ID   BROMI_HUMAN             Reviewed;        1257 AA.
AC   Q96NH3; Q5SZD6; Q5SZM6; Q6ZMY4; Q6ZUR7; Q8NB47;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 4.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Protein broad-minded;
DE   AltName: Full=TBC1 domain family member 32;
GN   Name=TBC1D32; Synonyms=BROMI, C6orf170, C6orf171;
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] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 408-1257 (ISOFORM 2), AND VARIANTS GLN-82 AND
RP   LYS-375.
RC   TISSUE=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=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [3]
RP   INTERACTION WITH FAM149B1.
RX   PubMed=30905400; DOI=10.1016/j.ajhg.2019.02.018;
RA   Shaheen R., Jiang N., Alzahrani F., Ewida N., Al-Sheddi T., Alobeid E.,
RA   Musaev D., Stanley V., Hashem M., Ibrahim N., Abdulwahab F., Alshenqiti A.,
RA   Sonmez F.M., Saqati N., Alzaidan H., Al-Qattan M.M., Al-Mohanna F.,
RA   Gleeson J.G., Alkuraya F.S.;
RT   "Bi-allelic mutations in FAM149B1 cause abnormal primary cilium and a range
RT   of ciliopathy phenotypes in humans.";
RL   Am. J. Hum. Genet. 104:731-737(2019).
CC   -!- FUNCTION: Required for high-level Shh responses in the developing
CC       neural tube. Together with CDK20, controls the structure of the primary
CC       cilium by coordinating assembly of the ciliary membrane and axoneme,
CC       allowing GLI2 to be properly activated in response to Shh signaling (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CDK20, which promotes CDK20 stability and
CC       function (By similarity). Interacts with FAM149B1; may play a role in
CC       cilium assembly. {ECO:0000250|UniProtKB:Q3URV1,
CC       ECO:0000269|PubMed:30905400}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, cilium
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q96NH3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96NH3-4; Sequence=VSP_014546;
CC       Name=3;
CC         IsoId=Q96NH3-5; Sequence=VSP_035579, VSP_035580;
CC   -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- CAUTION: The Rab-GAP TBC domain appears to be inactive, probably due to
CC       a lack of the essential Arg and Gln in the catalytic finger motifs.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB70925.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAC03694.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAC03694.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC       Sequence=BAC86152.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD18591.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR   EMBL; AK055461; BAB70925.1; ALT_FRAME; mRNA.
DR   EMBL; AK091554; BAC03694.1; ALT_SEQ; mRNA.
DR   EMBL; AK125385; BAC86152.1; ALT_INIT; mRNA.
DR   EMBL; AK131446; BAD18591.1; ALT_SEQ; mRNA.
DR   EMBL; AL035593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL139098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL365508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL589910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL590225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS43501.1; -. [Q96NH3-1]
DR   CCDS; CCDS93996.1; -. [Q96NH3-4]
DR   RefSeq; NP_689943.4; NM_152730.5. [Q96NH3-1]
DR   RefSeq; XP_005266918.1; XM_005266861.2.
DR   RefSeq; XP_016865886.1; XM_017010397.1.
DR   RefSeq; XP_016865887.1; XM_017010398.1. [Q96NH3-4]
DR   RefSeq; XP_016865890.1; XM_017010401.1.
DR   AlphaFoldDB; Q96NH3; -.
DR   BioGRID; 128710; 92.
DR   IntAct; Q96NH3; 10.
DR   MINT; Q96NH3; -.
DR   STRING; 9606.ENSP00000381270; -.
DR   GlyGen; Q96NH3; 1 site.
DR   iPTMnet; Q96NH3; -.
DR   PhosphoSitePlus; Q96NH3; -.
DR   BioMuta; TBC1D32; -.
DR   DMDM; 296439461; -.
DR   EPD; Q96NH3; -.
DR   MassIVE; Q96NH3; -.
DR   PaxDb; 9606-ENSP00000381270; -.
DR   PeptideAtlas; Q96NH3; -.
DR   ProteomicsDB; 77512; -. [Q96NH3-1]
DR   ProteomicsDB; 77513; -. [Q96NH3-4]
DR   Antibodypedia; 35180; 59 antibodies from 14 providers.
DR   DNASU; 221322; -.
DR   Ensembl; ENST00000275159.11; ENSP00000275159.6; ENSG00000146350.14. [Q96NH3-4]
DR   Ensembl; ENST00000398212.7; ENSP00000381270.2; ENSG00000146350.14. [Q96NH3-1]
DR   Ensembl; ENST00000464622.5; ENSP00000428839.1; ENSG00000146350.14. [Q96NH3-5]
DR   GeneID; 221322; -.
DR   KEGG; hsa:221322; -.
DR   MANE-Select; ENST00000398212.7; ENSP00000381270.2; NM_152730.6; NP_689943.4.
DR   UCSC; uc003pyo.3; human. [Q96NH3-1]
DR   AGR; HGNC:21485; -.
DR   CTD; 221322; -.
DR   DisGeNET; 221322; -.
DR   GeneCards; TBC1D32; -.
DR   HGNC; HGNC:21485; TBC1D32.
DR   HPA; ENSG00000146350; Tissue enhanced (retina).
DR   MalaCards; TBC1D32; -.
DR   MIM; 615867; gene.
DR   neXtProt; NX_Q96NH3; -.
DR   OpenTargets; ENSG00000146350; -.
DR   PharmGKB; PA134871908; -.
DR   VEuPathDB; HostDB:ENSG00000146350; -.
DR   eggNOG; ENOG502QR93; Eukaryota.
DR   GeneTree; ENSGT00940000153528; -.
DR   HOGENOM; CLU_260246_0_0_1; -.
DR   InParanoid; Q96NH3; -.
DR   OMA; FIHSAYI; -.
DR   OrthoDB; 5475462at2759; -.
DR   PhylomeDB; Q96NH3; -.
DR   TreeFam; TF329092; -.
DR   PathwayCommons; Q96NH3; -.
DR   SignaLink; Q96NH3; -.
DR   BioGRID-ORCS; 221322; 8 hits in 1136 CRISPR screens.
DR   ChiTaRS; TBC1D32; human.
DR   GenomeRNAi; 221322; -.
DR   Pharos; Q96NH3; Tbio.
DR   PRO; PR:Q96NH3; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q96NH3; Protein.
DR   Bgee; ENSG00000146350; Expressed in primordial germ cell in gonad and 141 other cell types or tissues.
DR   ExpressionAtlas; Q96NH3; baseline and differential.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
DR   GO; GO:1905515; P:non-motile cilium assembly; IBA:GO_Central.
DR   GO; GO:0061512; P:protein localization to cilium; IEA:Ensembl.
DR   GO; GO:0003406; P:retinal pigment epithelium development; IEA:Ensembl.
DR   GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR   GO; GO:0060831; P:smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IEA:Ensembl.
DR   Gene3D; 1.10.472.80; Ypt/Rab-GAP domain of gyp1p, domain 3; 1.
DR   InterPro; IPR032735; BROMI.
DR   InterPro; IPR039156; PHAF1/BROMI.
DR   InterPro; IPR035969; Rab-GAP_TBC_sf.
DR   PANTHER; PTHR13465:SF3; PROTEIN BROAD-MINDED; 1.
DR   PANTHER; PTHR13465; UPF0183 PROTEIN; 1.
DR   Pfam; PF14961; BROMI; 2.
DR   SUPFAM; SSF47923; Ypt/Rab-GAP domain of gyp1p; 1.
DR   Genevisible; Q96NH3; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Cilium; Cytoplasm;
KW   Developmental protein; Reference proteome.
FT   CHAIN           1..1257
FT                   /note="Protein broad-minded"
FT                   /id="PRO_0000089557"
FT   DOMAIN          1119..1242
FT                   /note="Rab-GAP TBC"
FT   REGION          131..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         106..108
FT                   /note="EYK -> ELP (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_035579"
FT   VAR_SEQ         109..1257
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_035580"
FT   VAR_SEQ         857
FT                   /note="R -> RLLSVICCDLDTLLLLEAQYQVSEMLLNAQEENILEISESHR (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_014546"
FT   VARIANT         82
FT                   /note="R -> Q (in dbSNP:rs7767455)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_046958"
FT   VARIANT         280
FT                   /note="I -> V (in dbSNP:rs9490157)"
FT                   /id="VAR_046959"
FT   VARIANT         375
FT                   /note="T -> K (in dbSNP:rs9387944)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_046960"
FT   VARIANT         599
FT                   /note="I -> V (in dbSNP:rs7745023)"
FT                   /id="VAR_046961"
FT   CONFLICT        554
FT                   /note="A -> V (in Ref. 1; BAC86152)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        906
FT                   /note="Y -> H (in Ref. 1; BAC03694)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1210
FT                   /note="T -> A (in Ref. 1; BAC86152)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1257 AA;  144756 MW;  3370457AB4238DC0 CRC64;
     MAHFSSEDQA MLQAMLRRLF QSVKEKITGA PSLECAEEIL LHLEETDENF HNYEFVKYLR
     QHIGNTLGSM IEEEMEKCTS DRNQGEECGY DTVVQQVTKR TQESKEYKEM MHYLKNIMIA
     VVESMINKFE EDETRNQERQ KKIQKEKSHS YRTDNCSDSD SSLNQSYKFC QGKLQLILDQ
     LDPGQPKEVR YEALQTLCSA PPSDVLNCEN WTTLCEKLTV SLSDPDPVFS DRILKFCAQT
     FLLSPLHMTK EIYTSLAKYL ESYFLSRENH IPTLSAGVDI TNPNMTRLLK KVRLLNEYQK
     EAPSFWIRHP EKYMEEIVES TLSLLTVKHN QSHVVSQKIL DPIYFFALVD TKAVWFKKWM
     HAHYSRTTVL RLLETKYKSL VTTAIQQCVQ YFEMCKTRKA DETLGHSKHC RNKQKTFYYL
     GQELQYIYFI HSLCLLGRLL IYKQGRKLFP IKLKNKKGLV SLIDLLVLFT QLIYYSPSCP
     KMTSAAHSEN YSPASMVTEV LWILSDQKEC AVECLYNNIV IETLLQPIHN LMKGNEASPN
     CSETALIHIA GILARIASVE EGLILLLYGA NMNSSEESPT GAHIIAQFSK KLLDEDISIF
     SGSEMLPVVK GAFISVCRHI YSTCEGLQVL ITYNLHESIA KAWKKTSLLS ERIPTPVEGS
     DSVSSVSQES QNIMAWEDNL LDDLLHFAAT PKGLLLLQRT GAINECVTFI FNRYAKKLQV
     SRHKKFGYGV LVTRVASTAA GGIALKKSGF INELITELWS NLEYGRDDVR VTHPRTTPVD
     PIDRSCQKSF LALVNLLSYP AIYELVRNQD LPNKTEYSLR EVPTCVIDII DRLIILNSEA
     KIRSLFNYEQ SHIFGLRDFI IDGLSVERNH VLVRINLVGG PLERILPPRL LEKSDNPYPW
     PMFSSYPLPN CYLSDITRNA GIKQDNDLDK LLLCLKISDK QTEWIENCQR QFCKMMKAKP
     DIISGEALIE LLEKFVLHLT ESPSECYFPS VEYTATDANV KNESLSSVQQ LGIKMTVRYG
     KFLSLLKDGA ENDLTWVLKH CERFLKQQQT SIKSSLLCLQ GNYAGHDWFV SSLFMIMLGD
     KEKTFQFLHQ FSRLLTSAFL WLPRLHISSY LPNDTVESGI HPVYFCSTHY IEMLLKAELP
     LVFSAFHMSG FAPSQICLQW ITQCFWNYLD WIEICHYIAT CVFLGPDYQV YICIAVFKHL
     QQDILQHTQT QDLQVFLKEE ALHGFRVSDY FEYMEILEQN YRTVLLRDMR NIRLQST
//