to nuclear envelope at
G2/M (PubMed:23904267). {ECO:0000269|PubMed:19357193,
ECO:0000269|PubMed:23904267}.
-!- TISSUE SPECIFICITY: Expressed in nurse cells at stages 9-10 of
oogenesis and exported to the oocyte. Also expressed in the follicle
cells surrounding the oocyte. {ECO:0000269|PubMed:9799434}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
Expressed in the nucleus during the G2 phase of primary spermatocytes
at stages S3-S4. Distributed between the nucleus and the cytoplasm in
G2 phase of primary spermatocytes at stage S5. Localized in the
cytoplasm in G2 phase of primary spermatocytes at stage S6. Remains
dispersed throughout the cell until the completion of meiosis when it
becomes restricted from nuclei of onion-stage spermatides.
{ECO:0000269|PubMed:9799434}.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:15737938}.
-!- DISRUPTION PHENOTYPE: Results in almost complete steril males. Mature
sperm formed in small amounts in testes are immotile or weakly motile;
seminal vesicles are largely empty. Primary spermatocytes appeared
normal (Cysts of 16 cells); however, spermatids show irregularities in
nuclear size and number. Spermatocytes I exhibit failure of nucleus-
centrosome coupling that normally occur upon meiotic phase entry; those
that progress through meiotic divisions exhibit defects in spindle
assembly and chromosome segregation. When injected into Xenopus
embryos, causes developmental arrest with gastrulation defects and
defective cell cycles resulting in polyploid nuclei. RNAi injection
into HeLa cells or Drosophila syncytial embryos causes mitotic cell
cycle, giving rise to multinucleated polyploidy cells.
{ECO:0000269|PubMed:15737938}.
-!- SIMILARITY: Belongs to the asunder family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA90969.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAA90969.1; Type=Frameshift; Evidence={ECO:0000305};
Sequence=AAA90971.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
Sequence=AAA90971.1; Type=Frameshift; Evidence={ECO:0000305};
---------------------------------------------------------------------------
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EMBL; U47618; AAA90969.1; ALT_SEQ; Genomic_DNA.
EMBL; U47619; AAA90971.1; ALT_SEQ; mRNA.
EMBL; AE014297; AAF55290.1; -; Genomic_DNA.
EMBL; AY118550; AAM49919.1; -; mRNA.
RefSeq; NP_524379.2; NM_079655.4.
SMR; Q9VEX5; -.
BioGRID; 67019; 8.
IntAct; Q9VEX5; 1.
STRING; 7227.FBpp0082713; -.
PaxDb; Q9VEX5; -.
PRIDE; Q9VEX5; -.
DNASU; 41971; -.
EnsemblMetazoa; FBtr0083259; FBpp0082713; FBgn0020407.
GeneID; 41971; -.
KEGG; dme:Dmel_CG6814; -.
UCSC; CG6814-RA; d. melanogaster.
CTD; 41971; -.
FlyBase; FBgn0020407; asun.
eggNOG; KOG3711; Eukaryota.
GeneTree; ENSGT00390000002793; -.
HOGENOM; CLU_012654_1_0_1; -.
InParanoid; Q9VEX5; -.
OMA; KQDEVRC; -.
OrthoDB; 676663at2759; -.
PhylomeDB; Q9VEX5; -.
Reactome; R-DME-6807505; RNA polymerase II transcribes snRNA genes.
BioGRID-ORCS; 41971; 1 hit in 1 CRISPR screen.
GenomeRNAi; 41971; -.
PRO; PR:Q9VEX5; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0020407; Expressed in embryo and 32 other tissues.
Genevisible; Q9VEX5; DM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0032039; C:integrator complex; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0051642; P:centrosome localization; IMP:FlyBase.
GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
GO; GO:0051663; P:oocyte nucleus localization involved in oocyte dorsal/ventral axis specification; IMP:FlyBase.
GO; GO:0060814; P:posterior mRNA localization involved in anterior/posterior axis specification; IMP:FlyBase.
GO; GO:0080154; P:regulation of fertilization; IMP:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0034472; P:snRNA 3'-end processing; IDA:FlyBase.
GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
InterPro; IPR019355; Cell_cycle_regulator_Mat89Bb.
PANTHER; PTHR12955; PTHR12955; 2.
Pfam; PF10221; DUF2151; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Coiled coil; Cytoplasm; Developmental protein;
Differentiation; Meiosis; Mitosis; Nucleus; Phosphoprotein;
Reference proteome; Spermatogenesis.
CHAIN 1..689
/note="Protein asunder"
/id="PRO_0000385342"
REGION 592..619
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 665..689
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COILED 521..550
/evidence="ECO:0000255"
MOTIF 613..619
/note="Nuclear localization signal (NLS)"
/evidence="ECO:0000269|PubMed:23904267"
COMPBIAS 600..619
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 670..689
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MUTAGEN 617..619
/note="KRR->AAA: Loss of nuclear location. Location is
mainly cytoplasmic or diffuse."
/evidence="ECO:0000269|PubMed:23904267"
CONFLICT 54
/note="S -> T (in Ref. 1; AAA90971)"
/evidence="ECO:0000305"
CONFLICT 147..151
/note="TDEQL -> PMSSW (in Ref. 1; AAA90971)"
/evidence="ECO:0000305"
CONFLICT 199
/note="T -> S (in Ref. 1; AAA90971)"
/evidence="ECO:0000305"
CONFLICT 257..258
/note="KL -> NV (in Ref. 1; AAA90971)"
/evidence="ECO:0000305"
CONFLICT 438
/note="V -> M (in Ref. 1; AAA90969/AAA90971)"
/evidence="ECO:0000305"
CONFLICT 602
/note="G -> V (in Ref. 1; AAA90969/AAA90971)"
/evidence="ECO:0000305"
SEQUENCE 689 AA; 75728 MW; E02C1F79DA88AE79 CRC64;
MFERNQKTIF VLDHTRYFSI ASEEYISMDF LKGKPSADGG ATGAAGNATG SGGSQFSKSL
WTCACESSIE YCRVVWDLFP GKKHVRFIVS DTAAHIVNTW RPSTQNMAHV MNAMLIVGVP
SRNVPTSSDY SVIHGLRAAI EALAEPTDEQ LAAMADFGTD ELPRIPNKGR VICITSARDN
TSMKSLEDIF NTVLVQQNTL AAPPSKKGLV IDHCHLVILN IVPLGVESLV TNRSLLKISP
LLDVEIHTVS APDISYKLTH LILNHYDLAS TTVTNIPMKE EQNANSSANY DVEILHSRRA
HSITCGPDFS LPTSIKQGAT YETVTLKWCT PRGCGSADLQ PCLGQFLVTP VDVTSRPSSC
LINFLLNGRS VLLEMPRKTG SKATSHMLSA RGGEIFVHSL CITRSCMDEA PSITDGPGGR
VSDYRTAELG QLIKMSRVVP LKVKDPSAPP LTRRLPRYFP LTTSSSILFH LQRHISWLPH
FLHLLVKEDM DKQDEVRCQQ HIHELYKSAS RGDVLPFTHT NGARLKLSKA KDQYRLLYRE
LEQLIQLNAT TMHHKNLLES LQSLRAAYGD APLKSEPGAS LLRTYTESPL SPERLEPISS
VGASGSSSSN SLLKASKRRM SSCGQRSLLD IISSAERSQS NKRLDFSGRL CTPLGQVAKL
YPDFGTKDKD TVTTGASITP NVKEESVRS


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WP1659: Glycine, serine and threonine metabolism
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WP844: Cell cycle
WP1049: G Protein Signaling Pathways
WP1665: Limonene and pinene degradation
WP232: G Protein Signaling Pathways
WP1083: Cell cycle
WP1713: Two-component system
WP731: Sterol regulatory element binding protein related
WP1616: ABC transporters
WP1775: Cell Cycle Checkpoints

Related Genes :
[Asun IntS13 Mat89Bb ovary2 CG6814] Protein asunder (Cell cycle regulator Mat89Bb) (Integrator complex subunit 13) (Maternal transcript 89Bb) (Set apart in position or space protein)
[INTS13 ASUN C12orf11 GCT1] Integrator complex subunit 13 (Cell cycle regulator Mat89Bb homolog) (Germ cell tumor 1) (Protein asunder homolog) (Sarcoma antigen NY-SAR-95)
[IntS13 Asun Spata30] Integrator complex subunit 13 (Cell cycle regulator Mat89Bb homolog) (Protein asunder homolog) (Spermatogenesis-associated protein 30)
[asun Mat89Bb GI22939] Protein asunder (Cell cycle regulator Mat89Bb) (Maternal transcript 89Bb) (Set apart in position or space protein)
[asun Mat89Bb GK13769] Protein asunder (Cell cycle regulator Mat89Bb) (Maternal transcript 89Bb) (Set apart in position or space protein)
[asun Mat89Bb GE24382] Protein asunder (Cell cycle regulator Mat89Bb) (Maternal transcript 89Bb) (Set apart in position or space protein)
[asun Mat89Bb GG16989] Protein asunder (Cell cycle regulator Mat89Bb) (Maternal transcript 89Bb) (Set apart in position or space protein)
[asun Mat89Bb GM15141] Protein asunder (Cell cycle regulator Mat89Bb) (Maternal transcript 89Bb) (Set apart in position or space protein)
[asun Mat89Bb GD19084] Protein asunder (Cell cycle regulator Mat89Bb) (Maternal transcript 89Bb) (Set apart in position or space protein)
[asun Mat89Bb GJ23719] Protein asunder (Cell cycle regulator Mat89Bb) (Maternal transcript 89Bb) (Set apart in position or space protein)
[asun Mat89Bb GH19540] Protein asunder (Cell cycle regulator Mat89Bb) (Maternal transcript 89Bb) (Set apart in position or space protein)
[asun Mat89Bb GL21594] Protein asunder (Cell cycle regulator Mat89Bb) (Maternal transcript 89Bb) (Set apart in position or space protein)
[asun Mat89Bb GF16409] Protein asunder (Cell cycle regulator Mat89Bb) (Maternal transcript 89Bb) (Set apart in position or space protein)
[asun Mat89Bb GA19879] Protein asunder (Cell cycle regulator Mat89Bb) (Set apart in position or space protein)
[FL82_03420] Cell cycle regulator Mat89Bb (EC 6.1.1.11) (Protein asunder) (Seryl-tRNA synthetase) (Set apart in position or space protein) (Fragment)
[WBGene00106791] Cell cycle regulator Mat89Bb (Protein asunder) (Set apart in position or space protein)
[CRE_10056] Cell cycle regulator Mat89Bb (Protein asunder) (Set apart in position or space protein)
[ints-13 CELE_R02D3.4 R02D3.4] Cell cycle regulator Mat89Bb (Protein asunder) (Set apart in position or space protein)
[C0J52_03451] Cell cycle regulator Mat89Bb (EC 2.3.2.26) (Protein asunder) (Set apart in position or space protein)
[ints-13 CBG01667 CBG_01667] Cell cycle regulator Mat89Bb (Protein asunder) (Set apart in position or space protein)
[1269269 AgaP_AGAP002295] Cell cycle regulator Mat89Bb (Protein asunder) (Set apart in position or space protein)
[8040136 IscW_ISCW022242] Cell cycle regulator Mat89Bb (Protein asunder) (Set apart in position or space protein)
[PRIPAC_42692] Cell cycle regulator Mat89Bb (Protein asunder) (Set apart in position or space protein)
[ints-13 CELE_R02D3.4 R02D3.4] Cell cycle regulator Mat89Bb (Protein asunder) (Set apart in position or space protein)
[ints-13 CELE_R02D3.4 R02D3.4] Cell cycle regulator Mat89Bb (Protein asunder) (Set apart in position or space protein)
[DAPPUDRAFT_335678] Cell cycle regulator Mat89Bb (Protein asunder) (Set apart in position or space protein)
[LOC108131008] Cell cycle regulator Mat89Bb (Protein asunder) (Set apart in position or space protein)
[ASUN] Cell cycle regulator Mat89Bb (Protein asunder) (Set apart in position or space protein)
[LOC108102242] Cell cycle regulator Mat89Bb (Protein asunder) (Set apart in position or space protein)
[LOC108052511] Cell cycle regulator Mat89Bb (Protein asunder) (Set apart in position or space protein)

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