Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9BW19 (KIFC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kinesin-like protein KIFC1
Alternative name(s):
Kinesin-like protein 2
Kinesin-related protein HSET
Gene names
Name:KIFC1
Synonyms:HSET, KNSL2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length673 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Minus end-directed microtubule-dependent motor required for bipolar spindle formation. May contribute to movement of early endocytic vesicles. Ref.5

Subunit structure

Binds NUBP1 and NUBP2. Interacts with PPP1R42 By similarity.

Subcellular location

Nucleus By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytoskeletonspindle By similarity. Early endosome By similarity. Note: Associated with nucleus during interphase, centrosomes in early and spindle in later mitosis By similarity.

Miscellaneous

HeLa cells lacking KIFC1 show multipolar mitotic spindles and a defect in chromosome congression and chromosome alignment during mitosis.

Sequence similarities

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. NCD subfamily.

Contains 1 kinesin motor domain.

Sequence caution

The sequence AAH00712.2 differs from that shown. Reason: Erroneous initiation.

The sequence AAH63567.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH73878.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH98438.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA03509.1 differs from that shown. Reason: Frameshift at positions 223 and 256.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 673673Kinesin-like protein KIFC1
PRO_0000125428

Regions

Domain310 – 663354Kinesin motor
Nucleotide binding410 – 4178ATP By similarity
Coiled coil142 – 306165 Potential

Amino acid modifications

Modified residue311Phosphoserine Ref.7

Natural variations

Natural variant2191R → Q. Ref.1
VAR_012650

Experimental info

Sequence conflict3681T → P in AAH00712. Ref.3

Secondary structure

..................................................... 673
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BW19 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 9E99737665BF1E92

FASTA67373,748
        10         20         30         40         50         60 
MDPQRSPLLE VKGNIELKRP LIKAPSQLPL SGSRLKRRPD QMEDGLEPEK KRTRGLGATT 

        70         80         90        100        110        120 
KITTSHPRVP SLTTVPQTQG QTTAQKVSKK TGPRCSTAIA TGLKNQKPVP AVPVQKSGTS 

       130        140        150        160        170        180 
GVPPMAGGKK PSKRPAWDLK GQLCDLNAEL KRCRERTQTL DQENQQLQDQ LRDAQQQVKA 

       190        200        210        220        230        240 
LGTERTTLEG HLAKVQAQAE QGQQELKNLR ACVLELEERL STQEGLVQEL QKKQVELQEE 

       250        260        270        280        290        300 
RRGLMSQLEE KERRLQTSEA ALSSSQAEVA SLRQETVAQA ALLTEREERL HGLEMERRRL 

       310        320        330        340        350        360 
HNQLQELKGN IRVFCRVRPV LPGEPTPPPG LLLFPSGPGG PSDPPTRLSL SRSDERRGTL 

       370        380        390        400        410        420 
SGAPAPPTRH DFSFDRVFPP GSGQDEVFEE IAMLVQSALD GYPVCIFAYG QTGSGKTFTM 

       430        440        450        460        470        480 
EGGPGGDPQL EGLIPRALRH LFSVAQELSG QGWTYSFVAS YVEIYNETVR DLLATGTRKG 

       490        500        510        520        530        540 
QGGECEIRRA GPGSEELTVT NARYVPVSCE KEVDALLHLA RQNRAVARTA QNERSSRSHS 

       550        560        570        580        590        600 
VFQLQISGEH SSRGLQCGAP LSLVDLAGSE RLDPGLALGP GERERLRETQ AINSSLSTLG 

       610        620        630        640        650        660 
LVIMALSNKE SHVPYRNSKL TYLLQNSLGG SAKMLMFVNI SPLEENVSES LNSLRFASKV 

       670 
NQCVIGTAQA NRK 

« Hide

References

« Hide 'large scale' references
[1]"Genomic organization of the HSET locus and the possible association of HLA-linked genes with immotile cilia syndrome (ICS)."
Janitz K., Wild A., Beck S., Savasta S., Beluffi G., Ziegler A., Volz A.
Immunogenetics 49:644-652(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-219.
[2]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [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].
Tissue: Brain, Kidney, Muscle and Uterus.
[4]"Cloning of a new kinesin-related gene located at the centromeric end of the human MHC region."
Ando A., Yara-Kikuti Y., Kawata H., Okamoto N., Imai T., Eki T., Yokoyama K., Soeda E., Ikemura T., Abe K., Inoko H.
Immunogenetics 39:194-200(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 155-673.
Tissue: Testis.
[5]"Functional analysis of human microtubule-based motor proteins, the kinesins and dyneins, in mitosis/cytokinesis using RNA interference."
Zhu C., Zhao J., Bibikova M., Leverson J.D., Bossy-Wetzel E., Fan J.-B., Abraham R.T., Jiang W.
Mol. Biol. Cell 16:3187-3199(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ010479 mRNA. Translation: CAA09217.1.
AL021366 Genomic DNA. Translation: CAA16157.1.
AL050332 Genomic DNA. Translation: CAB63782.1.
AL662799 Genomic DNA. Translation: CAI18269.1.
BX088650 Genomic DNA. Translation: CAM26294.1.
BX248088 Genomic DNA. Translation: CAI41792.1.
BC000712 mRNA. Translation: AAH00712.2. Different initiation.
BC063567 mRNA. Translation: AAH63567.1. Different initiation.
BC073878 mRNA. Translation: AAH73878.1. Different initiation.
BC098438 mRNA. Translation: AAH98438.1. Different initiation.
BC121041 mRNA. Translation: AAI21042.1.
BC121042 mRNA. Translation: AAI21043.1.
D14678 mRNA. Translation: BAA03509.1. Frameshift.
CCDSCCDS34430.1.
PIRI54523.
RefSeqNP_002254.2. NM_002263.3.
UniGeneHs.436912.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2REPX-ray2.60A307-663[»]
ProteinModelPortalQ9BW19.
SMRQ9BW19. Positions 138-167, 193-661.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110031. 5 interactions.
IntActQ9BW19. 5 interactions.
MINTMINT-3062538.

PTM databases

PhosphoSiteQ9BW19.

Polymorphism databases

DMDM20138710.

Proteomic databases

MaxQBQ9BW19.
PaxDbQ9BW19.
PeptideAtlasQ9BW19.
PRIDEQ9BW19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374523; ENSP00000363647; ENSG00000204197.
ENST00000428849; ENSP00000393963; ENSG00000237649.
ENST00000448818; ENSP00000407885; ENSG00000233450.
GeneID3833.
KEGGhsa:3833.
UCSCuc003oef.4. human.

Organism-specific databases

CTD3833.
GeneCardsGC06P033359.
GC06Pn33288.
GC06Po33498.
HGNCHGNC:6389. KIFC1.
HPAHPA055997.
MIM603763. gene.
neXtProtNX_Q9BW19.
PharmGKBPA30178.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5059.
HOVERGENHBG001080.
InParanoidQ9BW19.
KOK10405.
OMAQISGEHS.
PhylomeDBQ9BW19.
TreeFamTF105237.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ9BW19.
BgeeQ9BW19.
CleanExHS_KIFC1.
GenevestigatorQ9BW19.

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_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9BW19.
GeneWikiKIFC1.
GenomeRNAi3833.
NextBio15065.
PROQ9BW19.
SOURCESearch...

Entry information

Entry nameKIFC1_HUMAN
AccessionPrimary (citable) accession number: Q9BW19
Secondary accession number(s): O60887 expand/collapse secondary AC list , Q14834, Q4KMP0, Q5SU09, Q6GMS7, Q6P4A5, Q9UQP7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2002
Last modified: July 9, 2014
This is version 125 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 6

Human chromosome 6: entries, gene names and cross-references to MIM