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O60282 (KIF5C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kinesin heavy chain isoform 5C
Alternative name(s):
Kinesin heavy chain neuron-specific 2
Gene names
Name:KIF5C
Synonyms:KIAA0531, NKHC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length957 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Oligomer composed of two heavy chains and two light chains. Interacts with GRIP1 and KLC3 By similarity. Interacts with TRAK1. Ref.5

Subcellular location

Cytoplasmcytoskeleton Probable.

Tissue specificity

Highest expression in brain, prostate and testis, and moderate expression in kidney, small intestine and ovary.

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.

Involvement in disease

Cortical dysplasia, complex, with other brain malformations 2 (CDCBM2) [MIM:615282]: A disorder of aberrant neuronal migration and disturbed axonal guidance. Clinical features include intrauterine growth retardation, fetal akinesia, seizures, microcephaly, lack of psychomotor development, and arthrogryposis. Brain imaging shows malformations of cortical development, including polymicrogyria, gyral simplification, and thin corpus callosum.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8

Sequence similarities

Belongs to the kinesin-like protein family. Kinesin subfamily.

Contains 1 kinesin-motor domain.

Sequence caution

The sequence BAA25457.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60282-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O60282-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-232: Missing.
     233-238: LAGSEK → MATYIH

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 957957Kinesin heavy chain isoform 5C
PRO_0000125355

Regions

Domain2 – 386385Kinesin-motor
Nucleotide binding86 – 938ATP By similarity
Region174 – 315142Microtubule-binding
Region859 – 95698Globular
Coiled coil406 – 923518

Natural variations

Alternative sequence1 – 232232Missing in isoform 2.
VSP_035715
Alternative sequence233 – 2386LAGSEK → MATYIH in isoform 2.
VSP_035716
Natural variant2371E → K Found in a patient with mental retardation, severe delay in motor development, seizures and no speech. Ref.7
VAR_069389
Natural variant2371E → V in CDCBM2; the mutant protein has a complete loss of ATP hydrolysis activity; colocalizes with microtubules throughout the cell but does not appear as puncta or accumulates in cortical clusters as does the wild-type protein. Ref.8
VAR_070574

Experimental info

Sequence conflict355 – 3606TLKNVI → STHASV in AAD01436. Ref.4
Sequence conflict583 – 5853EFT → DRV in AAD01436. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: A9F25BB1C994322A

FASTA957109,495
        10         20         30         40         50         60 
MADPAECSIK VMCRFRPLNE AEILRGDKFI PKFKGDETVV 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 EKNKTLKNVI 

       370        380        390        400        410        420 
QHLEMELNRW RNGEAVPEDE QISAKDQKNL EPCDNTPIID NIAPVVAGIS TEEKEKYDEE 

       430        440        450        460        470        480 
ISSLYRQLDD KDDEINQQSQ LAEKLKQQML DQDELLASTR RDYEKIQEEL TRLQIENEAA 

       490        500        510        520        530        540 
KDEVKEVLQA LEELAVNYDQ KSQEVEDKTR ANEQLTDELA QKTTTLTTTQ RELSQLQELS 

       550        560        570        580        590        600 
NHQKKRATEI LNLLLKDLGE IGGIIGTNDV KTLADVNGVI EEEFTMARLY ISKMKSEVKS 

       610        620        630        640        650        660 
LVNRSKQLES AQMDSNRKMN ASERELAACQ LLISQHEAKI KSLTDYMQNM EQKRRQLEES 

       670        680        690        700        710        720 
QDSLSEELAK LRAQEKMHEV SFQDKEKEHL TRLQDAEEMK KALEQQMESH REAHQKQLSR 

       730        740        750        760        770        780 
LRDEIEEKQK IIDEIRDLNQ KLQLEQEKLS SDYNKLKIED QEREMKLEKL LLLNDKREQA 

       790        800        810        820        830        840 
REDLKGLEET VSRELQTLHN LRKLFVQDLT TRVKKSVELD NDDGGGSAAQ KQKISFLENN 

       850        860        870        880        890        900 
LEQLTKVHKQ LVRDNADLRC ELPKLEKRLR ATAERVKALE SALKEAKENA MRDRKRYQQE 

       910        920        930        940        950 
VDRIKEAVRA KNMARRAHSA QIAKPIRPGH YPASSPTAVH AIRGGGGSSS NSTHYQK 

« Hide

Isoform 2 [UniParc].

Checksum: 323C36FF4653E281
Show »

FASTA72583,178

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] (ISOFORM 2).
Tissue: Brain.
[4]"Huntingtin-associated protein 1 (HAP1) interacts with the p150Glued subunit of dynactin."
Engelender S., Sharp A.H., Colomer V., Tokito M.K., Lanahan A., Worley P., Holzbaur E.L.F., Ross C.A.
Hum. Mol. Genet. 6:2205-2212(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 355-585 (ISOFORMS 1/2).
[5]"GRIF-1 and OIP106, members of a novel gene family of coiled-coil domain proteins: association in vivo and in vitro with kinesin."
Brickley K., Smith M.J., Beck M., Stephenson F.A.
J. Biol. Chem. 280:14723-14732(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAK1.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Diagnostic exome sequencing in persons with severe intellectual disability."
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., Veltman J.A., Vissers L.E.
N. Engl. J. Med. 367:1921-1929(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LYS-237.
[8]"Mutations in TUBG1, DYNC1H1, KIF5C and KIF2A cause malformations of cortical development and microcephaly."
Poirier K., Lebrun N., Broix L., Tian G., Saillour Y., Boscheron C., Parrini E., Valence S., Pierre B.S., Oger M., Lacombe D., Genevieve D., Fontana E., Darra F., Cances C., Barth M., Bonneau D., Bernadina B.D. expand/collapse author list , N'guyen S., Gitiaux C., Parent P., des Portes V., Pedespan J.M., Legrez V., Castelnau-Ptakine L., Nitschke P., Hieu T., Masson C., Zelenika D., Andrieux A., Francis F., Guerrini R., Cowan N.J., Bahi-Buisson N., Chelly J.
Nat. Genet. 45:639-647(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CDCBM2 VAL-237, CHARACTERIZATION OF VARIANT CDCBM2 VAL-237.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB011103 mRNA. Translation: BAA25457.2. Different initiation.
AC105402 Genomic DNA. No translation available.
AC108512 Genomic DNA. No translation available.
AC144443 Genomic DNA. No translation available.
AC144611 Genomic DNA. No translation available.
BC110287 mRNA. Translation: AAI10288.1.
AF010146 mRNA. Translation: AAD01436.1.
RefSeqNP_004513.1. NM_004522.2.
UniGeneHs.435557.
Hs.660699.

3D structure databases

ProteinModelPortalO60282.
SMRO60282. Positions 2-372.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110001. 15 interactions.
IntActO60282. 8 interactions.
STRING9606.ENSP00000393379.

Chemistry

ChEMBLCHEMBL2029194.

PTM databases

PhosphoSiteO60282.

Proteomic databases

PaxDbO60282.
PRIDEO60282.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000397413; ENSP00000380560; ENSG00000168280. [O60282-2]
ENST00000435030; ENSP00000393379; ENSG00000168280. [O60282-1]
ENST00000574197; ENSP00000460677; ENSG00000262907. [O60282-2]
ENST00000576072; ENSP00000461857; ENSG00000262907. [O60282-1]
GeneID3800.
KEGGhsa:3800.
UCSCuc010zbu.2. human. [O60282-1]

Organism-specific databases

CTD3800.
GeneCardsGC02P149632.
HGNCHGNC:6325. KIF5C.
HPAHPA035210.
MIM604593. gene.
615282. phenotype.
neXtProtNX_O60282.
PharmGKBPA30109.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5059.
HOGENOMHOG000216718.
HOVERGENHBG006210.
InParanoidO60282.
KOK10396.
OMAGTMRENE.
PhylomeDBO60282.
TreeFamTF105225.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressO60282.
BgeeO60282.
CleanExHS_KIF5C.
GenevestigatorO60282.

Family and domain databases

Gene3D3.40.850.10. 1 hit.
InterProIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR24115. PTHR24115. 1 hit.
PfamPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSPR00380. KINESINHEAVY.
SMARTSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKIF5C. human.
GeneWikiKIF5C.
GenomeRNAi3800.
NextBio14921.
PROO60282.
SOURCESearch...

Entry information

Entry nameKIF5C_HUMAN
AccessionPrimary (citable) accession number: O60282
Secondary accession number(s): O95079, Q2YDC5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM