ID KIF27_HUMAN Reviewed; 1401 AA. AC Q86VH2; B2RTR8; Q5T6W0; Q86VH0; Q86VH1; Q9UF54; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 160. DE RecName: Full=Kinesin-like protein KIF27; GN Name=KIF27; 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] (ISOFORMS 1; 2 AND 3). RX PubMed=12783626; DOI=10.1186/1471-2164-4-22; RA Oduru S., Campbell J.L., Karri S., Hendry W.J., Khan S.A., Williams S.C.; RT "Gene discovery in the hamster: a comparative genomics approach for gene RT annotation by sequencing of hamster testis cDNAs."; RL BMC Genomics 4:22-22(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING RP (ISOFORM 4). RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [LARGE SCALE MRNA] OF 569-1401 (ISOFORM 1), AND VARIANT RP ASP-1036. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). CC -!- FUNCTION: Plays an essential role in motile ciliogenesis. CC {ECO:0000250}. CC -!- SUBUNIT: Interacts with STK36. {ECO:0000250}. CC -!- INTERACTION: CC Q86VH2; P43357: MAGEA3; NbExp=3; IntAct=EBI-7950718, EBI-5651459; CC Q86VH2; P43360: MAGEA6; NbExp=3; IntAct=EBI-7950718, EBI-1045155; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell CC projection, cilium {ECO:0000250}. Note=Localizes to centrioles and CC basal bodies. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=KIF27A; CC IsoId=Q86VH2-1; Sequence=Displayed; CC Name=2; Synonyms=KIF27B; CC IsoId=Q86VH2-2; Sequence=VSP_028603; CC Name=3; Synonyms=KIF27C; CC IsoId=Q86VH2-3; Sequence=VSP_028604; CC Name=4; CC IsoId=Q86VH2-4; Sequence=VSP_028602, VSP_028605, VSP_028606; CC -!- TISSUE SPECIFICITY: Testis, pancreatic islet, germ cell tumors and CC Jurkat T-cells. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Kinesin family. KIF27 subfamily. {ECO:0000255|PROSITE- CC ProRule:PRU00283}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB63770.1; 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; AY237536; AAP04413.1; -; mRNA. DR EMBL; AY237537; AAP04414.1; -; mRNA. DR EMBL; AY237538; AAP04415.1; -; mRNA. DR EMBL; AL354733; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC140788; AAI40789.1; -; mRNA. DR EMBL; AL133654; CAB63770.1; ALT_FRAME; mRNA. DR CCDS; CCDS65071.1; -. [Q86VH2-2] DR CCDS; CCDS65072.1; -. [Q86VH2-3] DR CCDS; CCDS6665.1; -. [Q86VH2-1] DR PIR; T43446; T43446. DR RefSeq; NP_001258856.1; NM_001271927.1. [Q86VH2-2] DR RefSeq; NP_001258857.1; NM_001271928.1. [Q86VH2-3] DR RefSeq; NP_060046.1; NM_017576.2. [Q86VH2-1] DR RefSeq; XP_016870392.1; XM_017014903.1. [Q86VH2-1] DR RefSeq; XP_016870393.1; XM_017014904.1. [Q86VH2-1] DR RefSeq; XP_016870396.1; XM_017014907.1. DR RefSeq; XP_016870397.1; XM_017014908.1. DR AlphaFoldDB; Q86VH2; -. DR SMR; Q86VH2; -. DR BioGRID; 120730; 15. DR IntAct; Q86VH2; 6. DR MINT; Q86VH2; -. DR STRING; 9606.ENSP00000297814; -. DR ChEMBL; CHEMBL3879867; -. DR GlyCosmos; Q86VH2; 2 sites, 1 glycan. DR GlyGen; Q86VH2; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q86VH2; -. DR PhosphoSitePlus; Q86VH2; -. DR BioMuta; KIF27; -. DR DMDM; 74750464; -. DR EPD; Q86VH2; -. DR jPOST; Q86VH2; -. DR MassIVE; Q86VH2; -. DR MaxQB; Q86VH2; -. DR PaxDb; 9606-ENSP00000297814; -. DR PeptideAtlas; Q86VH2; -. DR ProteomicsDB; 70013; -. [Q86VH2-1] DR ProteomicsDB; 70014; -. [Q86VH2-2] DR ProteomicsDB; 70015; -. [Q86VH2-3] DR ProteomicsDB; 70016; -. [Q86VH2-4] DR Antibodypedia; 13061; 71 antibodies from 15 providers. DR DNASU; 55582; -. DR Ensembl; ENST00000297814.7; ENSP00000297814.2; ENSG00000165115.15. [Q86VH2-1] DR Ensembl; ENST00000334204.6; ENSP00000333928.2; ENSG00000165115.15. [Q86VH2-3] DR Ensembl; ENST00000376347.1; ENSP00000365525.1; ENSG00000165115.15. [Q86VH2-4] DR Ensembl; ENST00000413982.5; ENSP00000401688.1; ENSG00000165115.15. [Q86VH2-2] DR GeneID; 55582; -. DR KEGG; hsa:55582; -. DR MANE-Select; ENST00000297814.7; ENSP00000297814.2; NM_017576.4; NP_060046.1. DR UCSC; uc004ana.6; human. [Q86VH2-1] DR AGR; HGNC:18632; -. DR CTD; 55582; -. DR DisGeNET; 55582; -. DR GeneCards; KIF27; -. DR HGNC; HGNC:18632; KIF27. DR HPA; ENSG00000165115; Tissue enhanced (testis). DR MIM; 611253; gene. DR neXtProt; NX_Q86VH2; -. DR OpenTargets; ENSG00000165115; -. DR PharmGKB; PA134912901; -. DR VEuPathDB; HostDB:ENSG00000165115; -. DR eggNOG; KOG0244; Eukaryota. DR GeneTree; ENSGT00940000157487; -. DR HOGENOM; CLU_005591_0_0_1; -. DR InParanoid; Q86VH2; -. DR OMA; YVIMNTF; -. DR OrthoDB; 5395177at2759; -. DR PhylomeDB; Q86VH2; -. DR TreeFam; TF325946; -. DR PathwayCommons; Q86VH2; -. DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic. DR Reactome; R-HSA-983189; Kinesins. DR SignaLink; Q86VH2; -. DR BioGRID-ORCS; 55582; 12 hits in 1147 CRISPR screens. DR ChiTaRS; KIF27; human. DR GenomeRNAi; 55582; -. DR Pharos; Q86VH2; Tbio. DR PRO; PR:Q86VH2; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q86VH2; Protein. DR Bgee; ENSG00000165115; Expressed in right uterine tube and 103 other cell types or tissues. DR ExpressionAtlas; Q86VH2; baseline and differential. DR GO; GO:0005929; C:cilium; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005576; C:extracellular region; IEA:GOC. 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:0060271; P:cilium assembly; ISS:UniProtKB. DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IEA:Ensembl. DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl. DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central. DR GO; GO:0021591; P:ventricular system development; IEA:Ensembl. DR CDD; cd01372; KISc_KIF4; 1. 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; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1. DR PANTHER; PTHR47969:SF22; KINESIN FAMILY MEMBER 27; 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; Q86VH2; HS. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cell projection; Cilium; KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton; KW Microtubule; Motor protein; Nucleotide-binding; Phosphoprotein; KW Reference proteome. FT CHAIN 1..1401 FT /note="Kinesin-like protein KIF27" FT /id="PRO_0000307143" FT DOMAIN 5..341 FT /note="Kinesin motor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" FT REGION 643..662 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1259..1332 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 352..413 FT /evidence="ECO:0000255" FT COILED 489..557 FT /evidence="ECO:0000255" FT COILED 705..886 FT /evidence="ECO:0000255" FT COILED 916..1070 FT /evidence="ECO:0000255" FT COILED 1118..1154 FT /evidence="ECO:0000255" FT COILED 1190..1219 FT /evidence="ECO:0000255" FT COMPBIAS 643..659 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1264..1282 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 84..91 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" FT MOD_RES 643 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7M6Z4" FT MOD_RES 646 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7M6Z4" FT MOD_RES 672 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7M6Z5" FT MOD_RES 675 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7M6Z5" FT MOD_RES 704 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7M6Z5" FT MOD_RES 999 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7M6Z5" FT MOD_RES 1367 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7M6Z5" FT MOD_RES 1389 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7M6Z5" FT VAR_SEQ 1..609 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_028602" FT VAR_SEQ 816..881 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12783626" FT /id="VSP_028603" FT VAR_SEQ 882..978 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12783626" FT /id="VSP_028604" FT VAR_SEQ 882..896 FT /note="EIQLKTGQEEGLKPK -> VILSYIPAKYNMKC (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_028605" FT VAR_SEQ 897..1401 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_028606" FT VARIANT 213 FT /note="I -> V (in dbSNP:rs12001918)" FT /id="VAR_035361" FT VARIANT 300 FT /note="R -> Q (in dbSNP:rs35594736)" FT /id="VAR_035362" FT VARIANT 1036 FT /note="N -> D (in dbSNP:rs55654273)" FT /evidence="ECO:0000269|PubMed:17974005" FT /id="VAR_061286" SQ SEQUENCE 1401 AA; 160283 MW; 4563BA414C30DB21 CRC64; MEEIPVKVAV RIRPLLCKEA LHNHQVCVRV IPNSQQVIIG RDRVFTFDFV FGKNSTQDEV YNTCIKPLVL SLIEGYNATV FAYGQTGSGK TYTIGGGHIA SVVEGQKGII PRAIQEIFQS ISEHPSIDFN VKVSYIEVYK EDLRDLLELE TSMKDLHIRE DEKGNTVIVG AKECHVESAG EVMSLLEMGN AARHTGTTQM NEHSSRSHAI FTISICQVHK NMEAAEDGSW YSPRHIVSKF HFVDLAGSER VTKTGNTGER FKESIQINSG LLALGNVISA LGDPRRKSSH IPYRDAKITR LLKDSLGGSA KTVMITCVSP SSSNFDESLN SLKYANRARN IRNKPTVNFS PESDRIDEME FEIKLLREAL QSQQAGVSQT TQINREGSPD TNRIHSLEEQ VAQLQGECLG YQCCVEEAFT FLVDLKDTVR LNEKQQHKLQ EWFNMIQEVR KAVLTSFRGI GGTASLEEGP QHVTVLQLKR ELKKCQCVLA ADEVVFNQKE LEVKELKNQV QMMVQENKGH AVSLKEAQKV NRLQNEKIIE QQLLVDQLSE ELTKLNLSVT SSAKENCGDG PDARIPERRP YTVPFDTHLG HYIYIPSRQD SRKVHTSPPM YSLDRIFAGF RTRSQMLLGH IEEQDKVLHC QFSDNSDDEE SEGQEKSGTR CRSRSWIQKP DSVCSLVELS DTQDETQKSD LENEDLKIDC LQESQELNLQ KLKNSERILT EAKQKMRELT INIKMKEDLI KELIKTGNDA KSVSKQYSLK VTKLEHDAEQ AKVELIETQK QLQELENKDL SDVAMKVKLQ KEFRKKMDAA KLRVQVLQKK QQDSKKLASL SIQNEKRANE LEQSVDHMKY QKIQLQRKLR EENEKRKQLD AVIKRDQQKI KEIQLKTGQE EGLKPKAEDL DACNLKRRKG SFGSIDHLQK LDEQKKWLDE EVEKVLNQRQ ELEELEADLK KREAIVSKKE ALLQEKSHLE NKKLRSSQAL NTDSLKISTR LNLLEQELSE KNVQLQTSTA EEKTKISEQV EVLQKEKDQL QKRRHNVDEK LKNGRVLSPE EEHVLFQLEE GIEALEAAIE YRNESIQNRQ KSLRASFHNL SRGEANVLEK LACLSPVEIR TILFRYFNKV VNLREAERKQ QLYNEEMKMK VLERDNMVRE LESALDHLKL QCDRRLTLQQ KEHEQKMQLL LHHFKEQDGE GIMETFKTYE DKIQQLEKDL YFYKKTSRDH KKKLKELVGE AIRRQLAPSE YQEAGDGVLK PEGGGMLSEE LKWASRPESM KLSGREREMD SSASSLRTQP NPQKLWEDIP ELPPIHSSLA PPSGHMLGNE NKTETDDNQF TKSHSRLSSQ IQVVGNVGRL HGVTPVKLCR KELRQISALE LSLRRSSLGV GIGSMAADSI EVSRKPRDLK T //