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Ubiquitin conjugation factor E4 B (EC 2.3.2.27) (Homozygously deleted in neuroblastoma 1) (RING-type E3 ubiquitin transferase E4 B) (Ubiquitin fusion degradation protein 2)

 UBE4B_HUMAN             Reviewed;        1302 AA.
O95155; A8K8S9; G0ZJH6; O75169; O95338; Q5SZ12; Q5SZ16; Q96QD4;
Q9BYI7;
01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
25-OCT-2017, entry version 156.
RecName: Full=Ubiquitin conjugation factor E4 B {ECO:0000305};
EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9ES00};
AltName: Full=Homozygously deleted in neuroblastoma 1 {ECO:0000312|EMBL:BAB40446.1};
AltName: Full=RING-type E3 ubiquitin transferase E4 B;
AltName: Full=Ubiquitin fusion degradation protein 2 {ECO:0000312|EMBL:AAD02233.1};
Name=UBE4B {ECO:0000312|HGNC:HGNC:12500};
Synonyms=HDNB1 {ECO:0000312|EMBL:BAB40446.1},
KIAA0684 {ECO:0000312|EMBL:BAA31659.3},
UFD2 {ECO:0000312|EMBL:AAD02233.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9653645; DOI=10.1006/geno.1997.5186;
Onyango P., Lubyova B., Gardellin P., Kurzbauer R., Weith A.;
"Molecular cloning and expression analysis of five novel genes in
chromosome 1p36.";
Genomics 50:187-198(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Substantia nigra;
PubMed=10980605; DOI=10.1038/sj.onc.1203786;
Ohira M., Kageyama H., Mihara M., Furuta S., Machida T.,
Shishikura T., Takayasu H., Islam A., Nakamura Y., Takahashi M.,
Tomioka N., Sakiyama S., Kaneko Y., Toyoda A., Hattori M., Sakaki Y.,
Ohki M., Horii A., Soeda E., Inazawa J., Seki N., Kuma H., Nozawa I.,
Nakagawara A.;
"Identification and characterization of a 500-kb homozygously deleted
region at 1p36.2-p36.3 in a neuroblastoma cell line.";
Oncogene 19:4302-4307(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY,
MUTAGENESIS OF ASP-109; ASP-121 AND ASP-123, AND CLEAVAGE BY CASPASES.
PubMed=11802788; DOI=10.1042/0264-6021:3610587;
Mahoney J.A., Odin J.A., White S.M., Shaffer D., Koff A.,
Casciola-Rosen L., Rosen A.;
"The human homologue of the yeast polyubiquitination factor Ufd2p is
cleaved by caspase 6 and granzyme B during apoptosis.";
Biochem. J. 361:587-595(2002).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND ALTERNATIVE SPLICING.
TISSUE=Skeletal muscle;
PubMed=22174917; DOI=10.1371/journal.pone.0028861;
Mammen A.L., Mahoney J.A., St Germain A., Badders N., Taylor J.P.,
Rosen A., Spinette S.;
"A novel conserved isoform of the ubiquitin ligase UFD2a/UBE4B is
expressed exclusively in mature striated muscle cells.";
PLoS ONE 6:E28861-E28861(2011).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. X.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:169-176(1998).
[6]
SEQUENCE REVISION.
Ohara O., Suyama M., Nagase T., Ishikawa K.;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cerebellum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1112-1302.
Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.;
"Full-insert sequence of mapped XREF EST.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-803, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-803, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-88; SER-90;
SER-101 AND SER-803, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-88; SER-90 AND
SER-101, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-803 AND SER-1265, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-803, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-31; SER-101;
SER-105; SER-124; SER-238; SER-383; SER-803 AND SER-1265, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Ubiquitin-protein ligase that probably functions as an
E3 ligase in conjunction with specific E1 and E2 ligases. May also
function as an E4 ligase mediating the assembly of polyubiquitin
chains on substrates ubiquitinated by another E3 ubiquitin ligase.
{ECO:0000250|UniProtKB:P54860, ECO:0000250|UniProtKB:Q9ES00}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000250|UniProtKB:Q9ES00}.
-!- SUBUNIT: Interacts with VCP. {ECO:0000250|UniProtKB:Q9ES00}.
-!- INTERACTION:
P62837:UBE2D2; NbExp=2; IntAct=EBI-15869194, EBI-347677;
P61077-1:UBE2D3; NbExp=3; IntAct=EBI-15869194, EBI-15567256;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ES00}.
Nucleus {ECO:0000250|UniProtKB:Q9ES00}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O95155-1; Sequence=Displayed;
Name=2;
IsoId=O95155-2; Sequence=VSP_007102;
Name=3;
IsoId=O95155-3; Sequence=VSP_007101, VSP_007102, VSP_007103;
Note=No experimental confirmation available.;
Name=4; Synonyms=UFD2a-7/7a, UFD2A-III;
IsoId=O95155-4; Sequence=VSP_053372;
Note=Expressed exclusively in mature striated muscle cells.;
-!- TISSUE SPECIFICITY: Highest expression in ovary, testis, heart and
skeletal muscle. Expression is low in colon, thymus and peripheral
blood leukocytes. Almost undetectable in lung and spleen.
{ECO:0000269|PubMed:11802788}.
-!- DOMAIN: The U-box domain is required for the ubiquitin protein
ligase activity. {ECO:0000250|UniProtKB:Q9ES00}.
-!- PTM: 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. {ECO:0000269|PubMed:11802788}.
-!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA31659.3; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF043117; AAD02233.1; -; mRNA.
EMBL; AB028839; BAB40446.1; -; mRNA.
EMBL; AF331520; AAK69622.1; -; mRNA.
EMBL; JF289274; AEK06331.1; -; mRNA.
EMBL; AB014584; BAA31659.3; ALT_INIT; mRNA.
EMBL; AK292444; BAF85133.1; -; mRNA.
EMBL; AL590639; CAI14687.1; -; Genomic_DNA.
EMBL; AL096841; CAI14687.1; JOINED; Genomic_DNA.
EMBL; AL590639; CAI14688.1; -; Genomic_DNA.
EMBL; AL096841; CAI14688.1; JOINED; Genomic_DNA.
EMBL; AL096841; CAI21859.1; -; Genomic_DNA.
EMBL; AL590639; CAI21859.1; JOINED; Genomic_DNA.
EMBL; AL096841; CAI21860.1; -; Genomic_DNA.
EMBL; AL590639; CAI21860.1; JOINED; Genomic_DNA.
EMBL; BC093696; AAH93696.1; -; mRNA.
EMBL; AF091093; AAC72962.1; ALT_SEQ; mRNA.
CCDS; CCDS110.1; -. [O95155-2]
CCDS; CCDS41245.1; -. [O95155-1]
PIR; T00358; T00358.
RefSeq; NP_001099032.1; NM_001105562.2. [O95155-1]
RefSeq; NP_006039.2; NM_006048.4. [O95155-2]
RefSeq; XP_005263479.1; XM_005263422.1. [O95155-4]
UniGene; Hs.593974; -.
PDB; 2KRE; NMR; -; A=1208-1302.
PDB; 3L1X; X-ray; 2.60 A; A=1208-1302.
PDB; 3L1Z; X-ray; 3.17 A; B=1208-1302.
PDBsum; 2KRE; -.
PDBsum; 3L1X; -.
PDBsum; 3L1Z; -.
ProteinModelPortal; O95155; -.
SMR; O95155; -.
BioGrid; 115566; 81.
DIP; DIP-40309N; -.
IntAct; O95155; 11.
MINT; MINT-2798575; -.
STRING; 9606.ENSP00000343001; -.
iPTMnet; O95155; -.
PhosphoSitePlus; O95155; -.
BioMuta; UBE4B; -.
EPD; O95155; -.
MaxQB; O95155; -.
PaxDb; O95155; -.
PeptideAtlas; O95155; -.
PRIDE; O95155; -.
Ensembl; ENST00000253251; ENSP00000253251; ENSG00000130939. [O95155-2]
Ensembl; ENST00000343090; ENSP00000343001; ENSG00000130939. [O95155-1]
GeneID; 10277; -.
KEGG; hsa:10277; -.
UCSC; uc001aqr.5; human. [O95155-1]
CTD; 10277; -.
DisGeNET; 10277; -.
EuPathDB; HostDB:ENSG00000130939.18; -.
GeneCards; UBE4B; -.
HGNC; HGNC:12500; UBE4B.
HPA; HPA019219; -.
MIM; 613565; gene.
neXtProt; NX_O95155; -.
OpenTargets; ENSG00000130939; -.
PharmGKB; PA37148; -.
eggNOG; KOG2042; Eukaryota.
eggNOG; COG5113; LUCA.
GeneTree; ENSGT00390000009300; -.
HOGENOM; HOG000294109; -.
HOVERGEN; HBG058129; -.
InParanoid; O95155; -.
KO; K10597; -.
OMA; AMWNHEL; -.
OrthoDB; EOG091G02B4; -.
PhylomeDB; O95155; -.
TreeFam; TF300802; -.
BRENDA; 2.3.2.B12; 2681.
UniPathway; UPA00143; -.
ChiTaRS; UBE4B; human.
EvolutionaryTrace; O95155; -.
GeneWiki; UBE4B; -.
GenomeRNAi; 10277; -.
PMAP-CutDB; O95155; -.
PRO; PR:O95155; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000130939; -.
CleanEx; HS_UBE4B; -.
ExpressionAtlas; O95155; baseline and differential.
Genevisible; O95155; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0000151; C:ubiquitin ligase complex; TAS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:Ensembl.
GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IBA:GO_Central.
GO; GO:0008626; P:granzyme-mediated apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:MGI.
GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; TAS:UniProtKB.
GO; GO:0009411; P:response to UV; IDA:UniProtKB.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IEA:Ensembl.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR019474; Ub_conjug_fac_E4_core.
InterPro; IPR003613; Ubox_domain.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF04564; U-box; 1.
Pfam; PF10408; Ufd2P_core; 1.
SMART; SM00504; Ubox; 1.
PROSITE; PS51698; U_BOX; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Transferase; Ubl conjugation pathway.
CHAIN 1 1302 Ubiquitin conjugation factor E4 B.
/FTId=PRO_0000194993.
DOMAIN 1227 1300 U-box.
SITE 109 110 Cleavage; by caspase-3 and caspase-7.
SITE 123 124 Cleavage; by caspase-6 and granzyme B.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 84 84 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 88 88 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 90 90 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 101 101 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 103 103 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 105 105 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 124 124 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 238 238 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 383 383 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 803 803 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 969 969 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ES00}.
MOD_RES 1265 1265 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 116 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_007101.
VAR_SEQ 270 398 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:10980605,
ECO:0000303|PubMed:11802788,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9734811}.
/FTId=VSP_007102.
VAR_SEQ 398 398 P -> PSMYDNPFSFLFLALSGDSSDEEDEEEDDDDGDGDD
EGGGGGDDFSCVQFGS (in isoform 4).
{ECO:0000303|PubMed:22174917}.
/FTId=VSP_053372.
VAR_SEQ 1234 1234 D -> GKWTH (in isoform 3). {ECO:0000305}.
/FTId=VSP_007103.
VARIANT 605 605 V -> I (in dbSNP:rs17034499).
/FTId=VAR_052437.
MUTAGEN 109 109 D->A: Abolishes cleavage by caspase-3 and
caspase-7. {ECO:0000269|PubMed:11802788}.
MUTAGEN 121 121 D->A: Abolishes cleavage by caspase-6. No
effect on cleavage by granzyme B.
{ECO:0000269|PubMed:11802788}.
MUTAGEN 123 123 D->A: Abolishes cleavage by caspase-6 and
granzyme B.
{ECO:0000269|PubMed:11802788}.
HELIX 1230 1232 {ECO:0000244|PDB:3L1X}.
TURN 1235 1237 {ECO:0000244|PDB:3L1X}.
STRAND 1242 1246 {ECO:0000244|PDB:3L1X}.
TURN 1248 1250 {ECO:0000244|PDB:2KRE}.
STRAND 1252 1254 {ECO:0000244|PDB:3L1X}.
HELIX 1255 1264 {ECO:0000244|PDB:3L1X}.
TURN 1269 1271 {ECO:0000244|PDB:3L1X}.
HELIX 1277 1279 {ECO:0000244|PDB:3L1X}.
HELIX 1284 1298 {ECO:0000244|PDB:3L1X}.
SEQUENCE 1302 AA; 146185 MW; 6BAA80984B03E43B CRC64;
MEELSADEIR RRRLARLAGG QTSQPTTPLT SPQRENPPGP PIAASAPGPS QSLGLNVHNM
TPATSPIGAS GVAHRSQSSE GVSSLSSSPS NSLETQSQSL SRSQSMDIDG VSCEKSMSQV
DVDSGIENME VDENDRREKR SLSDKEPSSG PEVSEEQALQ LVCKIFRVSW KDRDRDVIFL
SSLSAQFKQN PKEVFSDFKD LIGQILMEVL MMSTQTRDEN PFASLTATSQ PIAAAARSPD
RNLLLNTGSN PGTSPMFCSV ASFGASSLSS LYESSPAPTP SFWSSVPVMG PSLASPSRAA
SQLAVPSTPL SPHSAASGTA AGSQPSSPRY RPYTVTHPWA SSGVSILSSS PSPPALASSP
QAVPASSSRQ RPSSTGPPLP PASPSATSRR PSSLRISPSL GASGGASNWD SYSDHFTIET
CKETDMLNYL IECFDRVGIE EKKAPKMCSQ PAVSQLLSNI RSQCISHTAL VLQGSLTQPR
SLQQPSFLVP YMLCRNLPYG FIQELVRTTH QDEEVFKQIF IPILQGLALA AKECSLDSDY
FKYPLMALGE LCETKFGKTH PVCNLVASLR LWLPKSLSPG CGRELQRLSY LGAFFSFSVF
AEDDVKVVEK YFSGPAITLE NTRVVSQSLQ HYLELGRQEL FKILHSILLN GETREAALSY
MAAVVNANMK KAQMQTDDRL VSTDGFMLNF LWVLQQLSTK IKLETVDPTY IFHPRCRITL
PNDETRVNAT MEDVNDWLTE LYGDQPPFSE PKFPTECFFL TLHAHHLSIL PSCRRYIRRL
RAIRELNRTV EDLKNNESQW KDSPLATRHR EMLKRCKTQL KKLVRCKACA DAGLLDESFL
RRCLNFYGLL IQLLLRILDP AYPDITLPLN SDVPKVFAAL PEFYVEDVAE FLFFIVQYSP
QALYEPCTQD IVMFLVVMLC NQNYIRNPYL VAKLVEVMFM TNPAVQPRTQ KFFEMIENHP
LSTKLLVPSL MKFYTDVEHT GATSEFYDKF TIRYHISTIF KSLWQNIAHH GTFMEEFNSG
KQFVRYINML INDTTFLLDE SLESLKRIHE VQEEMKNKEQ WDQLPRDQQQ ARQSQLAQDE
RVSRSYLALA TETVDMFHIL TKQVQKPFLR PELGPRLAAM LNFNLQQLCG PKCRDLKVEN
PEKYGFEPKK LLDQLTDIYL QLDCARFAKA IADDQRSYSK ELFEEVISKM RKAGIKSTIA
IEKFKLLAEK VEEIVAKNAR AEIDYSDAPD EFRDPLMDTL MTDPVRLPSG TIMDRSIILR
HLLNSPTDPF NRQTLTESML EPVPELKEQI QAWMREKQNS DH


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