Kinesin heavy chain isoform 5C - Mus musculus (Mouse)

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P28738 (KIF5C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 114. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Kinesin heavy chain isoform 5C

Alternative name(s):
Kinesin heavy chain neuron-specific 2

Gene names

Name:	Kif5c
Synonyms:	Nkhc2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	956 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Mediates dendritic trafficking of mRNAs. Ref.9
Subunit structure	Oligomer composed of two heavy chains and two light chains. Interacts with GRIP1 and KLC3. Interacts with TRAK1 By similarity. Ref.7 Ref.10
Subcellular location	Cytoplasm › cytoskeleton Probable.
Domain	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 similarities	Belongs to the kinesin-like protein family. Kinesin subfamily. Contains 1 kinesin-motor domain.
Sequence caution	The sequence CAA43677.1 differs from that shown. Reason: Chimeric cDNA. The C-terminus (up to position 300) corresponds to KIF5C sequence.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm Cytoskeleton Microtubule
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Motor protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA transport Inferred from mutant phenotype Ref.9. Source: UniProtKB microtubule-based movement Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW microtubule Inferred from electronic annotation. Source: UniProtKB-KW microtubule associated complex Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule motor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 956

955

Kinesin heavy chain isoform 5C

PRO_0000125356

Regions

Domain

2 – 386

385

Kinesin-motor

Nucleotide binding

86 – 93

ATP By similarity

Region

174 – 315

142

Microtubule-binding

Region

859 – 956

Globular

Coiled coil

406 – 923

518

Amino acid modifications

Modified residue

338

Phosphothreonine Ref.8

Modified residue

796

Phosphothreonine Ref.8

Experimental info

Sequence conflict

387

Q → H in AAC79804. Ref.2

Sequence conflict

792

R → I in AAC79804. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P28738 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: A36BC903603D8748
Show »

FASTA

956

109,275

        10         20         30         40         50         60 
MADPAECSIK VMCRFRPLNE AEILRGDKFI PKFKGEETVV IGQGKPYVFD RVLPPNTTQE 

        70         80         90        100        110        120 
QVYNACAKQI VKDVLEGYNG TIFAYGQTSS GKTHTMEGKL HDPQLMGIIP RIAHDIFDHI 

       130        140        150        160        170        180 
YSMDENLEFH IKVSYFEIYL DKIRDLLDVS KTNLAVHEDK NRVPYVKGCT ERFVSSPEEV 

       190        200        210        220        230        240 
MDVIDEGKAN RHVAVTNMNE HSSRSHSIFL INIKQENVET EKKLSGKLYL VDLAGSEKVS 

       250        260        270        280        290        300 
KTGAEGAVLD EAKNINKSLS ALGNVISALA EGTKTHVPYR DSKMTRILQD SLGGNCRTTI 

       310        320        330        340        350        360 
VICCSPSVFN EAETKSTLMF GQRAKTIKNT VSVNLELTAE EWKKKYEKEK EKNKALKSVL 

       370        380        390        400        410        420 
QHLEMELNRW RNGEAVPEDE QISAKDQKSL EPCDNTPIID NITPVVDGIS AEKEKYDEEI 

       430        440        450        460        470        480 
TSLYRQLDDK DDEINQQSQL AEKLKQQMLD QDELLASTRR DYEKIQEELT RLQIENEAAK 

       490        500        510        520        530        540 
DEVKEVLQAL EELAVNYDQK SQEVEDKTRA NEQLTDELAQ KTTTLTTTQR ELSQLQELSN 

       550        560        570        580        590        600 
HQKKRATEIL NLLLKDLGEI GGIIGTNDVK TLADVNGVIE EEFTMARLYI SKMKSEVKSL 

       610        620        630        640        650        660 
VNRSKQLESA QMDSNRKMNA SERELAACQL LISQHEAKIK SLTDYMQNME QKRRQLEESQ 

       670        680        690        700        710        720 
DSLSEELAKL RAQEKMHEVS FQDKEKEHLT RLQDAEEVKK ALEQQMESHR EAHQKQLSRL 

       730        740        750        760        770        780 
RDEIEEKQRI IDEIRDLNQK LQLEQERLSS DYNKLKIEDQ EREVKLEKLL LLNDKREQAR 

       790        800        810        820        830        840 
EDLKGLEETV SRELQTLHNL RKLFVQDLTT RVKKSVELDS DDGGGSAAQK QKISFLENNL 

       850        860        870        880        890        900 
EQLTKVHKQL VRDNADLRCE LPKLEKRLRA TAERVKALES ALKEAKENAM RDRKRYQQEV 

       910        920        930        940        950 
DRIKEAVRAK NMARRAHSAQ IAKPIRPGHY PASSPTAVHA VRGGGGGSSN STHYQK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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, 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]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-338 AND THR-796, MASS SPECTROMETRY. Tissue: Liver.
[9]	"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.
[10]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00421137.

PIR

S37711.

RefSeq

NP_032475.2. NM_008449.2.

UniGene

Mm.256342.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P28738.

SMR

P28738. Positions 2-372.

ModBase

Search...

Protein-protein interaction databases

IntAct

P28738. 3 interactions.

MINT

MINT-236700.

STRING

10090.ENSMUSP00000028102.

PTM databases

PhosphoSite

P28738.

Proteomic databases

PaxDb

P28738.

PRIDE

P28738.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000028102; ENSMUSP00000028102; ENSMUSG00000026764.

GeneID

16574.

KEGG

mmu:16574.

Organism-specific databases

CTD

3800.

MGI

MGI:1098269. Kif5c.

Phylogenomic databases

eggNOG

COG5059.

GeneTree

ENSGT00690000101739.

HOVERGEN

HBG006210.

InParanoid

Q6NXI9.

K10396.

OMA

GQGKPYV.

OrthoDB

EOG4Q2DDS.

Gene expression databases

ArrayExpress

P28738.

Bgee

P28738.

CleanEx

MM_KIF5C.

Genevestigator

P28738.

GermOnline

ENSMUSG00000026764. Mus musculus.

Family and domain databases

Gene3D

3.40.850.10. 1 hit.

InterPro

IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
[Graphical view]

Pfam

PF00225. Kinesin. 1 hit.
[Graphical view]

PRINTS

PR00380. KINESINHEAVY.

SMART

SM00129. KISc. 1 hit.
[Graphical view]

PROSITE

PS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P28738.

NextBio

290099.

SOURCE

Search...

Entry information

Entry name

KIF5C_MOUSE

Accession

Primary (citable) accession number: P28738
Secondary accession number(s): Q6NXI9, Q9Z2F8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 114 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents