KBP_HUMAN
ID KBP_HUMAN Reviewed; 621 AA.
AC Q96EK5; A8K5M8; Q9BR89; Q9ULE1; Q9Y428;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=KIF-binding protein;
DE AltName: Full=KIF1-binding protein {ECO:0000305|PubMed:16225668};
DE AltName: Full=Kinesin family binding protein {ECO:0000312|HGNC:HGNC:23419};
GN Name=KIFBP {ECO:0000312|HGNC:HGNC:23419};
GN Synonyms=KBP {ECO:0000303|PubMed:16225668},
GN KIAA1279 {ECO:0000303|PubMed:10574462},
GN KIF1BP {ECO:0000303|PubMed:16225668};
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], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP INTERACTION WITH KIF1B, AND FUNCTION.
RX PubMed=16225668; DOI=10.1186/1471-2121-6-35;
RA Wozniak M.J., Melzer M., Dorner C., Haring H.U., Lammers R.;
RT "The novel protein KBP regulates mitochondria localization by interaction
RT with a kinesin-like protein.";
RL BMC Cell Biol. 6:35-35(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], TISSUE SPECIFICITY, AND VARIANT
RP SER-66.
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].
RC TISSUE=Tongue;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 314-621.
RC TISSUE=Uterus;
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 [8]
RP INVOLVEMENT IN GOSHS.
RX PubMed=15883926; DOI=10.1086/431244;
RA Brooks A.S., Bertoli-Avella A.M., Burzynski G.M., Breedveld G.J.,
RA Osinga J., Boven L.G., Hurst J.A., Mancini G.M.S., Lequin M.H.,
RA de Coo R.F., Matera I., de Graaff E., Meijers C., Willems P.J., Tibboel D.,
RA Oostra B.A., Hofstra R.M.W.;
RT "Homozygous nonsense mutations in KIAA1279 are associated with
RT malformations of the central and enteric nervous systems.";
RL Am. J. Hum. Genet. 77:120-126(2005).
RN [9]
RP FUNCTION, INTERACTION WITH STMN2, AND SUBCELLULAR LOCATION.
RX PubMed=20621975; DOI=10.1093/hmg/ddq280;
RA Alves M.M., Burzynski G., Delalande J.M., Osinga J., van der Goot A.,
RA Dolga A.M., de Graaff E., Brooks A.S., Metzger M., Eisel U.L., Shepherd I.,
RA Eggen B.J., Hofstra R.M.;
RT "KBP interacts with SCG10, linking Goldberg-Shprintzen syndrome to
RT microtubule dynamics and neuronal differentiation.";
RL Hum. Mol. Genet. 19:3642-3651(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP INVOLVEMENT IN GOSHS, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23427148; DOI=10.1093/hmg/ddt083;
RA Drevillon L., Megarbane A., Demeer B., Matar C., Benit P.,
RA Briand-Suleau A., Bodereau V., Ghoumid J., Nasser M., Decrouy X.,
RA Doco-Fenzy M., Rustin P., Gaillard D., Goossens M., Giurgea I.;
RT "KBP-cytoskeleton interactions underlie developmental anomalies in
RT Goldberg-Shprintzen syndrome.";
RL Hum. Mol. Genet. 22:2387-2399(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP 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: Required for organization of axonal microtubules, and axonal
CC outgrowth and maintenance during peripheral and central nervous system
CC development. {ECO:0000269|PubMed:16225668, ECO:0000269|PubMed:20621975,
CC ECO:0000269|PubMed:23427148}.
CC -!- SUBUNIT: Interacts with KIF1B (PubMed:16225668). Interacts with STMN2
CC (PubMed:20621975). {ECO:0000269|PubMed:16225668,
CC ECO:0000269|PubMed:20621975}.
CC -!- INTERACTION:
CC Q96EK5; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-744150, EBI-25840379;
CC Q96EK5; P16444: DPEP1; NbExp=2; IntAct=EBI-744150, EBI-749514;
CC Q96EK5; P47804: RGR; NbExp=2; IntAct=EBI-744150, EBI-745818;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16225668, ECO:0000269|PubMed:20621975,
CC ECO:0000269|PubMed:23427148}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, brain, ovary, testis,
CC spinal cord and all specific brain regions examined. Moderate expressed
CC at intermediate level in all other adult tissues examined, as well as
CC in fetal liver and brain. Not expressed in blood leukocytes.
CC {ECO:0000269|PubMed:10574462, ECO:0000269|PubMed:16225668}.
CC -!- DISEASE: Goldberg-Shprintzen syndrome (GOSHS) [MIM:609460]: A disorder
CC characterized by intellectual disability, microcephaly, and dysmorphic
CC facial features. Most patients also have Hirschsprung disease.
CC {ECO:0000269|PubMed:15883926, ECO:0000269|PubMed:23427148}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the KIF-binding protein family. {ECO:0000305}.
CC -!- CAUTION: Was originally shown to localize in the mitochondrion and to
CC play a role in mitochondrial transport (PubMed:16225668). Recent
CC articles, however, have shown that it does not localize to
CC mitochondria, it interacts with the cytoskeleton and does not have a
CC role in mitochondrial function (PubMed:20621975, PubMed:23427148).
CC {ECO:0000305|PubMed:16225668, ECO:0000305|PubMed:20621975,
CC ECO:0000305|PubMed:23427148}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86593.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB033105; BAA86593.1; ALT_INIT; mRNA.
DR EMBL; AL359844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK291343; BAF84032.1; -; mRNA.
DR EMBL; BC012180; AAH12180.1; -; mRNA.
DR EMBL; AL050190; CAB43311.1; -; mRNA.
DR CCDS; CCDS7284.1; -.
DR PIR; T08798; T08798.
DR RefSeq; NP_056449.1; NM_015634.3.
DR PDB; 6ZPG; EM; 4.60 A; A=1-621.
DR PDB; 6ZPH; EM; 6.90 A; A=1-621.
DR PDB; 7RSI; EM; 4.90 A; B=1-621.
DR PDB; 7RSQ; EM; 3.80 A; B=1-621.
DR PDB; 7RYP; EM; 4.80 A; B=1-621.
DR PDB; 7RYQ; EM; 4.60 A; B=1-621.
DR PDBsum; 6ZPG; -.
DR PDBsum; 6ZPH; -.
DR PDBsum; 7RSI; -.
DR PDBsum; 7RSQ; -.
DR PDBsum; 7RYP; -.
DR PDBsum; 7RYQ; -.
DR AlphaFoldDB; Q96EK5; -.
DR SMR; Q96EK5; -.
DR BioGRID; 117567; 151.
DR IntAct; Q96EK5; 51.
DR MINT; Q96EK5; -.
DR STRING; 9606.ENSP00000354848; -.
DR GlyGen; Q96EK5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96EK5; -.
DR MetOSite; Q96EK5; -.
DR PhosphoSitePlus; Q96EK5; -.
DR SwissPalm; Q96EK5; -.
DR BioMuta; KIF1BP; -.
DR DMDM; 73920081; -.
DR EPD; Q96EK5; -.
DR jPOST; Q96EK5; -.
DR MassIVE; Q96EK5; -.
DR MaxQB; Q96EK5; -.
DR PaxDb; Q96EK5; -.
DR PeptideAtlas; Q96EK5; -.
DR PRIDE; Q96EK5; -.
DR ProteomicsDB; 76417; -.
DR Antibodypedia; 28675; 102 antibodies from 20 providers.
DR DNASU; 26128; -.
DR Ensembl; ENST00000361983.7; ENSP00000354848.4; ENSG00000198954.9.
DR GeneID; 26128; -.
DR KEGG; hsa:26128; -.
DR MANE-Select; ENST00000361983.7; ENSP00000354848.4; NM_015634.4; NP_056449.1.
DR UCSC; uc001joy.4; human.
DR CTD; 26128; -.
DR DisGeNET; 26128; -.
DR GeneCards; KIFBP; -.
DR HGNC; HGNC:23419; KIFBP.
DR HPA; ENSG00000198954; Low tissue specificity.
DR MalaCards; KIFBP; -.
DR MIM; 609367; gene.
DR MIM; 609460; phenotype.
DR neXtProt; NX_Q96EK5; -.
DR OpenTargets; ENSG00000198954; -.
DR Orphanet; 66629; Goldberg-Shprintzen megacolon syndrome.
DR VEuPathDB; HostDB:ENSG00000198954; -.
DR eggNOG; ENOG502QPZT; Eukaryota.
DR GeneTree; ENSGT00390000013819; -.
DR HOGENOM; CLU_019859_1_0_1; -.
DR InParanoid; Q96EK5; -.
DR OMA; ICRECWY; -.
DR OrthoDB; 1516717at2759; -.
DR PhylomeDB; Q96EK5; -.
DR TreeFam; TF324211; -.
DR PathwayCommons; Q96EK5; -.
DR SignaLink; Q96EK5; -.
DR BioGRID-ORCS; 26128; 73 hits in 1078 CRISPR screens.
DR ChiTaRS; KIF1BP; human.
DR GeneWiki; KIAA1279; -.
DR GenomeRNAi; 26128; -.
DR Pharos; Q96EK5; Tbio.
DR PRO; PR:Q96EK5; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q96EK5; protein.
DR Bgee; ENSG00000198954; Expressed in frontal pole and 205 other tissues.
DR ExpressionAtlas; Q96EK5; baseline and differential.
DR Genevisible; Q96EK5; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0006839; P:mitochondrial transport; IMP:UniProtKB.
DR GO; GO:1990535; P:neuron projection maintenance; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR022083; KBP.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR46321; PTHR46321; 1.
DR Pfam; PF12309; KBP_C; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Hirschsprung disease; Neurogenesis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..621
FT /note="KIF-binding protein"
FT /id="PRO_0000050791"
FT REGION 51..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 66
FT /note="G -> S (in dbSNP:rs2255607)"
FT /evidence="ECO:0000269|PubMed:10574462"
FT /id="VAR_023311"
FT CONFLICT 139
FT /note="I -> T (in Ref. 4; BAF84032)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="G -> A (in Ref. 4; BAF84032)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="H -> R (in Ref. 4; BAF84032)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 621 AA; 71814 MW; DA86308364D31335 CRC64;
MANVPWAEVC EKFQAALALS RVELHKNPEK EPYKSKYSAR ALLEEVKALL GPAPEDEDER
PEAEDGPGAG DHALGLPAEV VEPEGPVAQR AVRLAVIEFH LGVNHIDTEE LSAGEEHLVK
CLRLLRRYRL SHDCISLCIQ AQNNLGILWS EREEIETAQA YLESSEALYN QYMKEVGSPP
LDPTERFLPE EEKLTEQERS KRFEKVYTHN LYYLAQVYQH LEMFEKAAHY CHSTLKRQLE
HNAYHPIEWA INAATLSQFY INKLCFMEAR HCLSAANVIF GQTGKISATE DTPEAEGEVP
ELYHQRKGEI ARCWIKYCLT LMQNAQLSMQ DNIGELDLDK QSELRALRKK ELDEEESIRK
KAVQFGTGEL CDAISAVEEK VSYLRPLDFE EARELFLLGQ HYVFEAKEFF QIDGYVTDHI
EVVQDHSALF KVLAFFETDM ERRCKMHKRR IAMLEPLTVD LNPQYYLLVN RQIQFEIAHA
YYDMMDLKVA IADRLRDPDS HIVKKINNLN KSALKYYQLF LDSLRDPNKV FPEHIGEDVL
RPAMLAKFRV ARLYGKIITA DPKKELENLA TSLEHYKFIV DYCEKHPEAA QEIEVELELS
KEMVSLLPTK MERFRTKMAL T
