UniProtKB - Q99661 (KIF2C_HUMAN)
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- BLAST>sp|Q99661|KIF2C_HUMAN Kinesin-like protein KIF2C OS=Homo sapiens OX=9606 GN=KIF2C PE=1 SV=2 MAMDSSLQARLFPGLAIKIQRSNGLIHSANVRTVNLEKSCVSVEWAEGGATKGKEIDFDD VAAINPELLQLLPLHPKDNLPLQENVTIQKQKRRSVNSKIPAPKESLRSRSTRMSTVSEL RITAQENDMEVELPAAANSRKQFSVPPAPTRPSCPAVAEIPLRMVSEEMEEQVHSIRGSS SANPVNSVRRKSCLVKEVEKMKNKREEKKAQNSEMRMKRAQEYDSSFPNWEFARMIKEFR ATLECHPLTMTDPIEEHRICVCVRKRPLNKQELAKKEIDVISIPSKCLLLVHEPKLKVDL TKYLENQAFCFDFAFDETASNEVVYRFTARPLVQTIFEGGKATCFAYGQTGSGKTHTMGG DLSGKAQNASKGIYAMASRDVFLLKNQPCYRKLGLEVYVTFFEIYNGKLFDLLNKKAKLR VLEDGKQQVQVVGLQEHLVNSADDVIKMIDMGSACRTSGQTFANSNSSRSHACFQIILRA KGRMHGKFSLVDLAGNERGADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHTPFR ESKLTQVLRDSFIGENSRTCMIATISPGISSCEYTLNTLRYADRVKELSPHSGPSGEQLI QMETEEMEACSNGALIPGNLSKEEEELSSQMSSFNEAMTQIRELEEKAMEELKEIIQQGP DWLELSEMTEQPDYDLETFVNKAESALAQQAKHFSALRDVIKALRLAMQLEEQASRQISS KKRPQ
- Align
Kinesin-like protein KIF2C
KIF2C
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>Select a section on the left to see content.
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.16"Genome stability is ensured by temporal control of kinetochore-microtubule dynamics."
Bakhoum S.F., Thompson S.L., Manning A.L., Compton D.A.
Nat. Cell Biol. 11:27-35(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.21"A complex of Kif18b and MCAK promotes microtubule depolymerization and is negatively regulated by Aurora kinases."
Tanenbaum M.E., Macurek L., van der Vaart B., Galli M., Akhmanova A., Medema R.H.
Curr. Biol. 21:1356-1365(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH KIF18B, SUBCELLULAR LOCATION. - Ref.23"Lateral to end-on conversion of chromosome-microtubule attachment requires kinesins CENP-E and MCAK."
Shrestha R.L., Draviam V.M.
Curr. Biol. 23:1514-1526(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 264 | ATPBy similarity | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 348 – 355 | ATP | 8 |
<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 - Molecular functioni
- ATPase activity Source: GO_Central
- ATP binding Source: UniProtKB-KW
- centromeric DNA binding Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- microtubule motor activity Source: GO_Central
- microtubule plus-end binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<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
- antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
- attachment of mitotic spindle microtubules to kinetochore Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- cell division Source: UniProtKB-KW
- cell proliferation Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- establishment or maintenance of microtubule cytoskeleton polarity Source: HGNC <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- metaphase plate congression Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- microtubule-based movement Source: GO_Central
- microtubule depolymerization Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- mitotic cell cycle Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- mitotic metaphase plate congression Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of chromosome segregation Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- retrograde vesicle-mediated transport, Golgi to ER Source: Reactome
<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 process | Cell cycle, Cell division, Chromosome partition, Mitosis |
| Ligand | ATP-binding, Nucleotide-binding |
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-2132295 MHC class II antigen presentation R-HSA-2467813 Separation of Sister Chromatids R-HSA-2500257 Resolution of Sister Chromatid Cohesion R-HSA-5663220 RHO GTPases Activate Formins R-HSA-6811434 COPI-dependent Golgi-to-ER retrograde traffic R-HSA-68877 Mitotic Prometaphase R-HSA-983189 Kinesins |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q99661 |
<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: Kinesin-like protein KIF2CAlternative name(s): Kinesin-like protein 6 Mitotic centromere-associated kinesin Short name: MCAK |
| <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:KIF2C Synonyms:KNSL6 |
| <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>Organismi | Homo 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 identifieri | 9606 [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 lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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 |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000142945.12 |
Human Gene Nomenclature Database More...HGNCi | HGNC:6393 KIF2C |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 604538 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q99661 |
<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
Cytoskeleton
- cytoskeleton 3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"An EB1-binding motif acts as a microtubule tip localization signal."
Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S., Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A., Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.
Cell 138:366-376(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MAPRE1, SUBCELLULAR LOCATION, DOMAIN MICROTUBULE TIP LOCALIZATION SIGNAL, MUTAGENESIS OF SER-95; 100-ILE-PRO-101; SER-109 AND SER-111. - Ref.21"A complex of Kif18b and MCAK promotes microtubule depolymerization and is negatively regulated by Aurora kinases."
Tanenbaum M.E., Macurek L., van der Vaart B., Galli M., Akhmanova A., Medema R.H.
Curr. Biol. 21:1356-1365(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH KIF18B, SUBCELLULAR LOCATION. - Ref.23"Lateral to end-on conversion of chromosome-microtubule attachment requires kinesins CENP-E and MCAK."
Shrestha R.L., Draviam V.M.
Curr. Biol. 23:1514-1526(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
- cytoskeleton 3 Publications
Nucleus
- Nucleus By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- Nucleus By similarity
Other locations
- centromere 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"Aurora B regulates MCAK at the mitotic centromere."
Andrews P.D., Ovechkina Y., Morrice N., Wagenbach M., Duncan K., Wordeman L., Swedlow J.R.
Dev. Cell 6:253-268(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT SER-95 BY AURKB, SUBCELLULAR LOCATION. - Ref.11"Tripin/hSgo2 recruits MCAK to the inner centromere to correct defective kinetochore attachments."
Huang H., Feng J., Famulski J., Rattner J.B., Liu S.T., Kao G.D., Muschel R., Chan G.K., Yen T.J.
J. Cell Biol. 177:413-424(2007) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION.
- kinetochore 3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"Aurora B regulates MCAK at the mitotic centromere."
Andrews P.D., Ovechkina Y., Morrice N., Wagenbach M., Duncan K., Wordeman L., Swedlow J.R.
Dev. Cell 6:253-268(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT SER-95 BY AURKB, SUBCELLULAR LOCATION. - Ref.11"Tripin/hSgo2 recruits MCAK to the inner centromere to correct defective kinetochore attachments."
Huang H., Feng J., Famulski J., Rattner J.B., Liu S.T., Kao G.D., Muschel R., Chan G.K., Yen T.J.
J. Cell Biol. 177:413-424(2007) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.23"Lateral to end-on conversion of chromosome-microtubule attachment requires kinesins CENP-E and MCAK."
Shrestha R.L., Draviam V.M.
Curr. Biol. 23:1514-1526(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
Note: Associates with the microtubule network at the growing distal tip (the plus-end) of microtubules, probably through interaction with MTUS2/TIP150 and MAPRE1 (By similarity). Association with microtubule plus ends is also mediated by interaction with KIF18B. Centromeric localization requires the presence of BUB1 and SGO2.By similarity- centromere 2 Publications
- Ref.11"Tripin/hSgo2 recruits MCAK to the inner centromere to correct defective kinetochore attachments."
Huang H., Feng J., Famulski J., Rattner J.B., Liu S.T., Kao G.D., Muschel R., Chan G.K., Yen T.J.
J. Cell Biol. 177:413-424(2007) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.21"A complex of Kif18b and MCAK promotes microtubule depolymerization and is negatively regulated by Aurora kinases."
Tanenbaum M.E., Macurek L., van der Vaart B., Galli M., Akhmanova A., Medema R.H.
Curr. Biol. 21:1356-1365(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH KIF18B, SUBCELLULAR LOCATION.
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Cytoskeleton
- kinesin complex Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- microtubule cytoskeleton Source: LIFEdb
- microtubule plus-end Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Cytosol
- cytosol Source: Reactome
Nucleus
- nucleus Source: UniProtKB-SubCell
Other locations
- chromosome, centromeric region Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- condensed chromosome kinetochore Source: UniProtKB-SubCell
- kinetochore Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- membrane Source: UniProtKBInferred from high throughput direct assayi
<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>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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Mutagenesisi | 95 | S → E: Alters interaction with MAPRE1 and association with microtubule growing ends; when associated with E-109 and E-111. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 100 – 101 | IP → NN: Loss of interaction with MAPRE1 and association with microtubule growing ends. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 2 | |
| <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>Mutagenesisi | 109 | S → E: Alters interaction with MAPRE1 and association with microtubule growing ends; when associated with E-95 and E-111. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 111 | S → E: Alters interaction with MAPRE1 and association with microtubule growing ends; when associated with E-95 and E-109. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 11004 |
Open Targets More...OpenTargetsi | ENSG00000142945 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA30182 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL5967 |
Drug and drug target database More...DrugBanki | DB04395 Phosphoaminophosphonic Acid-Adenylate Ester |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | KIF2C |
Domain mapping of disease mutations (DMDM) More...DMDMi | 20141607 |
<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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | RemovedCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| |||
| <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_0000125418 | 2 – 725 | Kinesin-like protein KIF2CAdd BLAST | 724 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 residuei | 2 | N-acetylalanineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 6 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 22 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 95 | Phosphoserine; by AURKB1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 residuei | 106 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 109 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <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 residuei | 111 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <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 residuei | 115 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 166 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 175 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 187 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 192 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <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 residuei | 519 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 621 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 633 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"Aurora B regulates MCAK at the mitotic centromere."
Andrews P.D., Ovechkina Y., Morrice N., Wagenbach M., Duncan K., Wordeman L., Swedlow J.R.
Dev. Cell 6:253-268(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT SER-95 BY AURKB, SUBCELLULAR LOCATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.18"Development and validation of a method for profiling post-translational modification activities using protein microarrays."
Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B., Spruck C.
PLoS ONE 5:E11332-E11332(2010) [PubMed] [Europe PMC] [Abstract]Cited for: UBIQUITINATION.
<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>Keywords - PTMi
Acetylation, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q99661 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q99661 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q99661 |
PeptideAtlas More...PeptideAtlasi | Q99661 |
PRoteomics IDEntifications database More...PRIDEi | Q99661 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 78382 78383 [Q99661-2] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q99661 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q99661 |
<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 a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Cloning and expression of human mitotic centromere-associated kinesin gene."
Kim I.-G., Jun D.Y., Sohn U., Kim Y.H.
Biochim. Biophys. Acta 1359:181-186(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-449, TISSUE SPECIFICITY. - Ref.2"Expression of a novel HsMCAK mRNA splice variant, tsMCAK gene, in human testis."
Cheng L.J., Zhou Z.M., Li J.M., Zhu H., Zhu H., Zhou Y.D., Wang L.R., Lin M., Sha J.H.
Life Sci. 71:2741-2757(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-449, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.2"Expression of a novel HsMCAK mRNA splice variant, tsMCAK gene, in human testis."
Cheng L.J., Zhou Z.M., Li J.M., Zhu H., Zhu H., Zhou Y.D., Wang L.R., Lin M., Sha J.H.
Life Sci. 71:2741-2757(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-449, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000142945 |
CleanEx database of gene expression profiles More...CleanExi | HS_KIF2C |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q99661 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q99661 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA006219 |
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Human CENP-H multimers colocalize with CENP-A and CENP-C at active centromere-kinetochore complexes."
Sugata N., Li S., Earnshaw W.C., Yen T.J., Yoda K., Masumoto H., Munekata E., Warburton P.E., Todokoro K.
Hum. Mol. Genet. 9:2919-2926(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CENPH. - Ref.14"An EB1-binding motif acts as a microtubule tip localization signal."
Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S., Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A., Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.
Cell 138:366-376(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MAPRE1, SUBCELLULAR LOCATION, DOMAIN MICROTUBULE TIP LOCALIZATION SIGNAL, MUTAGENESIS OF SER-95; 100-ILE-PRO-101; SER-109 AND SER-111. - Ref.15"TIP150 interacts with and targets MCAK at the microtubule plus ends."
Jiang K., Wang J., Liu J., Ward T., Wordeman L., Davidson A., Wang F., Yao X.
EMBO Rep. 10:857-865(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MTUS2 AND MAPRE1. - Ref.21"A complex of Kif18b and MCAK promotes microtubule depolymerization and is negatively regulated by Aurora kinases."
Tanenbaum M.E., Macurek L., van der Vaart B., Galli M., Akhmanova A., Medema R.H.
Curr. Biol. 21:1356-1365(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH KIF18B, SUBCELLULAR LOCATION. - Ref.25"Crystal structure of the KIF2C motor domain."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bankCited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 225-593 IN COMPLEX WITH ADP.
<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
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| MAPRE1 | Q15691 | 8 | EBI-1642317,EBI-1004115 | |
| MTUS2 | Q5JR59 | 4 | EBI-1642317,EBI-742948 |
<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 - Molecular functioni
- microtubule plus-end binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 116195, 83 interactors |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | Q99661 |
Protein interaction database and analysis system More...IntActi | Q99661, 47 interactors |
Molecular INTeraction database More...MINTi | Q99661 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000361298 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q99661 |
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 230 – 242 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 250 – 252 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 258 – 265 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 270 – 274 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 285 – 296 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 297 – 299 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 302 – 310 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 312 – 315 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 321 – 327 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 330 – 337 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 341 – 348 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 354 – 358 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 373 – 385 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 388 – 391 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 392 – 394 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 396 – 405 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 408 – 411 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 412 – 416 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 420 – 423 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 425 – 427 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 429 – 432 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 437 – 441 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 442 – 455 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 467 – 469 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 470 – 492 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 23 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 499 – 502 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 507 – 509 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 514 – 531 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 539 – 541 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 543 – 547 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 549 – 552 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 557 – 565 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 569 – 571 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 572 – 585 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q99661 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q99661 |
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 | Q99661 |
<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
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 258 – 588 | Kinesin motorPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 331 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Regioni | 2 – 254 | GlobularSequence analysisAdd BLAST | 253 | |
| <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>Regioni | 207 – 238 | Negative regulator of microtubule-bindingBy similarityAdd BLAST | 32 |
Coiled coil
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili | 618 – 658 | Sequence analysisAdd BLAST | 41 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Motifi | 98 – 101 | Microtubule tip localization signal | 4 | |
| <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>Motifi | 415 – 418 | Nuclear localization signalSequence analysis | 4 |
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"An EB1-binding motif acts as a microtubule tip localization signal."
Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S., Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A., Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.
Cell 138:366-376(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MAPRE1, SUBCELLULAR LOCATION, DOMAIN MICROTUBULE TIP LOCALIZATION SIGNAL, MUTAGENESIS OF SER-95; 100-ILE-PRO-101; SER-109 AND SER-111.
<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
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
<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>Keywords - Domaini
Coiled coilPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0246 Eukaryota COG5059 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000148953 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG003875 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q99661 |
KEGG Orthology (KO) More...KOi | K10393 |
Identification of Orthologs from Complete Genome Data More...OMAi | FAFDETA |
Database of Orthologous Groups More...OrthoDBi | EOG091G06V3 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q99661 |
TreeFam database of animal gene trees More...TreeFami | TF105222 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.850.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR027640 Kinesin-like_fam IPR019821 Kinesin_motor_CS IPR001752 Kinesin_motor_dom IPR036961 Kinesin_motor_dom_sf IPR027417 P-loop_NTPase |
The PANTHER Classification System More...PANTHERi | PTHR24115 PTHR24115, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00225 Kinesin, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00380 KINESINHEAVY |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00129 KISc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF52540 SSF52540, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00411 KINESIN_MOTOR_1, 1 hit PS50067 KINESIN_MOTOR_2, 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.
<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
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 basketAdded 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.
10 20 30 40 50
MAMDSSLQAR LFPGLAIKIQ RSNGLIHSAN VRTVNLEKSC VSVEWAEGGA
60 70 80 90 100
TKGKEIDFDD VAAINPELLQ LLPLHPKDNL PLQENVTIQK QKRRSVNSKI
110 120 130 140 150
PAPKESLRSR STRMSTVSEL RITAQENDME VELPAAANSR KQFSVPPAPT
160 170 180 190 200
RPSCPAVAEI PLRMVSEEME EQVHSIRGSS SANPVNSVRR KSCLVKEVEK
210 220 230 240 250
MKNKREEKKA QNSEMRMKRA QEYDSSFPNW EFARMIKEFR ATLECHPLTM
260 270 280 290 300
TDPIEEHRIC VCVRKRPLNK QELAKKEIDV ISIPSKCLLL VHEPKLKVDL
310 320 330 340 350
TKYLENQAFC FDFAFDETAS NEVVYRFTAR PLVQTIFEGG KATCFAYGQT
360 370 380 390 400
GSGKTHTMGG DLSGKAQNAS KGIYAMASRD VFLLKNQPCY RKLGLEVYVT
410 420 430 440 450
FFEIYNGKLF DLLNKKAKLR VLEDGKQQVQ VVGLQEHLVN SADDVIKMID
460 470 480 490 500
MGSACRTSGQ TFANSNSSRS HACFQIILRA KGRMHGKFSL VDLAGNERGA
510 520 530 540 550
DTSSADRQTR MEGAEINKSL LALKECIRAL GQNKAHTPFR ESKLTQVLRD
560 570 580 590 600
SFIGENSRTC MIATISPGIS SCEYTLNTLR YADRVKELSP HSGPSGEQLI
610 620 630 640 650
QMETEEMEAC SNGALIPGNL SKEEEELSSQ MSSFNEAMTQ IRELEEKAME
660 670 680 690 700
ELKEIIQQGP DWLELSEMTE QPDYDLETFV NKAESALAQQ AKHFSALRDV
710 720
IKALRLAMQL EEQASRQISS KKRPQ
The sequence of this isoform differs from the canonical sequence as follows:
1-55: MAMDSSLQARLFPGLAIKIQRSNGLIHSANVRTVNLEKSCVSVEWAEGGATKGKE → M
10 20 30 40 50
MIDFDDVAAI NPELLQLLPL HPKDNLPLQE NVTIQKQKRR SVNSKIPAPK
60 70 80 90 100
ESLRSRSTRM STVSELRITA QENDMEVELP AAANSRKQFS VPPAPTRPSC
110 120 130 140 150
PAVAEIPLRM VSEEMEEQVH SIRGSSSANP VNSVRRKSCL VKEVEKMKNK
160 170 180 190 200
REEKKAQNSE MRMKRAQEYD SSFPNWEFAR MIKEFRATLE CHPLTMTDPI
210 220 230 240 250
EEHRICVCVR KRPLNKQELA KKEIDVISIP SKCLLLVHEP KLKVDLTKYL
260 270 280 290 300
ENQAFCFDFA FDETASNEVV YRFTARPLVQ TIFEGGKATC FAYGQTGSGK
310 320 330 340 350
THTMGGDLSG KAQNASKGIY AMASRDVFLL KNQPCYRKLG LEVYVTFFEI
360 370 380 390 400
YNGKLFDLLN KKAKLRVLED GKQQVQVVGL QEHLVNSADD VIKMIDMGSA
410 420 430 440 450
CRTSGQTFAN SNSSRSHACF QIILRAKGRM HGKFSLVDLA GNERGADTSS
460 470 480 490 500
ADRQTRMEGA EINKSLLALK ECIRALGQNK AHTPFRESKL TQVLRDSFIG
510 520 530 540 550
ENSRTCMIAT ISPGISSCEY TLNTLRYADR VKELSPHSGP SGEQLIQMET
560 570 580 590 600
EEMEACSNGA LIPGNLSKEE EELSSQMSSF NEAMTQIREL EEKAMEELKE
610 620 630 640 650
IIQQGPDWLE LSEMTEQPDY DLETFVNKAE SALAQQAKHF SALRDVIKAL
660 670
RLAMQLEEQA SRQISSKKRP Q
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 conflicti | 698 | R → P in AAH08764 (PubMed:15489334).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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_049683 | 449 | I → L3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_002866 | 1 – 55 | MAMDS…TKGKE → M in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 55 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | U63743 mRNA Translation: AAC27660.1 AY026505 mRNA Translation: AAK20168.1 BT006759 mRNA Translation: AAP35405.1 CR450302 mRNA Translation: CAG29298.1 AB264115 mRNA Translation: BAG50306.1 AL592166 Genomic DNA No translation available. CH471059 Genomic DNA Translation: EAX07025.1 BC008764 mRNA Translation: AAH08764.1 BC014924 mRNA Translation: AAH14924.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS512.1 [Q99661-1] CCDS72774.1 [Q99661-2] |
NCBI Reference Sequences More...RefSeqi | NP_001284584.1, NM_001297655.1 NP_001284585.1, NM_001297656.1 [Q99661-2] NP_001284586.1, NM_001297657.1 NP_006836.2, NM_006845.3 [Q99661-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.720061 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000372217; ENSP00000361291; ENSG00000142945 [Q99661-2] ENST00000372224; ENSP00000361298; ENSG00000142945 [Q99661-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 11004 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:11004 |
UCSC genome browser More...UCSCi | uc001cmg.5 human [Q99661-1] |
<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>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
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q99661 | Kinesin-like protein | 725 | |||
| Kinesin-like protein | 612 | ||||
| Kinesin-like protein (Fragment) | 468 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q99661 | Kinesin-like protein | 725 | |||
| Kinesin-like protein | 763 | ||||
| Kinesin-like protein | 729 | ||||
| Kinesin-like protein | 729 | ||||
| Kinesin-like protein | 729 | ||||
| +93 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q99661 | Kinesin-like protein | 725 | |||
| Kinesin-like protein | 763 | ||||
| Kinesin-like protein | 729 | ||||
| Kinesin-like protein | 729 | ||||
| Kinesin-like protein | 729 | ||||
| +222 | |||||
<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: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | U63743 mRNA Translation: AAC27660.1 AY026505 mRNA Translation: AAK20168.1 BT006759 mRNA Translation: AAP35405.1 CR450302 mRNA Translation: CAG29298.1 AB264115 mRNA Translation: BAG50306.1 AL592166 Genomic DNA No translation available. CH471059 Genomic DNA Translation: EAX07025.1 BC008764 mRNA Translation: AAH08764.1 BC014924 mRNA Translation: AAH14924.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS512.1 [Q99661-1] CCDS72774.1 [Q99661-2] |
NCBI Reference Sequences More...RefSeqi | NP_001284584.1, NM_001297655.1 NP_001284585.1, NM_001297656.1 [Q99661-2] NP_001284586.1, NM_001297657.1 NP_006836.2, NM_006845.3 [Q99661-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.720061 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2HEH | X-ray | 2.15 | A | 225-593 | [»] | |
| 4UBF | X-ray | 3.00 | A/B/C/D | 225-593 | [»] | |
| P | 709-720 | [»] | ||||
| 4Y05 | X-ray | 2.59 | A | 216-599 | [»] | |
| 5MIO | X-ray | 3.19 | C | 216-598 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q99661 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q99661 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 116195, 83 interactors |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | Q99661 |
Protein interaction database and analysis system More...IntActi | Q99661, 47 interactors |
Molecular INTeraction database More...MINTi | Q99661 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000361298 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q99661 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL5967 |
Drug and drug target database More...DrugBanki | DB04395 Phosphoaminophosphonic Acid-Adenylate Ester |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q99661 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q99661 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | KIF2C |
Domain mapping of disease mutations (DMDM) More...DMDMi | 20141607 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q99661 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q99661 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q99661 |
PeptideAtlas More...PeptideAtlasi | Q99661 |
PRoteomics IDEntifications database More...PRIDEi | Q99661 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 78382 78383 [Q99661-2] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 11004 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000372217; ENSP00000361291; ENSG00000142945 [Q99661-2] ENST00000372224; ENSP00000361298; ENSG00000142945 [Q99661-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 11004 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:11004 |
UCSC genome browser More...UCSCi | uc001cmg.5 human [Q99661-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 11004 |
DisGeNET More...DisGeNETi | 11004 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000142945.12 |
GeneCards: human genes, protein and diseases More...GeneCardsi | KIF2C |
Human Gene Nomenclature Database More...HGNCi | HGNC:6393 KIF2C |
Human Protein Atlas More...HPAi | HPA006219 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 604538 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q99661 |
Open Targets More...OpenTargetsi | ENSG00000142945 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA30182 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0246 Eukaryota COG5059 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000148953 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG003875 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q99661 |
KEGG Orthology (KO) More...KOi | K10393 |
Identification of Orthologs from Complete Genome Data More...OMAi | FAFDETA |
Database of Orthologous Groups More...OrthoDBi | EOG091G06V3 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q99661 |
TreeFam database of animal gene trees More...TreeFami | TF105222 |
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-2132295 MHC class II antigen presentation R-HSA-2467813 Separation of Sister Chromatids R-HSA-2500257 Resolution of Sister Chromatid Cohesion R-HSA-5663220 RHO GTPases Activate Formins R-HSA-6811434 COPI-dependent Golgi-to-ER retrograde traffic R-HSA-68877 Mitotic Prometaphase R-HSA-983189 Kinesins |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q99661 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | KIF2C human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q99661 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | KIF2C |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 11004 |
Protein Ontology More...PROi | PR:Q99661 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000142945 |
CleanEx database of gene expression profiles More...CleanExi | HS_KIF2C |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q99661 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q99661 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.850.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR027640 Kinesin-like_fam IPR019821 Kinesin_motor_CS IPR001752 Kinesin_motor_dom IPR036961 Kinesin_motor_dom_sf IPR027417 P-loop_NTPase |
The PANTHER Classification System More...PANTHERi | PTHR24115 PTHR24115, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00225 Kinesin, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00380 KINESINHEAVY |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00129 KISc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF52540 SSF52540, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00411 KINESIN_MOTOR_1, 1 hit PS50067 KINESIN_MOTOR_2, 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 namei | KIF2C_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>Accessioni | Q99661Primary (citable) accession number: Q99661 Secondary accession number(s): B3ITR9 , Q5JR88, Q6ICU1, Q96C18, Q96HB8, Q9BWV8 | |
| <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 historyi | Integrated into UniProtKB/Swiss-Prot: | January 11, 2001 |
| Last sequence update: | January 23, 2002 | |
| Last modified: | July 18, 2018 | |
| This is version 187 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 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. | |
<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
<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>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
