UBL4A_HUMAN
ID UBL4A_HUMAN Reviewed; 157 AA.
AC P11441; Q5HY80;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Ubiquitin-like protein 4A {ECO:0000305};
DE AltName: Full=Ubiquitin-like protein GDX;
GN Name=UBL4A {ECO:0000312|HGNC:HGNC:12505}; Synonyms=DXS254E, GDX, UBL4;
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 [GENOMIC DNA].
RX PubMed=2829204; DOI=10.1073/pnas.85.3.851;
RA Toniolo D., Persico M., Alcalay M.;
RT "A 'housekeeping' gene on the X chromosome encodes a protein similar to
RT ubiquitin.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:851-855(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8733135; DOI=10.1093/hmg/5.5.659;
RA Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L.,
RA Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.;
RT "Long-range sequence analysis in Xq28: thirteen known and six candidate
RT genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci.";
RL Hum. Mol. Genet. 5:659-668(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lung;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, 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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP IDENTIFICATION IN THE BAG6/BAT3 COMPLEX.
RX PubMed=20676083; DOI=10.1038/nature09296;
RA Mariappan M., Li X., Stefanovic S., Sharma A., Mateja A., Keenan R.J.,
RA Hegde R.S.;
RT "A ribosome-associating factor chaperones tail-anchored membrane
RT proteins.";
RL Nature 466:1120-1124(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, 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 [10]
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 [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21636303; DOI=10.1016/j.molcel.2011.05.010;
RA Wang Q., Liu Y., Soetandyo N., Baek K., Hegde R., Ye Y.;
RT "A ubiquitin ligase-associated chaperone holdase maintains polypeptides in
RT soluble states for proteasome degradation.";
RL Mol. Cell 42:758-770(2011).
RN [12]
RP FUNCTION.
RX PubMed=21743475; DOI=10.1038/nature10181;
RA Hessa T., Sharma A., Mariappan M., Eshleman H.D., Gutierrez E., Hegde R.S.;
RT "Protein targeting and degradation are coupled for elimination of
RT mislocalized proteins.";
RL Nature 475:394-397(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP INTERACTION WITH USP13, UBIQUITINATION AT LYS-48 BY AMFR, DEUBIQUITINATION
RP BY USP13, AND MUTAGENESIS OF LYS-48.
RX PubMed=24424410; DOI=10.7554/elife.01369;
RA Liu Y., Soetandyo N., Lee J.G., Liu L., Xu Y., Clemons W.M. Jr., Ye Y.;
RT "USP13 antagonizes gp78 to maintain functionality of a chaperone in ER-
RT associated degradation.";
RL Elife 3:E01369-E01369(2014).
RN [16]
RP FUNCTION.
RX PubMed=28104892; DOI=10.1126/science.aah6130;
RA Shao S., Rodrigo-Brenni M.C., Kivlen M.H., Hegde R.S.;
RT "Mechanistic basis for a molecular triage reaction.";
RL Science 355:298-302(2017).
RN [17]
RP STRUCTURE BY NMR OF 1-74.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the N-terminal ubiquitin-like domain in human
RT ubiquitin-like protein 4A (GDX).";
RL Submitted (MAR-2007) to the PDB data bank.
RN [18] {ECO:0007744|PDB:4X86}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 95-147 IN COMPLEX WITH BAG6,
RP INTERACTION WITH BAG6, AND MUTAGENESIS OF VAL-102; ARG-105; HIS-106;
RP PHE-107; TYR-123 AND LEU-130.
RX PubMed=25713138; DOI=10.1074/jbc.m114.631804;
RA Kuwabara N., Minami R., Yokota N., Matsumoto H., Senda T., Kawahara H.,
RA Kato R.;
RT "Structure of a BAG6 (Bcl-2-associated athanogene 6)-Ubl4a (ubiquitin-like
RT protein 4a) complex reveals a novel binding interface that functions in
RT tail-anchored protein biogenesis.";
RL J. Biol. Chem. 290:9387-9398(2015).
RN [19] {ECO:0007744|PDB:4WWR}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 93-139 IN COMPLEX WITH BAG6,
RP INTERACTION WITH BAG6, IDENTIFICATION IN THE BAG6/BAT3 COMPLEX, MUTAGENESIS
RP OF LEU-43, AND FUNCTION.
RX PubMed=25535373; DOI=10.1073/pnas.1402745112;
RA Mock J.Y., Chartron J.W., Zaslaver M., Xu Y., Ye Y., Clemons W.M. Jr.;
RT "Bag6 complex contains a minimal tail-anchor-targeting module and a mock
RT BAG domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:106-111(2015).
CC -!- FUNCTION: As part of a cytosolic protein quality control complex, the
CC BAG6/BAT3 complex, maintains misfolded and hydrophobic patches-
CC containing proteins in a soluble state and participates in their proper
CC delivery to the endoplasmic reticulum or alternatively can promote
CC their sorting to the proteasome where they undergo degradation
CC (PubMed:20676083, PubMed:21636303, PubMed:21743475, PubMed:28104892).
CC The BAG6/BAT3 complex is involved in the post-translational delivery of
CC tail-anchored/type II transmembrane proteins to the endoplasmic
CC reticulum membrane. Recruited to ribosomes, it interacts with the
CC transmembrane region of newly synthesized tail-anchored proteins and
CC together with SGTA and ASNA1 mediates their delivery to the endoplasmic
CC reticulum (PubMed:20676083, PubMed:28104892, PubMed:25535373). Client
CC proteins that cannot be properly delivered to the endoplasmic reticulum
CC are ubiquitinated and sorted to the proteasome (PubMed:28104892).
CC Similarly, the BAG6/BAT3 complex also functions as a sorting platform
CC for proteins of the secretory pathway that are mislocalized to the
CC cytosol either delivering them to the proteasome for degradation or to
CC the endoplasmic reticulum (PubMed:21743475). The BAG6/BAT3 complex also
CC plays a role in the endoplasmic reticulum-associated degradation
CC (ERAD), a quality control mechanism that eliminates unwanted proteins
CC of the endoplasmic reticulum through their retrotranslocation to the
CC cytosol and their targeting to the proteasome. It maintains these
CC retrotranslocated proteins in an unfolded yet soluble state condition
CC in the cytosol to ensure their proper delivery to the proteasome
CC (PubMed:21636303). {ECO:0000269|PubMed:20676083,
CC ECO:0000269|PubMed:21636303, ECO:0000269|PubMed:21743475,
CC ECO:0000269|PubMed:25535373, ECO:0000269|PubMed:28104892}.
CC -!- SUBUNIT: Component of the BAG6/BAT3 complex, at least composed of BAG6,
CC UBL4A and GET4/TRC35 (PubMed:20676083, PubMed:25535373). Interacts with
CC BAG6; the interaction is direct and required for UBL4A protein
CC stability (PubMed:25713138, PubMed:25535373). Interacts with USP13; may
CC be indirect via BAG6 (PubMed:24424410). {ECO:0000269|PubMed:20676083,
CC ECO:0000269|PubMed:24424410, ECO:0000269|PubMed:25535373,
CC ECO:0000269|PubMed:25713138}.
CC -!- INTERACTION:
CC P11441; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-356983, EBI-5278764;
CC P11441; P28329-3: CHAT; NbExp=3; IntAct=EBI-356983, EBI-25837549;
CC P11441; Q96DN0: ERP27; NbExp=3; IntAct=EBI-356983, EBI-953772;
CC P11441; P22607: FGFR3; NbExp=3; IntAct=EBI-356983, EBI-348399;
CC P11441; P50222: MEOX2; NbExp=3; IntAct=EBI-356983, EBI-748397;
CC P11441; O15055: PER2; NbExp=3; IntAct=EBI-356983, EBI-1054296;
CC P11441; P25815: S100P; NbExp=3; IntAct=EBI-356983, EBI-743700;
CC P11441; O43765: SGTA; NbExp=5; IntAct=EBI-356983, EBI-347996;
CC P11441; Q96EQ0: SGTB; NbExp=4; IntAct=EBI-356983, EBI-744081;
CC P11441; Q9BUZ4: TRAF4; NbExp=6; IntAct=EBI-356983, EBI-3650647;
CC P11441; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-356983, EBI-2130429;
CC P11441; P12504: vif; Xeno; NbExp=2; IntAct=EBI-356983, EBI-779991;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20676083,
CC ECO:0000269|PubMed:21636303}. Nucleus {ECO:0000269|PubMed:21636303}.
CC -!- PTM: Polyubiquitinated. Ubiquitination by AMFR and deubiquitination by
CC USP13 may regulate the interaction between the BAG6/BAT3 complex and
CC SGTA and therefore may regulate client proteins fate.
CC {ECO:0000269|PubMed:24424410}.
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DR EMBL; J03589; AAA36790.1; -; Genomic_DNA.
DR EMBL; L44140; AAA92650.1; -; Genomic_DNA.
DR EMBL; BX664739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471172; EAW72700.1; -; Genomic_DNA.
DR EMBL; BC043346; AAH43346.1; -; mRNA.
DR EMBL; BC053589; AAH53589.1; -; mRNA.
DR CCDS; CCDS14754.1; -.
DR PIR; A31084; A31084.
DR RefSeq; NP_055050.1; NM_014235.4.
DR PDB; 2DZI; NMR; -; A=1-74.
DR PDB; 4WWR; X-ray; 2.00 A; B/D/F/H=93-139.
DR PDB; 4X86; X-ray; 1.85 A; A=95-147.
DR PDB; 7RU9; EM; 3.30 A; E/H=1-157.
DR PDB; 7RUA; EM; 3.40 A; E/H=1-157.
DR PDB; 7RUC; EM; 3.60 A; H=1-157.
DR PDBsum; 2DZI; -.
DR PDBsum; 4WWR; -.
DR PDBsum; 4X86; -.
DR PDBsum; 7RU9; -.
DR PDBsum; 7RUA; -.
DR PDBsum; 7RUC; -.
DR AlphaFoldDB; P11441; -.
DR BMRB; P11441; -.
DR SMR; P11441; -.
DR BioGRID; 113885; 368.
DR ComplexPortal; CPX-132; BAT3 complex.
DR CORUM; P11441; -.
DR IntAct; P11441; 62.
DR MINT; P11441; -.
DR STRING; 9606.ENSP00000358674; -.
DR iPTMnet; P11441; -.
DR MetOSite; P11441; -.
DR PhosphoSitePlus; P11441; -.
DR BioMuta; UBL4A; -.
DR DMDM; 136662; -.
DR EPD; P11441; -.
DR jPOST; P11441; -.
DR MassIVE; P11441; -.
DR MaxQB; P11441; -.
DR PaxDb; P11441; -.
DR PeptideAtlas; P11441; -.
DR PRIDE; P11441; -.
DR ProteomicsDB; 52774; -.
DR Antibodypedia; 504; 229 antibodies from 26 providers.
DR DNASU; 8266; -.
DR Ensembl; ENST00000369660.9; ENSP00000358674.4; ENSG00000102178.13.
DR GeneID; 8266; -.
DR KEGG; hsa:8266; -.
DR MANE-Select; ENST00000369660.9; ENSP00000358674.4; NM_014235.5; NP_055050.1.
DR UCSC; uc004flo.4; human.
DR CTD; 8266; -.
DR DisGeNET; 8266; -.
DR GeneCards; UBL4A; -.
DR HGNC; HGNC:12505; UBL4A.
DR HPA; ENSG00000102178; Tissue enhanced (skeletal).
DR MIM; 312070; gene.
DR neXtProt; NX_P11441; -.
DR OpenTargets; ENSG00000102178; -.
DR PharmGKB; PA37152; -.
DR VEuPathDB; HostDB:ENSG00000102178; -.
DR eggNOG; KOG0001; Eukaryota.
DR GeneTree; ENSGT00730000111022; -.
DR HOGENOM; CLU_119809_0_0_1; -.
DR InParanoid; P11441; -.
DR OMA; SMDTSYM; -.
DR OrthoDB; 1586605at2759; -.
DR PhylomeDB; P11441; -.
DR TreeFam; TF354228; -.
DR PathwayCommons; P11441; -.
DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR SignaLink; P11441; -.
DR BioGRID-ORCS; 8266; 11 hits in 708 CRISPR screens.
DR ChiTaRS; UBL4A; human.
DR EvolutionaryTrace; P11441; -.
DR GeneWiki; UBL4A; -.
DR GenomeRNAi; 8266; -.
DR Pharos; P11441; Tbio.
DR PRO; PR:P11441; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P11441; protein.
DR Bgee; ENSG00000102178; Expressed in hindlimb stylopod muscle and 183 other tissues.
DR ExpressionAtlas; P11441; baseline and differential.
DR Genevisible; P11441; HS.
DR GO; GO:0071818; C:BAT3 complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
DR GO; GO:0019787; F:ubiquitin-like protein transferase activity; TAS:ProtInc.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IDA:ComplexPortal.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0031647; P:regulation of protein stability; IDA:ComplexPortal.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR CDD; cd01807; Ubl_UBL4A_like; 1.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR InterPro; IPR041421; Ubl4_C_TUGS.
DR InterPro; IPR044724; Ubl_UBL4A-like.
DR Pfam; PF17840; Tugs; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..157
FT /note="Ubiquitin-like protein 4A"
FT /id="PRO_0000114864"
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 96..138
FT /note="Required and sufficient for interaction with BAG6"
FT /evidence="ECO:0000269|PubMed:25535373,
FT ECO:0000269|PubMed:25713138"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:24424410"
FT MUTAGEN 43
FT /note="L->A: Reduces tail-anchored proteins delivery."
FT /evidence="ECO:0000269|PubMed:25535373"
FT MUTAGEN 48
FT /note="K->R: Loss of polyubiquitination by AMFR."
FT /evidence="ECO:0000269|PubMed:24424410"
FT MUTAGEN 102
FT /note="V->E,K: No effect on interaction with BAG6."
FT /evidence="ECO:0000269|PubMed:25713138"
FT MUTAGEN 105
FT /note="R->E: No effect on interaction with BAG6."
FT /evidence="ECO:0000269|PubMed:25713138"
FT MUTAGEN 106
FT /note="H->E: Strongly inhibits interaction with BAG6."
FT /evidence="ECO:0000269|PubMed:25713138"
FT MUTAGEN 107
FT /note="F->E,K: Strongly inhibits interaction with BAG6."
FT /evidence="ECO:0000269|PubMed:25713138"
FT MUTAGEN 123
FT /note="Y->E: No effect on interaction with BAG6."
FT /evidence="ECO:0000269|PubMed:25713138"
FT MUTAGEN 130
FT /note="L->E,K: No effect on interaction with BAG6."
FT /evidence="ECO:0000269|PubMed:25713138"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:2DZI"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:2DZI"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:2DZI"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:2DZI"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:2DZI"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:2DZI"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2DZI"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2DZI"
FT HELIX 95..106
FT /evidence="ECO:0007829|PDB:4X86"
FT HELIX 109..129
FT /evidence="ECO:0007829|PDB:4X86"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:4X86"
SQ SEQUENCE 157 AA; 17777 MW; 9D6EE2D20D2C4C60 CRC64;
MQLTVKALQG RECSLQVPED ELVSTLKQLV SEKLNVPVRQ QRLLFKGKAL ADGKRLSDYS
IGPNSKLNLV VKPLEKVLLE EGEAQRLADS PPPQVWQLIS KVLARHFSAA DASRVLEQLQ
RDYERSLSRL TLDDIERLAS RFLHPEVTET MEKGFSK
