KIF4B_HUMAN
ID KIF4B_HUMAN Reviewed; 1234 AA.
AC Q2VIQ3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Chromosome-associated kinesin KIF4B;
DE AltName: Full=Chromokinesin-B;
GN Name=KIF4B;
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].
RX PubMed=10978527; DOI=10.1016/s0167-4781(00)00151-2;
RA Oh S.J., Hahn H., Torrey T.A., Shin H., Choi W., Lee Y.M., Morse H.C. III,
RA Kim W.;
RT "Identification of the human homologue of mouse KIF4, a kinesin superfamily
RT motor protein.";
RL Biochim. Biophys. Acta 1493:219-224(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1185, TISSUE SPECIFICITY, AND
RP VARIANTS LEU-580 AND HIS-680.
RX PubMed=16201836; DOI=10.1371/journal.pbio.0030357;
RA Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.;
RT "Emergence of young human genes after a burst of retroposition in
RT primates.";
RL PLoS Biol. 3:E357-E357(2005).
CC -!- FUNCTION: Iron-sulfur (Fe-S) cluster binding motor protein that has a
CC role in chromosome segregation during mitosis (By similarity).
CC Translocates PRC1 to the plus ends of interdigitating spindle
CC microtubules during the metaphase to anaphase transition, an essential
CC step for the formation of an organized central spindle midzone and
CC midbody and for successful cytokinesis (By similarity). May play a role
CC in mitotic chromosomal positioning and bipolar spindle stabilization
CC (By similarity). {ECO:0000250|UniProtKB:O95239,
CC ECO:0000250|UniProtKB:P33174}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:O95239};
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:O95239};
CC Note=Binds 1 [4Fe-4S] cluster (By similarity). In the presence of
CC oxygen, the [4Fe-4S] cluster may be converted to [2Fe-2S] (By
CC similarity). {ECO:0000250|UniProtKB:O95239};
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:O95239}.
CC Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in testis.
CC {ECO:0000269|PubMed:16201836}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Chromokinesin subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; AF241316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ120629; ABB92415.1; -; Genomic_DNA.
DR CCDS; CCDS47324.1; -.
DR RefSeq; NP_001092763.1; NM_001099293.2.
DR AlphaFoldDB; Q2VIQ3; -.
DR SMR; Q2VIQ3; -.
DR BioGRID; 130168; 12.
DR IntAct; Q2VIQ3; 6.
DR STRING; 9606.ENSP00000387875; -.
DR iPTMnet; Q2VIQ3; -.
DR PhosphoSitePlus; Q2VIQ3; -.
DR BioMuta; KIF4B; -.
DR DMDM; 158564279; -.
DR EPD; Q2VIQ3; -.
DR jPOST; Q2VIQ3; -.
DR MassIVE; Q2VIQ3; -.
DR MaxQB; Q2VIQ3; -.
DR PaxDb; Q2VIQ3; -.
DR PeptideAtlas; Q2VIQ3; -.
DR PRIDE; Q2VIQ3; -.
DR ProteomicsDB; 61511; -.
DR Antibodypedia; 77177; 13 antibodies from 10 providers.
DR DNASU; 285643; -.
DR Ensembl; ENST00000435029.6; ENSP00000387875.3; ENSG00000226650.6.
DR GeneID; 285643; -.
DR KEGG; hsa:285643; -.
DR MANE-Select; ENST00000435029.6; ENSP00000387875.3; NM_001099293.3; NP_001092763.1.
DR UCSC; uc010jih.2; human.
DR CTD; 285643; -.
DR DisGeNET; 285643; -.
DR GeneCards; KIF4B; -.
DR HGNC; HGNC:6322; KIF4B.
DR HPA; ENSG00000226650; Tissue enriched (testis).
DR MIM; 609184; gene.
DR neXtProt; NX_Q2VIQ3; -.
DR OpenTargets; ENSG00000226650; -.
DR PharmGKB; PA30106; -.
DR VEuPathDB; HostDB:ENSG00000226650; -.
DR eggNOG; KOG0244; Eukaryota.
DR GeneTree; ENSGT00940000164190; -.
DR HOGENOM; CLU_001485_4_1_1; -.
DR InParanoid; Q2VIQ3; -.
DR OMA; KEMCDME; -.
DR OrthoDB; 369179at2759; -.
DR PhylomeDB; Q2VIQ3; -.
DR TreeFam; TF105224; -.
DR PathwayCommons; Q2VIQ3; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-437239; Recycling pathway of L1.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q2VIQ3; -.
DR BioGRID-ORCS; 285643; 12 hits in 1066 CRISPR screens.
DR ChiTaRS; KIF4B; human.
DR GenomeRNAi; 285643; -.
DR Pharos; Q2VIQ3; Tbio.
DR PRO; PR:Q2VIQ3; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q2VIQ3; protein.
DR Bgee; ENSG00000226650; Expressed in testis and 3 other tissues.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; IMP:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0051231; P:spindle elongation; IBA:GO_Central.
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 InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM01114; CXC; 1.
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 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; DNA-binding; Iron;
KW Iron-sulfur; Isopeptide bond; Metal-binding; Microtubule; Motor protein;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..1234
FT /note="Chromosome-associated kinesin KIF4B"
FT /id="PRO_0000301666"
FT DOMAIN 9..336
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 494..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..1234
FT /note="Interaction with PRC1"
FT /evidence="ECO:0000250|UniProtKB:O95239"
FT REGION 712..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1234
FT /note="Globular"
FT /evidence="ECO:0000250"
FT REGION 1007..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1144
FT /note="CRD; required for [4Fe-4S] cluster binding and
FT localization to the spindle midzone and midbody during
FT anaphase and telophase"
FT /evidence="ECO:0000250|UniProtKB:O95239"
FT REGION 1122..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 350..999
FT /evidence="ECO:0000255"
FT MOTIF 793..798
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O95239"
FT COMPBIAS 497..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33174"
FT MOD_RES 799
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95239"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95239"
FT MOD_RES 951
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95239"
FT MOD_RES 1001
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95239"
FT MOD_RES 1013
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95239"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95239"
FT MOD_RES 1028
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95239"
FT MOD_RES 1128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95239"
FT MOD_RES 1183
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95239"
FT MOD_RES 1188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95239"
FT MOD_RES 1227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33174"
FT CROSSLNK 1196
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95239"
FT VARIANT 494
FT /note="E -> Q (in dbSNP:rs17116709)"
FT /id="VAR_049695"
FT VARIANT 580
FT /note="R -> L (in dbSNP:rs6580126)"
FT /evidence="ECO:0000269|PubMed:16201836"
FT /id="VAR_049696"
FT VARIANT 680
FT /note="R -> H (in dbSNP:rs17116710)"
FT /evidence="ECO:0000269|PubMed:16201836"
FT /id="VAR_049697"
FT VARIANT 684
FT /note="Y -> C (in dbSNP:rs10056252)"
FT /id="VAR_061281"
FT CONFLICT 128
FT /note="K -> Q (in Ref. 1; AF241316)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="I -> L (in Ref. 1; AF241316)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="R -> G (in Ref. 1; AF241316)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="C -> S (in Ref. 1; AF241316)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="V -> A (in Ref. 1; AF241316)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="V -> A (in Ref. 1; AF241316)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="H -> R (in Ref. 1; AF241316)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="W -> R (in Ref. 1; AF241316)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="K -> R (in Ref. 1; AF241316)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="S -> N (in Ref. 1; AF241316)"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="T -> A (in Ref. 1; AF241316)"
FT /evidence="ECO:0000305"
FT CONFLICT 734..739
FT /note="HGKEGI -> RGMEGT (in Ref. 1; AF241316)"
FT /evidence="ECO:0000305"
FT CONFLICT 755
FT /note="V -> I (in Ref. 3; ABB92415)"
FT /evidence="ECO:0000305"
FT CONFLICT 957
FT /note="Q -> P (in Ref. 1; AF241316)"
FT /evidence="ECO:0000305"
FT CONFLICT 1029
FT /note="R -> H (in Ref. 3; ABB92415)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1234 AA; 140035 MW; 13B1A8ADC95A735B CRC64;
MKEEVKGIPV RVALRCRPLV PKEISEGCQM CLSFVPGETQ VVVGTDKSFT YDFVFDPCTE
QEEVFNKAVA PLIKGIFKGY NATVLAYGQT GSGKTYSMGG AYTAEQENEP TVGIIPRVIQ
LLFKEIDKKS DFEFTLKVSY LEIYNEEILD LLCPSREKAQ INIREDPKEG IKIVGLTEKT
VLVALDTVSC LEQGNNSRTV ASTAMNSQSS RSHAIFTISI EQRKKSDKNC SFRSKLHLVD
LAGSERQKKT KAEGDRLKEG ININRGLLCL GNVISALGDD KKGSFVPYRD SKLTRLLQDS
LGGNSHTLMI ACVSPADSNL EETLSTLRYA DRARKIKNKP IVNIDPHTAE LNHLKQQVQQ
LQVLLLQAHG GTLPGSINAE PSENLQSLME KNQSLVEENE KLSRCLSKAA GQTAQMLERI
ILTEQVNEKL NAKLEELRQH VACKLDLQKL VETLEDQELK ENVEIICNLQ QLITQLSDET
VACTAAAIDT AVEEEAQVET SPETSRSSDA FTTQHALHQA QMSKEVVELN NALALKEALV
RKMTQNDNQL QPIQFQYQDN IKNLELEVIN LQKEKEELVR ELQTAKKNVN QAKLSEHRHK
LLQELEGQIA DLKKKLNEQS KLLKLKESTE RTVSKLNQEI WMMKNQRVQL MRQMKEDAEK
FRQWKQKKDK EVIQLKERDR KRQYELLKLE RNFQKQSSVL RRKTEEAAAA NKRLKDALQK
QREVTDKRKE TQSHGKEGIA ARVRNWLGNE IEVMVSTEEA KRHLNDLLED RKILAQDVVQ
LKEKKESREN PPPKLRKCTF SLSEVHGQVL ESEDCITKQI ESLETEMELR SAQIADLQQK
LLDAESEDRP KQCWENIATI LEAKCALKYL IGELVSSKIH VTKLENSLRQ SKASCADMQK
MLFEEQNHFS EIETELQAEL VRMEQQHQEK VLYLVSQLQE SQMAEKQLEK SASEKEQQLV
STLQCQDEEL EKMREVCEQN QQLLQENEII KQKLILLQVA SRQKHLPNDT LLSPDSSFEY
IPPKPKPSRV KEKFLEQSMD IEDLKYCSEH SVNEHEDGDG DGDSDEGDDE EWKPTKLVKV
SRKNIQGCSC KGWCGNKQCG CRKQKSDCGV DCSCDPTKCR NRQQGKDSLG TVEQTQDSEG
SFKLEDPTEV TPGLSFFNPV CATPNSKILK EMCDMEQVLS KKTAPAPSPF DLPESKHGAT
EYQQNKPPGK KKKRALASNT SFFSGCSPIE EEAH
