BBIP1_HUMAN
ID BBIP1_HUMAN Reviewed; 92 AA.
AC A8MTZ0; E9PIY9; E9PM41; E9PRI7;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=BBSome-interacting protein 1;
DE AltName: Full=BBSome-interacting protein of 10 kDa;
GN Name=BBIP1; Synonyms=BBIP10, NCRNA00081;
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 MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Fetal brain, and Testis;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow;
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 IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
RP SUBUNIT, AND INTERACTION WITH HDAC6.
RA Loktev A.V., Zhang Q., Beck J.S., Searby C.C., Scheetz T.E., Bazan F.,
RA Slusarski D.C., Sheffield V.C., Jackson P.K., Nachury M.V.;
RT "A BBSome subunit links ciliogenesis, microtubule stability and
RT acetylation.";
RL Dev. Cell 15:854-865(2008).
RN [5]
RP INVOLVEMENT IN BBS18.
RX PubMed=24026985; DOI=10.1136/jmedgenet-2013-101785;
RA Scheidecker S., Etard C., Pierce N.W., Geoffroy V., Schaefer E., Muller J.,
RA Chennen K., Flori E., Pelletier V., Poch O., Marion V., Stoetzel C.,
RA Straehle U., Nachury M.V., Dollfus H.;
RT "Exome sequencing of Bardet-Biedl syndrome patient identifies a null
RT mutation in the BBSome subunit BBIP1 (BBS18).";
RL J. Med. Genet. 51:132-136(2014).
CC -!- FUNCTION: The BBSome complex is thought to function as a coat complex
CC required for sorting of specific membrane proteins to the primary
CC cilia. The BBSome complex is required for ciliogenesis but is
CC dispensable for centriolar satellite function. This ciliogenic function
CC is mediated in part by the Rab8 GDP/GTP exchange factor, which
CC localizes to the basal body and contacts the BBSome. Rab8(GTP) enters
CC the primary cilium and promotes extension of the ciliary membrane.
CC Firstly the BBSome associates with the ciliary membrane and binds to
CC RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the
CC Rab8-GTP localizes to the cilium and promotes docking and fusion of
CC carrier vesicles to the base of the ciliary membrane. Required for
CC primary cilia assembly and BBSome stability. Regulates cytoplasmic
CC microtubule stability and acetylation. {ECO:0000269|Ref.4}.
CC -!- SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5,
CC BBS7, BBS8, BBS9 and BBIP10. Interacts with HDAC6. {ECO:0000269|Ref.4}.
CC -!- INTERACTION:
CC A8MTZ0; Q96RK4: BBS4; NbExp=14; IntAct=EBI-2892417, EBI-1805814;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|Ref.4}.
CC Cytoplasm {ECO:0000269|Ref.4}. Note=Localizes inside the primary cilium
CC but not at centriolar satellites.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A8MTZ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A8MTZ0-2; Sequence=VSP_045981;
CC Name=3;
CC IsoId=A8MTZ0-3; Sequence=VSP_046434;
CC Name=4;
CC IsoId=A8MTZ0-4; Sequence=VSP_046433;
CC -!- DISEASE: Bardet-Biedl syndrome 18 (BBS18) [MIM:615995]: A syndrome
CC characterized by usually severe pigmentary retinopathy, early-onset
CC obesity, polydactyly, hypogenitalism, renal malformation and
CC intellectual disability. Secondary features include diabetes mellitus,
CC hypertension and congenital heart disease. Bardet-Biedl syndrome
CC inheritance is autosomal recessive, but three mutated alleles (two at
CC one locus, and a third at a second locus) may be required for clinical
CC manifestation of some forms of the disease.
CC {ECO:0000269|PubMed:24026985}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the BBIP10 family. {ECO:0000305}.
CC -!- CAUTION: Was previously thought to be non-coding and described as 'non-
CC protein coding RNA 81', abbreviated NCRNA00081. {ECO:0000305}.
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DR EMBL; AK307126; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK307314; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; DA520878; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL158163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015550; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BU189144; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS55726.1; -. [A8MTZ0-3]
DR CCDS; CCDS55727.1; -. [A8MTZ0-1]
DR CCDS; CCDS55728.1; -. [A8MTZ0-4]
DR CCDS; CCDS58094.1; -. [A8MTZ0-2]
DR RefSeq; NP_001182233.1; NM_001195304.1. [A8MTZ0-4]
DR RefSeq; NP_001182234.1; NM_001195305.1. [A8MTZ0-1]
DR RefSeq; NP_001182235.1; NM_001195306.1. [A8MTZ0-1]
DR RefSeq; NP_001182236.1; NM_001195307.1. [A8MTZ0-3]
DR RefSeq; NP_001230712.1; NM_001243783.1. [A8MTZ0-2]
DR PDB; 6XT9; EM; 3.80 A; J=1-92.
DR PDBsum; 6XT9; -.
DR AlphaFoldDB; A8MTZ0; -.
DR SMR; A8MTZ0; -.
DR BioGRID; 124949; 4.
DR ComplexPortal; CPX-1908; BBSome complex.
DR CORUM; A8MTZ0; -.
DR IntAct; A8MTZ0; 10.
DR iPTMnet; A8MTZ0; -.
DR PhosphoSitePlus; A8MTZ0; -.
DR BioMuta; BBIP1; -.
DR MassIVE; A8MTZ0; -.
DR PeptideAtlas; A8MTZ0; -.
DR PRIDE; A8MTZ0; -.
DR ProteomicsDB; 2063; -. [A8MTZ0-1]
DR ProteomicsDB; 20964; -.
DR ProteomicsDB; 23327; -.
DR Antibodypedia; 64208; 32 antibodies from 8 providers.
DR DNASU; 92482; -.
DR Ensembl; ENST00000423273.5; ENSP00000432274.1; ENSG00000214413.9. [A8MTZ0-3]
DR Ensembl; ENST00000436562.1; ENSP00000431936.1; ENSG00000214413.9. [A8MTZ0-2]
DR Ensembl; ENST00000447005.5; ENSP00000432849.1; ENSG00000214413.9. [A8MTZ0-2]
DR Ensembl; ENST00000448814.7; ENSP00000436622.2; ENSG00000214413.9. [A8MTZ0-1]
DR Ensembl; ENST00000454061.5; ENSP00000433157.1; ENSG00000214413.9. [A8MTZ0-4]
DR Ensembl; ENST00000605742.5; ENSP00000474675.1; ENSG00000214413.9. [A8MTZ0-1]
DR Ensembl; ENST00000651952.1; ENSP00000498552.1; ENSG00000214413.9. [A8MTZ0-2]
DR Ensembl; ENST00000652043.1; ENSP00000498430.1; ENSG00000214413.9. [A8MTZ0-1]
DR Ensembl; ENST00000652396.1; ENSP00000498843.1; ENSG00000214413.9. [A8MTZ0-2]
DR Ensembl; ENST00000652400.1; ENSP00000498614.1; ENSG00000214413.9. [A8MTZ0-2]
DR GeneID; 92482; -.
DR KEGG; hsa:92482; -.
DR MANE-Select; ENST00000448814.7; ENSP00000436622.2; NM_001195305.3; NP_001182234.1.
DR UCSC; uc001kzi.4; human. [A8MTZ0-1]
DR CTD; 92482; -.
DR DisGeNET; 92482; -.
DR GeneCards; BBIP1; -.
DR GeneReviews; BBIP1; -.
DR HGNC; HGNC:28093; BBIP1.
DR HPA; ENSG00000214413; Tissue enhanced (testis).
DR MalaCards; BBIP1; -.
DR MIM; 613605; gene.
DR MIM; 615995; phenotype.
DR neXtProt; NX_A8MTZ0; -.
DR OpenTargets; ENSG00000214413; -.
DR Orphanet; 110; Bardet-Biedl syndrome.
DR VEuPathDB; HostDB:ENSG00000214413; -.
DR GeneTree; ENSGT00390000009265; -.
DR HOGENOM; CLU_185680_0_0_1; -.
DR InParanoid; A8MTZ0; -.
DR OMA; MKSMFRE; -.
DR OrthoDB; 1627836at2759; -.
DR PhylomeDB; A8MTZ0; -.
DR PathwayCommons; A8MTZ0; -.
DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium.
DR SignaLink; A8MTZ0; -.
DR SIGNOR; A8MTZ0; -.
DR BioGRID-ORCS; 92482; 13 hits in 1077 CRISPR screens.
DR ChiTaRS; BBIP1; human.
DR GenomeRNAi; 92482; -.
DR Pharos; A8MTZ0; Tdark.
DR PRO; PR:A8MTZ0; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; A8MTZ0; protein.
DR Bgee; ENSG00000214413; Expressed in epithelium of nasopharynx and 209 other tissues.
DR ExpressionAtlas; A8MTZ0; baseline and differential.
DR Genevisible; A8MTZ0; HS.
DR GO; GO:0034464; C:BBSome; IDA:UniProtKB.
DR GO; GO:0060170; C:ciliary membrane; IDA:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0042755; P:eating behavior; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0097500; P:receptor localization to non-motile cilium; IBA:GO_Central.
DR InterPro; IPR028233; BBIP10.
DR PANTHER; PTHR28596; PTHR28596; 1.
DR Pfam; PF14777; BBIP10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Bardet-Biedl syndrome; Cell projection;
KW Ciliopathy; Cilium; Cilium biogenesis/degradation; Cytoplasm; Obesity;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..92
FT /note="BBSome-interacting protein 1"
FT /id="PRO_0000342378"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..22
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045981"
FT VAR_SEQ 14..92
FT /note="KNTISNNSDMAEVKSMFREVLPKQGPLFVEDIMTMVLCKPKLLPLKSLTLEK
FT LEKMHQAAQNTIRQQEMAEKDQRQITH -> LLKFNNYGILSESPLTSQRTTWLLYQSP
FT SFIPGFAYPSRCLKTIGGVYKQARKKHYIQQLRYGRSEVNVPGSSSKARATVCGRYNDN
FT GAV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046433"
FT VAR_SEQ 14..38
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046434"
SQ SEQUENCE 92 AA; 10506 MW; 25F2EE32DF0B948D CRC64;
MLKAAAKRPE LSGKNTISNN SDMAEVKSMF REVLPKQGPL FVEDIMTMVL CKPKLLPLKS
LTLEKLEKMH QAAQNTIRQQ EMAEKDQRQI TH
