KI26B_HUMAN
ID KI26B_HUMAN Reviewed; 2108 AA.
AC Q2KJY2; Q6ZQR9; Q6ZUZ0; Q8IUN3; Q8IVR1; Q9NWB4;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Kinesin-like protein KIF26B;
GN Name=KIF26B;
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] (ISOFORM 1).
RA Parnau J., Cox J., Mallya U., Raymond L.;
RT "Cloning, characterization and tissue expression of the novel human gene
RT KIF26B.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-349 AND 701-1443 (ISOFORM 1),
RP AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1542-2108 (ISOFORMS 1/2).
RC TISSUE=Brain, Embryo, and Peripheral blood;
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 MRNA] OF 1-1203 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-333 (ISOFORM 1).
RC TISSUE=Brain;
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 VARIANT ASN-1904.
RX PubMed=29053796; DOI=10.1093/brain/awx251;
RA Nibbeling E.A.R., Duarri A., Verschuuren-Bemelmans C.C., Fokkens M.R.,
RA Karjalainen J.M., Smeets C.J.L.M., de Boer-Bergsma J.J., van der Vries G.,
RA Dooijes D., Bampi G.B., van Diemen C., Brunt E., Ippel E., Kremer B.,
RA Vlak M., Adir N., Wijmenga C., van de Warrenburg B.P.C., Franke L.,
RA Sinke R.J., Verbeek D.S.;
RT "Exome sequencing and network analysis identifies shared mechanisms
RT underlying spinocerebellar ataxia.";
RL Brain 140:2860-2878(2017).
CC -!- FUNCTION: Essential for embryonic kidney development. Plays an
CC important role in the compact adhesion between mesenchymal cells
CC adjacent to the ureteric buds, possibly by interacting with MYH10. This
CC could lead to the establishment of the basolateral integrity of the
CC mesenchyme and the polarized expression of ITGA8, which maintains the
CC GDNF expression required for further ureteric bud attraction. Although
CC it seems to lack ATPase activity it is constitutively associated with
CC microtubules (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MYH10. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2KJY2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2KJY2-2; Sequence=VSP_028687, VSP_028693;
CC -!- PTM: Phosphorylation at Thr-1855 and Ser-1958 by CDKs, mainly CDK2 and
CC CDK5, enhances the interaction with NEDD4, polyubiquitination, and
CC subsequent proteasomal degradation. Phosphorylation occurs upon loss of
CC interaction with microtubules (By similarity). {ECO:0000250}.
CC -!- PTM: Polyubiquitinated by NEDD4, resulting in proteasomal degradation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIF26 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH42481.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAA91469.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC86076.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAC87614.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AY923834; AAY17361.1; -; mRNA.
DR EMBL; AK001019; BAA91469.1; ALT_INIT; mRNA.
DR EMBL; AK125187; BAC86076.1; ALT_SEQ; mRNA.
DR EMBL; AK128806; BAC87614.1; ALT_SEQ; mRNA.
DR EMBL; BC035896; AAH35896.1; -; mRNA.
DR EMBL; BC042481; AAH42481.1; ALT_SEQ; mRNA.
DR CCDS; CCDS44342.1; -. [Q2KJY2-1]
DR RefSeq; NP_060482.2; NM_018012.3. [Q2KJY2-1]
DR AlphaFoldDB; Q2KJY2; -.
DR SMR; Q2KJY2; -.
DR BioGRID; 120398; 40.
DR IntAct; Q2KJY2; 19.
DR STRING; 9606.ENSP00000385545; -.
DR iPTMnet; Q2KJY2; -.
DR PhosphoSitePlus; Q2KJY2; -.
DR BioMuta; KIF26B; -.
DR DMDM; 121948325; -.
DR jPOST; Q2KJY2; -.
DR MassIVE; Q2KJY2; -.
DR MaxQB; Q2KJY2; -.
DR PaxDb; Q2KJY2; -.
DR PeptideAtlas; Q2KJY2; -.
DR PRIDE; Q2KJY2; -.
DR ProteomicsDB; 61325; -. [Q2KJY2-1]
DR ProteomicsDB; 61326; -. [Q2KJY2-2]
DR Antibodypedia; 34719; 97 antibodies from 23 providers.
DR DNASU; 55083; -.
DR Ensembl; ENST00000407071.7; ENSP00000385545.2; ENSG00000162849.16. [Q2KJY2-1]
DR GeneID; 55083; -.
DR KEGG; hsa:55083; -.
DR MANE-Select; ENST00000407071.7; ENSP00000385545.2; NM_018012.4; NP_060482.2.
DR UCSC; uc001ibf.1; human. [Q2KJY2-1]
DR CTD; 55083; -.
DR DisGeNET; 55083; -.
DR GeneCards; KIF26B; -.
DR HGNC; HGNC:25484; KIF26B.
DR HPA; ENSG00000162849; Tissue enhanced (brain).
DR MIM; 614026; gene.
DR neXtProt; NX_Q2KJY2; -.
DR OpenTargets; ENSG00000162849; -.
DR PharmGKB; PA145148575; -.
DR VEuPathDB; HostDB:ENSG00000162849; -.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000156992; -.
DR InParanoid; Q2KJY2; -.
DR OMA; CRPTSII; -.
DR OrthoDB; 29955at2759; -.
DR PhylomeDB; Q2KJY2; -.
DR TreeFam; TF105235; -.
DR PathwayCommons; Q2KJY2; -.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q2KJY2; -.
DR BioGRID-ORCS; 55083; 7 hits in 1072 CRISPR screens.
DR ChiTaRS; KIF26B; human.
DR GenomeRNAi; 55083; -.
DR Pharos; Q2KJY2; Tbio.
DR PRO; PR:Q2KJY2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q2KJY2; protein.
DR Bgee; ENSG00000162849; Expressed in ventricular zone and 89 other tissues.
DR ExpressionAtlas; Q2KJY2; baseline and differential.
DR Genevisible; Q2KJY2; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0072092; P:ureteric bud invasion; IEA:Ensembl.
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 Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton;
KW Developmental protein; Disease variant; Microtubule; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..2108
FT /note="Kinesin-like protein KIF26B"
FT /id="PRO_0000307301"
FT DOMAIN 450..801
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1519..1653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1685..1799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1814..1974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1485..1501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1524..1542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1713..1731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1898..1929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 546..553
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 1855
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7TNC6"
FT MOD_RES 1958
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TNC6"
FT VAR_SEQ 1..383
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028687"
FT VAR_SEQ 384..389
FT /note="ASFFAR -> MDWKAV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028693"
FT VARIANT 1904
FT /note="D -> N (found in a patient with spinocerebellar
FT ataxia; unknown pathological significance;
FT dbSNP:rs749953234)"
FT /evidence="ECO:0000269|PubMed:29053796"
FT /id="VAR_080730"
FT CONFLICT 83
FT /note="G -> S (in Ref. 2; BAC86076)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="T -> A (in Ref. 2; BAC86076)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="R -> M (in Ref. 3; AAH35896)"
FT /evidence="ECO:0000305"
FT CONFLICT 1682
FT /note="L -> P (in Ref. 2; BAA91469)"
FT /evidence="ECO:0000305"
FT CONFLICT 1746
FT /note="R -> H (in Ref. 2; BAA91469)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2108 AA; 223883 MW; 18F9ED20A1E119E2 CRC64;
MNSVAGNKER LAVSTRGKKY GVNEVCSPTK PAAPFSPESW YRKAYEESRA GSRPTPEGAG
SALGSSGTPS PGSGTSSPSS FTGSPGPASP GIGTSSPGSL GGSPGFGTGS PGSGSGGGSS
PGSDRGVWCE NCNARLVELK RQALRLLLPG PFPGKDPAFS AVIHDKLQVP NTIRKAWNDR
DNRCDICATH LNQLKQEAIQ MVLTLEQAAG SEHYDASPCS PPPLSNIPTL VGSRHVGGLQ
QPRDWAFVPA PCATSNYTGF ANKHGSKPSS LGVSNGAEKK SGSPTHQAKV SLQMATSPSN
GNILNSVAIQ AHQYLDGTWS LSRTNGVTLY PYQISQLMTE SSREGLTEAV LNRYNADKPS
ACSVPASQGS CVASETSTGT SVAASFFARA AQKLNLSSKK KKHRPSTSSA AEPPLFATSF
SGILQTSPPP APPCLLRAVN KVKDTPGLGK VKVMLRICST LARDTSESSS FLKVDPRKKQ
ITLYDPLTCG GQNAFQKRGN QVPPKMFAFD AVFPQDASQA EVCAGTVAEV IQSVVNGADG
CVFCFGHAKL GKSYTMIGKD DSMQNLGIIP CAISWLFKLI NERKEKTGAR FSVRVSAVEV
WGKEENLRDL LSEVATGSLQ DGQSPGVYLC EDPICGTQLQ NQSELRAPTA EKAAFFLDAA
IASRRSHQQD CDEDDHRNSH VFFTLHIYQY RMEKSGKGGM SGGRSRLHLI DLGSCVKALS
KNREGGSGLC LSLSALGNVI LALVNGSKHI PYKESKLAML LRESLGNMNC RTTMIAHISA
AVGSYAETLS TIQIASRVLR MKKKKTKYTS SSSGGESSCE EGRMRRPTQL RPFHTRATVD
PDFPIAHLSS DPDYSSSSEQ SCDTVIYIGP NGTALSDKEL TDNEGPPDFV PIVPALQKTR
GDSRPAEAGE AAAGKSERDC LKCNTFAELQ ERLDCIDGSE EPSSFPFEEL PAQFGPEQAS
RGPRLSQAAG ASPLSESDKE DNGSEGQLTN REGPELPASK MQRSHSPVPA AAPAHSPSPA
SPRSVPGSSS QHSASPLVQS PSLQSSRESL NSCGFVEGKP RPMGSPRLGI ASLSKTSEYK
PPSSPSQRCK VYTQKGVLPS PAPLPPSSKD SGVASRESLL QPEVRTPPVG MSPQVLKKSM
SAGSEGFPET PVDDEQQAAT PSESKKEILS TTMVTVQQPL ELNGEDELVF TLVEELTISG
VLDSGRPTSI ISFNSDCSAR ALASGSRPVS IISSISEDLE CYSSTAPVSE VSITQFLPLP
KMSLDEKAQD AGSRRSSISS WLSEMSAGSE GEQSCHSFIA QTCFGHGEAM AEPVASEFVS
SLQNTAVVCR EKPKASPDNL LILSEMGDDS FNKAAPIKGC KISTVSKAMV TISNTANLSS
CEGYIPMKTN ITVYPCIAMS PRNIQEPEAP TATPKAGPTL AQSRESKENS AKKEMKFEDP
WLKREEEVKK ETAHPNEEGM MRCETATGPS NAETRAEQEQ DGKPSPGDRL SSSSGEVSAS
PVTDNFRRVV DGCEMALPGL ATQSPVHPNK SVKSSSLPRA FQKASRQEEP DSLSYYCAAE
TNGVGAASGT PPSKATLEGK VASPKHCVLA RPKGTPPLPP VRKSSLDQKN RASPQHSASG
SGTSSPLNQP AAFPAGLPDE PSGKTKDASS SSKLFSAKLE QLASRSNSLG RATVSHYECL
SLERAESLSS VSSRLHAGKD GTMPRAGRSL GRSAGTSPPS SGASPKAGQS KISAVSRLLL
ASPRARGPSA STTKTLSFST KSLPQAVGQG SSSPPGGKHT PWSTQSLSRN RSSGLASKLP
LRAVSGRISE LLQGGAGARG LQLRAGPEAE ARGGALAEDE PAAAHLLPSP YSKITPPRRP
HRCSSGHGSD NSSVLSGELP PAMGKTALFY HSGGSSGYES VMRDSEATGS ASSAQDSTSE
NSSSVGGRCR SLKTPKKRSN PGSQRRRLIP ALSLDTSSPV RKPPNSTGVR WVDGPLRSSP
RGLGEPFEIK VYEIDDVERL QRRRGGASKE AMCFNAKLKI LEHRQQRIAE VRAKYEWLMK
ELEATKQYLM LDPNKWLSEF DLEQVWELDS LEYLEALECV TERLESRVNF CKAHLMMITC
FDITSRRR
