Reviewed,
UniProtKB/Swiss-Prot Q53HL2 (BOREA_HUMAN)
Last modified
February 9, 2010.
Version 51.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Borealin Alternative name(s): Dasra-B Short name=hDasra-B Cell division cycle-associated protein 8 Pluripotent embryonic stem cell-related gene 3 protein | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 280 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. In the complex, it may be required to direct the CPC to centromeric DNA. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment. Ref.6 Ref.7 Ref.13 Ref.19 |
| Subunit structure | May form homooligomers and homodimers. Component of the CPC at least composed of BIRC5/survivin, CDCA8/borealin, INCENP and AURKB/Aurora-B. Interacts with BIRC5/survivin and INCENP; interaction is direct. Interacts with SENP3, UBE2I and RANBP2. Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.23 Ref.26 Ref.27 |
| Subcellular location | Nucleus › nucleolus. Cytoplasm. Cytoplasm › cytoskeleton › spindle. Centromere. Note: Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. Colocalizes with SENP3 in the nucleolus in interphase cells. Ref.7 Ref.10 Ref.12 Ref.23 Ref.8 Ref.14 |
| Developmental stage | Cell-cycle regulated. Increases during G2/M phase and then reduces after exit from M phase. Ref.10 |
| Domain | The C-terminal region (aa 207-280) represents the dimerization motif. |
| Post-translational modification | Phosphorylated by TTK, essentially at Thr-88, Thr94, Thr-169 and Thr-230. Ref.7 Ref.19 Ref.23 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.25 Sumoylated by UBE2I and RANBP2. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3. Ref.23 |
| Miscellaneous | Cells lacking CDCA8 display a slight decrease in histone H3 'Ser-10' phosphorylation, suggesting that the CPC complex mediates phosphorylation of 'Ser-10' of histone H3. |
| Sequence similarities | Belongs to the borealin family. |
| Sequence caution | The sequence BG354581 differs from that shown. Reason: Frameshift at positions 123 and 200. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| BIRC5 | O15392 | 2 | EBI-979174,EBI-518823 | |
| BIRC5 | O15392-1 | 2 | EBI-979174,EBI-518838 | |
| BIRC5 | O15392-2 | 2 | EBI-979174,EBI-518842 | |
| TTK | P33981 | 1 | EBI-979174,EBI-1645856 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||
Molecule processing | |||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 280 | 280 | Borealin | PRO_0000247075 | |||||||||||
Regions | |||||||||||||||
| Region | 1 – 140 | 140 | Required for interaction with SENP3 | ||||||||||||
| Region | 1 – 88 | 88 | Required for centromere localization | ||||||||||||
| Region | 1 – 58 | 58 | Required for interaction with INCENP | ||||||||||||
| Region | 10 – 109 | 100 | Required to form a minimal CPC core complex that localizes to the central spindle and midbody and properly executes the role of the CPC during cytokinesis | ||||||||||||
| Region | 20 – 78 | 59 | Required for interaction with INCENP and BIRC5 | ||||||||||||
| Compositional bias | 125 – 133 | 9 | Poly-Glu | ||||||||||||
Amino acid modifications | |||||||||||||||
| Modified residue | 15 | 1 | Phosphoserine Ref.20 | ||||||||||||
| Modified residue | 23 | 1 | Phosphoserine Ref.20 | ||||||||||||
| Modified residue | 88 | 1 | Phosphothreonine; by TTK Ref.23 | ||||||||||||
| Modified residue | 94 | 1 | Phosphothreonine; by TTK | ||||||||||||
| Modified residue | 106 | 1 | Phosphothreonine Ref.17 Ref.18 Ref.20 Ref.21 Ref.25 | ||||||||||||
| Modified residue | 110 | 1 | Phosphoserine Ref.20 | ||||||||||||
| Modified residue | 154 | 1 | Phosphoserine Ref.18 Ref.20 | ||||||||||||
| Modified residue | 164 | 1 | Phosphoserine Ref.20 | ||||||||||||
| Modified residue | 165 | 1 | Phosphoserine Ref.7 Ref.20 | ||||||||||||
| Modified residue | 169 | 1 | Phosphothreonine; by TTK Ref.23 Ref.18 | ||||||||||||
| Modified residue | 171 | 1 | Phosphothreonine Ref.18 | ||||||||||||
| Modified residue | 180 | 1 | Phosphoserine Ref.18 | ||||||||||||
| Modified residue | 189 | 1 | Phosphothreonine Ref.20 Ref.21 | ||||||||||||
| Modified residue | 194 | 1 | Phosphoserine Ref.20 | ||||||||||||
| Modified residue | 199 | 1 | Phosphothreonine Ref.18 | ||||||||||||
| Modified residue | 204 | 1 | Phosphothreonine Ref.18 Ref.20 Ref.21 | ||||||||||||
| Modified residue | 212 | 1 | Phosphotyrosine | ||||||||||||
| Modified residue | 215 | 1 | Phosphoserine Ref.18 | ||||||||||||
| Modified residue | 219 | 1 | Phosphoserine Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.25 | ||||||||||||
| Modified residue | 224 | 1 | Phosphoserine | ||||||||||||
| Modified residue | 230 | 1 | Phosphothreonine; by TTK Ref.23 | ||||||||||||
| Modified residue | 238 | 1 | Phosphoserine Ref.23 | ||||||||||||
| Modified residue | 244 | 1 | Phosphoserine Ref.20 | ||||||||||||
| Modified residue | 274 | 1 | Phosphoserine Ref.20 | ||||||||||||
Natural variations | |||||||||||||||
| Natural variant | 12 | 1 | K → N: dbSNP rs17851453. Ref.5 | VAR_027063 | |||||||||||
Experimental info | |||||||||||||||
| Mutagenesis | 17 | 1 | R → E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-19 and E-20. Ref.26 | ||||||||||||
| Mutagenesis | 19 | 1 | R → E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-17 and E-20. Ref.26 | ||||||||||||
| Mutagenesis | 20 | 1 | K → E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-17 and E-19. Ref.26 | ||||||||||||
| Mutagenesis | 26 | 1 | K → R: Fails to exhibit normal localization to the nucleolus in interphase depleted cells. Ref.23 | ||||||||||||
| Mutagenesis | 35 | 1 | R → E: Loss of binding to INCENP; when associated with Y-46. Ref.26 | ||||||||||||
| Mutagenesis | 46 | 1 | L → Y: Loss of binding to INCENP; when associated with E-35. Ref.26 | ||||||||||||
| Mutagenesis | 70 | 1 | W → E: Loss of binding to BIRC5; when associated with E-74. Ref.26 | ||||||||||||
| Mutagenesis | 74 | 1 | F → E: Loss of binding to BIRC5; when associated with E-70. Ref.26 | ||||||||||||
| Mutagenesis | 88 | 1 | T → A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-94; A-169 and A-230. Ref.27 | ||||||||||||
| Mutagenesis | 94 | 1 | T → A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-169 and A-230. Ref.27 | ||||||||||||
| Mutagenesis | 165 | 1 | S → A: Results in reduction but not abolition of phosphorylation. Ref.7 | ||||||||||||
| Mutagenesis | 169 | 1 | T → A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-94 and A-230. Ref.27 | ||||||||||||
| Mutagenesis | 219 | 1 | S → D or K: No effect on the structure. | ||||||||||||
| Mutagenesis | 230 | 1 | T → A: Decrease in AURKB activity and dimer disruption. Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-94 and A-230. Ref.27 | ||||||||||||
| Mutagenesis | 230 | 1 | T → D or K: Substantial loss of structure. Ref.27 | ||||||||||||
| Mutagenesis | 230 | 1 | T → V: Decrease in AURKB activity and no effect on the structure. Ref.27 | ||||||||||||
| Sequence conflict | 155 | 1 | I → M in BAD96288. Ref.4 | ||||||||||||
| Sequence conflict | 213 | 1 | N → D in BAD96269. Ref.4 | ||||||||||||
Secondary structure | |||||||||||||||
Helix Strand Turn | |||||||||||||||
| Helix | 16 – 60 | 45 | |||||||||||||
| Helix | 63 – 66 | 4 | |||||||||||||
| Helix | 70 – 75 | 6 | |||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Drug target discovery by gene expression analysis: cell cycle genes." Walker M.G. Curr. Cancer Drug Targets 1:73-83(2001) [PubMed: 12188893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "The cloning and functional analysis of HPESCRG3." Nie Z., Du J., Lin G., Lu G. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [3] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Embryo. |
| [4] | Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Coronary arterial endothelium. |
| [5] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-12. Tissue: Colon, Kidney and Lung. |
| [6] | "The chromosomal passenger complex is required for chromatin-induced microtubule stabilization and spindle assembly." Sampath S.C., Ohi R., Leismann O., Salic A., Pozniakovski A., Funabiki H. Cell 118:187-202(2004) [PubMed: 15260989] [Abstract] Cited for: FUNCTION, COMPONENT OF THE CPC COMPLEX. |
| [7] | "Borealin: a novel chromosomal passenger required for stability of the bipolar mitotic spindle." Gassmann R., Carvalho A., Henzing A.J., Ruchaud S., Hudson D.F., Honda R., Nigg E.A., Gerloff D.L., Earnshaw W.C. J. Cell Biol. 166:179-191(2004) [PubMed: 15249581] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BIRC5 AND INCENP, PHOSPHORYLATION AT SER-165, MUTAGENESIS OF SER-165. |
| [8] | "Proteome analysis of the human mitotic spindle." Sauer G., Koerner R., Hanisch A., Ries A., Nigg E.A., Sillje H.H.W. Mol. Cell. Proteomics 4:35-43(2005) [PubMed: 15561729] [Abstract] Cited for: SUBCELLULAR LOCATION, MASS SPECTROMETRY. |
| [9] | "Survivin mediates targeting of the chromosomal passenger complex to the centromere and midbody." Vader G., Kauw J.J.W., Medema R.H., Lens S.M.A. EMBO Rep. 7:85-92(2006) [PubMed: 16239925] [Abstract] Cited for: INTERACTION WITH BIRC5. |
| [10] | "Borealin/Dasra B is a cell cycle-regulated chromosomal passenger protein and its nuclear accumulation is linked to poor prognosis for human gastric cancer." Chang J.-L., Chen T.-H., Wang C.-F., Chiang Y.-H., Huang Y.-L., Wong F.-H., Chou C.-K., Chen C.-M. Exp. Cell Res. 312:962-973(2006) [PubMed: 16427043] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BIRC5, DEVELOPMENTAL STAGE. |
| [11] | "Molecular analysis of survivin isoforms: evidence that alternatively spliced variants do not play a role in mitosis." Noton E.A., Colnaghi R., Tate S., Starck C., Carvalho A., Ko Ferrigno P., Wheatley S.P. J. Biol. Chem. 281:1286-1295(2006) [PubMed: 16291752] [Abstract] Cited for: INTERACTION WITH BIRC5. |
| [12] | "Uncoupling the central spindle-associated function of the chromosomal passenger complex from its role at centromeres." Lens S.M.A., Rodriguez J.A., Vader G., Span S.W., Giaccone G., Medema R.H. Mol. Biol. Cell 17:1897-1909(2006) [PubMed: 16436504] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BIRC5. |
| [13] | "Centromere targeting of the chromosomal passenger complex requires a ternary subcomplex of borealin, survivin, and the N-terminal domain of INCENP." Klein U.R., Nigg E.A., Gruneberg U. Mol. Biol. Cell 17:2547-2558(2006) [PubMed: 16571674] [Abstract] Cited for: FUNCTION. |
| [14] | "Subcellular localization and nucleocytoplasmic transport of the chromosomal passenger proteins before nuclear envelope breakdown." Rodriguez J.A., Lens S.M.A., Span S.W., Vader G., Medema R.H., Kruyt F.A.E., Giaccone G. Oncogene 25:4867-4879(2006) [PubMed: 16547492] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [15] | "A survivin-ran complex regulates spindle formation in tumor cells." Xia F., Canovas P.M., Guadagno T.M., Altieri D.C. Mol. Cell. Biol. 28:5299-5311(2008) [PubMed: 18591255] [Abstract] Cited for: INTERACTION WITH BIRC5. |
| [16] | "Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, MASS SPECTROMETRY. Tissue: Epithelium. |
| [17] | "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106 AND SER-219, MASS SPECTROMETRY. |
| [18] | "Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106; SER-154; THR-169; THR-171; SER-180; THR-199; THR-204; SER-215 AND SER-219, MASS SPECTROMETRY. |
| [19] | "Mps1 phosphorylates Borealin to control Aurora B activity and chromosome alignment." Jelluma N., Brenkman A.B., van den Broek N.J., Cruijsen C.W.A., van Osch M.H.J., Lens S.M.A., Medema R.H., Kops G.J.P.L. Cell 132:233-246(2008) [PubMed: 18243099] [Abstract] Cited for: PHOSPHORYLATION BY TTK, FUNCTION. |
| [20] | "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-23; THR-106; SER-110; SER-154; SER-164; SER-165; THR-189; SER-194; THR-204; SER-219; SER-244 AND SER-274, MASS SPECTROMETRY. |
| [21] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106; THR-189; THR-204 AND SER-219, MASS SPECTROMETRY. |
| [22] | "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, MASS SPECTROMETRY. |
| [23] | "RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin." Klein U.R., Haindl M., Nigg E.A., Muller S. Mol. Biol. Cell 20:410-418(2009) [PubMed: 18946085] [Abstract] Cited for: INTERACTION WITH SENP3; UBE2I AND RANBP2, SUMOYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-26, PHOSPHORYLATION AT THR-88; THR94; THR-169; THR-230 AND SER-238. |
| [24] | "Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-212; SER-219 AND SER-224, MASS SPECTROMETRY. |
| [25] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106 AND SER-219, MASS SPECTROMETRY. Tissue: T-cell. |
| [26] | "Structure of a Survivin-Borealin-INCENP core complex reveals how chromosomal passengers travel together." Jeyaprakash A.A., Klein U.R., Lindner D., Ebert J., Nigg E.A., Conti E. Cell 131:271-285(2007) [PubMed: 17956729] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 15-76, INTERACTION WITH BIRC5 AND INCENP, MUTAGENESIS OF ARG-17; ARG-19; LYS-20; ARG-35; LEU-46; TRP-70 AND PHE-74. |
| [27] | "Phosphorylation of a borealin dimerization domain is required for proper chromosome segregation." Bourhis E., Lingel A., Phung Q., Fairbrother W.J., Cochran A.G. Biochemistry 48:6783-6793(2009) [PubMed: 19530738] [Abstract] Cited for: STRUCTURE BY NMR OF 207-280, X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-78, OLIGOMERIZATION, MUTAGENESIS OF THR-88; THR-94; THR-169 AND THR-230. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | BG354581 mRNA. No translation available. AY508815 mRNA. Translation: AAR91699.1. AK001330 mRNA. Translation: BAA91629.1. AK022104 mRNA. Translation: BAB13961.1. AK022606 mRNA. Translation: BAB14125.1. AK222549 mRNA. Translation: BAD96269.1. AK222568 mRNA. Translation: BAD96288.1. BC000703 mRNA. Translation: AAH00703.1. BC001651 mRNA. Translation: AAH01651.1. BC016944 mRNA. Translation: AAH16944.1. BC008079 mRNA. Translation: AAH08079.1. | ||||||||||||||||||||||||||||||
| IPI | IPI00303099. | ||||||||||||||||||||||||||||||
| RefSeq | NP_060571.1. | ||||||||||||||||||||||||||||||
| UniGene | Hs.524571 | ||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ModBase | Search... | ||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||
| IntAct | Q53HL2. 6 interactions. | ||||||||||||||||||||||||||||||
| STRING | Q53HL2. | ||||||||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||||||||
| PhosphoSite | Q53HL2. | ||||||||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||||||||
| PeptideAtlas | Q53HL2. | ||||||||||||||||||||||||||||||
| PRIDE | Q53HL2. | ||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||
| Ensembl | ENST00000327331; ENSP00000316121; ENSG00000134690; Homo sapiens. [Genome view] ENST00000373055; ENSP00000362146; ENSG00000134690; Homo sapiens. [Genome view] | ||||||||||||||||||||||||||||||
| GeneID | 55143. | ||||||||||||||||||||||||||||||
| KEGG | hsa:55143. | ||||||||||||||||||||||||||||||
| UCSC | uc001cbr.1. human. | ||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||
| CTD | 55143. | ||||||||||||||||||||||||||||||
| GeneCards | GC01P037931. | ||||||||||||||||||||||||||||||
| HGNC | HGNC:14629. CDCA8. | ||||||||||||||||||||||||||||||
| MIM | 609977. gene. | ||||||||||||||||||||||||||||||
| PharmGKB | PA26281. | ||||||||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||
| eggNOG | prNOG06446. | ||||||||||||||||||||||||||||||
| HOGENOM | HBG714853. | ||||||||||||||||||||||||||||||
| HOVERGEN | Q53HL2. | ||||||||||||||||||||||||||||||
| InParanoid | Q53HL2. | ||||||||||||||||||||||||||||||
| OMA | VDEMIVE. | ||||||||||||||||||||||||||||||
| OrthoDB | EOG969TDW. | ||||||||||||||||||||||||||||||
| PhylomeDB | Q53HL2. | ||||||||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||||||||
| Pathway_Interaction_DB | aurora_b_pathway. Aurora B signaling. | ||||||||||||||||||||||||||||||
| Reactome | REACT_152. Cell Cycle, Mitotic. | ||||||||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||||||||
| ArrayExpress | Q53HL2. | ||||||||||||||||||||||||||||||
| Bgee | Q53HL2. | ||||||||||||||||||||||||||||||
| CleanEx | HS_CDCA8. | ||||||||||||||||||||||||||||||
| Genevestigator | Q53HL2. | ||||||||||||||||||||||||||||||
| GermOnline | ENSG00000134690. Homo sapiens. | ||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||
| InterPro | IPR018867. Cdc_assoc-8. [Graphical view] | ||||||||||||||||||||||||||||||
| Pfam | PF10512. Borealin. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||
Other Resources | |||||||||||||||||||||||||||||||
| NextBio | 58844. | ||||||||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||||||||
Entry information
| Entry name | BOREA_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q53HL2 Secondary accession number(s): Q53HN1, Q96AM3, Q9NVW5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 1 Human chromosome 1: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


