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P28738

- KIF5C_MOUSE

UniProt

P28738 - KIF5C_MOUSE

Protein

Kinesin heavy chain isoform 5C

Gene

Kif5c

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Mediates dendritic trafficking of mRNAs.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi86 – 938ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. microtubule motor activity Source: InterPro
    3. protein binding Source: IntAct

    GO - Biological processi

    1. microtubule-based movement Source: InterPro
    2. mRNA transport Source: UniProtKB

    Keywords - Molecular functioni

    Motor protein

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kinesin heavy chain isoform 5C
    Alternative name(s):
    Kinesin heavy chain neuron-specific 2
    Gene namesi
    Name:Kif5c
    Synonyms:Nkhc2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1098269. Kif5c.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. kinesin complex Source: InterPro
    3. microtubule Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 956956Kinesin heavy chain isoform 5CPRO_0000125356Add
    BLAST

    Proteomic databases

    MaxQBiP28738.
    PaxDbiP28738.
    PRIDEiP28738.

    PTM databases

    PhosphoSiteiP28738.

    Expressioni

    Gene expression databases

    ArrayExpressiP28738.
    BgeeiP28738.
    CleanExiMM_KIF5C.
    GenevestigatoriP28738.

    Interactioni

    Subunit structurei

    Oligomer composed of two heavy chains and two light chains. Interacts with GRIP1 and KLC3. Interacts with TRAK1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Mapk8ip3Q9ESN98EBI-2506834,EBI-301496

    Protein-protein interaction databases

    BioGridi200947. 6 interactions.
    IntActiP28738. 9 interactions.
    MINTiMINT-236700.
    STRINGi10090.ENSMUSP00000028102.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VFVX-ray1.85A329-334[»]
    1VFWX-ray2.30A329-334[»]
    1VFXX-ray2.55A329-334[»]
    1VFZX-ray2.24A329-334[»]
    ProteinModelPortaliP28738.
    SMRiP28738. Positions 2-372.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28738.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 327320Kinesin motorPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni174 – 315142Microtubule-bindingAdd
    BLAST
    Regioni859 – 95698GlobularAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili406 – 923518Add
    BLAST

    Domaini

    Composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it hydrolyzes ATP and binds microtubule), a central alpha-helical coiled coil domain that mediates the heavy chain dimerization; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains), vesicles and membranous organelles.

    Sequence similaritiesi

    Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Kinesin subfamily.PROSITE-ProRule annotation
    Contains 1 kinesin motor domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5059.
    GeneTreeiENSGT00730000110208.
    HOVERGENiHBG006210.
    InParanoidiQ6NXI9.
    KOiK10396.
    OMAiIRDMNQK.
    OrthoDBiEOG7T4MJD.
    TreeFamiTF105225.

    Family and domain databases

    Gene3Di3.40.850.10. 1 hit.
    InterProiIPR027640. Kinesin-like_fam.
    IPR019821. Kinesin_motor_CS.
    IPR001752. Kinesin_motor_dom.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR24115. PTHR24115. 1 hit.
    PfamiPF00225. Kinesin. 1 hit.
    [Graphical view]
    PRINTSiPR00380. KINESINHEAVY.
    SMARTiSM00129. KISc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
    PS50067. KINESIN_MOTOR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P28738-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADPAECSIK VMCRFRPLNE AEILRGDKFI PKFKGEETVV IGQGKPYVFD    50
    RVLPPNTTQE QVYNACAKQI VKDVLEGYNG TIFAYGQTSS GKTHTMEGKL 100
    HDPQLMGIIP RIAHDIFDHI YSMDENLEFH IKVSYFEIYL DKIRDLLDVS 150
    KTNLAVHEDK NRVPYVKGCT ERFVSSPEEV MDVIDEGKAN RHVAVTNMNE 200
    HSSRSHSIFL INIKQENVET EKKLSGKLYL VDLAGSEKVS KTGAEGAVLD 250
    EAKNINKSLS ALGNVISALA EGTKTHVPYR DSKMTRILQD SLGGNCRTTI 300
    VICCSPSVFN EAETKSTLMF GQRAKTIKNT VSVNLELTAE EWKKKYEKEK 350
    EKNKALKSVL QHLEMELNRW RNGEAVPEDE QISAKDQKSL EPCDNTPIID 400
    NITPVVDGIS AEKEKYDEEI TSLYRQLDDK DDEINQQSQL AEKLKQQMLD 450
    QDELLASTRR DYEKIQEELT RLQIENEAAK DEVKEVLQAL EELAVNYDQK 500
    SQEVEDKTRA NEQLTDELAQ KTTTLTTTQR ELSQLQELSN HQKKRATEIL 550
    NLLLKDLGEI GGIIGTNDVK TLADVNGVIE EEFTMARLYI SKMKSEVKSL 600
    VNRSKQLESA QMDSNRKMNA SERELAACQL LISQHEAKIK SLTDYMQNME 650
    QKRRQLEESQ DSLSEELAKL RAQEKMHEVS FQDKEKEHLT RLQDAEEVKK 700
    ALEQQMESHR EAHQKQLSRL RDEIEEKQRI IDEIRDLNQK LQLEQERLSS 750
    DYNKLKIEDQ EREVKLEKLL LLNDKREQAR EDLKGLEETV SRELQTLHNL 800
    RKLFVQDLTT RVKKSVELDS DDGGGSAAQK QKISFLENNL EQLTKVHKQL 850
    VRDNADLRCE LPKLEKRLRA TAERVKALES ALKEAKENAM RDRKRYQQEV 900
    DRIKEAVRAK NMARRAHSAQ IAKPIRPGHY PASSPTAVHA VRGGGGGSSN 950
    STHYQK 956
    Length:956
    Mass (Da):109,275
    Last modified:July 27, 2011 - v3
    Checksum:iA36BC903603D8748
    GO

    Sequence cautioni

    The sequence CAA43677.1 differs from that shown. Reason: Chimeric cDNA. The C-terminus (up to position 300) corresponds to KIF5C sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti387 – 3871Q → H in AAC79804. (PubMed:9782088)Curated
    Sequence conflicti792 – 7921R → I in AAC79804. (PubMed:9782088)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61435 mRNA. Translation: CAA43677.1. Sequence problems.
    AF067180 mRNA. Translation: AAC79804.1.
    AL845332, AL929069 Genomic DNA. Translation: CAM20914.1.
    AL929069, AL845332 Genomic DNA. Translation: CAM25239.1.
    CH466519 Genomic DNA. Translation: EDL26880.1.
    BC067051 mRNA. Translation: AAH67051.1.
    CCDSiCCDS16024.1.
    PIRiS37711.
    RefSeqiNP_032475.2. NM_008449.2.
    UniGeneiMm.256342.

    Genome annotation databases

    EnsembliENSMUST00000028102; ENSMUSP00000028102; ENSMUSG00000026764.
    GeneIDi16574.
    KEGGimmu:16574.
    UCSCiuc008jpy.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61435 mRNA. Translation: CAA43677.1 . Sequence problems.
    AF067180 mRNA. Translation: AAC79804.1 .
    AL845332 , AL929069 Genomic DNA. Translation: CAM20914.1 .
    AL929069 , AL845332 Genomic DNA. Translation: CAM25239.1 .
    CH466519 Genomic DNA. Translation: EDL26880.1 .
    BC067051 mRNA. Translation: AAH67051.1 .
    CCDSi CCDS16024.1.
    PIRi S37711.
    RefSeqi NP_032475.2. NM_008449.2.
    UniGenei Mm.256342.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VFV X-ray 1.85 A 329-334 [» ]
    1VFW X-ray 2.30 A 329-334 [» ]
    1VFX X-ray 2.55 A 329-334 [» ]
    1VFZ X-ray 2.24 A 329-334 [» ]
    ProteinModelPortali P28738.
    SMRi P28738. Positions 2-372.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200947. 6 interactions.
    IntActi P28738. 9 interactions.
    MINTi MINT-236700.
    STRINGi 10090.ENSMUSP00000028102.

    PTM databases

    PhosphoSitei P28738.

    Proteomic databases

    MaxQBi P28738.
    PaxDbi P28738.
    PRIDEi P28738.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028102 ; ENSMUSP00000028102 ; ENSMUSG00000026764 .
    GeneIDi 16574.
    KEGGi mmu:16574.
    UCSCi uc008jpy.1. mouse.

    Organism-specific databases

    CTDi 3800.
    MGIi MGI:1098269. Kif5c.

    Phylogenomic databases

    eggNOGi COG5059.
    GeneTreei ENSGT00730000110208.
    HOVERGENi HBG006210.
    InParanoidi Q6NXI9.
    KOi K10396.
    OMAi IRDMNQK.
    OrthoDBi EOG7T4MJD.
    TreeFami TF105225.

    Miscellaneous databases

    EvolutionaryTracei P28738.
    NextBioi 290099.
    PROi P28738.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28738.
    Bgeei P28738.
    CleanExi MM_KIF5C.
    Genevestigatori P28738.

    Family and domain databases

    Gene3Di 3.40.850.10. 1 hit.
    InterProi IPR027640. Kinesin-like_fam.
    IPR019821. Kinesin_motor_CS.
    IPR001752. Kinesin_motor_dom.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR24115. PTHR24115. 1 hit.
    Pfami PF00225. Kinesin. 1 hit.
    [Graphical view ]
    PRINTSi PR00380. KINESINHEAVY.
    SMARTi SM00129. KISc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS00411. KINESIN_MOTOR_1. 1 hit.
    PS50067. KINESIN_MOTOR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A collection of cDNA clones with specific expression patterns in mouse brain."
      Kato K.
      Eur. J. Neurosci. 2:704-711(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: BALB/c.
      Tissue: Brain.
    2. "Chromosomal localization reveals three kinesin heavy chain genes in mouse."
      Xia C., Rahman A., Yang Z., Goldstein L.S.B.
      Genomics 52:209-213(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Brain.
    6. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 133-142; 242-253; 258-274; 287-297; 546-555 AND 815-830, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    7. "Glutamate-receptor-interacting protein GRIP1 directly steers kinesin to dendrites."
      Setou M., Seog D.-H., Tanaka Y., Kanai Y., Takei Y., Kawagishi M., Hirokawa N.
      Nature 417:83-87(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRIP1.
    8. "Dendritic mRNA targeting of Jacob and N-methyl-d-aspartate-induced nuclear translocation after calpain-mediated proteolysis."
      Kindler S., Dieterich D.C., Schutt J., Sahin J., Karpova A., Mikhaylova M., Schob C., Gundelfinger E.D., Kreienkamp H.J., Kreutz M.R.
      J. Biol. Chem. 284:25431-25440(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "KIF1A alternately uses two loops to bind microtubules."
      Nitta R., Kikkawa M., Okada Y., Hirokawa N.
      Science 305:678-683(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 329-334 IN COMPLEXES WITH KIF1A, SUBUNIT, INTERACTION WITH MICROTUBULES.

    Entry informationi

    Entry nameiKIF5C_MOUSE
    AccessioniPrimary (citable) accession number: P28738
    Secondary accession number(s): Q6NXI9, Q9Z2F8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 126 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3