KIFC1_HUMAN
ID KIFC1_HUMAN Reviewed; 673 AA.
AC Q9BW19; O60887; Q14834; Q4KMP0; Q5SU09; Q6GMS7; Q6P4A5; Q9UQP7;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Kinesin-like protein KIFC1;
DE AltName: Full=Kinesin-like protein 2;
DE AltName: Full=Kinesin-related protein HSET;
GN Name=KIFC1; Synonyms=HSET, KNSL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-219.
RX PubMed=10369922; DOI=10.1007/s002510050660;
RA Janitz K., Wild A., Beck S., Savasta S., Beluffi G., Ziegler A., Volz A.;
RT "Genomic organization of the HSET locus and the possible association of
RT HLA-linked genes with immotile cilia syndrome (ICS).";
RL Immunogenetics 49:644-652(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Kidney, Muscle, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 155-673.
RC TISSUE=Testis;
RX PubMed=8276466; DOI=10.1007/bf00241260;
RA Ando A., Yara-Kikuti Y., Kawata H., Okamoto N., Imai T., Eki T.,
RA Yokoyama K., Soeda E., Ikemura T., Abe K., Inoko H.;
RT "Cloning of a new kinesin-related gene located at the centromeric end of
RT the human MHC region.";
RL Immunogenetics 39:194-200(1994).
RN [5]
RP FUNCTION.
RX PubMed=15843429; DOI=10.1091/mbc.e05-02-0167;
RA Zhu C., Zhao J., Bibikova M., Leverson J.D., Bossy-Wetzel E., Fan J.-B.,
RA Abraham R.T., Jiang W.;
RT "Functional analysis of human microtubule-based motor proteins, the
RT kinesins and dyneins, in mitosis/cytokinesis using RNA interference.";
RL Mol. Biol. Cell 16:3187-3199(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-26; SER-33 AND
RP THR-359, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Minus end-directed microtubule-dependent motor required for
CC bipolar spindle formation (PubMed:15843429). May contribute to movement
CC of early endocytic vesicles (By similarity). Regulates cilium formation
CC and structure (By similarity). {ECO:0000250|UniProtKB:Q9QWT9,
CC ECO:0000269|PubMed:15843429}.
CC -!- SUBUNIT: Binds NUBP1 and NUBP2. Interacts with PPP1R42 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9QWT9}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q9QWT9}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q9QWT9}. Early endosome
CC {ECO:0000250|UniProtKB:Q9QWT9}. Note=Associated with nucleus during
CC interphase, centrosomes in early and spindle in later mitosis.
CC {ECO:0000250|UniProtKB:Q9QWT9}.
CC -!- MISCELLANEOUS: HeLa cells lacking KIFC1 show multipolar mitotic
CC spindles and a defect in chromosome congression and chromosome
CC alignment during mitosis.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. NCD subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00712.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH63567.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH73878.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH98438.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA03509.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ010479; CAA09217.1; -; mRNA.
DR EMBL; AL021366; CAA16157.1; -; Genomic_DNA.
DR EMBL; AL050332; CAB63782.1; -; Genomic_DNA.
DR EMBL; AL662799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX088650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX248088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000712; AAH00712.2; ALT_INIT; mRNA.
DR EMBL; BC063567; AAH63567.1; ALT_INIT; mRNA.
DR EMBL; BC073878; AAH73878.1; ALT_INIT; mRNA.
DR EMBL; BC098438; AAH98438.1; ALT_INIT; mRNA.
DR EMBL; BC121041; AAI21042.1; -; mRNA.
DR EMBL; BC121042; AAI21043.1; -; mRNA.
DR EMBL; D14678; BAA03509.1; ALT_FRAME; mRNA.
DR CCDS; CCDS34430.1; -.
DR PIR; I54523; I54523.
DR RefSeq; NP_002254.2; NM_002263.3.
DR PDB; 5WDH; X-ray; 2.25 A; A=307-663.
DR PDBsum; 5WDH; -.
DR AlphaFoldDB; Q9BW19; -.
DR SMR; Q9BW19; -.
DR BioGRID; 110031; 73.
DR IntAct; Q9BW19; 29.
DR MINT; Q9BW19; -.
DR STRING; 9606.ENSP00000393963; -.
DR BindingDB; Q9BW19; -.
DR ChEMBL; CHEMBL3351200; -.
DR iPTMnet; Q9BW19; -.
DR PhosphoSitePlus; Q9BW19; -.
DR SwissPalm; Q9BW19; -.
DR BioMuta; KIFC1; -.
DR DMDM; 20138710; -.
DR EPD; Q9BW19; -.
DR jPOST; Q9BW19; -.
DR MassIVE; Q9BW19; -.
DR MaxQB; Q9BW19; -.
DR PaxDb; Q9BW19; -.
DR PeptideAtlas; Q9BW19; -.
DR PRIDE; Q9BW19; -.
DR ProteomicsDB; 79250; -.
DR Antibodypedia; 29133; 159 antibodies from 29 providers.
DR DNASU; 3833; -.
DR Ensembl; ENST00000374523.8; ENSP00000363647.4; ENSG00000204197.9.
DR Ensembl; ENST00000428849.7; ENSP00000393963.2; ENSG00000237649.8.
DR Ensembl; ENST00000448818.6; ENSP00000407885.2; ENSG00000233450.7.
DR GeneID; 3833; -.
DR KEGG; hsa:3833; -.
DR MANE-Select; ENST00000428849.7; ENSP00000393963.2; NM_002263.4; NP_002254.2.
DR UCSC; uc003oef.5; human.
DR CTD; 3833; -.
DR DisGeNET; 3833; -.
DR GeneCards; KIFC1; -.
DR HGNC; HGNC:6389; KIFC1.
DR HPA; ENSG00000237649; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 603763; gene.
DR neXtProt; NX_Q9BW19; -.
DR OpenTargets; ENSG00000237649; -.
DR PharmGKB; PA30178; -.
DR VEuPathDB; HostDB:ENSG00000237649; -.
DR eggNOG; KOG0239; Eukaryota.
DR GeneTree; ENSGT00940000161735; -.
DR HOGENOM; CLU_001485_12_4_1; -.
DR InParanoid; Q9BW19; -.
DR OMA; TWTYHDE; -.
DR OrthoDB; 364605at2759; -.
DR PhylomeDB; Q9BW19; -.
DR TreeFam; TF105237; -.
DR PathwayCommons; Q9BW19; -.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q9BW19; -.
DR SIGNOR; Q9BW19; -.
DR BioGRID-ORCS; 3833; 40 hits in 1075 CRISPR screens.
DR ChiTaRS; KIFC1; human.
DR EvolutionaryTrace; Q9BW19; -.
DR GeneWiki; KIFC1; -.
DR GenomeRNAi; 3833; -.
DR Pharos; Q9BW19; Tchem.
DR PRO; PR:Q9BW19; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9BW19; protein.
DR Bgee; ENSG00000237649; Expressed in ventricular zone and 101 other tissues.
DR ExpressionAtlas; Q9BW19; baseline and differential.
DR Genevisible; Q9BW19; HS.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; NAS:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Endosome; Microtubule; Mitosis; Motor protein;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..673
FT /note="Kinesin-like protein KIFC1"
FT /id="PRO_0000125428"
FT DOMAIN 310..663
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 23..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 142..306
FT /evidence="ECO:0000255"
FT COMPBIAS 36..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..342
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 410..417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 359
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 219
FT /note="R -> Q (in dbSNP:rs61736175)"
FT /evidence="ECO:0000269|PubMed:10369922"
FT /id="VAR_012650"
FT CONFLICT 368
FT /note="T -> P (in Ref. 3; AAH00712)"
FT /evidence="ECO:0000305"
FT STRAND 311..317
FT /evidence="ECO:0007829|PDB:5WDH"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:5WDH"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:5WDH"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:5WDH"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:5WDH"
FT HELIX 384..389
FT /evidence="ECO:0007829|PDB:5WDH"
FT HELIX 392..396
FT /evidence="ECO:0007829|PDB:5WDH"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:5WDH"
FT STRAND 404..411
FT /evidence="ECO:0007829|PDB:5WDH"
FT HELIX 416..420
FT /evidence="ECO:0007829|PDB:5WDH"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:5WDH"
FT HELIX 433..449
FT /evidence="ECO:0007829|PDB:5WDH"
FT TURN 450..452
FT /evidence="ECO:0007829|PDB:5WDH"
FT STRAND 453..465
FT /evidence="ECO:0007829|PDB:5WDH"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:5WDH"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:5WDH"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:5WDH"
FT HELIX 510..526
FT /evidence="ECO:0007829|PDB:5WDH"
FT HELIX 535..537
FT /evidence="ECO:0007829|PDB:5WDH"
FT STRAND 538..554
FT /evidence="ECO:0007829|PDB:5WDH"
FT STRAND 556..565
FT /evidence="ECO:0007829|PDB:5WDH"
FT HELIX 596..607
FT /evidence="ECO:0007829|PDB:5WDH"
FT HELIX 615..617
FT /evidence="ECO:0007829|PDB:5WDH"
FT HELIX 619..624
FT /evidence="ECO:0007829|PDB:5WDH"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:5WDH"
FT STRAND 633..640
FT /evidence="ECO:0007829|PDB:5WDH"
FT HELIX 644..646
FT /evidence="ECO:0007829|PDB:5WDH"
FT HELIX 647..662
FT /evidence="ECO:0007829|PDB:5WDH"
SQ SEQUENCE 673 AA; 73748 MW; 9E99737665BF1E92 CRC64;
MDPQRSPLLE VKGNIELKRP LIKAPSQLPL SGSRLKRRPD QMEDGLEPEK KRTRGLGATT
KITTSHPRVP SLTTVPQTQG QTTAQKVSKK TGPRCSTAIA TGLKNQKPVP AVPVQKSGTS
GVPPMAGGKK PSKRPAWDLK GQLCDLNAEL KRCRERTQTL DQENQQLQDQ LRDAQQQVKA
LGTERTTLEG HLAKVQAQAE QGQQELKNLR ACVLELEERL STQEGLVQEL QKKQVELQEE
RRGLMSQLEE KERRLQTSEA ALSSSQAEVA SLRQETVAQA ALLTEREERL HGLEMERRRL
HNQLQELKGN IRVFCRVRPV LPGEPTPPPG LLLFPSGPGG PSDPPTRLSL SRSDERRGTL
SGAPAPPTRH DFSFDRVFPP GSGQDEVFEE IAMLVQSALD GYPVCIFAYG QTGSGKTFTM
EGGPGGDPQL EGLIPRALRH LFSVAQELSG QGWTYSFVAS YVEIYNETVR DLLATGTRKG
QGGECEIRRA GPGSEELTVT NARYVPVSCE KEVDALLHLA RQNRAVARTA QNERSSRSHS
VFQLQISGEH SSRGLQCGAP LSLVDLAGSE RLDPGLALGP GERERLRETQ AINSSLSTLG
LVIMALSNKE SHVPYRNSKL TYLLQNSLGG SAKMLMFVNI SPLEENVSES LNSLRFASKV
NQCVIGTAQA NRK
