Q03188 · CENPC_HUMAN
- ProteinCentromere protein C
- GeneCENPC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids943 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPC recruits DNA methylation and DNMT3B to both centromeric and pericentromeric satellite repeats and regulates the histone code in these regions.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | condensed chromosome, centromeric region | |
Cellular Component | cytosol | |
Cellular Component | inner kinetochore | |
Cellular Component | kinetochore | |
Cellular Component | midbody | |
Cellular Component | nuclear body | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | pericentric heterochromatin | |
Molecular Function | centromeric DNA binding | |
Molecular Function | DNA binding | |
Molecular Function | identical protein binding | |
Biological Process | attachment of mitotic spindle microtubules to kinetochore | |
Biological Process | cell division | |
Biological Process | chromosome segregation | |
Biological Process | kinetochore assembly | |
Biological Process | mitotic cell cycle | |
Biological Process | spindle attachment to meiosis I kinetochore |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCentromere protein C
- Short namesCENP-C
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ03188
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes exclusively in the kinetochore domain of centromeres.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_069295 | 341 | in dbSNP:rs11250 | |||
Sequence: L → F | ||||||
Natural variant | VAR_069296 | 389 | in dbSNP:rs1056787 | |||
Sequence: G → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,019 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, cross-link, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000089474 | 1-943 | UniProt | Centromere protein C | |||
Sequence: MAASGLDHLKNGYRRRFCRPSRARDINTEQGQNVLEILQDCFEEKSLANDFSTNSTKSVPNSTRKIKDTCIQSPSKECQKSHPKSVPVSSKKKEASLQFVVEPSEATNRSVQAHEVHQKILATDVSSKNTPDSKKISSRNINDHHSEADEEFYLSVGSPSVLLDAKTSVSQNVIPSSAQKRETYTFENSVNMLPSSTEVSVKTKKRLNFDDKVMLKKIEIDNKVSDEEDKTSEGQERKPSGSSQNRIRDSEYEIQRQAKKSFSTLFLETVKRKSESSPIVRHAATAPPHSCPPDDTKLIEDEFIIDESDQSFASRSWITIPRKAGSLKQRTISPAESTALLQGRKSREKHHNILPKTLANDKHSHKPHPVETSQPSDKTVLDTSYALIGETVNNYRSTKYEMYSKNAEKPSRSKRTIKQKQRRKFMAKPAEEQLDVGQSKDENIHTSHITQDEFQRNSDRNMEEHEEMGNDCVSKKQMPPVGSKKSSTRKDKEESKKKRFSSESKNKLVPEEVTSTVTKSRRISRRPSDWWVVKSEESPVYSNSSVRNELPMHHNSSRKSTKKTNQSSKNIRKKTIPLKRQKTATKGNQRVQKFLNAEGSGGIVGHDEISRCSLSEPLESDEADLAKKKNLDCSRSTRSSKNEDNIMTAQNVPLKPQTSGYTCNIPTESNLDSGEHKTSVLEESGPSRLNNNYLMSGKNDVDDEEVHGSSDDSKQSKVIPKNRIHHKLVLPSNTPNVRRTKRTRLKPLEYWRGERIDYQGRPSGGFVISGVLSPDTISSKRKAKENIGKVNKKSNKKRICLDNDERKTNLMVNLGIPLGDPLQPTRVKDPETREIILMDLVRPQDTYQFFVKHGELKVYKTLDTPFFSTGKLILGPQEEKGKQHVGQDILVFYVNFGDLLCTLHETPYILSTGDSFYVPSGNYYNIKNLRNEESVLLFTQIKR | |||||||
Cross-link | 45 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 46 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 52 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 55 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 56 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 73 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 73 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 75 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 96 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 96 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 110 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 119 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 126 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 127 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 130 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 130 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 133 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 134 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 146 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 146 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 158 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 170 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 176 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 177 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 180 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 183 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 189 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 189 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 212 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 217 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 225 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 225 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 231 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 232 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 238 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 250 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 260 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 261 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 261 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 271 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 273 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 277 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 290 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 296 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 297 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 308 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 311 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 316 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 331 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 333 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 333 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 337 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 372 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 373 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 376 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 376 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 384 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 397 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 439 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 439 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 440 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 447 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 515 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 516 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 528 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 528 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 534 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 535 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 538 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 538 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 542 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 556 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 600 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 610 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 613 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 615 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 620 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 673 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 677 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 679 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 684 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 684 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 709 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 709 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 710 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 710 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 713 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 727 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 732 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 734 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 734 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 763 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 763 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 769 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 773 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 773 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 776 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 807 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Expression varies across the cell cycle, with high levels in G2 phase (at the mRNA level).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Oligomer. Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU (PubMed:16622419).
The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Binds to DAXX (PubMed:9645950).
Interacts with DNMT3B (PubMed:19482874).
Interacts directly with CENPA (PubMed:19503796).
Identified in a centromere complex containing histones H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1 (PubMed:27499292).
Interacts with MEIKIN (By similarity).
The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Binds to DAXX (PubMed:9645950).
Interacts with DNMT3B (PubMed:19482874).
Interacts directly with CENPA (PubMed:19503796).
Identified in a centromere complex containing histones H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1 (PubMed:27499292).
Interacts with MEIKIN (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q03188 | CENPA P49450 | 4 | EBI-295799, EBI-1751979 | |
BINARY | Q03188 | CENPC Q03188 | 4 | EBI-295799, EBI-295799 | |
BINARY | Q03188 | H1-5 P16401 | 2 | EBI-295799, EBI-5327611 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 70-85 | Polar residues | ||||
Sequence: CIQSPSKECQKSHPKS | ||||||
Region | 70-91 | Disordered | ||||
Sequence: CIQSPSKECQKSHPKSVPVSSK | ||||||
Region | 224-250 | Disordered | ||||
Sequence: VSDEEDKTSEGQERKPSGSSQNRIRDS | ||||||
Motif | 259-273 | Nuclear localization signal | ||||
Sequence: KKSFSTLFLETVKRK | ||||||
Compositional bias | 358-372 | Basic and acidic residues | ||||
Sequence: LANDKHSHKPHPVET | ||||||
Region | 358-377 | Disordered | ||||
Sequence: LANDKHSHKPHPVETSQPSD | ||||||
Region | 403-513 | Disordered | ||||
Sequence: YSKNAEKPSRSKRTIKQKQRRKFMAKPAEEQLDVGQSKDENIHTSHITQDEFQRNSDRNMEEHEEMGNDCVSKKQMPPVGSKKSSTRKDKEESKKKRFSSESKNKLVPEEV | ||||||
Compositional bias | 424-472 | Basic and acidic residues | ||||
Sequence: KFMAKPAEEQLDVGQSKDENIHTSHITQDEFQRNSDRNMEEHEEMGNDC | ||||||
Motif | 484-499 | Nuclear localization signal | ||||
Sequence: KKSSTRKDKEESKKKR | ||||||
Compositional bias | 485-506 | Basic and acidic residues | ||||
Sequence: KSSTRKDKEESKKKRFSSESKN | ||||||
Compositional bias | 537-551 | Polar residues | ||||
Sequence: ESPVYSNSSVRNELP | ||||||
Region | 537-587 | Disordered | ||||
Sequence: ESPVYSNSSVRNELPMHHNSSRKSTKKTNQSSKNIRKKTIPLKRQKTATKG | ||||||
Compositional bias | 557-580 | Basic residues | ||||
Sequence: SRKSTKKTNQSSKNIRKKTIPLKR | ||||||
Motif | 558-574 | Nuclear localization signal | ||||
Sequence: RKSTKKTNQSSKNIRKK | ||||||
Region | 632-717 | Disordered | ||||
Sequence: DCSRSTRSSKNEDNIMTAQNVPLKPQTSGYTCNIPTESNLDSGEHKTSVLEESGPSRLNNNYLMSGKNDVDDEEVHGSSDDSKQSK | ||||||
Compositional bias | 640-674 | Polar residues | ||||
Sequence: SKNEDNIMTAQNVPLKPQTSGYTCNIPTESNLDSG | ||||||
Compositional bias | 683-697 | Polar residues | ||||
Sequence: ESGPSRLNNNYLMSG | ||||||
Compositional bias | 698-717 | Basic and acidic residues | ||||
Sequence: KNDVDDEEVHGSSDDSKQSK | ||||||
Region | 737-759 | MIF2 homology domain II | ||||
Sequence: VRRTKRTRLKPLEYWRGERIDYQ | ||||||
Motif | 780-798 | Nuclear localization signal | ||||
Sequence: KRKAKENIGKVNKKSNKKR | ||||||
Region | 890-943 | MIF2 homology domain III | ||||
Sequence: LVFYVNFGDLLCTLHETPYILSTGDSFYVPSGNYYNIKNLRNEESVLLFTQIKR |
Domain
The MIF2 homology domain II targets centromeres and binds the alpha satellite DNA in vivo. The MIF2 homology domain III can induce CENPC dimerization/oligomerization.
Sequence similarities
Belongs to the CENP-C/MIF2 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q03188-1
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.
- Name1
- Length943
- Mass (Da)106,834
- Last updated2010-05-18 v2
- Checksum2AA5AF82BA88C809
Q03188-2
- Name2
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 70-85 | Polar residues | ||||
Sequence: CIQSPSKECQKSHPKS | ||||||
Sequence conflict | 179 | in Ref. 1; AAA51974 | ||||
Sequence: Q → K | ||||||
Compositional bias | 358-372 | Basic and acidic residues | ||||
Sequence: LANDKHSHKPHPVET | ||||||
Compositional bias | 424-472 | Basic and acidic residues | ||||
Sequence: KFMAKPAEEQLDVGQSKDENIHTSHITQDEFQRNSDRNMEEHEEMGNDC | ||||||
Compositional bias | 485-506 | Basic and acidic residues | ||||
Sequence: KSSTRKDKEESKKKRFSSESKN | ||||||
Compositional bias | 537-551 | Polar residues | ||||
Sequence: ESPVYSNSSVRNELP | ||||||
Alternative sequence | VSP_057280 | 539-542 | in isoform 2 | |||
Sequence: PVYS → CLKC | ||||||
Alternative sequence | VSP_057281 | 543-943 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 557-580 | Basic residues | ||||
Sequence: SRKSTKKTNQSSKNIRKKTIPLKR | ||||||
Compositional bias | 640-674 | Polar residues | ||||
Sequence: SKNEDNIMTAQNVPLKPQTSGYTCNIPTESNLDSG | ||||||
Compositional bias | 683-697 | Polar residues | ||||
Sequence: ESGPSRLNNNYLMSG | ||||||
Compositional bias | 698-717 | Basic and acidic residues | ||||
Sequence: KNDVDDEEVHGSSDDSKQSK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M95724 EMBL· GenBank· DDBJ | AAA51974.1 EMBL· GenBank· DDBJ | mRNA | ||
AC104806 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC109356 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471057 EMBL· GenBank· DDBJ | EAX05545.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC030695 EMBL· GenBank· DDBJ | AAH30695.1 EMBL· GenBank· DDBJ | mRNA | ||
BC041117 EMBL· GenBank· DDBJ | AAH41117.1 EMBL· GenBank· DDBJ | mRNA | ||
AF151723 EMBL· GenBank· DDBJ | AAF73191.1 EMBL· GenBank· DDBJ | Genomic DNA |