KI26A_HUMAN
ID KI26A_HUMAN Reviewed; 1882 AA.
AC Q9ULI4; Q8TAZ7; Q96GK3; Q9UFL3;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Kinesin-like protein KIF26A;
GN Name=KIF26A; Synonyms=KIAA1236;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 43-1882.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1284-1882.
RC TISSUE=Brain, and Muscle;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1615-1882.
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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-885; SER-1262 AND
RP SER-1662, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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: Atypical kinesin that plays a key role in enteric neuron
CC development. Acts by repressing a cell growth signaling pathway in the
CC enteric nervous system development, possibly via its interaction with
CC GRB2 that prevents GRB2-binding to SHC, thereby attenating the GDNF-Ret
CC signaling. Binds to microtubules but lacks microtubule-based motility
CC due to the absence of ATPase activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GRB2 (via SH2 domain). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9ULI4; P78358: CTAG1B; NbExp=3; IntAct=EBI-1642152, EBI-1188472;
CC Q9ULI4; Q8IYX1: TBC1D21; NbExp=9; IntAct=EBI-1642152, EBI-12018146;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIF26 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
CC -!- CAUTION: In contrast to other kinesin-like proteins, residues required
CC for ATPase activity are missing. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH09415.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL359399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB033062; BAA86550.2; -; mRNA.
DR EMBL; BC009415; AAH09415.1; ALT_INIT; mRNA.
DR EMBL; BC025353; AAH25353.1; -; mRNA.
DR EMBL; AL117589; CAB56009.1; -; mRNA.
DR CCDS; CCDS45171.1; -.
DR PIR; T17319; T17319.
DR RefSeq; NP_056471.1; NM_015656.1.
DR AlphaFoldDB; Q9ULI4; -.
DR SMR; Q9ULI4; -.
DR BioGRID; 117584; 14.
DR IntAct; Q9ULI4; 14.
DR STRING; 9606.ENSP00000388241; -.
DR iPTMnet; Q9ULI4; -.
DR PhosphoSitePlus; Q9ULI4; -.
DR BioMuta; KIF26A; -.
DR DMDM; 160014128; -.
DR EPD; Q9ULI4; -.
DR jPOST; Q9ULI4; -.
DR MassIVE; Q9ULI4; -.
DR MaxQB; Q9ULI4; -.
DR PaxDb; Q9ULI4; -.
DR PeptideAtlas; Q9ULI4; -.
DR PRIDE; Q9ULI4; -.
DR ProteomicsDB; 85039; -.
DR Antibodypedia; 28168; 85 antibodies from 14 providers.
DR DNASU; 26153; -.
DR Ensembl; ENST00000423312.7; ENSP00000388241.2; ENSG00000066735.15.
DR GeneID; 26153; -.
DR KEGG; hsa:26153; -.
DR MANE-Select; ENST00000423312.7; ENSP00000388241.2; NM_015656.2; NP_056471.1.
DR UCSC; uc001yos.5; human.
DR CTD; 26153; -.
DR DisGeNET; 26153; -.
DR GeneCards; KIF26A; -.
DR HGNC; HGNC:20226; KIF26A.
DR HPA; ENSG00000066735; Low tissue specificity.
DR MIM; 613231; gene.
DR neXtProt; NX_Q9ULI4; -.
DR OpenTargets; ENSG00000066735; -.
DR PharmGKB; PA134888008; -.
DR VEuPathDB; HostDB:ENSG00000066735; -.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000159075; -.
DR InParanoid; Q9ULI4; -.
DR OMA; GECDAQA; -.
DR OrthoDB; 29955at2759; -.
DR PhylomeDB; Q9ULI4; -.
DR TreeFam; TF105235; -.
DR PathwayCommons; Q9ULI4; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q9ULI4; -.
DR BioGRID-ORCS; 26153; 5 hits in 1065 CRISPR screens.
DR ChiTaRS; KIF26A; human.
DR GenomeRNAi; 26153; -.
DR Pharos; Q9ULI4; Tbio.
DR PRO; PR:Q9ULI4; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9ULI4; protein.
DR Bgee; ENSG00000066735; Expressed in ganglionic eminence and 119 other tissues.
DR ExpressionAtlas; Q9ULI4; baseline and differential.
DR Genevisible; Q9ULI4; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0048484; P:enteric nervous system development; ISS:UniProtKB.
DR GO; GO:0009968; P:negative regulation of signal transduction; ISS:UniProtKB.
DR GO; GO:0001560; P:regulation of cell growth by extracellular stimulus; ISS:UniProtKB.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..1882
FT /note="Kinesin-like protein KIF26A"
FT /id="PRO_0000307299"
FT DOMAIN 371..725
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1784..1812
FT /evidence="ECO:0000255"
FT COMPBIAS 947..961
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1475
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1620..1638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1660..1690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 469..476
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 1284..1287
FT /note="VDGC -> ERER (in Ref. 4; AAH25353)"
FT /evidence="ECO:0000305"
FT CONFLICT 1513
FT /note="P -> L (in Ref. 4; AAH25353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1882 AA; 194590 MW; C35E3458BCF3D147 CRC64;
MVGRGVPLCA AQPAVAEGGP AREPPPLLEV SPRKRLPAGP DQDPCGSRPA PEGAGAGPEQ
GHSAGGGGWC RHCHTKLVEL KRQAWKLVSG PGTTLRDPCL SALLLDKLPA PGALPACRPE
AERRCDVCAT HLQQLTREAM HLLQAPASHE DLDAPHGGPS LAPPSTTTSS RDTPGPAGPA
GRQPGRAGPD RTKGLAWSPG PSVQVSVAPA GLGGALSTVT IQAQQCLEGM WSVSRVNSFL
PPACLAEAAV AAVAVADTVR ECPPVAGPDG LSKAWGRGGV CTSALVTPTP GSVGGSTGPS
AAASFFIRAM QKLSLASKRK KPHPPPPPAT RGTSTYPTDF SGVLQLWPPP APPCLLRAAS
KTKDNPGSIG KVKVMLRIWP AQGAQRSAEA MSFLKVDPRK KQVILYDPAA GPPGSAGPRR
AATAAVPKMF AFDAVFPQDS EQAEVCSGTV ADVLQSVVSG ADGCIFSFGH MSLGKSYTMI
GKDSSPQSLG IVPCAISWLF RLIEERRERT GTRFSVRVSA VEVCGRDQSL RDLLAEVAPG
SLQDTQSPGV YLREDPVCGA QLQNQSELRA PTAEKAAFYL DAALAARSTS RAGCGEDARR
SSHMLFTLHV YQYRMEKCGR GGMSGGRSRL HLIDLGSCEA AAGRAGEAAG GPLCLSLSAL
GSVILALVNG AKHVPYRDHR LTMLLRESLA TAGCRTTMIA HVSDAPAQHA ETLSTVQLAA
RIHRLRRKKA KYASSSSGGE SSCEEGRARR PPHLRPFHPR TVALDPDRTP PCLPGDPDYS
SSSEQSCDTV IYVGPGGAAL SDRELTDNEG PPDFVPIIPA LSRHRPSKGP RDADHFRCST
FAELQERLEC MDGNEGPSGG PGGTDGAQAS PARGGRKPSP PEAASPRKAV GTPMAASTPR
GSSGPDTHQG TPEPCKAIVW GDQREDSSAW PELLVPEKAA VSGGRRPLPS PAPPPPQLLE
ACRAPEEPGG GGTDGVARTP PVGMSGQVAG SPMLPGATCP RLAAGSRCPE RGLLTTTVTL
QRPVELNGED ELVFTVVEEL SLGALAGAGR PTSLASFDSD CSLRALASGS RPVSIISSIN
DEFDAYTSQA PEGGPLEGAA WAGSSHGSSI SSWLSEVSVC TADSRDPTPQ PRFSPDSLAG
LDPGGPPALD GSLGDGSSGF LGPDRPDSPG PTWGPCPGEV AAVAPSRPGR EPQAGPSRWA
SAAQTIHSSL PRKPRTASAT TRVGCARLGQ SPPGRGGLFE DPWLLRVGEC DTQAASAGRA
PSPTLGSPRL PEAQVMLACA QRVVDGCEVA ARAARRPEAV ARIPPLRRGA TTLGVTTPAV
SWGDAPTEVV ACSGSLKASP TSKKGLAPKA GFLPRPSGAA PPAPPTRKSS LEQRSSPASA
PPHAVNPARV GAAAVLRGEE EPRPSSRADH SVPRATSSLK ARASKVEAAH RLAGHASLER
YEGLAHSSSK GREAPGRPPR AVPKLGVPPS SPTHGPAPAC RSGAAKAVGA PKPPVGGGKG
RGLVAGGSRA LGPSVKLSTA SVTGRSPGGP VAGPRAAPRA GPSVGAKAGR GTVMGTKQAL
RAAHSRVHEL SASGAPGRGG SSWGSADSDS GHDSGVNVGE ERPPTGPALP SPYSKVTAPR
RPQRYSSGHG SDNSSVLSGE LPPAMGRTAL FHHSGGSSGY ESLRRDSEAT GSASSAPDSM
SESGAASPGA RTRSLKSPKK RATGLQRRRL IPAPLPDTTA LGRKPSLPGQ WVDLPPPLAG
SLKEPFEIKV YEIDDVERLQ RPRPTPREAP TQGLACVSTR LRLAERRQQR LREVQAKHKH
LCEELAETQG RLMLEPGRWL EQFEVDPELE PESAEYLAAL ERATAALEQC VNLCKAHVMM
VTCFDISVAA SAAIPGPQEV DV
