KIF27_HUMAN
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 03-AUG-2022, entry version 152.
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};
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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. [Q86VH2-2]
DR RefSeq; XP_016870397.1; XM_017014908.1. [Q86VH2-3]
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 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; Q86VH2; -.
DR PeptideAtlas; Q86VH2; -.
DR PRIDE; Q86VH2; -.
DR ProteomicsDB; 70013; -. [Q86VH2-1]
DR ProteomicsDB; 70014; -. [Q86VH2-2]
DR ProteomicsDB; 70015; -. [Q86VH2-3]
DR ProteomicsDB; 70016; -. [Q86VH2-4]
DR Antibodypedia; 13061; 68 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 CTD; 55582; -.
DR DisGeNET; 55582; -.
DR GeneCards; KIF27; -.
DR HGNC; HGNC:18632; KIF27.
DR HPA; ENSG00000165115; Tissue enhanced (choroid plexus, 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; SDLCGTE; -.
DR OrthoDB; 369179at2759; -.
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 1071 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 102 other tissues.
DR ExpressionAtlas; Q86VH2; baseline and differential.
DR Genevisible; Q86VH2; HS.
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 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 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
