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Protein

Kinesin-like protein KIFC1

Gene

KIFC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Minus end-directed microtubule-dependent motor required for bipolar spindle formation. May contribute to movement of early endocytic vesicles.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi410 – 4178ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • ATP-dependent microtubule motor activity, minus-end-directed Source: GO_Central
  • microtubule motor activity Source: UniProtKB

GO - Biological processi

  • blood coagulation Source: Reactome
  • cell division Source: UniProtKB-KW
  • metabolic process Source: GOC
  • microtubule-based movement Source: GO_Central
  • mitotic metaphase plate congression Source: UniProtKB
  • mitotic sister chromatid segregation Source: UniProtKB
  • mitotic spindle assembly Source: UniProtKB
  • spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_25201. Kinesins.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-like protein KIFC1
Alternative name(s):
Kinesin-like protein 2
Kinesin-related protein HSET
Gene namesi
Name:KIFC1
Synonyms:HSET, KNSL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:6389. KIFC1.

Subcellular locationi

GO - Cellular componenti

  • early endosome Source: UniProtKB-SubCell
  • kinesin complex Source: GO_Central
  • membrane Source: UniProtKB
  • microtubule Source: UniProtKB-KW
  • microtubule organizing center Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
  • spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Endosome, Microtubule, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30178.

Polymorphism and mutation databases

BioMutaiKIFC1.
DMDMi20138710.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 673673Kinesin-like protein KIFC1PRO_0000125428Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BW19.
PaxDbiQ9BW19.
PeptideAtlasiQ9BW19.
PRIDEiQ9BW19.

PTM databases

PhosphoSiteiQ9BW19.

Expressioni

Gene expression databases

BgeeiQ9BW19.
CleanExiHS_KIFC1.
ExpressionAtlasiQ9BW19. baseline and differential.
GenevisibleiQ9BW19. HS.

Organism-specific databases

HPAiHPA055997.

Interactioni

Subunit structurei

Binds NUBP1 and NUBP2. Interacts with PPP1R42 (By similarity).By similarity

Protein-protein interaction databases

BioGridi110031. 5 interactions.
IntActiQ9BW19. 5 interactions.
MINTiMINT-3062538.
STRINGi9606.ENSP00000393963.

Structurei

Secondary structure

1
673
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi311 – 3177Combined sources
Helixi329 – 3313Combined sources
Beta strandi347 – 3493Combined sources
Beta strandi371 – 3733Combined sources
Beta strandi375 – 3784Combined sources
Helixi384 – 39613Combined sources
Helixi397 – 4004Combined sources
Beta strandi404 – 4096Combined sources
Helixi416 – 4205Combined sources
Helixi428 – 4303Combined sources
Helixi433 – 44715Combined sources
Helixi448 – 4514Combined sources
Beta strandi453 – 46513Combined sources
Beta strandi468 – 4714Combined sources
Beta strandi487 – 4893Combined sources
Beta strandi497 – 4993Combined sources
Beta strandi505 – 5073Combined sources
Helixi510 – 52617Combined sources
Helixi535 – 5373Combined sources
Beta strandi538 – 55316Combined sources
Beta strandi556 – 56510Combined sources
Helixi596 – 60712Combined sources
Helixi615 – 6173Combined sources
Helixi619 – 6235Combined sources
Helixi625 – 6273Combined sources
Beta strandi633 – 6408Combined sources
Helixi644 – 6463Combined sources
Helixi647 – 66014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2REPX-ray2.60A307-663[»]
ProteinModelPortaliQ9BW19.
SMRiQ9BW19. Positions 262-661.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BW19.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini310 – 663354Kinesin motorPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili142 – 306165Sequence AnalysisAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5059.
GeneTreeiENSGT00550000074610.
HOVERGENiHBG001080.
InParanoidiQ9BW19.
KOiK10405.
OMAiWQETAAQ.
PhylomeDBiQ9BW19.
TreeFamiTF105237.

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.

Q9BW19-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPQRSPLLE VKGNIELKRP LIKAPSQLPL SGSRLKRRPD QMEDGLEPEK
60 70 80 90 100
KRTRGLGATT KITTSHPRVP SLTTVPQTQG QTTAQKVSKK TGPRCSTAIA
110 120 130 140 150
TGLKNQKPVP AVPVQKSGTS GVPPMAGGKK PSKRPAWDLK GQLCDLNAEL
160 170 180 190 200
KRCRERTQTL DQENQQLQDQ LRDAQQQVKA LGTERTTLEG HLAKVQAQAE
210 220 230 240 250
QGQQELKNLR ACVLELEERL STQEGLVQEL QKKQVELQEE RRGLMSQLEE
260 270 280 290 300
KERRLQTSEA ALSSSQAEVA SLRQETVAQA ALLTEREERL HGLEMERRRL
310 320 330 340 350
HNQLQELKGN IRVFCRVRPV LPGEPTPPPG LLLFPSGPGG PSDPPTRLSL
360 370 380 390 400
SRSDERRGTL SGAPAPPTRH DFSFDRVFPP GSGQDEVFEE IAMLVQSALD
410 420 430 440 450
GYPVCIFAYG QTGSGKTFTM EGGPGGDPQL EGLIPRALRH LFSVAQELSG
460 470 480 490 500
QGWTYSFVAS YVEIYNETVR DLLATGTRKG QGGECEIRRA GPGSEELTVT
510 520 530 540 550
NARYVPVSCE KEVDALLHLA RQNRAVARTA QNERSSRSHS VFQLQISGEH
560 570 580 590 600
SSRGLQCGAP LSLVDLAGSE RLDPGLALGP GERERLRETQ AINSSLSTLG
610 620 630 640 650
LVIMALSNKE SHVPYRNSKL TYLLQNSLGG SAKMLMFVNI SPLEENVSES
660 670
LNSLRFASKV NQCVIGTAQA NRK
Length:673
Mass (Da):73,748
Last modified:January 23, 2002 - v2
Checksum:i9E99737665BF1E92
GO

Sequence cautioni

The sequence AAH00712.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH63567.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH73878.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH98438.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA03509.1 differs from that shown. Reason: Frameshift at positions 223 and 256. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti368 – 3681T → P in AAH00712 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti219 – 2191R → Q.1 Publication
VAR_012650

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34430.1.
PIRiI54523.
RefSeqiNP_002254.2. NM_002263.3.
UniGeneiHs.436912.

Genome annotation databases

EnsembliENST00000374523; ENSP00000363647; ENSG00000204197.
ENST00000428849; ENSP00000393963; ENSG00000237649.
ENST00000448818; ENSP00000407885; ENSG00000233450.
GeneIDi3833.
KEGGihsa:3833.
UCSCiuc003oef.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34430.1.
PIRiI54523.
RefSeqiNP_002254.2. NM_002263.3.
UniGeneiHs.436912.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2REPX-ray2.60A307-663[»]
ProteinModelPortaliQ9BW19.
SMRiQ9BW19. Positions 262-661.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110031. 5 interactions.
IntActiQ9BW19. 5 interactions.
MINTiMINT-3062538.
STRINGi9606.ENSP00000393963.

PTM databases

PhosphoSiteiQ9BW19.

Polymorphism and mutation databases

BioMutaiKIFC1.
DMDMi20138710.

Proteomic databases

MaxQBiQ9BW19.
PaxDbiQ9BW19.
PeptideAtlasiQ9BW19.
PRIDEiQ9BW19.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374523; ENSP00000363647; ENSG00000204197.
ENST00000428849; ENSP00000393963; ENSG00000237649.
ENST00000448818; ENSP00000407885; ENSG00000233450.
GeneIDi3833.
KEGGihsa:3833.
UCSCiuc003oef.4. human.

Organism-specific databases

CTDi3833.
GeneCardsiGC06P033359.
GC06Pn33288.
GC06Po33498.
HGNCiHGNC:6389. KIFC1.
HPAiHPA055997.
MIMi603763. gene.
neXtProtiNX_Q9BW19.
PharmGKBiPA30178.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5059.
GeneTreeiENSGT00550000074610.
HOVERGENiHBG001080.
InParanoidiQ9BW19.
KOiK10405.
OMAiWQETAAQ.
PhylomeDBiQ9BW19.
TreeFamiTF105237.

Enzyme and pathway databases

ReactomeiREACT_25201. Kinesins.

Miscellaneous databases

ChiTaRSiKIFC1. human.
EvolutionaryTraceiQ9BW19.
GeneWikiiKIFC1.
GenomeRNAii3833.
NextBioi15065.
PROiQ9BW19.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BW19.
CleanExiHS_KIFC1.
ExpressionAtlasiQ9BW19. baseline and differential.
GenevisibleiQ9BW19. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKIFC1_HUMAN
AccessioniPrimary (citable) accession number: Q9BW19
Secondary accession number(s): O60887
, Q14834, Q4KMP0, Q5SU09, Q6GMS7, Q6P4A5, Q9UQP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2002
Last modified: July 22, 2015
This is version 136 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.