Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9BW19

- KIFC1_HUMAN

UniProt

Q9BW19 - KIFC1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Kinesin-like protein KIFC1

Gene

KIFC1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. ATPase activity Source: RefGenome
  2. ATP binding Source: UniProtKB
  3. microtubule motor activity Source: UniProtKB
  4. minus-end-directed microtubule motor activity Source: RefGenome

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. blood coagulation Source: Reactome
  3. metabolic process Source: GOC
  4. microtubule-based movement Source: RefGenome
  5. mitotic sister chromatid segregation Source: UniProtKB
  6. spindle assembly Source: RefGenome
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: Chromosome 6

Organism-specific databases

HGNCiHGNC:6389. KIFC1.

Subcellular locationi

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

GO - Cellular componenti

  1. endosome Source: UniProtKB-KW
  2. kinesin complex Source: RefGenome
  3. membrane Source: UniProtKB
  4. microtubule Source: UniProtKB-KW
  5. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Endosome, Microtubule, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30178.

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.
GenevestigatoriQ9BW19.

Organism-specific databases

HPAiHPA055997.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi110031. 7 interactions.
IntActiQ9BW19. 5 interactions.
MINTiMINT-3062538.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiQISGEHS.
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 BAA03509.1 differs from that shown. Reason: Frameshift at positions 223 and 256.
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.

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:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi20138710.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS34430.1.
PIRi I54523.
RefSeqi NP_002254.2. NM_002263.3.
UniGenei Hs.436912.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2REP X-ray 2.60 A 307-663 [» ]
ProteinModelPortali Q9BW19.
SMRi Q9BW19. Positions 262-661.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110031. 7 interactions.
IntActi Q9BW19. 5 interactions.
MINTi MINT-3062538.

PTM databases

PhosphoSitei Q9BW19.

Polymorphism databases

DMDMi 20138710.

Proteomic databases

MaxQBi Q9BW19.
PaxDbi Q9BW19.
PeptideAtlasi Q9BW19.
PRIDEi Q9BW19.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374523 ; ENSP00000363647 ; ENSG00000204197 .
ENST00000428849 ; ENSP00000393963 ; ENSG00000237649 .
ENST00000448818 ; ENSP00000407885 ; ENSG00000233450 .
GeneIDi 3833.
KEGGi hsa:3833.
UCSCi uc003oef.4. human.

Organism-specific databases

CTDi 3833.
GeneCardsi GC06P033359.
GC06Pn33288.
GC06Po33498.
HGNCi HGNC:6389. KIFC1.
HPAi HPA055997.
MIMi 603763. gene.
neXtProti NX_Q9BW19.
PharmGKBi PA30178.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5059.
GeneTreei ENSGT00550000074610.
HOVERGENi HBG001080.
InParanoidi Q9BW19.
KOi K10405.
OMAi QISGEHS.
PhylomeDBi Q9BW19.
TreeFami TF105237.

Enzyme and pathway databases

Reactomei REACT_25201. Kinesins.

Miscellaneous databases

EvolutionaryTracei Q9BW19.
GeneWikii KIFC1.
GenomeRNAii 3833.
NextBioi 15065.
PROi Q9BW19.
SOURCEi Search...

Gene expression databases

Bgeei Q9BW19.
CleanExi HS_KIFC1.
ExpressionAtlasi Q9BW19. baseline and differential.
Genevestigatori Q9BW19.

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

« 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: October 29, 2014
This is version 128 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