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UniProtKB - Q53HL2 (BOREA_HUMAN)

Entry version 134 (08 May 2019)
Sequence version 2 (25 Jul 2006)
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Protein

Borealin

Gene

CDCA8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment.4 Publications

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.

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell cycle, Cell division, Mitosis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-68877 Mitotic Prometaphase

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q53HL2

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Borealin
Alternative name(s):
Cell division cycle-associated protein 8
Dasra-B
Short name:
hDasra-B
Pluripotent embryonic stem cell-related gene 3 protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CDCA8
Synonyms:PESCRG3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:14629 CDCA8

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		609977 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q53HL2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi17R → E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-19 and E-20. 1 Publication1
Mutagenesisi19R → E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-17 and E-20. 1 Publication1
Mutagenesisi20K → E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-17 and E-19. 1 Publication1
Mutagenesisi26K → R: Fails to exhibit normal localization to the nucleolus in interphase depleted cells. 1 Publication1
Mutagenesisi35R → E: Loss of binding to INCENP; when associated with Y-46. 1 Publication1
Mutagenesisi46L → Y: Loss of binding to INCENP; when associated with E-35. 1 Publication1
Mutagenesisi70W → E: Loss of binding to BIRC5; when associated with E-74. 1 Publication1
Mutagenesisi74F → E: Loss of binding to BIRC5; when associated with E-70. 1 Publication1
Mutagenesisi88T → A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-94; A-169 and A-230. 1 Publication1
Mutagenesisi94T → A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-169 and A-230. 1 Publication1
Mutagenesisi106T → A: Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-171, A-185, A-189, A-199, A-204 and A-219. 1 Publication1
Mutagenesisi165S → A: Results in reduction but not abolition of phosphorylation. 1 Publication1
Mutagenesisi169T → A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-94 and A-230. 1 Publication1
Mutagenesisi171T → A: Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-185, A-189, A-199, A-204 and A-219. 1 Publication1
Mutagenesisi185T → A: Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-171, A-189, A-199, A-204 and A-219. 1 Publication1
Mutagenesisi189T → A: Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-171, A-185, A-199, A-204 and A-219. 1 Publication1
Mutagenesisi199T → A: Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-171, A-185, A-189, A-204, A-219. 1 Publication1
Mutagenesisi204T → A: Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-171, A-185, A-189, A-199 and A-219. 1 Publication1
Mutagenesisi219S → A: Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-171, A-185, A-189, A-199 and A-204. 1 Publication1
Mutagenesisi219S → D or K: No effect on the structure. 1
Mutagenesisi230T → 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. 1 Publication1
Mutagenesisi230T → D or K: Substantial loss of structure. 1 Publication1
Mutagenesisi230T → V: Decrease in AURKB activity and no effect on the structure. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		55143

Open Targets

More...OpenTargetsi		ENSG00000134690

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA26281

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		CDCA8

Domain mapping of disease mutations (DMDM)

More...DMDMi		110832774

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002470751 – 280BorealinAdd BLAST280

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei88Phosphothreonine; by TTK1 Publication1
Modified residuei94Phosphothreonine; by TTK1 Publication1
Modified residuei106PhosphothreonineCombined sources1
Modified residuei110PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki135Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei165Phosphoserine; by AURKB1 Publication1
Modified residuei169Phosphothreonine; by TTK1 Publication1
Modified residuei189PhosphothreonineCombined sources1
Modified residuei204PhosphothreonineCombined sources1
Modified residuei219PhosphoserineCombined sources1
Modified residuei224PhosphoserineCombined sources1
Modified residuei230Phosphothreonine; by TTK1 Publication1
Modified residuei238Phosphoserine1 Publication1
Modified residuei244PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by TTK, essentially at Thr-88, Thr94, Thr-169 and Thr-230. Phosphorylation (probably by CDK1) promotes targeting of the CPC to centromeric DNA.3 Publications
Sumoylated by UBE2I and RANBP2. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q53HL2

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q53HL2

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q53HL2

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q53HL2

PeptideAtlas

More...PeptideAtlasi		Q53HL2

PRoteomics IDEntifications database

More...PRIDEi		Q53HL2

ProteomicsDB human proteome resource

More...ProteomicsDBi		62507

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q53HL2

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q53HL2

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Cell-cycle regulated. Increases during G2/M phase and then reduces after exit from M phase.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000134690 Expressed in 126 organ(s), highest expression level in oocyte

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q53HL2 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB040294
HPA028120
HPA028258
HPA028783

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

May form homooligomers and homodimers.

Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; in the complex forms a triple-helix bundle-based subcomplex with INCENP and BIRC5 (PubMed:17956729).

Interacts with SENP3, UBE2I and RANBP2.

Interacts (phosphorylated) with SGO1 and SGO2; the association is dependent on CDK1.

9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		120446, 68 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-116 Chromosomal passenger complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q53HL2

Database of interacting proteins

More...DIPi		DIP-37995N

Protein interaction database and analysis system

More...IntActi		Q53HL2, 27 interactors

Molecular INTeraction database

More...MINTi		Q53HL2

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000362146

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1280
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q53HL2

Database of comparative protein structure models

More...ModBasei		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q53HL2

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 140Required for interaction with SENP31 PublicationAdd BLAST140
Regioni1 – 88Required for centromere localizationAdd BLAST88
Regioni1 – 58Required for interaction with INCENP1 PublicationAdd BLAST58
Regioni10 – 109Required to form a minimal CPC core complex that localizes to the central spindle and midbody and properly executes the role of the CPC during cytokinesisAdd BLAST100
Regioni20 – 78Required for interaction with INCENP and BIRC51 PublicationAdd BLAST59

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi125 – 133Poly-Glu9

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C-terminal region (aa 207-280) represents the dimerization motif.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the borealin family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410IICJ Eukaryota
ENOG4111N8R LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00390000011115

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000261628

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q53HL2

KEGG Orthology (KO)

More...KOi		K11514

Identification of Orthologs from Complete Genome Data

More...OMAi		TSRVKRC

Database of Orthologous Groups

More...OrthoDBi		1587028at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q53HL2

TreeFam database of animal gene trees

More...TreeFami		TF101077

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR018851 Borealin_N
IPR018867 Cell_div_borealin

Pfam protein domain database

More...Pfami		View protein in Pfam
PF10512 Borealin, 1 hit
PF10444 Nbl1_Borealin_N, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q53HL2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAPRKGSSRV AKTNSLRRRK LASFLKDFDR EVEIRIKQIE SDRQNLLKEV 
        60         70         80         90        100
DNLYNIEILR LPKALREMNW LDYFALGGNK QALEEAATAD LDITEINKLT 
       110        120        130        140        150
AEAIQTPLKS AKTRKVIQVD EMIVEEEEEE ENERKNLQTA RVKRCPPSKK 
       160        170        180        190        200
RTQSIQGKGK GKRSSRANTV TPAVGRLEVS MVKPTPGLTP RFDSRVFKTP 
       210        220        230        240        250
GLRTPAAGER IYNISGNGSP LADSKEIFLT VPVGGGESLR LLASDLQRHS 
       260        270        280
IAQLDPEALG NIKKLSNRLA QICSSIRTHK
Length:280
Mass (Da):31,323
Last modified:July 25, 2006 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i519978A7C295C571
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BG354581 differs from that shown. Reason: Frameshift at positions 123 and 200.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti155I → M in BAD96288 (Ref. 4) Curated1
Sequence conflicti213N → D in BAD96269 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_02706312K → N1 PublicationCorresponds to variant dbSNP:rs17851453Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
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
CH471059 Genomic DNA Translation: EAX07324.1
CH471059 Genomic DNA Translation: EAX07325.1
BC000703 mRNA Translation: AAH00703.1
BC001651 mRNA Translation: AAH01651.1
BC016944 mRNA Translation: AAH16944.1
BC008079 mRNA Translation: AAH08079.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS424.1

NCBI Reference Sequences

More...RefSeqi		NP_001243804.1, NM_001256875.1
NP_060571.1, NM_018101.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000327331; ENSP00000316121; ENSG00000134690
ENST00000373055; ENSP00000362146; ENSG00000134690

Database of genes from NCBI RefSeq genomes

More...GeneIDi		55143

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:55143

UCSC genome browser

More...UCSCi		uc001cbr.5 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CH471059 Genomic DNA Translation: EAX07324.1
CH471059 Genomic DNA Translation: EAX07325.1
BC000703 mRNA Translation: AAH00703.1
BC001651 mRNA Translation: AAH01651.1
BC016944 mRNA Translation: AAH16944.1
BC008079 mRNA Translation: AAH08079.1
CCDSiCCDS424.1
RefSeqiNP_001243804.1, NM_001256875.1
NP_060571.1, NM_018101.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KDDNMR-A/B207-280[»]
2QFAX-ray1.40B15-76[»]
2RAWX-ray2.40B20-78[»]
2RAXX-ray3.30B/F/Y20-78[»]
SMRiQ53HL2
ModBaseiSearch...

Protein-protein interaction databases

BioGridi120446, 68 interactors
ComplexPortaliCPX-116 Chromosomal passenger complex
CORUMiQ53HL2
DIPiDIP-37995N
IntActiQ53HL2, 27 interactors
MINTiQ53HL2
STRINGi9606.ENSP00000362146

PTM databases

iPTMnetiQ53HL2
PhosphoSitePlusiQ53HL2

Polymorphism and mutation databases

BioMutaiCDCA8
DMDMi110832774

Proteomic databases

EPDiQ53HL2
jPOSTiQ53HL2
MaxQBiQ53HL2
PaxDbiQ53HL2
PeptideAtlasiQ53HL2
PRIDEiQ53HL2
ProteomicsDBi62507

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		55143
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000327331; ENSP00000316121; ENSG00000134690
ENST00000373055; ENSP00000362146; ENSG00000134690
GeneIDi55143
KEGGihsa:55143
UCSCiuc001cbr.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		55143
DisGeNETi55143

GeneCards: human genes, protein and diseases

More...GeneCardsi		CDCA8
HGNCiHGNC:14629 CDCA8
HPAiCAB040294
HPA028120
HPA028258
HPA028783
MIMi609977 gene
neXtProtiNX_Q53HL2
OpenTargetsiENSG00000134690
PharmGKBiPA26281

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410IICJ Eukaryota
ENOG4111N8R LUCA
GeneTreeiENSGT00390000011115
HOGENOMiHOG000261628
InParanoidiQ53HL2
KOiK11514
OMAiTSRVKRC
OrthoDBi1587028at2759
PhylomeDBiQ53HL2
TreeFamiTF101077

Enzyme and pathway databases

ReactomeiR-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-68877 Mitotic Prometaphase
SIGNORiQ53HL2

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		CDCA8 human
EvolutionaryTraceiQ53HL2

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		CDCA8

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		55143

Protein Ontology

More...PROi		PR:Q53HL2

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000134690 Expressed in 126 organ(s), highest expression level in oocyte
GenevisibleiQ53HL2 HS

Family and domain databases

InterProiView protein in InterPro
IPR018851 Borealin_N
IPR018867 Cell_div_borealin
PfamiView protein in Pfam
PF10512 Borealin, 1 hit
PF10444 Nbl1_Borealin_N, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiBOREA_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q53HL2
Secondary accession number(s): D3DPT4
, Q53HN1, Q96AM3, Q9NVW5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: May 8, 2019
This is version 134 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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