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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
 
 
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