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UniProtKB - Q15058 (KIF14_HUMAN)

Protein

Kinesin-like protein KIF14

Gene

KIF14

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

Annotation score:5 out of 5

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

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

Microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity (By similarity). Plays a role in many processes like cell division, cytokinesis and also in cell proliferation and apoptosis (PubMed:24784001, PubMed:16648480). During cytokinesis, targets to central spindle and midbody through its interaction with PRC1 and CIT respectively (PubMed:16431929). Regulates cell growth through regulation of cell cycle progression and cytokinesis (PubMed:24854087). During cell cycle progression acts through SCF-dependent proteasomal ubiquitin-dependent protein catabolic process which controls CDKN1B degradation, resulting in positive regulation of cyclins, including CCNE1, CCND1 and CCNB1 (PubMed:24854087). During late neurogenesis, regulates the cerebellar, cerebral cortex and olfactory bulb development through regulation of apoptosis, cell proliferation and cell division (By similarity). Also is required for chromosome congression and alignment during mitotic cell cycle process (PubMed:15843429). Regulates cell spreading, focal adhesion dynamics, and cell migration through its interaction with RADIL resulting in regulation of RAP1A-mediated inside-out integrin activation by tethering RADIL on microtubules (PubMed:23209302).By similarity6 Publications

Miscellaneous

It is resistant to docetaxel anhydrous.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi447 – 454ATPPROSITE-ProRule annotation8

<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: UniProtKB
  • ATP binding Source: UniProtKB
  • ATP-dependent microtubule motor activity, plus-end-directed Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • microtubule motor activity Source: GO_Central
  • PDZ domain binding Source: MGI
  • protein kinase binding Source: UniProtKB
  • tubulin binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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

Molecular functionMotor protein
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-5625900 RHO GTPases activate CIT

<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 KIF14Curated
<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:KIF14Imported
Synonyms:KIAA0042Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000118193.11

Human Gene Nomenclature Database

More...HGNCi		HGNC:19181 KIF14

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		611279 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q15058

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

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, 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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Meckel syndrome 12 (MKS12)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Meckel syndrome, a disorder characterized by a combination of renal cysts and variably associated features including developmental anomalies of the central nervous system (typically encephalocele), hepatic ductal dysplasia and cysts, and polydactyly.
See also OMIM:616258
Microcephaly 20, primary, autosomal recessive (MCPH20)2 Publications
The disease is caused by mutations affecting the gene represented in this entry. The disease-causing variant NM_014875.2:c.263T>A, which produces a premature truncation of the protein at Leu-88 (p.Leu88Ter), may also partly result in the deletion of 372 bp of exon 2 of KIF14 by activation of a cryptic splice site. This in-frame deletion predicts a protein that lacks 124 aa (p.Gly58-Leu181del). The disease-causing mutation NM_014875.2:c.3662G>T, resulting in the missence variant p.Gly1221Val, may also induce the skipping of exon 24, resulting in a protein that misses 76 aa (p.Gly1221_ Lys1296delinsVal).1 Publication
Disease descriptionA form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age, sex and ethnically matched mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. MCPH20 features include mild to moderate intellectual disability, autistic features, poor speech. Disease severity is highly variable.
See also OMIM:617914
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_08062388 – 1648Missing in MCPH20; drastically decreased expression at the mRNA level; loss of localization at the midbody during cytokinesis and consequently loss of CIT/CRIK recruitment to the midbody. 1 PublicationAdd BLAST1561
Natural variantiVAR_080624459G → R in MCPH20; unknown pathological significance. 1 Publication1
Natural variantiVAR_080625827Missing in MCPH20; unknown pathological significance. 1 Publication1
Natural variantiVAR_080626841S → F in MCPH20; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs139385693Ensembl.1
Natural variantiVAR_080627849H → D in MCPH20; Decreased expression at the mRNA level and loss of localization at the midbody during cytokinesis and consequently loss of CIT/CRIK recruitment to the midbody, when analyzed in primary fibroblasts from a patient who is a compound heterozygous with variant V-1221. 1 Publication1
Natural variantiVAR_0806281221G → V in MCPH20; Decreased expression at the mRNA level and loss of localization at the midbody during cytokinesis and consequently loss of CIT/CRIK recruitment to the midbody, when analyzed in primary fibroblasts from a patient who is a compound heterozygous with variant D-849. 1 Publication1

Keywords - Diseasei

Ciliopathy, Disease mutation, Meckel syndrome, Primary microcephaly

Organism-specific databases

DisGeNET

More...DisGeNETi		9928

MalaCards human disease database

More...MalaCardsi		KIF14
MIMi616258 phenotype
617914 phenotype

Open Targets

More...OpenTargetsi		ENSG00000118193

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		2512 Autosomal recessive primary microcephaly
439897 Lethal fetal cerebrorenogenitourinary agenesis/hypoplasia syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA38820

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5576

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		KIF14

Domain mapping of disease mutations (DMDM)

More...DMDMi		23396633

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001254491 – 1648Kinesin-like protein KIF14Add BLAST1648

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei12PhosphoserineCombined sources1
Modified residuei272PhosphoserineCombined sources1
Modified residuei277PhosphothreonineCombined sources1
Modified residuei346PhosphoserineCombined sources1
Modified residuei915PhosphothreonineCombined sources1
Modified residuei937PhosphoserineCombined sources1
Modified residuei1292PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q15058

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q15058

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q15058

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

More...PaxDbi		Q15058

PeptideAtlas

More...PeptideAtlasi		Q15058

PRoteomics IDEntifications database

More...PRIDEi		Q15058

ProteomicsDB human proteome resource

More...ProteomicsDBi		60413

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q15058

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

More...PhosphoSitePlusi		Q15058

<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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated in cells progressing through G2/M phase.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000118193 Expressed in 107 organ(s), highest expression level in bone marrow

CleanEx database of gene expression profiles

More...CleanExi		HS_KIF14

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q15058 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA038061
HPA058220

<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

Directly interacts with PRC1 within a complex also containing KIF4A, KIF20A and KIF23; targets to the central spindle. Directly interacts with CIT depending on the activation state of the kinase (stronger interaction with the kinase-dead form); targets to the midbody. Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation. Interacts with AKT1; the interaction is detected in the plasma membrane upon INS stimulation and promotes AKT1 phosphorylation. Interacts with SVIL; at midbody during cytokinesis. Interacts with RADIL (via PDZ domain); recruits RADIL to the microtubule network restricting RADIL from interaction with activated RAP1A (PubMed:23209302).5 Publications

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

WithEntry#Exp.IntActNotes
SVILO463853EBI-1045252,EBI-6995105From Bos taurus.

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		115256, 93 interactors

Protein interaction database and analysis system

More...IntActi		Q15058, 41 interactors

Molecular INTeraction database

More...MINTi		Q15058

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000356319

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q15058

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q15058

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

More...SMRi		Q15058

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Domaini358 – 701Kinesin motorPROSITE-ProRule annotationAdd BLAST344
Domaini825 – 891FHAAdd BLAST67

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 356Required for PRC1-bindingAdd BLAST356
Regioni356 – 737Required for microtubule-binding with high affinityBy similarityAdd BLAST382
Regioni901 – 1648Required for CIT-bindingAdd BLAST748

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 coili705 – 791Sequence analysisAdd BLAST87
Coiled coili922 – 1079Sequence analysisAdd BLAST158
Coiled coili1332 – 1348Sequence analysisAdd BLAST17
Coiled coili1468 – 1500Sequence analysisAdd BLAST33

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

The kinesin motor domain binds to microtubules with high affinity and has a robust ATPase activity but a very slow motility. The kinesin motor domain protects microtubules from cold depolymerization. Binds to each tubulin heterodimer resulting in a microtubule complexes. Binds at the tubulin intradimer interface, at the crest of the protofilament, and orients slightly toward the next protofilament.By similarity

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

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0245 Eukaryota
COG5059 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156834

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000113224

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG052249

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q15058

KEGG Orthology (KO)

More...KOi		K17915

Identification of Orthologs from Complete Genome Data

More...OMAi		QEVSYHL

Database of Orthologous Groups

More...OrthoDBi		76316at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q15058

TreeFam database of animal gene trees

More...TreeFami		TF105221

Family and domain databases

Conserved Domains Database

More...CDDi		cd00060 FHA, 1 hit

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
IPR000253 FHA_dom
IPR027640 Kinesin-like_fam
IPR032405 Kinesin_assoc
IPR019821 Kinesin_motor_CS
IPR001752 Kinesin_motor_dom
IPR036961 Kinesin_motor_dom_sf
IPR027417 P-loop_NTPase
IPR008984 SMAD_FHA_dom_sf

The PANTHER Classification System

More...PANTHERi		PTHR24115 PTHR24115, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00498 FHA, 1 hit
PF00225 Kinesin, 1 hit
PF16183 Kinesin_assoc, 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
SM00240 FHA, 1 hit
SM00129 KISc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF49879 SSF49879, 1 hit
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>Sequencei

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

Q15058-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLHSTHNRN NSGDILDIPS SQNSSSLNAL THSSRLKLHL KSDMSECEND 
        60         70         80         90        100
DPLLRSAGKV RDINRTYVIS ASRKTADMPL TPNPVGRLAL QRRTTRNKES 
       110        120        130        140        150
SLLVSELEDT TEKTAETRLT LQRRAKTDSA EKWKTAEIDS VKMTLNVGGE 
       160        170        180        190        200
TENNGVSKES RTNVRIVNNA KNSFVASSVP LDEDPQVIEM MADKKYKETF 
       210        220        230        240        250
SAPSRANENV ALKYSSNRPP IASLSQTEVV RSGHLTTKPT QSKLDIKVLG 
       260        270        280        290        300
TGNLYHRSIG KEIAKTSNKF GSLEKRTPTK CTTEHKLTTK CSLPQLKSPA 
       310        320        330        340        350
PSILKNRMSN LQVKQRPKSS FLANKQERSA ENTILPEEET VVQNTSAGKD 
       360        370        380        390        400
PLKVENSQVT VAVRVRPFTK REKIEKASQV VFMSGKEITV EHPDTKQVYN 
       410        420        430        440        450
FIYDVSFWSF DECHPHYASQ TTVYEKLAAP LLERAFEGFN TCLFAYGQTG 
       460        470        480        490        500
SGKSYTMMGF SEEPGIIPRF CEDLFSQVAR KQTQEVSYHI EMSFFEVYNE 
       510        520        530        540        550
KIHDLLVCKD ENGQRKQPLR VREHPVYGPY VEALSMNIVS SYADIQSWLE 
       560        570        580        590        600
LGNKQRATAA TGMNDKSSRS HSVFTLVMTQ TKTEFVEGEE HDHRITSRIN 
       610        620        630        640        650
LIDLAGSERC STAHTNGDRL KEGVSINKSL LTLGKVISAL SEQANQRSVF 
       660        670        680        690        700
IPYRESVLTW LLKESLGGNS KTAMIATISP AASNIEETLS TLRYANQARL 
       710        720        730        740        750
IVNIAKVNED MNAKLIRELK AEIAKLKAAQ RNSRNIDPER YRLCRQEITS 
       760        770        780        790        800
LRMKLHQQER DMAEMQRVWK EKFEQAEKRK LQETKELQKA GIMFQMDNHL 
       810        820        830        840        850
PNLVNLNEDP QLSEMLLYMI KEGTTTVGKY KPNSSHDIQL SGVLIADDHC 
       860        870        880        890        900
TIKNFGGTVS IIPVGEAKTY VNGKHILEIT VLRHGDRVIL GGDHYFRFNH 
       910        920        930        940        950
PVEVQKGKRP SGRDTPISEG PKDFEFAKNE LLMAQRSQLE AEIKEAQLKA 
       960        970        980        990       1000
KEEMMQGIQI AKEMAQQELS SQKAAYESKI KALEAELREE SQRKKMQEIN 
      1010       1020       1030       1040       1050
NQKANHKIEE LEKAKQHLEQ EIYVNKKRLE METLATKQAL EDHSIRHARI 
      1060       1070       1080       1090       1100
LEALETEKQK IAKEVQILQQ NRNNRDKTFT VQTTWSSMKL SMMIQEANAI 
      1110       1120       1130       1140       1150
SSKLKTYYVF GRHDISDKSS SDTSIRVRNL KLGISTFWSL EKFESKLAAM 
      1160       1170       1180       1190       1200
KELYESNGSN RGEDAFCDPE DEWEPDITDA PVSSLSRRRS RSLMKNRRIS 
      1210       1220       1230       1240       1250
GCLHDIQVHP IKNLHSSHSS GLMDKSSTIY SNSAESFLPG ICKELIGSSL 
      1260       1270       1280       1290       1300
DFFGQSYDEE RTIADSLINS FLKIYNGLFA ISKAHEEQDE ESQDNLFSSD 
      1310       1320       1330       1340       1350
RAIQSLTIQT ACAFEQLVVL MKHWLSDLLP CTNIARLEDE LRQEVKKLGG 
      1360       1370       1380       1390       1400
YLQLFLQGCC LDISSMIKEA QKNAIQIVQQ AVKYVGQLAV LKGSKLHFLE 
      1410       1420       1430       1440       1450
NGNNKAASVQ EEFMDAVCDG VGLGMKILLD SGLEKAKELQ HELFRQCTKN 
      1460       1470       1480       1490       1500
EVTKEMKTNA MGLIRSLENI FAESKIKSFR RQVQEENFEY QDFKRMVNRA 
      1510       1520       1530       1540       1550
PEFLKLKHCL EKAIEIIISA LKGCHSDINL LQTCVESIRN LASDFYSDFS 
      1560       1570       1580       1590       1600
VPSTSVGSYE SRVTHIVHQE LESLAKSLLF CFESEESPDL LKPWETYNQN 
      1610       1620       1630       1640 
TKEEHQQSKS SGIDGSKNKG VPKRVYELHG SSPAVSSEEC TPSRIQWV
Length:1,648
Mass (Da):186,492
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iFB1423668A7B79D7
GO

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

The sequence BAA05392 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti660W → C in AAH98582 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_08062388 – 1648Missing in MCPH20; drastically decreased expression at the mRNA level; loss of localization at the midbody during cytokinesis and consequently loss of CIT/CRIK recruitment to the midbody. 1 PublicationAdd BLAST1561
Natural variantiVAR_080624459G → R in MCPH20; unknown pathological significance. 1 Publication1
Natural variantiVAR_080625827Missing in MCPH20; unknown pathological significance. 1 Publication1
Natural variantiVAR_080626841S → F in MCPH20; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs139385693Ensembl.1
Natural variantiVAR_080627849H → D in MCPH20; Decreased expression at the mRNA level and loss of localization at the midbody during cytokinesis and consequently loss of CIT/CRIK recruitment to the midbody, when analyzed in primary fibroblasts from a patient who is a compound heterozygous with variant V-1221. 1 Publication1
Natural variantiVAR_0806281221G → V in MCPH20; Decreased expression at the mRNA level and loss of localization at the midbody during cytokinesis and consequently loss of CIT/CRIK recruitment to the midbody, when analyzed in primary fibroblasts from a patient who is a compound heterozygous with variant D-849. 1 Publication1
Natural variantiVAR_0377771633P → A1 PublicationCorresponds to variant dbSNP:rs12120084Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
D26361 mRNA Translation: BAA05392.2 Different initiation.
AL445483 Genomic DNA No translation available.
CH471067 Genomic DNA Translation: EAW91316.1
BC098582 mRNA Translation: AAH98582.1
BC113742 mRNA Translation: AAI13743.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS30963.1

NCBI Reference Sequences

More...RefSeqi		NP_001292721.1, NM_001305792.1
NP_055690.1, NM_014875.2
XP_011508533.1, XM_011510231.2
XP_011508534.1, XM_011510232.2
XP_016858494.1, XM_017003005.1

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.3104

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000367350; ENSP00000356319; ENSG00000118193
ENST00000614960; ENSP00000483069; ENSG00000118193

Database of genes from NCBI RefSeq genomes

More...GeneIDi		9928

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:9928

UCSC genome browser

More...UCSCi		uc010ppk.2 human

Keywords - Coding sequence diversityi

Polymorphism

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

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26361 mRNA Translation: BAA05392.2 Different initiation.
AL445483 Genomic DNA No translation available.
CH471067 Genomic DNA Translation: EAW91316.1
BC098582 mRNA Translation: AAH98582.1
BC113742 mRNA Translation: AAI13743.1
CCDSiCCDS30963.1
RefSeqiNP_001292721.1, NM_001305792.1
NP_055690.1, NM_014875.2
XP_011508533.1, XM_011510231.2
XP_011508534.1, XM_011510232.2
XP_016858494.1, XM_017003005.1
UniGeneiHs.3104

3D structure databases

ProteinModelPortaliQ15058
SMRiQ15058
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115256, 93 interactors
IntActiQ15058, 41 interactors
MINTiQ15058
STRINGi9606.ENSP00000356319

Chemistry databases

BindingDBiQ15058
ChEMBLiCHEMBL5576

PTM databases

iPTMnetiQ15058
PhosphoSitePlusiQ15058

Polymorphism and mutation databases

BioMutaiKIF14
DMDMi23396633

Proteomic databases

EPDiQ15058
jPOSTiQ15058
MaxQBiQ15058
PaxDbiQ15058
PeptideAtlasiQ15058
PRIDEiQ15058
ProteomicsDBi60413

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		9928
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367350; ENSP00000356319; ENSG00000118193
ENST00000614960; ENSP00000483069; ENSG00000118193
GeneIDi9928
KEGGihsa:9928
UCSCiuc010ppk.2 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		9928
DisGeNETi9928
EuPathDBiHostDB:ENSG00000118193.11

GeneCards: human genes, protein and diseases

More...GeneCardsi		KIF14
HGNCiHGNC:19181 KIF14
HPAiHPA038061
HPA058220
MalaCardsiKIF14
MIMi611279 gene
616258 phenotype
617914 phenotype
neXtProtiNX_Q15058
OpenTargetsiENSG00000118193
Orphaneti2512 Autosomal recessive primary microcephaly
439897 Lethal fetal cerebrorenogenitourinary agenesis/hypoplasia syndrome
PharmGKBiPA38820

Human Unidentified Gene-Encoded large proteins database

More...HUGEi		Search...

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0245 Eukaryota
COG5059 LUCA
GeneTreeiENSGT00940000156834
HOGENOMiHOG000113224
HOVERGENiHBG052249
InParanoidiQ15058
KOiK17915
OMAiQEVSYHL
OrthoDBi76316at2759
PhylomeDBiQ15058
TreeFamiTF105221

Enzyme and pathway databases

ReactomeiR-HSA-5625900 RHO GTPases activate CIT

Miscellaneous databases

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

More...ChiTaRSi		KIF14 human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		KIF14

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

More...GenomeRNAii		9928

Protein Ontology

More...PROi		PR:Q15058

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000118193 Expressed in 107 organ(s), highest expression level in bone marrow
CleanExiHS_KIF14
GenevisibleiQ15058 HS

Family and domain databases

CDDicd00060 FHA, 1 hit
Gene3Di3.40.850.10, 1 hit
InterProiView protein in InterPro
IPR000253 FHA_dom
IPR027640 Kinesin-like_fam
IPR032405 Kinesin_assoc
IPR019821 Kinesin_motor_CS
IPR001752 Kinesin_motor_dom
IPR036961 Kinesin_motor_dom_sf
IPR027417 P-loop_NTPase
IPR008984 SMAD_FHA_dom_sf
PANTHERiPTHR24115 PTHR24115, 1 hit
PfamiView protein in Pfam
PF00498 FHA, 1 hit
PF00225 Kinesin, 1 hit
PF16183 Kinesin_assoc, 1 hit
PRINTSiPR00380 KINESINHEAVY
SMARTiView protein in SMART
SM00240 FHA, 1 hit
SM00129 KISc, 1 hit
SUPFAMiSSF49879 SSF49879, 1 hit
SSF52540 SSF52540, 1 hit
PROSITEiView 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 nameiKIF14_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q15058
Secondary accession number(s): Q14CI8, Q4G0A5, Q5T1W3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: November 1, 1996
Last modified: January 16, 2019
This is version 171 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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