ID   BBLN_HUMAN              Reviewed;          83 AA.
AC   Q9BUW7; Q5SYV8; Q9Y3F7;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 156.
DE   RecName: Full=Bublin coiled-coil protein {ECO:0000312|HGNC:HGNC:17823};
DE   AltName: Full=UPF0184 protein C9orf16;
GN   Name=BBLN {ECO:0000312|HGNC:HGNC:17823}; Synonyms=C9orf16;
GN   ORFNames=EST00098;
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].
RC   TISSUE=Thymus;
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=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Muscle;
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-83.
RX   PubMed=10369878; DOI=10.1093/hmg/8.7.1313;
RA   Gilley J., Fried M.;
RT   "Extensive gene order differences within regions of conserved synteny
RT   between the Fugu and human genomes: implications for chromosomal evolution
RT   and the cloning of disease genes.";
RL   Hum. Mol. Genet. 8:1313-1320(1999).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [12]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=33857431; DOI=10.1016/j.cub.2021.03.069;
RA   Remmelzwaal S., Geisler F., Stucchi R., van der Horst S., Pasolli M.,
RA   Kroll J.R., Jarosinska O.D., Akhmanova A., Richardson C.A., Altelaar M.,
RA   Leube R.E., Ramalho J.J., Boxem M.;
RT   "BBLN-1 is essential for intermediate filament organization and apical
RT   membrane morphology.";
RL   Curr. Biol. 31:2334-2346.e9(2021).
CC   -!- FUNCTION: Essential for intermediate filament organization in
CC       intestinal cells, interacts with intermediate filament and regulates
CC       intestinal lumen morphology. {ECO:0000269|PubMed:33857431}.
CC   -!- INTERACTION:
CC       Q9BUW7; Q92870-2: APBB2; NbExp=3; IntAct=EBI-752084, EBI-21535880;
CC       Q9BUW7; Q6PJ05: ATP6V1D; NbExp=5; IntAct=EBI-752084, EBI-10253919;
CC       Q9BUW7; Q9Y5K8: ATP6V1D; NbExp=5; IntAct=EBI-752084, EBI-2684998;
CC       Q9BUW7; Q96A05: ATP6V1E2; NbExp=3; IntAct=EBI-752084, EBI-8650380;
CC       Q9BUW7; O15078: CEP290; NbExp=6; IntAct=EBI-752084, EBI-1811944;
CC       Q9BUW7; Q49A55: FGD4; NbExp=3; IntAct=EBI-752084, EBI-12186431;
CC       Q9BUW7; P42858: HTT; NbExp=6; IntAct=EBI-752084, EBI-466029;
CC       Q9BUW7; Q70UQ0: IKBIP; NbExp=3; IntAct=EBI-752084, EBI-2557212;
CC       Q9BUW7; P35900: KRT20; NbExp=9; IntAct=EBI-752084, EBI-742094;
CC       Q9BUW7; Q7Z412: PEX26; NbExp=3; IntAct=EBI-752084, EBI-752057;
CC       Q9BUW7; D3DTS7: PMP22; NbExp=3; IntAct=EBI-752084, EBI-25882629;
CC   -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:33857431}.
CC       Cytoplasm, cytoskeleton {ECO:0000269|PubMed:33857431}. Note=In the
CC       intestine, localizes subapically and at cell junctions. Interacts with
CC       intermediate filament (IF) proteins and localizes to the IF network in
CC       an IF-dependent manner (PubMed:33857431). In dividing cells, localizes
CC       to interpolar and kinetochore microtubules (PubMed:33857431).
CC       {ECO:0000269|PubMed:33857431}.
CC   -!- SIMILARITY: Belongs to the UPF0184 (EST00098) family. {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; AK315753; BAG38107.1; -; mRNA.
DR   EMBL; AL590708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471090; EAW87751.1; -; Genomic_DNA.
DR   EMBL; BC001857; AAH01857.1; -; mRNA.
DR   EMBL; BC008887; AAH08887.1; -; mRNA.
DR   EMBL; Y17450; CAB44344.1; -; Genomic_DNA.
DR   CCDS; CCDS6893.1; -.
DR   RefSeq; NP_077017.1; NM_024112.3.
DR   AlphaFoldDB; Q9BUW7; -.
DR   SMR; Q9BUW7; -.
DR   BioGRID; 122542; 47.
DR   DIP; DIP-29481N; -.
DR   IntAct; Q9BUW7; 21.
DR   STRING; 9606.ENSP00000362085; -.
DR   GlyGen; Q9BUW7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BUW7; -.
DR   PhosphoSitePlus; Q9BUW7; -.
DR   BioMuta; C9orf16; -.
DR   DMDM; 20137930; -.
DR   EPD; Q9BUW7; -.
DR   jPOST; Q9BUW7; -.
DR   MassIVE; Q9BUW7; -.
DR   MaxQB; Q9BUW7; -.
DR   PaxDb; 9606-ENSP00000362085; -.
DR   PeptideAtlas; Q9BUW7; -.
DR   ProteomicsDB; 79140; -.
DR   Pumba; Q9BUW7; -.
DR   Antibodypedia; 17364; 88 antibodies from 17 providers.
DR   DNASU; 79095; -.
DR   Ensembl; ENST00000372994.2; ENSP00000362085.1; ENSG00000171159.5.
DR   GeneID; 79095; -.
DR   KEGG; hsa:79095; -.
DR   MANE-Select; ENST00000372994.2; ENSP00000362085.1; NM_024112.4; NP_077017.1.
DR   UCSC; uc004btp.1; human.
DR   AGR; HGNC:17823; -.
DR   CTD; 79095; -.
DR   DisGeNET; 79095; -.
DR   GeneCards; BBLN; -.
DR   HGNC; HGNC:17823; BBLN.
DR   HPA; ENSG00000171159; Tissue enhanced (brain).
DR   neXtProt; NX_Q9BUW7; -.
DR   OpenTargets; ENSG00000171159; -.
DR   VEuPathDB; HostDB:ENSG00000171159; -.
DR   eggNOG; ENOG502SAFB; Eukaryota.
DR   GeneTree; ENSGT00390000001761; -.
DR   HOGENOM; CLU_167244_0_0_1; -.
DR   InParanoid; Q9BUW7; -.
DR   OMA; EEYVAIN; -.
DR   OrthoDB; 2905809at2759; -.
DR   PhylomeDB; Q9BUW7; -.
DR   TreeFam; TF324640; -.
DR   PathwayCommons; Q9BUW7; -.
DR   SignaLink; Q9BUW7; -.
DR   BioGRID-ORCS; 79095; 63 hits in 1109 CRISPR screens.
DR   GenomeRNAi; 79095; -.
DR   Pharos; Q9BUW7; Tdark.
DR   PRO; PR:Q9BUW7; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q9BUW7; Protein.
DR   Bgee; ENSG00000171159; Expressed in right adrenal gland cortex and 204 other cell types or tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0030054; C:cell junction; IMP:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005882; C:intermediate filament; IEA:Ensembl.
DR   GO; GO:0120219; C:subapical part of cell; IMP:UniProtKB.
DR   GO; GO:0060090; F:molecular adaptor activity; IMP:UniProtKB.
DR   GO; GO:0045110; P:intermediate filament bundle assembly; IMP:UniProtKB.
DR   InterPro; IPR005374; BBLN_eukaryota.
DR   PANTHER; PTHR34344:SF1; BUBLIN COILED-COIL PROTEIN; 1.
DR   PANTHER; PTHR34344; UPF0184 PROTEIN C9ORF16; 1.
DR   Pfam; PF03670; UPF0184; 1.
DR   Genevisible; Q9BUW7; HS.
PE   1: Evidence at protein level;
KW   Cell junction; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..83
FT                   /note="Bublin coiled-coil protein"
FT                   /id="PRO_0000195161"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          25..74
FT                   /evidence="ECO:0000255"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT   CONFLICT        35
FT                   /note="L -> V (in Ref. 5; CAB44344)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   83 AA;  9054 MW;  EBE1D0AFAAD6DABB CRC64;
     MSGPNGDLGM PVEAGAEGEE DGFGEAEYAA INSMLDQINS CLDHLEEKND HLHARLQELL
     ESNRQTRLEF QQQLGEAPSD ASP
//