UniProtKB - Q9NQS7 (INCE_HUMAN)
Inner centromere protein
INCENP
Functioni
Caution
GO - Molecular functioni
- protein serine/threonine kinase activator activity Source: GO_Central
GO - Biological processi
- chromosome segregation Source: UniProtKB
- histone phosphorylation Source: GO_Central
- meiotic chromosome condensation Source: GO_Central
- meiotic spindle midzone assembly Source: GO_Central
- metaphase plate congression Source: GO_Central
- mitotic cytokinesis Source: UniProtKB
- mitotic sister chromatid segregation Source: InterPro
- positive regulation of protein serine/threonine kinase activity Source: GO_Central
- regulation of mitotic cytokinesis Source: InterPro
Keywordsi
Biological process | Cell cycle, Cell division, Chromosome partition, Mitosis |
Enzyme and pathway databases
PathwayCommonsi | Q9NQS7 |
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 R-HSA-9648025, EML4 and NUDC in mitotic spindle formation |
SIGNORi | Q9NQS7 |
Names & Taxonomyi
Protein namesi | Recommended name: Inner centromere protein |
Gene namesi | Name:INCENP |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000149503.12 |
HGNCi | HGNC:6058, INCENP |
MIMi | 604411, gene |
neXtProti | NX_Q9NQS7 |
Subcellular locationi
Cytoskeleton
- spindle 2 Publications
Nucleus
- Nucleus 1 Publication
Other locations
- centromere 4 Publications
- Midbody 1 Publication
- kinetochore 1 Publication
Note: Colocalized at synaptonemal complex central element from zygotene up to late pachytene when it begins to relocalize to heterochromatic chromocenters. Colocalizes with AURKB at a connecting strand traversing the centromere region and joining sister kinetochores, in metaphase II centromeres. This strand disappears at the metaphase II/anaphase II transition and relocalizes to the spindle midzone (By similarity). Colocalizes with AURKB at mitotic chromosomes (PubMed:11453556). Localizes to inner kinetochore (PubMed:16760428). Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis (PubMed:15316025). Cocalizes to the equatorial cell cortex at anaphase (PubMed:11453556).By similarity3 Publications
Cytoskeleton
- chromosome passenger complex Source: GO_Central
- meiotic spindle midzone Source: GO_Central
- microtubule Source: UniProtKB-KW
- spindle Source: UniProtKB
Cytosol
- cytosol Source: HPA
Nucleus
- central element Source: Ensembl
- lateral element Source: Ensembl
- nuclear body Source: HPA
- nucleoplasm Source: HPA
- nucleus Source: GO_Central
Other locations
- chromocenter Source: Ensembl
- chromosome, centromeric region Source: UniProtKB
- condensed chromosome Source: GO_Central
- condensed chromosome kinetochore Source: UniProtKB-SubCell
- kinetochore Source: UniProtKB
- midbody Source: HPA
- pericentric heterochromatin Source: UniProtKB
- protein-containing complex Source: UniProtKB
Keywords - Cellular componenti
Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 22 | F → R: Loss of binding to CDCA8 and BIRC5; when associated with R-34. 1 Publication | 1 | |
Mutagenesisi | 34 | L → R: Loss of binding to CDCA8 and BIRC5; when associated with R-22. 1 Publication | 1 | |
Mutagenesisi | 35 | E → 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 Publication | 1 | |
Mutagenesisi | 36 | E → 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 Publication | 1 | |
Mutagenesisi | 39 | E → 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 Publication | 1 | |
Mutagenesisi | 40 | E → 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 Publication | 1 | |
Mutagenesisi | 167 | P → A: Decreases interaction with CBX5, abolishes localization to centromeres in interphase; when associated with A-169 and A-171. 1 Publication | 1 | |
Mutagenesisi | 169 | V → A: Decreases interaction with CBX5, abolishes localization to centromeres in interphase; when associated with A-167 and A-171. 1 Publication | 1 | |
Mutagenesisi | 169 | V → E: Abolishes interaction with CBX5. 1 Publication | 1 | |
Mutagenesisi | 171 | I → A: Decreases interaction with CBX5, abolishes localization to centromeres in interphase; when associated with A-167 and A-169. 1 Publication | 1 | |
Mutagenesisi | 171 | I → E: Abolishes interaction with CBX5 and AURKB. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 3619 |
OpenTargetsi | ENSG00000149503 |
PharmGKBi | PA29868 |
Miscellaneous databases
Pharosi | Q9NQS7, Tbio |
Chemistry databases
ChEMBLi | CHEMBL3430907 CHEMBL4106141 |
DrugBanki | DB07340, Reversine |
Polymorphism and mutation databases
BioMutai | INCENP |
DMDMi | 212276501 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000084201 | 1 – 918 | Inner centromere proteinAdd BLAST | 918 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 72 | PhosphoserineCombined sources | 1 | |
Modified residuei | 119 | PhosphoserineCombined sources | 1 | |
Modified residuei | 143 | PhosphoserineCombined sources | 1 | |
Modified residuei | 148 | PhosphoserineCombined sources | 1 | |
Modified residuei | 150 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 195 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 197 | PhosphoserineCombined sources | 1 | |
Modified residuei | 199 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 213 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 214 | PhosphoserineCombined sources | 1 | |
Modified residuei | 219 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 239 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 263 | PhosphoserineCombined sources | 1 | |
Modified residuei | 269 | PhosphoserineCombined sources | 1 | |
Modified residuei | 275 | PhosphoserineCombined sources | 1 | |
Modified residuei | 292 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 296 | PhosphoserineCombined sources | 1 | |
Modified residuei | 306 | PhosphoserineCombined sources | 1 | |
Modified residuei | 312 | PhosphoserineCombined sources | 1 | |
Modified residuei | 314 | PhosphoserineCombined sources | 1 | |
Modified residuei | 330 | PhosphoserineCombined sources | 1 | |
Modified residuei | 400 | PhosphoserineCombined sources | 1 | |
Modified residuei | 406 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 446 | PhosphoserineCombined sources | 1 | |
Modified residuei | 476 | PhosphoserineCombined sources | 1 | |
Modified residuei | 478 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 480 | PhosphoserineBy similarity | 1 | |
Modified residuei | 510 | PhosphoserineCombined sources | 1 | |
Modified residuei | 514 | PhosphoserineCombined sources | 1 | |
Modified residuei | 828 | PhosphoserineCombined sources | 1 | |
Modified residuei | 831 | PhosphoserineCombined sources | 1 | |
Modified residuei | 832 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 892 | Phosphothreonine; by AURKB and AURKC2 Publications | 1 | |
Modified residuei | 893 | Phosphoserine; by AURKB and AURKC2 Publications | 1 | |
Modified residuei | 894 | Phosphoserine; by AURKB and AURKCCombined sources2 Publications | 1 | |
Modified residuei | 899 | PhosphoserineCombined sources | 1 | |
Modified residuei | 914 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
PhosphoproteinProteomic databases
EPDi | Q9NQS7 |
jPOSTi | Q9NQS7 |
MassIVEi | Q9NQS7 |
MaxQBi | Q9NQS7 |
PaxDbi | Q9NQS7 |
PeptideAtlasi | Q9NQS7 |
PRIDEi | Q9NQS7 |
ProteomicsDBi | 82181 [Q9NQS7-1] 82182 [Q9NQS7-2] |
PTM databases
iPTMneti | Q9NQS7 |
PhosphoSitePlusi | Q9NQS7 |
Expressioni
Gene expression databases
Bgeei | ENSG00000149503, Expressed in ventricular zone and 149 other tissues |
ExpressionAtlasi | Q9NQS7, baseline and differential |
Genevisiblei | Q9NQS7, HS |
Organism-specific databases
HPAi | ENSG00000149503, Tissue enhanced (lymphoid) |
Interactioni
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 H2AZ1 (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 PublicationsBinary interactionsi
Hide detailsQ9NQS7
Isoform 1 [Q9NQS7-1]
With | #Exp. | IntAct |
---|---|---|
AURKA [O14965] | 2 | EBI-15767972,EBI-448680 |
AURKB [Q96GD4] | 2 | EBI-15767972,EBI-624291 |
Protein-protein interaction databases
BioGRIDi | 109831, 31 interactors |
ComplexPortali | CPX-116, Chromosomal passenger complex |
CORUMi | Q9NQS7 |
DIPi | DIP-31304N |
IntActi | Q9NQS7, 23 interactors |
MINTi | Q9NQS7 |
STRINGi | 9606.ENSP00000378295 |
Chemistry databases
BindingDBi | Q9NQS7 |
Miscellaneous databases
RNActi | Q9NQS7, protein |
Structurei
Secondary structure
3D structure databases
SMRi | Q9NQS7 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q9NQS7 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 124 – 248 | Interaction with CBX51 PublicationAdd BLAST | 125 | |
Regioni | 531 – 765 | SAHBy similarityAdd BLAST | 235 | |
Regioni | 822 – 897 | Interaction with AURKC1 PublicationAdd BLAST | 76 | |
Regioni | 826 – 900 | IN boxCuratedAdd BLAST | 75 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 167 – 171 | PXVXL/I motif1 Publication | 5 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG4456, Eukaryota |
GeneTreei | ENSGT00730000111073 |
HOGENOMi | CLU_015997_0_0_1 |
InParanoidi | Q9NQS7 |
OMAi | DERYDHQ |
OrthoDBi | 671886at2759 |
PhylomeDBi | Q9NQS7 |
TreeFami | TF101172 |
Family and domain databases
IDEALi | IID00224 |
InterProi | View protein in InterPro IPR039130, INCENP IPR022006, INCENP_N IPR005635, Inner_centromere_prot_ARK-bd |
PANTHERi | PTHR13142, PTHR13142, 1 hit |
Pfami | View protein in Pfam PF03941, INCENP_ARK-bind, 1 hit PF12178, INCENP_N, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketE9PM67 | E9PM67_HUMAN | Inner centromere protein | INCENP | 167 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 715 | Q → QERREQ in AAF87584 (PubMed:11453556).Curated | 1 | |
Sequence conflicti | 804 – 806 | YQM → SPI in AAF87584 (PubMed:11453556).Curated | 3 | |
Sequence conflicti | 812 | R → K in AAF87584 (PubMed:11453556).Curated | 1 | |
Sequence conflicti | 816 | K → Q in AAF87584 (PubMed:11453556).Curated | 1 | |
Sequence conflicti | 820 | D → H in AAF87584 (PubMed:11453556).Curated | 1 | |
Sequence conflicti | 861 | H → Q in AAF87584 (PubMed:11453556).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_047127 | 2 | G → V. Corresponds to variant dbSNP:rs1792947Ensembl. | 1 | |
Natural variantiVAR_047128 | 100 | R → H. Corresponds to variant dbSNP:rs12281503EnsemblClinVar. | 1 | |
Natural variantiVAR_047129 | 137 | A → V. Corresponds to variant dbSNP:rs34441559Ensembl. | 1 | |
Natural variantiVAR_047130 | 506 | M → T. Corresponds to variant dbSNP:rs2277283Ensembl. | 1 | |
Natural variantiVAR_047131 | 644 | E → D3 PublicationsCorresponds to variant dbSNP:rs7129085Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_035651 | 532 – 535 | Missing in isoform 2. 1 Publication | 4 |
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 |
CCDSi | CCDS31582.1 [Q9NQS7-2] CCDS44624.1 [Q9NQS7-1] |
RefSeqi | NP_001035784.1, NM_001040694.1 [Q9NQS7-1] NP_064623.2, NM_020238.2 [Q9NQS7-2] |
Genome annotation databases
Ensembli | ENST00000278849; ENSP00000278849; ENSG00000149503 [Q9NQS7-2] ENST00000394818; ENSP00000378295; ENSG00000149503 [Q9NQS7-1] |
GeneIDi | 3619 |
KEGGi | hsa:3619 |
UCSCi | uc001nsw.2, human [Q9NQS7-1] |
Keywords - Coding sequence diversityi
Alternative splicing, PolymorphismSimilar proteinsi
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 |
CCDSi | CCDS31582.1 [Q9NQS7-2] CCDS44624.1 [Q9NQS7-1] |
RefSeqi | NP_001035784.1, NM_001040694.1 [Q9NQS7-1] NP_064623.2, NM_020238.2 [Q9NQS7-2] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2QFA | X-ray | 1.40 | C | 1-47 | [»] | |
4AF3 | X-ray | 2.75 | D | 835-903 | [»] | |
5IEH | X-ray | 1.50 | C | 47-55 | [»] | |
5IEK | X-ray | 1.80 | C | 47-55 | [»] | |
6GR8 | X-ray | 1.75 | B | 835-903 | [»] | |
6GR9 | X-ray | 2.25 | B | 835-903 | [»] | |
6YIE | X-ray | 3.49 | C/F | 1-58 | [»] | |
6YIF | X-ray | 1.81 | C | 7-57 | [»] | |
6YIH | X-ray | 2.55 | C | 5-80 | [»] | |
SMRi | Q9NQS7 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 109831, 31 interactors |
ComplexPortali | CPX-116, Chromosomal passenger complex |
CORUMi | Q9NQS7 |
DIPi | DIP-31304N |
IntActi | Q9NQS7, 23 interactors |
MINTi | Q9NQS7 |
STRINGi | 9606.ENSP00000378295 |
Chemistry databases
BindingDBi | Q9NQS7 |
ChEMBLi | CHEMBL3430907 CHEMBL4106141 |
DrugBanki | DB07340, Reversine |
PTM databases
iPTMneti | Q9NQS7 |
PhosphoSitePlusi | Q9NQS7 |
Polymorphism and mutation databases
BioMutai | INCENP |
DMDMi | 212276501 |
Proteomic databases
EPDi | Q9NQS7 |
jPOSTi | Q9NQS7 |
MassIVEi | Q9NQS7 |
MaxQBi | Q9NQS7 |
PaxDbi | Q9NQS7 |
PeptideAtlasi | Q9NQS7 |
PRIDEi | Q9NQS7 |
ProteomicsDBi | 82181 [Q9NQS7-1] 82182 [Q9NQS7-2] |
Protocols and materials databases
Antibodypediai | 4598, 171 antibodies |
Genome annotation databases
Ensembli | ENST00000278849; ENSP00000278849; ENSG00000149503 [Q9NQS7-2] ENST00000394818; ENSP00000378295; ENSG00000149503 [Q9NQS7-1] |
GeneIDi | 3619 |
KEGGi | hsa:3619 |
UCSCi | uc001nsw.2, human [Q9NQS7-1] |
Organism-specific databases
CTDi | 3619 |
DisGeNETi | 3619 |
EuPathDBi | HostDB:ENSG00000149503.12 |
GeneCardsi | INCENP |
HGNCi | HGNC:6058, INCENP |
HPAi | ENSG00000149503, Tissue enhanced (lymphoid) |
MIMi | 604411, gene |
neXtProti | NX_Q9NQS7 |
OpenTargetsi | ENSG00000149503 |
PharmGKBi | PA29868 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG4456, Eukaryota |
GeneTreei | ENSGT00730000111073 |
HOGENOMi | CLU_015997_0_0_1 |
InParanoidi | Q9NQS7 |
OMAi | DERYDHQ |
OrthoDBi | 671886at2759 |
PhylomeDBi | Q9NQS7 |
TreeFami | TF101172 |
Enzyme and pathway databases
PathwayCommonsi | Q9NQS7 |
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 R-HSA-9648025, EML4 and NUDC in mitotic spindle formation |
SIGNORi | Q9NQS7 |
Miscellaneous databases
BioGRID-ORCSi | 3619, 724 hits in 849 CRISPR screens |
ChiTaRSi | INCENP, human |
EvolutionaryTracei | Q9NQS7 |
GeneWikii | INCENP |
GenomeRNAii | 3619 |
Pharosi | Q9NQS7, Tbio |
PROi | PR:Q9NQS7 |
RNActi | Q9NQS7, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000149503, Expressed in ventricular zone and 149 other tissues |
ExpressionAtlasi | Q9NQS7, baseline and differential |
Genevisiblei | Q9NQS7, HS |
Family and domain databases
IDEALi | IID00224 |
InterProi | View protein in InterPro IPR039130, INCENP IPR022006, INCENP_N IPR005635, Inner_centromere_prot_ARK-bd |
PANTHERi | PTHR13142, PTHR13142, 1 hit |
Pfami | View protein in Pfam PF03941, INCENP_ARK-bind, 1 hit PF12178, INCENP_N, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | INCE_HUMAN | |
Accessioni | Q9NQS7Primary (citable) accession number: Q9NQS7 Secondary accession number(s): A8MQD2, Q5Y192 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 23, 2003 |
Last sequence update: | November 4, 2008 | |
Last modified: | December 2, 2020 | |
This is version 177 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- 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 - Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations