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Q9ES00

- UBE4B_MOUSE

UniProt

Q9ES00 - UBE4B_MOUSE

Protein

Ubiquitin conjugation factor E4 B

Gene

Ube4b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Binds to the ubiquitin moieties of preformed conjugates and catalyzes ubiquitin chain assembly in conjunction with E1, E2, and E3.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei109 – 1102Cleavage; by caspase-3 and caspase-7By similarity
    Sitei123 – 1242Cleavage; by caspase-6 and granzyme BBy similarity

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. ubiquitin-ubiquitin ligase activity Source: InterPro
    3. unfolded protein binding Source: UniProtKB

    GO - Biological processi

    1. granzyme-mediated apoptotic signaling pathway Source: UniProtKB
    2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
    3. protein folding Source: UniProtKB
    4. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
    5. response to UV Source: UniProtKB

    Keywords - Biological processi

    Ubl conjugation pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin conjugation factor E4 B
    Alternative name(s):
    Ubiquitin fusion degradation protein 2
    Ufd2a
    Gene namesi
    Name:Ube4b
    Synonyms:Ufd2
    OrganismiMus musculus (Mouse)Imported
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1927086. Ube4b.

    Subcellular locationi

    Cytoplasm 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11731173Ubiquitin conjugation factor E4 BPRO_0000194994Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei31 – 311PhosphoserineBy similarity
    Modified residuei84 – 841PhosphoserineBy similarity
    Modified residuei88 – 881PhosphoserineBy similarity
    Modified residuei90 – 901PhosphoserineBy similarity
    Modified residuei101 – 1011PhosphoserineBy similarity
    Modified residuei103 – 1031PhosphoserineBy similarity
    Modified residuei674 – 6741PhosphoserineBy similarity
    Modified residuei1136 – 11361PhosphoserineBy similarity

    Post-translational modificationi

    Proteolytically cleaved by caspases during apoptosis. Cleaved efficiently at Asp-123 by caspase-6 and granzyme B. Cleaved with approximately 10-fold less efficiency at Asp-109 by caspase-3 and caspase-7 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9ES00.
    PaxDbiQ9ES00.
    PRIDEiQ9ES00.

    PTM databases

    PhosphoSiteiQ9ES00.

    Expressioni

    Tissue specificityi

    Expressed predominantly in neuronal tissues.1 Publication

    Gene expression databases

    ArrayExpressiQ9ES00.
    BgeeiQ9ES00.
    GenevestigatoriQ9ES00.

    Interactioni

    Subunit structurei

    Interacts with VCP.1 Publication

    Protein-protein interaction databases

    BioGridi211009. 8 interactions.
    IntActiQ9ES00. 1 interaction.

    Structurei

    Secondary structure

    1
    1173
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni1101 – 11033
    Turni1106 – 11083
    Beta strandi1113 – 11175
    Beta strandi1123 – 11253
    Helixi1126 – 113510
    Turni1140 – 11423
    Helixi1148 – 11503
    Helixi1155 – 117016

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KR4NMR-A1092-1173[»]
    ProteinModelPortaliQ9ES00.
    SMRiQ9ES00. Positions 1092-1173.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1098 – 117174U-boxAdd
    BLAST

    Sequence similaritiesi

    Contains 1 U-box domain.Curated

    Phylogenomic databases

    eggNOGiCOG5113.
    GeneTreeiENSGT00390000009300.
    HOVERGENiHBG058129.
    InParanoidiQ6DID4.
    KOiK10597.
    OMAiTENMLEP.
    OrthoDBiEOG7TXKFT.
    TreeFamiTF300802.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR019474. Ub_conjug_fac_E4_core.
    IPR003613. Ubox_domain.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF04564. U-box. 1 hit.
    PF10408. Ufd2P_core. 1 hit.
    [Graphical view]
    SMARTiSM00504. Ubox. 1 hit.
    [Graphical view]
    PROSITEiPS51698. U_BOX. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9ES00-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEELSADEIR RRRLARLAGG QTSQPTTPLT SPQRENPPGP PIAASAPGPS     50
    QSLGLNVHNM TPATSPIGAA GVAHRSQSSE GVSSLSSSPS NSLETQSQSL 100
    SRSQSMDIDG VSCEKSMSQV DVDSGIENME VDENDRREKR SLSDKEPSSG 150
    PEVSEEQALQ LVCKIFRVSW KDRDRDVIFL SSLSAQFKQN PKEVFSDFKD 200
    LIGQILMEVL MMSTQTRDEN PFASLTATSQ PIATAARSPD RNLMLNTGSS 250
    SGTSPMFCNM GSFSTSSLSS LGASGGASNW DSYSDHFTIE TCKETDMLNY 300
    LIECFDRVGI EEKKAPKMCS QPAVSQLLSN IRSQCISHTA LVLQGSLTQP 350
    RSLQQPSFLV PYMLCRNLPY GFIQELVRTT HQDEEVFKQI FIPILQGLAL 400
    AAKECSLESD YFKYPLMALG ELCETKFGKT HPMCNLVASL PLWLPKSLSP 450
    GSGRELQRLS YLGAFFSFSV FAEDDAKVVE KYFSGPAITL ENTRVVSQSL 500
    QHYLELGRQE LFKILHSILL NGETREAALS YMAALVNANM KKAQMQADDR 550
    LVSTDGFMLN LLWVLQQLST KIKLETVDPT YIFHPRCRIT LPNDETRINA 600
    TMEDVNERLT ELYGDQPPFS EPKFPTECFF LTLHAHHLSI LPSCRRYIRR 650
    LRAIRELNRT VEDLKNNESQ WKDSPLATRH REMLKRCKTQ LKKLVRCKAC 700
    ADAGLLDESF LRRCLNFYGL LIQLMLRILD PAYPDVTLPL NSEVPKVFAA 750
    LPEFYVEDVA EFLFFIVQYS PQVLYEPCTQ DIVMFLVVML CNQNYIRNPY 800
    LVAKLVEVMF MTNPSVQPRT QKFFEMIENH PLSTKLLVPS LMKFYTDVEH 850
    TGATSEFYDK FTIRYHISTI FKSLWQNIAH HGTFMEEFNS GKQFVRYINM 900
    LINDTTFLLD ESLESLKRIH EVQEEMKNKE QWDQLPRDQQ QARQSQLAQD 950
    ERVSRSYLAL ATETVDMFHL LTKQVQKPFL RPELGPRLAA MLNFNLQQLC 1000
    GPKCRDLKVE NPEKYGFEPK KLLDQLTDIY LQLDCARFAK AIADDQRSYS 1050
    KELFEEVISK MRKAGIKSTI AIEKFKLLAE KVEEIVAKNA RAEIDYSDAP 1100
    DEFRDPLMDT LMTDPVRLPS GTVMDRSIIL RHLLNSPTDP FNRQMLTESM 1150
    LEPVPELKEQ IQAWMREKQS SDH 1173
    Length:1,173
    Mass (Da):133,318
    Last modified:July 27, 2011 - v3
    Checksum:iFC4879E47672E983
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti298 – 2981L → P in AAG17287. (PubMed:11027338)Curated
    Sequence conflicti408 – 4081E → D in AAG17287. (PubMed:11027338)Curated
    Sequence conflicti408 – 4081E → D in BAC56586. (PubMed:12504083)Curated
    Sequence conflicti674 – 6741S → T in BAC26672. (PubMed:16141072)Curated
    Sequence conflicti697 – 6971C → Y in AAG17287. (PubMed:11027338)Curated
    Sequence conflicti753 – 7531E → K in BAC26672. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF260924 mRNA. Translation: AAG17285.1. Different termination.
    AF260926 mRNA. Translation: AAG17287.1.
    AF260927 Genomic DNA. Translation: AAG38492.1.
    AB083274 Genomic DNA. Translation: BAC56586.1.
    AK029914 mRNA. Translation: BAC26672.1.
    AL606973 Genomic DNA. Translation: CAM16303.1.
    BC075620 mRNA. Translation: AAH75620.1.
    CCDSiCCDS18958.1.
    RefSeqiNP_071305.2. NM_022022.3.
    UniGeneiMm.415260.
    Mm.478205.

    Genome annotation databases

    EnsembliENSMUST00000103212; ENSMUSP00000099501; ENSMUSG00000028960.
    GeneIDi63958.
    KEGGimmu:63958.
    UCSCiuc012dpr.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF260924 mRNA. Translation: AAG17285.1 . Different termination.
    AF260926 mRNA. Translation: AAG17287.1 .
    AF260927 Genomic DNA. Translation: AAG38492.1 .
    AB083274 Genomic DNA. Translation: BAC56586.1 .
    AK029914 mRNA. Translation: BAC26672.1 .
    AL606973 Genomic DNA. Translation: CAM16303.1 .
    BC075620 mRNA. Translation: AAH75620.1 .
    CCDSi CCDS18958.1.
    RefSeqi NP_071305.2. NM_022022.3.
    UniGenei Mm.415260.
    Mm.478205.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KR4 NMR - A 1092-1173 [» ]
    ProteinModelPortali Q9ES00.
    SMRi Q9ES00. Positions 1092-1173.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211009. 8 interactions.
    IntActi Q9ES00. 1 interaction.

    PTM databases

    PhosphoSitei Q9ES00.

    Proteomic databases

    MaxQBi Q9ES00.
    PaxDbi Q9ES00.
    PRIDEi Q9ES00.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000103212 ; ENSMUSP00000099501 ; ENSMUSG00000028960 .
    GeneIDi 63958.
    KEGGi mmu:63958.
    UCSCi uc012dpr.1. mouse.

    Organism-specific databases

    CTDi 10277.
    MGIi MGI:1927086. Ube4b.

    Phylogenomic databases

    eggNOGi COG5113.
    GeneTreei ENSGT00390000009300.
    HOVERGENi HBG058129.
    InParanoidi Q6DID4.
    KOi K10597.
    OMAi TENMLEP.
    OrthoDBi EOG7TXKFT.
    TreeFami TF300802.

    Miscellaneous databases

    ChiTaRSi UBE4B. mouse.
    NextBioi 319825.
    PROi Q9ES00.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9ES00.
    Bgeei Q9ES00.
    Genevestigatori Q9ES00.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR019474. Ub_conjug_fac_E4_core.
    IPR003613. Ubox_domain.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF04564. U-box. 1 hit.
    PF10408. Ufd2P_core. 1 hit.
    [Graphical view ]
    SMARTi SM00504. Ubox. 1 hit.
    [Graphical view ]
    PROSITEi PS51698. U_BOX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A Ufd2/D4Cole1e chimeric protein and overexpression of Rbp7 in the slow Wallerian degeneration (WldS) mouse."
      Conforti L., Tarlton A., Mack T.G.A., Mi W., Buckmaster E.A., Wagner D., Perry V.H., Coleman M.P.
      Proc. Natl. Acad. Sci. U.S.A. 97:11377-11382(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: C57BL/Ola.
      Tissue: Brain.
    2. "Characterization of the mouse gene for the U-box-type ubiquitin ligase UFD2a."
      Kaneko C., Hatakeyama S., Matsumoto M., Yada M., Nakayama K., Nakayama K.
      Biochem. Biophys. Res. Commun. 300:297-304(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: T-cell.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Testis.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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].
      Strain: C57BL/6.
      Tissue: Brain.
    6. Cited for: SUBCELLULAR LOCATION, ROLE IN DELAY OF WALLERIAN DEGENERATION.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiUBE4B_MOUSE
    AccessioniPrimary (citable) accession number: Q9ES00
    Secondary accession number(s): Q6DID4, Q9EQE0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2003
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 111 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In strain C57BL/Ola, a 85 kb region on chromosome 4 containing Nmnat1 and Ube4b is triplicated. Ube4b becomes linked to Nmnat1 and encodes a fusion protein located in the nucleus which is responsible for the delayed Wallerian degeneration of injured axons in C57BL/Ola.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3