U119B_HUMAN
ID U119B_HUMAN Reviewed; 251 AA.
AC A6NIH7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Protein unc-119 homolog B;
GN Name=UNC119B;
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=Uterus;
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=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
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=Placenta;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-24, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
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 [7]
RP FUNCTION, LIPID-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH NPHP3; CYS1
RP AND MACIR, IDENTIFICATION IN A COMPLEX WITH ARL3 AND RP2, AND MUTAGENESIS
RP OF PHE-144; PHE-148 AND PHE-207.
RX PubMed=22085962; DOI=10.1101/gad.173443.111;
RA Wright K.J., Baye L.M., Olivier-Mason A., Mukhopadhyay S., Sang L.,
RA Kwong M., Wang W., Pretorius P.R., Sheffield V.C., Sengupta P.,
RA Slusarski D.C., Jackson P.K.;
RT "An ARL3-UNC119-RP2 GTPase cycle targets myristoylated NPHP3 to the primary
RT cilium.";
RL Genes Dev. 25:2347-2360(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Myristoyl-binding protein that acts as a cargo adapter:
CC specifically binds the myristoyl moiety of a subset of N-terminally
CC myristoylated proteins and is required for their localization. Binds
CC myristoylated NPHP3 and plays a key role in localization of NPHP3 to
CC the primary cilium membrane. Does not bind all myristoylated proteins.
CC Probably plays a role in trafficking proteins in photoreceptor cells.
CC {ECO:0000269|PubMed:22085962}.
CC -!- SUBUNIT: Found in a complex with ARL3, RP2 and UNC119B; RP2 induces
CC hydrolysis of GTP ARL3 in the complex, leading to the release of
CC UNC119B. Interacts with NPHP3 (when myristoylated). Interacts with CYS1
CC (when myristoylated). Interacts with MACIR; interaction only takes
CC place when UNC119B is not liganded with myristoylated proteins.
CC {ECO:0000269|PubMed:22085962}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:22085962}. Note=Enriched at the transition zone and
CC extended into the proximal end of the cilium.
CC -!- DOMAIN: Adopts an immunoglobulin-like beta-sandwich fold forming a
CC hydrophobic cavity that capture N-terminally myristoylated target
CC peptides. Phe residues within the hydrophobic beta sandwich are
CC required for myristate binding (PubMed:22085962).
CC {ECO:0000269|PubMed:22085962}.
CC -!- SIMILARITY: Belongs to the PDE6D/unc-119 family. {ECO:0000305}.
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DR EMBL; AK126367; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC069234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW98216.1; -; Genomic_DNA.
DR EMBL; BC004815; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS31914.1; -.
DR RefSeq; NP_001074002.1; NM_001080533.2.
DR PDB; 7OK6; X-ray; 1.95 A; AAA/HHH=66-251.
DR PDB; 7OK7; X-ray; 3.15 A; G/H/I/J/K/L=66-248.
DR PDBsum; 7OK6; -.
DR PDBsum; 7OK7; -.
DR AlphaFoldDB; A6NIH7; -.
DR SMR; A6NIH7; -.
DR BioGRID; 124237; 50.
DR DIP; DIP-61819N; -.
DR IntAct; A6NIH7; 9.
DR MINT; A6NIH7; -.
DR STRING; 9606.ENSP00000344942; -.
DR iPTMnet; A6NIH7; -.
DR PhosphoSitePlus; A6NIH7; -.
DR BioMuta; UNC119B; -.
DR EPD; A6NIH7; -.
DR jPOST; A6NIH7; -.
DR MassIVE; A6NIH7; -.
DR MaxQB; A6NIH7; -.
DR PaxDb; A6NIH7; -.
DR PeptideAtlas; A6NIH7; -.
DR PRIDE; A6NIH7; -.
DR ProteomicsDB; 1270; -.
DR Antibodypedia; 53998; 60 antibodies from 14 providers.
DR DNASU; 84747; -.
DR Ensembl; ENST00000344651.5; ENSP00000344942.4; ENSG00000175970.11.
DR GeneID; 84747; -.
DR KEGG; hsa:84747; -.
DR MANE-Select; ENST00000344651.5; ENSP00000344942.4; NM_001080533.3; NP_001074002.1.
DR UCSC; uc001tyz.4; human.
DR CTD; 84747; -.
DR DisGeNET; 84747; -.
DR GeneCards; UNC119B; -.
DR HGNC; HGNC:16488; UNC119B.
DR HPA; ENSG00000175970; Low tissue specificity.
DR neXtProt; NX_A6NIH7; -.
DR OpenTargets; ENSG00000175970; -.
DR PharmGKB; PA38152; -.
DR VEuPathDB; HostDB:ENSG00000175970; -.
DR eggNOG; KOG4037; Eukaryota.
DR GeneTree; ENSGT00390000014595; -.
DR HOGENOM; CLU_088825_0_0_1; -.
DR InParanoid; A6NIH7; -.
DR OMA; IAKPPHC; -.
DR OrthoDB; 1270912at2759; -.
DR PhylomeDB; A6NIH7; -.
DR TreeFam; TF314474; -.
DR PathwayCommons; A6NIH7; -.
DR Reactome; R-HSA-5624138; Trafficking of myristoylated proteins to the cilium.
DR SignaLink; A6NIH7; -.
DR BioGRID-ORCS; 84747; 24 hits in 1078 CRISPR screens.
DR ChiTaRS; UNC119B; human.
DR GenomeRNAi; 84747; -.
DR Pharos; A6NIH7; Tbio.
DR PRO; PR:A6NIH7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; A6NIH7; protein.
DR Bgee; ENSG00000175970; Expressed in ventricular zone and 98 other tissues.
DR Genevisible; A6NIH7; HS.
DR GO; GO:0035869; C:ciliary transition zone; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0042953; P:lipoprotein transport; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR Gene3D; 2.70.50.40; -; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR008015; PDED_dom.
DR InterPro; IPR037036; PDED_dom_sf.
DR Pfam; PF05351; GMP_PDE_delta; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Lipid-binding; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..251
FT /note="Protein unc-119 homolog B"
FT /id="PRO_0000337228"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 142
FT /ligand="tetradecanoate"
FT /ligand_id="ChEBI:CHEBI:30807"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MUTAGEN 144
FT /note="F->A: Reduced binding to myristoylated proteins;
FT when associated with A-148 and A-207."
FT /evidence="ECO:0000269|PubMed:22085962"
FT MUTAGEN 148
FT /note="F->A: Reduced binding to myristoylated proteins;
FT when associated with A-144 and A-207."
FT /evidence="ECO:0000269|PubMed:22085962"
FT MUTAGEN 207
FT /note="F->A: Reduced binding to myristoylated proteins;
FT when associated with A-144 and A-148."
FT /evidence="ECO:0000269|PubMed:22085962"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:7OK7"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:7OK7"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:7OK7"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:7OK7"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:7OK7"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:7OK7"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:7OK7"
FT STRAND 152..161
FT /evidence="ECO:0007829|PDB:7OK7"
FT STRAND 167..178
FT /evidence="ECO:0007829|PDB:7OK7"
FT STRAND 181..193
FT /evidence="ECO:0007829|PDB:7OK7"
FT STRAND 198..206
FT /evidence="ECO:0007829|PDB:7OK7"
FT HELIX 212..220
FT /evidence="ECO:0007829|PDB:7OK7"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:7OK7"
FT STRAND 236..247
FT /evidence="ECO:0007829|PDB:7OK7"
SQ SEQUENCE 251 AA; 28137 MW; 3041B68EE89B3BD4 CRC64;
MSGSNPKAAA AASAAGPGGL VAGKEEKKKA GGGVLNRLKA RRQAPHHAAD DGVGAAVTEQ
ELLALDTIRP EHVLRLSRVT ENYLCKPEDN IYSIDFTRFK IRDLETGTVL FEIAKPCVSD
QEEDEEEGGG DVDISAGRFV RYQFTPAFLR LRTVGATVEF TVGDKPVSNF RMIERHYFRE
HLLKNFDFDF GFCIPSSRNT CEHIYEFPQL SEDVIRLMIE NPYETRSDSF YFVDNKLIMH
NKADYAYNGG Q