ID   KIF25_HUMAN             Reviewed;         384 AA.
AC   Q9UIL4; A8K0C3; O94775; Q5SZU9;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   24-JAN-2024, entry version 178.
DE   RecName: Full=Kinesin-like protein KIF25 {ECO:0000305};
DE   AltName: Full=Kinesin-like protein 3 {ECO:0000303|PubMed:9925916};
GN   Name=KIF25 {ECO:0000312|HGNC:HGNC:6390};
GN   Synonyms=KNSL3 {ECO:0000303|PubMed:9925916};
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 [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING, AND VARIANT
RP   MET-28.
RX   PubMed=9925916; DOI=10.1159/000015159;
RA   Okamoto S., Matsushima M., Nakamura Y.;
RT   "Identification, genomic organization, and alternative splicing of KNSL3, a
RT   novel human gene encoding a kinesin-like protein.";
RL   Cytogenet. Cell Genet. 83:25-29(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
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   [4]
RP   FUNCTION.
RX   PubMed=22354037; DOI=10.1038/emboj.2012.36;
RA   McKnight N.C., Jefferies H.B., Alemu E.A., Saunders R.E., Howell M.,
RA   Johansen T., Tooze S.A.;
RT   "Genome-wide siRNA screen reveals amino acid starvation-induced autophagy
RT   requires SCOC and WAC.";
RL   EMBO J. 31:1931-1946(2012).
RN   [5]
RP   FUNCTION.
RX   PubMed=28263957; DOI=10.1038/ncb3486;
RA   Decarreau J., Wagenbach M., Lynch E., Halpern A.R., Vaughan J.C.,
RA   Kollman J., Wordeman L.;
RT   "The tetrameric kinesin Kif25 suppresses pre-mitotic centrosome separation
RT   to establish proper spindle orientation.";
RL   Nat. Cell Biol. 19:384-390(2017).
CC   -!- FUNCTION: Minus-end microtubule-dependent motor protein (By
CC       similarity). Acts as a negative regulator of centrosome separation
CC       required to prevent premature centrosome separation during interphase
CC       (PubMed:28263957). Required to maintain a centered nucleus to ensure
CC       that the spindle is stably oriented at the onset of mitosis
CC       (PubMed:28263957). May also act as a negative regulator of amino acid
CC       starvation-induced autophagy (PubMed:22354037).
CC       {ECO:0000250|UniProtKB:Q4R918, ECO:0000269|PubMed:22354037,
CC       ECO:0000269|PubMed:28263957}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q4R918}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000250|UniProtKB:Q4R918}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UIL4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UIL4-2; Sequence=VSP_002867;
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC   -!- CAUTION: In contrast to the ortholog protein in primates, human KIF25
CC       protein is shorter at the N-terminus. While the kinesin motor domain is
CC       intact, it is unknown whether the absence of the N-terminus affects the
CC       microtubule-dependent motor activity. {ECO:0000305|PubMed:28263957}.
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DR   EMBL; AB012722; BAA36417.1; -; mRNA.
DR   EMBL; AK289488; BAF82177.1; -; mRNA.
DR   EMBL; AB012723; BAA36418.1; -; Genomic_DNA.
DR   EMBL; AL589733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS5305.1; -. [Q9UIL4-1]
DR   RefSeq; NP_005346.3; NM_005355.3. [Q9UIL4-2]
DR   RefSeq; NP_085118.2; NM_030615.2. [Q9UIL4-1]
DR   RefSeq; XP_011534104.1; XM_011535802.2.
DR   RefSeq; XP_011534105.1; XM_011535803.2. [Q9UIL4-2]
DR   AlphaFoldDB; Q9UIL4; -.
DR   SMR; Q9UIL4; -.
DR   BioGRID; 110032; 1.
DR   IntAct; Q9UIL4; 1.
DR   STRING; 9606.ENSP00000496229; -.
DR   iPTMnet; Q9UIL4; -.
DR   PhosphoSitePlus; Q9UIL4; -.
DR   BioMuta; KIF25; -.
DR   DMDM; 20138788; -.
DR   MassIVE; Q9UIL4; -.
DR   PaxDb; 9606-ENSP00000388878; -.
DR   PeptideAtlas; Q9UIL4; -.
DR   Antibodypedia; 20075; 346 antibodies from 19 providers.
DR   DNASU; 3834; -.
DR   Ensembl; ENST00000443060.6; ENSP00000388878.2; ENSG00000125337.21. [Q9UIL4-1]
DR   Ensembl; ENST00000643607.3; ENSP00000496229.1; ENSG00000125337.21. [Q9UIL4-1]
DR   GeneID; 3834; -.
DR   KEGG; hsa:3834; -.
DR   MANE-Select; ENST00000643607.3; ENSP00000496229.1; NM_030615.4; NP_085118.2.
DR   UCSC; uc003qwk.1; human. [Q9UIL4-1]
DR   AGR; HGNC:6390; -.
DR   CTD; 3834; -.
DR   DisGeNET; 3834; -.
DR   GeneCards; KIF25; -.
DR   HGNC; HGNC:6390; KIF25.
DR   HPA; ENSG00000125337; Tissue enhanced (brain, retina).
DR   MIM; 603815; gene.
DR   neXtProt; NX_Q9UIL4; -.
DR   OpenTargets; ENSG00000125337; -.
DR   PharmGKB; PA30179; -.
DR   VEuPathDB; HostDB:ENSG00000125337; -.
DR   eggNOG; KOG0239; Eukaryota.
DR   GeneTree; ENSGT00940000162166; -.
DR   HOGENOM; CLU_001485_2_2_1; -.
DR   InParanoid; Q9UIL4; -.
DR   OMA; CIGMSGV; -.
DR   OrthoDB; 453489at2759; -.
DR   PhylomeDB; Q9UIL4; -.
DR   TreeFam; TF105234; -.
DR   PathwayCommons; Q9UIL4; -.
DR   Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-HSA-983189; Kinesins.
DR   SignaLink; Q9UIL4; -.
DR   BioGRID-ORCS; 3834; 13 hits in 1152 CRISPR screens.
DR   GenomeRNAi; 3834; -.
DR   Pharos; Q9UIL4; Tbio.
DR   PRO; PR:Q9UIL4; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9UIL4; Protein.
DR   Bgee; ENSG00000125337; Expressed in primordial germ cell in gonad and 106 other cell types or tissues.
DR   ExpressionAtlas; Q9UIL4; baseline and differential.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0008569; F:minus-end-directed microtubule motor activity; ISS:UniProtKB.
DR   GO; GO:0051294; P:establishment of spindle orientation; IDA:UniProtKB.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; TAS:ProtInc.
DR   GO; GO:0010507; P:negative regulation of autophagy; IMP:BHF-UCL.
DR   GO; GO:0046603; P:negative regulation of mitotic centrosome separation; IDA:UniProtKB.
DR   GO; GO:0051647; P:nucleus localization; IDA:UniProtKB.
DR   GO; GO:0006996; P:organelle organization; TAS:ProtInc.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
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   PANTHER; PTHR24115:SF421; KINESIN-LIKE PROTEIN KIF25; 1.
DR   PANTHER; PTHR24115; KINESIN-RELATED; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   Genevisible; Q9UIL4; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton; Microtubule;
KW   Motor protein; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..384
FT                   /note="Kinesin-like protein KIF25"
FT                   /id="PRO_0000125435"
FT   DOMAIN          7..363
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          217..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   VAR_SEQ         278..329
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002867"
FT   VARIANT         28
FT                   /note="K -> M (in dbSNP:rs4708626)"
FT                   /evidence="ECO:0000269|PubMed:9925916"
FT                   /id="VAR_059369"
FT   VARIANT         41
FT                   /note="A -> T (in dbSNP:rs34049091)"
FT                   /id="VAR_061280"
FT   VARIANT         229
FT                   /note="T -> P (in dbSNP:rs12197062)"
FT                   /id="VAR_049687"
FT   VARIANT         255
FT                   /note="A -> T (in dbSNP:rs2073634)"
FT                   /id="VAR_049688"
FT   CONFLICT        185
FT                   /note="A -> T (in Ref. 2; BAF82177)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   384 AA;  40686 MW;  7739D463BCFDB429 CRC64;
     MTWTSGQLQR EKQARPGSGA VLAFPDDKDL RVYGPAESQS AVFGDVCPLL TSLLDGYNVC
     VMAYGQTGSG KSYTMLGRHS DDGPVLPLDP QSDLGIIPRV AEELFRLILE NTSRSPKVEV
     SIVEVYNNDI FDLLAKDSIA AVSGVKREVV TAKDGRTEVA LLASEAVGSA SKLMELVHGG
     LQLRAKHPTL VHADSSRSHL IITVTLTTAS CSDSTADQAC SATLPREQTE AGRAGRSRRA
     SQGALAPQLV PGNPAGHAEQ VQARLQLVDS AGSECVGVSG VTGLALREMA CISRSLAALA
     GVLGALLEHR GHAPYRNSRL THLLQDCLGG DAKLLVILCI SPSQRHLAQT LQGLGFGIRA
     RQVQRGPARK KPPSSQTEGK RRPD
//