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UniProtKB - Q9NQS7 (INCE_HUMAN)

Entry version 164 (13 Feb 2019)
Sequence version 3 (04 Nov 2008)
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Protein

Inner centromere protein

Gene

INCENP

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. Acts as a scaffold regulating CPC localization and activity. The C-terminus associates with AURKB or AURKC, the N-terminus associated with BIRC5/survivin and CDCA8/borealin tethers the CPC to the inner centromere, and the microtubule binding activity within the central SAH domain directs AURKB/C toward substrates near microtubules (PubMed:15316025, PubMed:12925766, PubMed:27332895). The flexibility of the SAH domain is proposed to allow AURKB/C to follow substrates on dynamic microtubules while ensuring CPC docking to static chromatin (By similarity). Activates AURKB and AURKC (PubMed:27332895). Required for localization of CBX5 to mitotic centromeres (PubMed:21346195). Controls the kinetochore localization of BUB1 (PubMed:16760428).By similarity5 Publications

Caution

PubMed:11139336 experiments have been carried out partly in chicken and partly in human.Curated
Originally predicted to contain a coiled coil domain but shown to contain a stable SAH domain instead.By similarity

<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

  • chromosome segregation Source: UniProtKB
  • mitotic cytokinesis Source: UniProtKB
  • mitotic sister chromatid segregation Source: InterPro
  • regulation of mitotic cytokinesis Source: InterPro
View the 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, Chromosome partition, 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		Q9NQS7

<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:
Inner centromere 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:INCENP
<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 11

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000149503.12

Human Gene Nomenclature Database

More...HGNCi		HGNC:6058 INCENP

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		604411 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9NQS7

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule, 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>Mutagenesisi22F → R: Loss of binding to CDCA8 and BIRC5; when associated with R-34. 1 Publication1
Mutagenesisi34L → R: Loss of binding to CDCA8 and BIRC5; when associated with R-22. 1 Publication1
Mutagenesisi35E → R: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-36; R-39 and R-40. 1 Publication1
Mutagenesisi36E → R: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-35; R-39 and R-40. 1 Publication1
Mutagenesisi39E → R: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-35; R-36 and R-40. 1 Publication1
Mutagenesisi40E → R: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-35; R-36 and R-39. 1 Publication1
Mutagenesisi167P → A: Decreases interaction with CBX5, abolishes localization to centromeres in interphase; when associated with A-169 and A-171. 1 Publication1
Mutagenesisi169V → A: Decreases interaction with CBX5, abolishes localization to centromeres in interphase; when associated with A-167 and A-171. 1 Publication1
Mutagenesisi169V → E: Abolishes interaction with CBX5. 1 Publication1
Mutagenesisi171I → A: Decreases interaction with CBX5, abolishes localization to centromeres in interphase; when associated with A-167 and A-169. 1 Publication1
Mutagenesisi171I → E: Abolishes interaction with CBX5 and AURKB. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		3619

Open Targets

More...OpenTargetsi		ENSG00000149503

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA29868

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3430907

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		INCENP

Domain mapping of disease mutations (DMDM)

More...DMDMi		212276501

<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_00000842011 – 918Inner centromere proteinAdd BLAST918

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 residuei72PhosphoserineCombined sources1
Modified residuei119PhosphoserineCombined sources1
Modified residuei143PhosphoserineCombined sources1
Modified residuei148PhosphoserineCombined sources1
Modified residuei150PhosphothreonineBy similarity1
Modified residuei195Phosphothreonine1 Publication1
Modified residuei197PhosphoserineCombined sources1
Modified residuei199PhosphothreonineCombined sources1
Modified residuei213PhosphothreonineCombined sources1
Modified residuei214PhosphoserineCombined sources1
Modified residuei219PhosphothreonineBy similarity1
Modified residuei239PhosphothreonineCombined sources1
Modified residuei263PhosphoserineCombined sources1
Modified residuei269PhosphoserineCombined sources1
Modified residuei275PhosphoserineCombined sources1
Modified residuei292PhosphothreonineCombined sources1
Modified residuei296PhosphoserineCombined sources1
Modified residuei306PhosphoserineCombined sources1
Modified residuei312PhosphoserineCombined sources1
Modified residuei314PhosphoserineCombined sources1
Modified residuei330PhosphoserineCombined sources1
Modified residuei400PhosphoserineCombined sources1
Modified residuei406PhosphothreonineCombined sources1
Modified residuei446PhosphoserineCombined sources1
Modified residuei476PhosphoserineCombined sources1
Modified residuei478PhosphothreonineBy similarity1
Modified residuei480PhosphoserineBy similarity1
Modified residuei510PhosphoserineCombined sources1
Modified residuei514PhosphoserineCombined sources1
Modified residuei828PhosphoserineCombined sources1
Modified residuei831PhosphoserineCombined sources1
Modified residuei832PhosphothreonineCombined sources1
Modified residuei892Phosphothreonine; by AURKB and AURKC2 Publications1
Modified residuei893Phosphoserine; by AURKB and AURKC2 Publications1
Modified residuei894Phosphoserine; by AURKB and AURKCCombined sources2 Publications1
Modified residuei899PhosphoserineCombined sources1
Modified residuei914PhosphoserineCombined 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

Phosphorylation by AURKB or AURKC at its C-terminal part is important for AURKB or AURKC activation by INCENP.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9NQS7

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9NQS7

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q9NQS7

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

More...PaxDbi		Q9NQS7

PeptideAtlas

More...PeptideAtlasi		Q9NQS7

PRoteomics IDEntifications database

More...PRIDEi		Q9NQS7

ProteomicsDB human proteome resource

More...ProteomicsDBi		82181
82182 [Q9NQS7-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9NQS7

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

More...PhosphoSitePlusi		Q9NQS7

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000149503 Expressed in 130 organ(s), highest expression level in cerebellum

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9NQS7 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9NQS7 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB013292
HPA051339
HPA070550

<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

Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; in the complex binds directly to AURKB or AURKC via the IN box, and forms a triple-helix bundle-based subcomplex with BIRC5 and CDCA8 via its N-terminus (PubMed:17956729, PubMed:27332895). The reported homodimerization is questioned as the SAH domain is shown to be monomeric (By similarity). Interacts with H2AFZ (By similarity). Interacts with CBX1 and CBX3. Interacts with tubulin beta chain. Interacts with EVI5. Interacts with CBX5; POGZ and INCENP compete for interaction with CBX5; regulates INCENP (and probably CPC) localization to centromeres in interphase and not required for proper mitotic progression or sister chromatid cohesion. Interacts with POGZ. Interacts with JTB.By similarity13 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		109831, 27 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-116 Chromosomal passenger complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q9NQS7

Database of interacting proteins

More...DIPi		DIP-31304N

Protein interaction database and analysis system

More...IntActi		Q9NQS7, 22 interactors

Molecular INTeraction database

More...MINTi		Q9NQS7

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000378295

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q9NQS7

<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

1918
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
2QFAX-ray1.40C1-47[»]
4AF3X-ray2.75D835-903[»]
5IEHX-ray1.50C47-55[»]
5IEKX-ray1.80C47-55[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q9NQS7

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

More...SMRi		Q9NQS7

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q9NQS7

<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>Regioni124 – 248Interaction with CBX51 PublicationAdd BLAST125
Regioni531 – 765SAHBy similarityAdd BLAST235
Regioni822 – 897Interaction with AURKC1 PublicationAdd BLAST76
Regioni826 – 900IN boxCuratedAdd BLAST75

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi167 – 171PXVXL/I motif1 Publication5

<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 IN box mediates interaction with AURKB and AURKC.By similarity1 Publication
The SAH (single alpha-helix) region is characterized by a high content of charged residues which are predicted to stabilize the alpha-helical structure by ionic bonds. It can refold after extension suggesting an in vivo force-dependent function. The isolated SAH domain is monomeric.By similarity

<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 INCENP family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4456 Eukaryota
ENOG410XRQ9 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00730000111073

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000113069

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG006157

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9NQS7

KEGG Orthology (KO)

More...KOi		K11515

Identification of Orthologs from Complete Genome Data

More...OMAi		RVDPKCS

Database of Orthologous Groups

More...OrthoDBi		671886at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9NQS7

TreeFam database of animal gene trees

More...TreeFami		TF101172

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR039130 INCENP
IPR022006 INCENP_N
IPR005635 Inner_centromere_prot_ARK-bd

The PANTHER Classification System

More...PANTHERi		PTHR13142 PTHR13142, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03941 INCENP_ARK-bind, 1 hit
PF12178 INCENP_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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9NQS7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MGTTAPGPIH LLELCDQKLM EFLCNMDNKD LVWLEEIQEE AERMFTREFS 
        60         70         80         90        100
KEPELMPKTP SQKNRRKKRR ISYVQDENRD PIRRRLSRRK SRSSQLSSRR 
       110        120        130        140        150
LRSKDSVEKL ATVVGENGSV LRRVTRAAAA AAAATMALAA PSSPTPESPT 
       160        170        180        190        200
MLTKKPEDNH TQCQLVPVVE IGISERQNAE QHVTQLMSTE PLPRTLSPTP 
       210        220        230        240        250
ASATAPTSQG IPTSDEESTP KKSKARILES ITVSSLMATP QDPKGQGVGT 
       260        270        280        290        300
GRSASKLRIA QVSPGPRDSP AFPDSPWRER VLAPILPDNF STPTGSRTDS 
       310        320        330        340        350
QSVRHSPIAP SSPSPQVLAQ KYSLVAKQES VVRRASRRLA KKTAEEPAAS 
       360        370        380        390        400
GRIICHSYLE RLLNVEVPQK VGSEQKEPPE EAEPVAAAEP EVPENNGNNS 
       410        420        430        440        450
WPHNDTEIAN STPNPKPAAS SPETPSAGQQ EAKTDQADGP REPPQSARRK 
       460        470        480        490        500
RSYKQAVSEL DEEQHLEDEE LQPPRSKTPS SPCPASKVVR PLRTFLHTVQ 
       510        520        530        540        550
RNQMLMTPTS APRSVMKSFI KRNTPLRMDP KCSFVEKERQ RLENLRRKEE 
       560        570        580        590        600
AEQLRRQKVE EDKRRRLEEV KLKREERLRK VLQARERVEQ MKEEKKKQIE 
       610        620        630        640        650
QKFAQIDEKT EKAKEERLAE EKAKKKAAAK KMEEVEARRK QEEEARRLRW 
       660        670        680        690        700
LQQEEEERRH QELLQKKKEE EQERLRKAAE AKRLAEQREQ ERREQERREQ 
       710        720        730        740        750
ERREQERREQ ERREQERQLA EQERRREQER LQAERELQER EKALRLQKEQ 
       760        770        780        790        800
LQRELEEKKK KEEQQRLAER QLQEEQEKKA KEAAGASKAL NVTVDVQSPA 
       810        820        830        840        850
CTSYQMTPQG HRAPPKINPD NYGMDLNSDD STDDEAHPRK PIPTWARGTP 
       860        870        880        890        900
LSQAIIHQYY HPPNLLELFG TILPLDLEDI FKKSKPRYHK RTSSAVWNSP 
       910 
PLQGARVPSS LAYSLKKH
Length:918
Mass (Da):105,429
Last modified:November 4, 2008 - v3
<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:i644D081DCC9035E8
GO
Isoform 2 (identifier: Q9NQS7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     532-535: Missing.

Show »
Length:914
Mass (Da):104,992
Checksum:i6E8C5E65A9C918E8
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PM67E9PM67_HUMAN
Inner centromere protein
INCENP
167Annotation score:

Annotation score:1 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 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 conflicti715Q → QERREQ in AAF87584 (PubMed:11453556).Curated1
Sequence conflicti804 – 806YQM → SPI in AAF87584 (PubMed:11453556).Curated3
Sequence conflicti812R → K in AAF87584 (PubMed:11453556).Curated1
Sequence conflicti816K → Q in AAF87584 (PubMed:11453556).Curated1
Sequence conflicti820D → H in AAF87584 (PubMed:11453556).Curated1
Sequence conflicti861H → Q in AAF87584 (PubMed:11453556).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_0471272G → V. Corresponds to variant dbSNP:rs1792947Ensembl.1
Natural variantiVAR_047128100R → H. Corresponds to variant dbSNP:rs12281503Ensembl.1
Natural variantiVAR_047129137A → V. Corresponds to variant dbSNP:rs34441559Ensembl.1
Natural variantiVAR_047130506M → T. Corresponds to variant dbSNP:rs2277283Ensembl.1
Natural variantiVAR_047131644E → D3 PublicationsCorresponds to variant dbSNP:rs7129085Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_035651532 – 535Missing in isoform 2. 1 Publication4

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
AF282265 mRNA Translation: AAF87584.1
AY714053 mRNA Translation: AAU04398.1
AP002793 Genomic DNA No translation available.
CH471076 Genomic DNA Translation: EAW74004.1
BC098576 mRNA Translation: AAH98576.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS31582.1 [Q9NQS7-2]
CCDS44624.1 [Q9NQS7-1]

NCBI Reference Sequences

More...RefSeqi		NP_001035784.1, NM_001040694.1 [Q9NQS7-1]
NP_064623.2, NM_020238.2 [Q9NQS7-2]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.142179

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000278849; ENSP00000278849; ENSG00000149503 [Q9NQS7-2]
ENST00000394818; ENSP00000378295; ENSG00000149503 [Q9NQS7-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3619

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:3619

UCSC genome browser

More...UCSCi		uc001nsw.2 human [Q9NQS7-1]

Keywords - Coding sequence diversityi

Alternative splicing, 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
AF282265 mRNA Translation: AAF87584.1
AY714053 mRNA Translation: AAU04398.1
AP002793 Genomic DNA No translation available.
CH471076 Genomic DNA Translation: EAW74004.1
BC098576 mRNA Translation: AAH98576.1
CCDSiCCDS31582.1 [Q9NQS7-2]
CCDS44624.1 [Q9NQS7-1]
RefSeqiNP_001035784.1, NM_001040694.1 [Q9NQS7-1]
NP_064623.2, NM_020238.2 [Q9NQS7-2]
UniGeneiHs.142179

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QFAX-ray1.40C1-47[»]
4AF3X-ray2.75D835-903[»]
5IEHX-ray1.50C47-55[»]
5IEKX-ray1.80C47-55[»]
ProteinModelPortaliQ9NQS7
SMRiQ9NQS7
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109831, 27 interactors
ComplexPortaliCPX-116 Chromosomal passenger complex
CORUMiQ9NQS7
DIPiDIP-31304N
IntActiQ9NQS7, 22 interactors
MINTiQ9NQS7
STRINGi9606.ENSP00000378295

Chemistry databases

BindingDBiQ9NQS7
ChEMBLiCHEMBL3430907

PTM databases

iPTMnetiQ9NQS7
PhosphoSitePlusiQ9NQS7

Polymorphism and mutation databases

BioMutaiINCENP
DMDMi212276501

Proteomic databases

EPDiQ9NQS7
jPOSTiQ9NQS7
MaxQBiQ9NQS7
PaxDbiQ9NQS7
PeptideAtlasiQ9NQS7
PRIDEiQ9NQS7
ProteomicsDBi82181
82182 [Q9NQS7-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000278849; ENSP00000278849; ENSG00000149503 [Q9NQS7-2]
ENST00000394818; ENSP00000378295; ENSG00000149503 [Q9NQS7-1]
GeneIDi3619
KEGGihsa:3619
UCSCiuc001nsw.2 human [Q9NQS7-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3619
DisGeNETi3619
EuPathDBiHostDB:ENSG00000149503.12

GeneCards: human genes, protein and diseases

More...GeneCardsi		INCENP

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0009706
HGNCiHGNC:6058 INCENP
HPAiCAB013292
HPA051339
HPA070550
MIMi604411 gene
neXtProtiNX_Q9NQS7
OpenTargetsiENSG00000149503
PharmGKBiPA29868

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG4456 Eukaryota
ENOG410XRQ9 LUCA
GeneTreeiENSGT00730000111073
HOGENOMiHOG000113069
HOVERGENiHBG006157
InParanoidiQ9NQS7
KOiK11515
OMAiRVDPKCS
OrthoDBi671886at2759
PhylomeDBiQ9NQS7
TreeFamiTF101172

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
SIGNORiQ9NQS7

Miscellaneous databases

EvolutionaryTraceiQ9NQS7

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		INCENP

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

More...GenomeRNAii		3619

Protein Ontology

More...PROi		PR:Q9NQS7

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000149503 Expressed in 130 organ(s), highest expression level in cerebellum
ExpressionAtlasiQ9NQS7 baseline and differential
GenevisibleiQ9NQS7 HS

Family and domain databases

InterProiView protein in InterPro
IPR039130 INCENP
IPR022006 INCENP_N
IPR005635 Inner_centromere_prot_ARK-bd
PANTHERiPTHR13142 PTHR13142, 1 hit
PfamiView protein in Pfam
PF03941 INCENP_ARK-bind, 1 hit
PF12178 INCENP_N, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		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 nameiINCE_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: Q9NQS7
Secondary accession number(s): A8MQD2, Q5Y192
<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: April 23, 2003
Last sequence update: November 4, 2008
Last modified: February 13, 2019
This is version 164 of the entry and version 3 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. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
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