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P11441

- UBL4A_HUMAN

UniProt

P11441 - UBL4A_HUMAN

Protein

Ubiquitin-like protein 4A

Gene

UBL4A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Component of the BAT3 complex, a multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. The complex acts by facilitating TA proteins capture by ASNA1/TRC40: it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins, and transfers them to ASNA1/TRC40 for targeting.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. small conjugating protein ligase activity Source: ProtInc

    GO - Biological processi

    1. cellular protein modification process Source: ProtInc
    2. tail-anchored membrane protein insertion into ER membrane Source: UniProtKB
    3. transport Source: UniProtKB-KW

    Keywords - Biological processi

    Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-like protein 4A
    Alternative name(s):
    Ubiquitin-like protein GDX
    Gene namesi
    Name:UBL4A
    Synonyms:DXS254E, GDX, UBL4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:12505. UBL4A.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication

    GO - Cellular componenti

    1. BAT3 complex Source: UniProtKB
    2. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37152.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 157157Ubiquitin-like protein 4APRO_0000114864Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei90 – 901Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP11441.
    PaxDbiP11441.
    PRIDEiP11441.

    PTM databases

    PhosphoSiteiP11441.

    Expressioni

    Gene expression databases

    ArrayExpressiP11441.
    BgeeiP11441.
    CleanExiHS_UBL4A.
    GenevestigatoriP11441.

    Organism-specific databases

    HPAiHPA003617.

    Interactioni

    Subunit structurei

    Component of the BAT3 complex, at least composed of BAG6/BAT3, UBL4A and GET4/TRC35.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    vifP125042EBI-356983,EBI-779991From a different organism.

    Protein-protein interaction databases

    BioGridi113885. 273 interactions.
    IntActiP11441. 16 interactions.
    MINTiMINT-1147351.
    STRINGi9606.ENSP00000358674.

    Structurei

    Secondary structure

    157
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1 – 77
    Beta strandi12 – 176
    Helixi23 – 3311
    Turni38 – 403
    Beta strandi42 – 454
    Helixi56 – 594
    Beta strandi63 – 653
    Beta strandi68 – 703

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DZINMR-A1-74[»]
    ProteinModelPortaliP11441.
    SMRiP11441. Positions 1-74.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11441.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 7676Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG265285.
    HOGENOMiHOG000006827.
    HOVERGENiHBG072205.
    OMAiCIHRAFR.
    PhylomeDBiP11441.
    TreeFamiTF354228.

    Family and domain databases

    InterProiIPR019956. Ubiquitin.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR019954. Ubiquitin_CS.
    [Graphical view]
    PfamiPF00240. ubiquitin. 1 hit.
    [Graphical view]
    PRINTSiPR00348. UBIQUITIN.
    SMARTiSM00213. UBQ. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    PROSITEiPS00299. UBIQUITIN_1. 1 hit.
    PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P11441-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQLTVKALQG RECSLQVPED ELVSTLKQLV SEKLNVPVRQ QRLLFKGKAL    50
    ADGKRLSDYS IGPNSKLNLV VKPLEKVLLE EGEAQRLADS PPPQVWQLIS 100
    KVLARHFSAA DASRVLEQLQ RDYERSLSRL TLDDIERLAS RFLHPEVTET 150
    MEKGFSK 157
    Length:157
    Mass (Da):17,777
    Last modified:October 1, 1989 - v1
    Checksum:i9D6EE2D20D2C4C60
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03589 Genomic DNA. Translation: AAA36790.1.
    L44140 Genomic DNA. Translation: AAA92650.1.
    BX664739 Genomic DNA. Translation: CAI43235.1.
    CH471172 Genomic DNA. Translation: EAW72700.1.
    BC043346 mRNA. Translation: AAH43346.1.
    BC053589 mRNA. Translation: AAH53589.1.
    CCDSiCCDS14754.1.
    PIRiA31084.
    RefSeqiNP_055050.1. NM_014235.4.
    UniGeneiHs.76480.

    Genome annotation databases

    EnsembliENST00000369660; ENSP00000358674; ENSG00000102178.
    GeneIDi8266.
    KEGGihsa:8266.
    UCSCiuc004flo.3. human.

    Polymorphism databases

    DMDMi136662.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03589 Genomic DNA. Translation: AAA36790.1 .
    L44140 Genomic DNA. Translation: AAA92650.1 .
    BX664739 Genomic DNA. Translation: CAI43235.1 .
    CH471172 Genomic DNA. Translation: EAW72700.1 .
    BC043346 mRNA. Translation: AAH43346.1 .
    BC053589 mRNA. Translation: AAH53589.1 .
    CCDSi CCDS14754.1.
    PIRi A31084.
    RefSeqi NP_055050.1. NM_014235.4.
    UniGenei Hs.76480.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DZI NMR - A 1-74 [» ]
    ProteinModelPortali P11441.
    SMRi P11441. Positions 1-74.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113885. 273 interactions.
    IntActi P11441. 16 interactions.
    MINTi MINT-1147351.
    STRINGi 9606.ENSP00000358674.

    PTM databases

    PhosphoSitei P11441.

    Polymorphism databases

    DMDMi 136662.

    Proteomic databases

    MaxQBi P11441.
    PaxDbi P11441.
    PRIDEi P11441.

    Protocols and materials databases

    DNASUi 8266.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369660 ; ENSP00000358674 ; ENSG00000102178 .
    GeneIDi 8266.
    KEGGi hsa:8266.
    UCSCi uc004flo.3. human.

    Organism-specific databases

    CTDi 8266.
    GeneCardsi GC0XM153712.
    HGNCi HGNC:12505. UBL4A.
    HPAi HPA003617.
    MIMi 312070. gene.
    neXtProti NX_P11441.
    PharmGKBi PA37152.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG265285.
    HOGENOMi HOG000006827.
    HOVERGENi HBG072205.
    OMAi CIHRAFR.
    PhylomeDBi P11441.
    TreeFami TF354228.

    Miscellaneous databases

    EvolutionaryTracei P11441.
    GeneWikii UBL4A.
    GenomeRNAii 8266.
    NextBioi 31028.
    PROi P11441.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11441.
    Bgeei P11441.
    CleanExi HS_UBL4A.
    Genevestigatori P11441.

    Family and domain databases

    InterProi IPR019956. Ubiquitin.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR019954. Ubiquitin_CS.
    [Graphical view ]
    Pfami PF00240. ubiquitin. 1 hit.
    [Graphical view ]
    PRINTSi PR00348. UBIQUITIN.
    SMARTi SM00213. UBQ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    PROSITEi PS00299. UBIQUITIN_1. 1 hit.
    PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A 'housekeeping' gene on the X chromosome encodes a protein similar to ubiquitin."
      Toniolo D., Persico M., Alcalay M.
      Proc. Natl. Acad. Sci. U.S.A. 85:851-855(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci."
      Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.
      Hum. Mol. Genet. 5:659-668(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain and Lung.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "A ribosome-associating factor chaperones tail-anchored membrane proteins."
      Mariappan M., Li X., Stefanovic S., Sharma A., Mateja A., Keenan R.J., Hegde R.S.
      Nature 466:1120-1124(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BAG6/BAT3 COMPLEX.
    9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Solution structure of the N-terminal ubiquitin-like domain in human ubiquitin-like protein 4A (GDX)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (MAR-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-74.

    Entry informationi

    Entry nameiUBL4A_HUMAN
    AccessioniPrimary (citable) accession number: P11441
    Secondary accession number(s): Q5HY80
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3