Full text data of UBL4A
UBL4A
(DXS254E, GDX, UBL4)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Ubiquitin-like protein 4A (Ubiquitin-like protein GDX)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin-like protein 4A (Ubiquitin-like protein GDX)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P11441
ID UBL4A_HUMAN Reviewed; 157 AA.
AC P11441; Q5HY80;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1989, sequence version 1.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Ubiquitin-like protein 4A;
DE AltName: Full=Ubiquitin-like protein GDX;
GN Name=UBL4A; Synonyms=DXS254E, GDX, UBL4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT to 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.,
RA Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D.,
RA D'Urso M.;
RT "Long-range sequence analysis in Xq28: thirteen known and six
RT candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and
RT 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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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,
RP AND 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
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.
CC -!- FUNCTION: Component of the BAT3 complex, a multiprotein complex
CC involved in the post-translational delivery of tail-anchored (TA)
CC membrane proteins to the endoplasmic reticulum membrane. TA
CC membrane proteins, also named type II transmembrane proteins,
CC contain a single C-terminal transmembrane region. The complex acts
CC by facilitating TA proteins capture by ASNA1/TRC40: it is
CC recruited to ribosomes synthesizing membrane proteins, interacts
CC with the transmembrane region of newly released TA proteins, and
CC transfers them to ASNA1/TRC40 for targeting.
CC -!- SUBUNIT: Component of the BAT3 complex, at least composed of
CC BAG6/BAT3, UBL4A and GET4/TRC35.
CC -!- INTERACTION:
CC P12504:vif (xeno); NbExp=2; IntAct=EBI-356983, EBI-779991;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol.
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
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DR EMBL; J03589; AAA36790.1; -; Genomic_DNA.
DR EMBL; L44140; AAA92650.1; -; Genomic_DNA.
DR EMBL; BX664739; CAI43235.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72700.1; -; Genomic_DNA.
DR EMBL; BC043346; AAH43346.1; -; mRNA.
DR EMBL; BC053589; AAH53589.1; -; mRNA.
DR PIR; A31084; A31084.
DR RefSeq; NP_055050.1; NM_014235.4.
DR UniGene; Hs.76480; -.
DR PDB; 2DZI; NMR; -; A=1-74.
DR PDBsum; 2DZI; -.
DR ProteinModelPortal; P11441; -.
DR SMR; P11441; 1-74.
DR IntAct; P11441; 16.
DR MINT; MINT-1147351; -.
DR STRING; 9606.ENSP00000358674; -.
DR PhosphoSite; P11441; -.
DR DMDM; 136662; -.
DR PaxDb; P11441; -.
DR PRIDE; P11441; -.
DR DNASU; 8266; -.
DR Ensembl; ENST00000369660; ENSP00000358674; ENSG00000102178.
DR Ensembl; ENST00000600314; ENSP00000469636; ENSG00000269715.
DR GeneID; 8266; -.
DR KEGG; hsa:8266; -.
DR UCSC; uc004flo.3; human.
DR CTD; 8266; -.
DR GeneCards; GC0XM153712; -.
DR HGNC; HGNC:12505; UBL4A.
DR HPA; HPA003617; -.
DR MIM; 312070; gene.
DR neXtProt; NX_P11441; -.
DR PharmGKB; PA37152; -.
DR eggNOG; NOG265285; -.
DR HOGENOM; HOG000006827; -.
DR HOVERGEN; HBG072205; -.
DR OMA; CIHRAFR; -.
DR PhylomeDB; P11441; -.
DR EvolutionaryTrace; P11441; -.
DR GeneWiki; UBL4A; -.
DR GenomeRNAi; 8266; -.
DR NextBio; 31028; -.
DR PRO; PR:P11441; -.
DR ArrayExpress; P11441; -.
DR Bgee; P11441; -.
DR CleanEx; HS_UBL4A; -.
DR Genevestigator; P11441; -.
DR GO; GO:0071818; C:BAT3 complex; IDA:UniProtKB.
DR GO; GO:0019787; F:small conjugating protein ligase activity; TAS:ProtInc.
DR GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IMP:UniProtKB.
DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR InterPro; IPR019956; Ubiquitin.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR000626; Ubiquitin_dom.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1 157 Ubiquitin-like protein 4A.
FT /FTId=PRO_0000114864.
FT DOMAIN 1 76 Ubiquitin-like.
FT MOD_RES 90 90 Phosphoserine.
FT STRAND 1 7
FT STRAND 12 17
FT HELIX 23 33
FT TURN 38 40
FT STRAND 42 45
FT HELIX 56 59
FT STRAND 63 65
FT STRAND 68 70
SQ SEQUENCE 157 AA; 17777 MW; 9D6EE2D20D2C4C60 CRC64;
MQLTVKALQG RECSLQVPED ELVSTLKQLV SEKLNVPVRQ QRLLFKGKAL ADGKRLSDYS
IGPNSKLNLV VKPLEKVLLE EGEAQRLADS PPPQVWQLIS KVLARHFSAA DASRVLEQLQ
RDYERSLSRL TLDDIERLAS RFLHPEVTET MEKGFSK
//
ID UBL4A_HUMAN Reviewed; 157 AA.
AC P11441; Q5HY80;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1989, sequence version 1.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Ubiquitin-like protein 4A;
DE AltName: Full=Ubiquitin-like protein GDX;
GN Name=UBL4A; Synonyms=DXS254E, GDX, UBL4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT to 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.,
RA Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D.,
RA D'Urso M.;
RT "Long-range sequence analysis in Xq28: thirteen known and six
RT candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and
RT 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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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,
RP AND 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
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.
CC -!- FUNCTION: Component of the BAT3 complex, a multiprotein complex
CC involved in the post-translational delivery of tail-anchored (TA)
CC membrane proteins to the endoplasmic reticulum membrane. TA
CC membrane proteins, also named type II transmembrane proteins,
CC contain a single C-terminal transmembrane region. The complex acts
CC by facilitating TA proteins capture by ASNA1/TRC40: it is
CC recruited to ribosomes synthesizing membrane proteins, interacts
CC with the transmembrane region of newly released TA proteins, and
CC transfers them to ASNA1/TRC40 for targeting.
CC -!- SUBUNIT: Component of the BAT3 complex, at least composed of
CC BAG6/BAT3, UBL4A and GET4/TRC35.
CC -!- INTERACTION:
CC P12504:vif (xeno); NbExp=2; IntAct=EBI-356983, EBI-779991;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol.
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
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DR EMBL; J03589; AAA36790.1; -; Genomic_DNA.
DR EMBL; L44140; AAA92650.1; -; Genomic_DNA.
DR EMBL; BX664739; CAI43235.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72700.1; -; Genomic_DNA.
DR EMBL; BC043346; AAH43346.1; -; mRNA.
DR EMBL; BC053589; AAH53589.1; -; mRNA.
DR PIR; A31084; A31084.
DR RefSeq; NP_055050.1; NM_014235.4.
DR UniGene; Hs.76480; -.
DR PDB; 2DZI; NMR; -; A=1-74.
DR PDBsum; 2DZI; -.
DR ProteinModelPortal; P11441; -.
DR SMR; P11441; 1-74.
DR IntAct; P11441; 16.
DR MINT; MINT-1147351; -.
DR STRING; 9606.ENSP00000358674; -.
DR PhosphoSite; P11441; -.
DR DMDM; 136662; -.
DR PaxDb; P11441; -.
DR PRIDE; P11441; -.
DR DNASU; 8266; -.
DR Ensembl; ENST00000369660; ENSP00000358674; ENSG00000102178.
DR Ensembl; ENST00000600314; ENSP00000469636; ENSG00000269715.
DR GeneID; 8266; -.
DR KEGG; hsa:8266; -.
DR UCSC; uc004flo.3; human.
DR CTD; 8266; -.
DR GeneCards; GC0XM153712; -.
DR HGNC; HGNC:12505; UBL4A.
DR HPA; HPA003617; -.
DR MIM; 312070; gene.
DR neXtProt; NX_P11441; -.
DR PharmGKB; PA37152; -.
DR eggNOG; NOG265285; -.
DR HOGENOM; HOG000006827; -.
DR HOVERGEN; HBG072205; -.
DR OMA; CIHRAFR; -.
DR PhylomeDB; P11441; -.
DR EvolutionaryTrace; P11441; -.
DR GeneWiki; UBL4A; -.
DR GenomeRNAi; 8266; -.
DR NextBio; 31028; -.
DR PRO; PR:P11441; -.
DR ArrayExpress; P11441; -.
DR Bgee; P11441; -.
DR CleanEx; HS_UBL4A; -.
DR Genevestigator; P11441; -.
DR GO; GO:0071818; C:BAT3 complex; IDA:UniProtKB.
DR GO; GO:0019787; F:small conjugating protein ligase activity; TAS:ProtInc.
DR GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IMP:UniProtKB.
DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR InterPro; IPR019956; Ubiquitin.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR000626; Ubiquitin_dom.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1 157 Ubiquitin-like protein 4A.
FT /FTId=PRO_0000114864.
FT DOMAIN 1 76 Ubiquitin-like.
FT MOD_RES 90 90 Phosphoserine.
FT STRAND 1 7
FT STRAND 12 17
FT HELIX 23 33
FT TURN 38 40
FT STRAND 42 45
FT HELIX 56 59
FT STRAND 63 65
FT STRAND 68 70
SQ SEQUENCE 157 AA; 17777 MW; 9D6EE2D20D2C4C60 CRC64;
MQLTVKALQG RECSLQVPED ELVSTLKQLV SEKLNVPVRQ QRLLFKGKAL ADGKRLSDYS
IGPNSKLNLV VKPLEKVLLE EGEAQRLADS PPPQVWQLIS KVLARHFSAA DASRVLEQLQ
RDYERSLSRL TLDDIERLAS RFLHPEVTET MEKGFSK
//
MIM
312070
*RECORD*
*FIELD* NO
312070
*FIELD* TI
*312070 UBIQUITIN-LIKE 4A; UBL4A
;;UBL4;;
GDX;;
DXS254E
*FIELD* TX
CLONING
Martini et al. (1986) isolated a ubiquitously transcribed region, which
read morethey provisionally named the GDX gene, about 40 kb downstream of the
glucose-6-phosphate dehydrogenase gene (G6PD; 305900) on the X
chromosome. Transcripts of this gene were detected in up to 10 different
cell types, suggesting to Martini et al. (1986) that it, like G6PD, is a
housekeeping gene.
Alcalay and Toniolo (1987) characterized 2 genes, P3 (312090) and GDX,
on Xq28. Several overlapping lambda and cosmid clones linked them to the
G6PD gene. Both lie about 40 kb downstream from the G6PD gene. P3 and
GDX show no sequence homology between themselves or G6PD or to any
previously described genes, but they appear to have been conserved in
evolution. Their expression is ubiquitous. In agreement with the
sequence of many housekeeping genes, their promoter region is GC rich
and lacks signals such as TATA and CAT boxes. GDX encodes a protein of
157 amino acids. It shows strong similarity in its 72 N-terminal amino
acids to ubiquitin (191339), a highly conserved 76-amino acid protein.
Moreover, in the middle of the C-terminus moiety of the GDX protein,
similarities to the thyroglobulin (188450) hormonogenic site, the
sequence that surrounds the tyrosines that will form thyroxine, have
been demonstrated. These similarities suggested to Alcalay and Toniolo
(1987) that the GDX protein plays a key and specific role in vital
functions of the cell.
GENE STRUCTURE
Martini et al. (1986) found that the GDX is transcribed in the same
direction as the upstream G6PD gene.
Alcalay and Toniolo (1987) found that protein P3 and protein GDX are
contained within 7 kb of DNA. The 3-prime end of the P3 gene is 0.5 kb
upstream from the GDX gene.
Filippi et al. (1990) showed that the murine equivalents of the P3 and
GDX genes lie in similar close physical proximity on the mouse X
chromosome. Furthermore, the relative orientation of the 2 genes is the
same. The sequence in both coding and noncoding regions is highly
conserved.
MAPPING
Alcalay and Toniolo (1987) mapped the GDX gene to chromosome Xq28.
GENE FUNCTION
Mariappan et al. (2010) identified a conserved 3-protein complex
composed of BAT3 (142590), TRC35 (612056), and UBL4A that facilitates
tail-anchored protein capture by TRC40 (601913). This BAT3 complex is
recruited to ribosomes synthesizing membrane proteins, interacts with
the transmembrane domains of newly released tail-anchored proteins, and
transfers them to TRC40 for targeting. Depletion of the BAT3 complex
allows non-TRC40 factors to compete for tail-anchored proteins,
explaining their mislocalization in the analogous yeast deletion
strains. Thus, the BAT3 complex acts as a transmembrane domain-selective
chaperone that effectively channels tail-anchored proteins to the TRC40
insertion pathway.
*FIELD* RF
1. Alcalay, M.; Toniolo, D.: Two new genes of the G6PD cluster on
the long arm of the X chromosome. (Abstract) Cytogenet. Cell Genet. 46:
569 only, 1987.
2. Filippi, M.; Tribioli, C.; Toniolo, D.: Linkage and sequence conservation
of the X-linked genes DXS253E (P3) and DXS254E (GdX) in mouse and
man. Genomics 7: 453-457, 1990.
3. Mariappan, M.; Li, X.; Stefanovic, S.; Sharma, A.; Mateja, A.;
Keenan, R. J.; Hegde, R. S.: A ribosome-associating factor chaperones
tail-anchored membrane proteins. Nature 466: 1120-1124, 2010.
4. Martini, G.; Toniolo, D.; Vulliamy, T.; Luzzatto, L.; Dono, R.;
Viglietto, G.; Paonessa, G.; D'Urso, M.; Persico, M. G.: Structural
analysis of the X-linked gene encoding human glucose 6-phosphate dehydrogenase. EMBO
J. 5: 1849-1855, 1986.
*FIELD* CN
Ada Hamosh - updated: 9/14/2010
*FIELD* CD
Victor A. McKusick: 8/31/1987
*FIELD* ED
alopez: 09/15/2010
alopez: 9/14/2010
terry: 9/14/2010
wwang: 6/20/2007
carol: 5/12/2004
mgross: 2/21/2000
mark: 7/5/1996
mimadm: 2/28/1994
carol: 8/31/1992
supermim: 3/17/1992
carol: 7/6/1990
supermim: 3/22/1990
supermim: 3/20/1990
*RECORD*
*FIELD* NO
312070
*FIELD* TI
*312070 UBIQUITIN-LIKE 4A; UBL4A
;;UBL4;;
GDX;;
DXS254E
*FIELD* TX
CLONING
Martini et al. (1986) isolated a ubiquitously transcribed region, which
read morethey provisionally named the GDX gene, about 40 kb downstream of the
glucose-6-phosphate dehydrogenase gene (G6PD; 305900) on the X
chromosome. Transcripts of this gene were detected in up to 10 different
cell types, suggesting to Martini et al. (1986) that it, like G6PD, is a
housekeeping gene.
Alcalay and Toniolo (1987) characterized 2 genes, P3 (312090) and GDX,
on Xq28. Several overlapping lambda and cosmid clones linked them to the
G6PD gene. Both lie about 40 kb downstream from the G6PD gene. P3 and
GDX show no sequence homology between themselves or G6PD or to any
previously described genes, but they appear to have been conserved in
evolution. Their expression is ubiquitous. In agreement with the
sequence of many housekeeping genes, their promoter region is GC rich
and lacks signals such as TATA and CAT boxes. GDX encodes a protein of
157 amino acids. It shows strong similarity in its 72 N-terminal amino
acids to ubiquitin (191339), a highly conserved 76-amino acid protein.
Moreover, in the middle of the C-terminus moiety of the GDX protein,
similarities to the thyroglobulin (188450) hormonogenic site, the
sequence that surrounds the tyrosines that will form thyroxine, have
been demonstrated. These similarities suggested to Alcalay and Toniolo
(1987) that the GDX protein plays a key and specific role in vital
functions of the cell.
GENE STRUCTURE
Martini et al. (1986) found that the GDX is transcribed in the same
direction as the upstream G6PD gene.
Alcalay and Toniolo (1987) found that protein P3 and protein GDX are
contained within 7 kb of DNA. The 3-prime end of the P3 gene is 0.5 kb
upstream from the GDX gene.
Filippi et al. (1990) showed that the murine equivalents of the P3 and
GDX genes lie in similar close physical proximity on the mouse X
chromosome. Furthermore, the relative orientation of the 2 genes is the
same. The sequence in both coding and noncoding regions is highly
conserved.
MAPPING
Alcalay and Toniolo (1987) mapped the GDX gene to chromosome Xq28.
GENE FUNCTION
Mariappan et al. (2010) identified a conserved 3-protein complex
composed of BAT3 (142590), TRC35 (612056), and UBL4A that facilitates
tail-anchored protein capture by TRC40 (601913). This BAT3 complex is
recruited to ribosomes synthesizing membrane proteins, interacts with
the transmembrane domains of newly released tail-anchored proteins, and
transfers them to TRC40 for targeting. Depletion of the BAT3 complex
allows non-TRC40 factors to compete for tail-anchored proteins,
explaining their mislocalization in the analogous yeast deletion
strains. Thus, the BAT3 complex acts as a transmembrane domain-selective
chaperone that effectively channels tail-anchored proteins to the TRC40
insertion pathway.
*FIELD* RF
1. Alcalay, M.; Toniolo, D.: Two new genes of the G6PD cluster on
the long arm of the X chromosome. (Abstract) Cytogenet. Cell Genet. 46:
569 only, 1987.
2. Filippi, M.; Tribioli, C.; Toniolo, D.: Linkage and sequence conservation
of the X-linked genes DXS253E (P3) and DXS254E (GdX) in mouse and
man. Genomics 7: 453-457, 1990.
3. Mariappan, M.; Li, X.; Stefanovic, S.; Sharma, A.; Mateja, A.;
Keenan, R. J.; Hegde, R. S.: A ribosome-associating factor chaperones
tail-anchored membrane proteins. Nature 466: 1120-1124, 2010.
4. Martini, G.; Toniolo, D.; Vulliamy, T.; Luzzatto, L.; Dono, R.;
Viglietto, G.; Paonessa, G.; D'Urso, M.; Persico, M. G.: Structural
analysis of the X-linked gene encoding human glucose 6-phosphate dehydrogenase. EMBO
J. 5: 1849-1855, 1986.
*FIELD* CN
Ada Hamosh - updated: 9/14/2010
*FIELD* CD
Victor A. McKusick: 8/31/1987
*FIELD* ED
alopez: 09/15/2010
alopez: 9/14/2010
terry: 9/14/2010
wwang: 6/20/2007
carol: 5/12/2004
mgross: 2/21/2000
mark: 7/5/1996
mimadm: 2/28/1994
carol: 8/31/1992
supermim: 3/17/1992
carol: 7/6/1990
supermim: 3/22/1990
supermim: 3/20/1990