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Q9ES00

- UBE4B_MOUSE

UniProt

Q9ES00 - UBE4B_MOUSE

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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

Functioni

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.By similarity1 Publication

Pathwayi

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
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin conjugation factor E4 BCurated (EC:6.3.2.-1 Publication)
Alternative name(s):
Ubiquitin fusion degradation protein 21 Publication
Gene namesi
Name:Ube4bImported
Synonyms:Ufd2Imported, Ufd2aImported
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1927086. Ube4b.

Subcellular locationi

Cytoplasm 3 Publications. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1140 – 11401P → A: Loss of E3 ubiquitin protein ligase activity. 1 Publication

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. Also detected in liver, heart, brain, kidney and testis.2 Publications

Gene expression databases

BgeeiQ9ES00.
ExpressionAtlasiQ9ES00. baseline and differential.
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 – 11033Combined sources
Turni1106 – 11083Combined sources
Beta strandi1113 – 11175Combined sources
Beta strandi1123 – 11253Combined sources
Helixi1126 – 113510Combined sources
Turni1140 – 11423Combined sources
Helixi1148 – 11503Combined sources
Helixi1155 – 117016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

Domaini

The U-box domain is required for the ubiquitin protein ligase activity.1 Publication

Sequence similaritiesi

Contains 1 U-box domain.Curated

Phylogenomic databases

eggNOGiCOG5113.
GeneTreeiENSGT00390000009300.
HOVERGENiHBG058129.
InParanoidiQ9ES00.
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

        10         20         30         40         50
MEELSADEIR RRRLARLAGG QTSQPTTPLT SPQRENPPGP PIAASAPGPS
60 70 80 90 100
QSLGLNVHNM TPATSPIGAA GVAHRSQSSE GVSSLSSSPS NSLETQSQSL
110 120 130 140 150
SRSQSMDIDG VSCEKSMSQV DVDSGIENME VDENDRREKR SLSDKEPSSG
160 170 180 190 200
PEVSEEQALQ LVCKIFRVSW KDRDRDVIFL SSLSAQFKQN PKEVFSDFKD
210 220 230 240 250
LIGQILMEVL MMSTQTRDEN PFASLTATSQ PIATAARSPD RNLMLNTGSS
260 270 280 290 300
SGTSPMFCNM GSFSTSSLSS LGASGGASNW DSYSDHFTIE TCKETDMLNY
310 320 330 340 350
LIECFDRVGI EEKKAPKMCS QPAVSQLLSN IRSQCISHTA LVLQGSLTQP
360 370 380 390 400
RSLQQPSFLV PYMLCRNLPY GFIQELVRTT HQDEEVFKQI FIPILQGLAL
410 420 430 440 450
AAKECSLESD YFKYPLMALG ELCETKFGKT HPMCNLVASL PLWLPKSLSP
460 470 480 490 500
GSGRELQRLS YLGAFFSFSV FAEDDAKVVE KYFSGPAITL ENTRVVSQSL
510 520 530 540 550
QHYLELGRQE LFKILHSILL NGETREAALS YMAALVNANM KKAQMQADDR
560 570 580 590 600
LVSTDGFMLN LLWVLQQLST KIKLETVDPT YIFHPRCRIT LPNDETRINA
610 620 630 640 650
TMEDVNERLT ELYGDQPPFS EPKFPTECFF LTLHAHHLSI LPSCRRYIRR
660 670 680 690 700
LRAIRELNRT VEDLKNNESQ WKDSPLATRH REMLKRCKTQ LKKLVRCKAC
710 720 730 740 750
ADAGLLDESF LRRCLNFYGL LIQLMLRILD PAYPDVTLPL NSEVPKVFAA
760 770 780 790 800
LPEFYVEDVA EFLFFIVQYS PQVLYEPCTQ DIVMFLVVML CNQNYIRNPY
810 820 830 840 850
LVAKLVEVMF MTNPSVQPRT QKFFEMIENH PLSTKLLVPS LMKFYTDVEH
860 870 880 890 900
TGATSEFYDK FTIRYHISTI FKSLWQNIAH HGTFMEEFNS GKQFVRYINM
910 920 930 940 950
LINDTTFLLD ESLESLKRIH EVQEEMKNKE QWDQLPRDQQ QARQSQLAQD
960 970 980 990 1000
ERVSRSYLAL ATETVDMFHL LTKQVQKPFL RPELGPRLAA MLNFNLQQLC
1010 1020 1030 1040 1050
GPKCRDLKVE NPEKYGFEPK KLLDQLTDIY LQLDCARFAK AIADDQRSYS
1060 1070 1080 1090 1100
KELFEEVISK MRKAGIKSTI AIEKFKLLAE KVEEIVAKNA RAEIDYSDAP
1110 1120 1130 1140 1150
DEFRDPLMDT LMTDPVRLPS GTVMDRSIIL RHLLNSPTDP FNRQMLTESM
1160 1170
LEPVPELKEQ IQAWMREKQS SDH
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 Q9ES00.
KOi K10597.
OMAi TENMLEP.
OrthoDBi EOG7TXKFT.
TreeFami TF300802.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

ChiTaRSi Ube4b. mouse.
NextBioi 319825.
PROi Q9ES00.
SOURCEi Search...

Gene expression databases

Bgeei Q9ES00.
ExpressionAtlasi Q9ES00. baseline and differential.
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

« Hide 'large scale' publications
  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], INTERACTION WITH VCP, 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. "U box proteins as a new family of ubiquitin-protein ligases."
    Hatakeyama S., Yada M., Matsumoto M., Ishida N., Nakayama K.I.
    J. Biol. Chem. 276:33111-33120(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, MUTAGENESIS OF PRO-1140.
  7. Cited for: SUBCELLULAR LOCATION, ROLE IN DELAY OF WALLERIAN DEGENERATION.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  9. 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: November 26, 2014
This is version 113 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.1 Publication

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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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