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 27-MAR-2024, entry version 99. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-10617; -. 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 ProteomicsDB; 2063; -. [A8MTZ0-1] DR ProteomicsDB; 20964; -. DR ProteomicsDB; 23327; -. DR Pumba; A8MTZ0; -. 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 AGR; HGNC:28093; -. 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; HQQEMTE; -. DR OrthoDB; 2882313at2759; -. 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; 14 hits in 1154 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 211 other cell types or tissues. DR ExpressionAtlas; A8MTZ0; baseline and differential. 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; BBSOME-INTERACTING PROTEIN 1; 1. DR PANTHER; PTHR28596:SF1; BBSOME-INTERACTING PROTEIN 1; 1. DR Pfam; PF14777; BBIP10; 1. DR Genevisible; A8MTZ0; HS. 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 //