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P68036 (UB2L3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 L3

EC=6.3.2.19
Alternative name(s):
L-UBC
UbcH7
Ubiquitin carrier protein L3
Ubiquitin-conjugating enzyme E2-F1
Ubiquitin-protein ligase L3
Gene names
Name:UBE2L3
Synonyms:UBCE7, UBCH7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length154 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis. Ref.12 Ref.16 Ref.18 Ref.20 Ref.21 Ref.23 Ref.25

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with PARK2; involved in ubiquitination and degradation of misfolded proteins. Interacts with UBE3A; used by the papilloma virus HPV-16 E6 protein to ubiquitinate p53/TP53. Interacts with CCNB1IP1, CBL, ZAP70, RNF19A, RNF19B and RNF144B. Interacts with ARIH1. Interacts with ARIH2 (via RING-type 1). Interacts with NCOA1; they functionally interact to regulate progesterone receptor transcriptional activity. May interact with NR3C1. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.25

Subcellular location

Nucleus. Cytoplasm Ref.14 Ref.18.

Tissue specificity

Ubiquitous, with highest expression in testis.

Domain

In contrast to other ubiquitin-conjugating enzymes E2, residues essential for lysine reactivity are absent: Pro and a His residues are present instead of an Asp and an Asp residues in positions 88 and 119,respectively. Ref.25

Post-translational modification

Ubiquitinated. The alteration of UBE2L3 protein levels during the S-phase of the cell cycle is due to ubiquitin-dependent proteasomal degradation. Ref.21

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Caution

Ref.11 reported that UBE2L1, UBE2L2 and UBE2L4 are most likely pseudogenes and the only expressed member of this subfamily seems to be UBE2L3.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from mutant phenotype Ref.21. Source: UniProtKB

cellular protein modification process

Traceable author statement Ref.2. Source: UniProtKB

cellular response to glucocorticoid stimulus

Inferred from direct assay Ref.18. Source: UniProtKB

cellular response to steroid hormone stimulus

Inferred from mutant phenotype Ref.16. Source: UniProtKB

protein K11-linked ubiquitination

Inferred from direct assay Ref.23. Source: UniProtKB

protein polyubiquitination

Inferred from direct assay Ref.12PubMed 14765125. Source: UniProtKB

protein ubiquitination

Inferred from direct assay Ref.25. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay Ref.18. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-dependent protein catabolic process

Traceable author statement Ref.1PubMed 8672131. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.14Ref.18. Source: UniProtKB

nucleus

Inferred from direct assay Ref.14Ref.18. Source: UniProtKB

ubiquitin ligase complex

Traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

enzyme binding

Traceable author statement Ref.1. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.12Ref.16PubMed 16118314Ref.18Ref.20. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.16. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction Ref.14Ref.25. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from direct assay PubMed 14765125Ref.23Ref.25. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARIH2O953763EBI-711173,EBI-711158
RNF19BQ6ZMZ02EBI-711173,EBI-2466594

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P68036-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P68036-2)

The sequence of this isoform differs from the canonical sequence as follows:
     10-41: Missing.
Isoform 3 (identifier: P68036-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: MAASRRLMK → MQVAAGTRGD...AGYRRAHGPE
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 154154Ubiquitin-conjugating enzyme E2 L3
PRO_0000082476

Sites

Active site861Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue91N6-acetyllysine Ref.22
Modified residue1311N6-acetyllysine Ref.22
Modified residue1381N6-acetyllysine Ref.22

Natural variations

Alternative sequence1 – 99MAASRRLMK → MQVAAGTRGDTRLQEVALLP QLFDLLVLGQRRARLLRQVP SALAGKDLAQLQAGATLAGY RRAHGPE in isoform 3.
VSP_047342
Alternative sequence10 – 4132Missing in isoform 2.
VSP_045152

Experimental info

Mutagenesis861C → S: Loss of catalytic activity. Prevents ubiquitin-dependent proteasomal degradation of UBE2L3. Ref.12 Ref.21
Mutagenesis881P → D: Does not convert into a lysine reactive E2; when associated with D-119. Ref.25
Mutagenesis1191H → D: Does not convert into a lysine reactive E2; when associated with D-88. Ref.25
Sequence conflict151R → S in BAG61806. Ref.6
Sequence conflict231R → C in AAG17922. Ref.4
Sequence conflict1181E → K in AAG17922. Ref.4

Secondary structure

................................ 154
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: F5A30243BE3C9985

FASTA15417,862
        10         20         30         40         50         60 
MAASRRLMKE LEEIRKCGMK NFRNIQVDEA NLLTWQGLIV PDNPPYDKGA FRIEINFPAE 

        70         80         90        100        110        120 
YPFKPPKITF KTKIYHPNID EKGQVCLPVI SAENWKPATK TDQVIQSLIA LVNDPQPEHP 

       130        140        150 
LRADLAEEYS KDRKKFCKNA EEFTKKYGEK RPVD 

« Hide

Isoform 2 [UniParc].

Checksum: B6D14D8ABF26E365
Show »

FASTA12214,121
Isoform 3 [UniParc].

Checksum: FBA57DE90E19DA78
Show »

FASTA21224,004

References

« Hide 'large scale' references
[1]"A human ubiquitin conjugating enzyme, L-UBC, maps in the Alzheimer's disease locus on chromosome 14q24.3."
Robinson P.A., Leek J.P., Thompson J., Carr I.M., Bailey A., Moynihan T.P., Coletta P.L., Lench N.J., Markham A.F.
Mamm. Genome 6:725-731(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5."
Nuber U., Schwarz S., Kaiser P., Schneider R., Scheffner M.
J. Biol. Chem. 271:2795-2800(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Fine-mapping, genomic organization, and transcript analysis of the human ubiquitin-conjugating enzyme gene UBE2L3."
Moynihan T.P., Cole C.G., Dunham I., O'Neil L., Markham A.F., Robinson P.A.
Genomics 51:124-127(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Testis.
[4]"Is retroposition a common way of spreading ubiquitin-conjugating enzyme genes throughout mammalian genomes?"
Poloumienko A.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.
[5]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
Tissue: Adrenal gland and Thalamus.
[7]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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] (ISOFORM 1).
Tissue: Brain.
[10]"Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non-'N-end rule' protein substrates."
Blumenfeld N., Gonen H., Mayer A., Smith C.E., Siegel N.R., Schwartz A.L., Ciechanover A.
J. Biol. Chem. 269:9574-9581(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 53-67; 67-74 AND 101-122.
[11]"Promoter analysis of the human ubiquitin-conjugating enzyme gene family UBE2L1-4, including UBE2L3 which encodes UbcH7."
Ardley H.C., Moynihan T.P., Markham A.F., Robinson P.A.
Biochim. Biophys. Acta 1491:57-64(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROMOTER ANALYSIS.
[12]"Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase."
Shimura H., Hattori N., Kubo S., Mizuno Y., Asakawa S., Minoshima S., Shimizu N., Iwai K., Chiba T., Tanaka K., Suzuki T.
Nat. Genet. 25:302-305(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PARK2, MUTAGENESIS OF CYS-86.
[13]"A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity."
Niwa J., Ishigaki S., Doyu M., Suzuki T., Tanaka K., Sobue G.
Biochem. Biophys. Res. Commun. 281:706-713(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF19A.
[14]"Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7."
Ardley H.C., Tan N.G.S., Rose S.A., Markham A.F., Robinson P.A.
J. Biol. Chem. 276:19640-19647(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARIH1, SUBCELLULAR LOCATION.
[15]"A novel RING finger protein, human enhancer of invasion 10, alters mitotic progression through regulation of cyclin B levels."
Toby G.G., Gherraby W., Coleman T.R., Golemis E.A.
Mol. Cell. Biol. 23:2109-2122(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CCNB1IP1.
[16]"The ubiquitin-conjugating enzyme UBCH7 acts as a coactivator for steroid hormone receptors."
Verma S., Ismail A., Gao X., Fu G., Li X., O'Malley B.W., Nawaz Z.
Mol. Cell. Biol. 24:8716-8726(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NCOA1.
[17]"The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosis."
Huang J., Xu L.-G., Liu T., Zhai Z., Shu H.-B.
FEBS Lett. 580:940-947(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF144B.
[18]"UbcH7 interacts with the glucocorticoid receptor and mediates receptor autoregulation."
Garside H., Waters C., Berry A., Rice L., Ardley H.C., White A., Robinson P.A., Ray D.
J. Endocrinol. 190:621-629(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NR3C1, SUBCELLULAR LOCATION.
[19]"NK lytic-associated molecule, involved in NK cytotoxic function, is an E3 ligase."
Fortier J.M., Kornbluth J.
J. Immunol. 176:6454-6463(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF19B.
[20]"The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains."
Marteijn J.A., van der Meer L.T., Smit J.J., Noordermeer S.M., Wissink W., Jansen P., Swarts H.G., Hibbert R.G., de Witte T., Sixma T.K., Jansen J.H., van der Reijden B.A.
Leukemia 23:1480-1489(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ARIH2.
[21]"Novel control of S phase of the cell cycle by ubiquitin-conjugating enzyme H7."
Whitcomb E.A., Dudek E.J., Liu Q., Taylor A.
Mol. Biol. Cell 20:1-9(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, UBIQUITINATION, MUTAGENESIS OF CYS-86.
[22]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9; LYS-131 AND LYS-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines."
David Y., Ziv T., Admon A., Navon A.
J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[24]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids."
Wenzel D.M., Lissounov A., Brzovic P.S., Klevit R.E.
Nature 474:105-108(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN, INTERACTION WITH PARK2 AND ARIH1, MUTAGENESIS OF PRO-88 AND HIS-119.
[26]"Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade."
Huang L., Kinnucan E., Wang G., Beaudenon S., Howley P.M., Huibregtse J.M., Pavletich N.P.
Science 286:1321-1326(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH UBE3A.
[27]"Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases."
Zheng N., Wang P., Jeffrey P.D., Pavletich N.P.
Cell 102:533-539(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH 47-434 OF CBL AND ZAP70.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S81003 mRNA. Translation: AAB36017.1.
X92962 mRNA. Translation: CAA63538.1.
AJ000519 mRNA. Translation: CAA04156.1.
AF300336 Genomic DNA. Translation: AAG17922.1.
CR456606 mRNA. Translation: CAG30492.1.
AK293179 mRNA. Translation: BAG56722.1.
AK299985 mRNA. Translation: BAG61806.1.
AK311761 mRNA. Translation: BAG34704.1.
AP000553 Genomic DNA. No translation available.
AP000557 Genomic DNA. No translation available.
AP000558 Genomic DNA. No translation available.
CH471095 Genomic DNA. Translation: EAW59459.1.
BC053368 mRNA. Translation: AAH53368.1.
CCDSCCDS13790.1. [P68036-1]
CCDS58795.1. [P68036-3]
CCDS58796.1. [P68036-2]
RefSeqNP_001243284.1. NM_001256355.1. [P68036-3]
NP_001243285.1. NM_001256356.1. [P68036-2]
NP_003338.1. NM_003347.3. [P68036-1]
UniGeneHs.108104.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C4ZX-ray2.60D1-154[»]
1FBVX-ray2.90C1-154[»]
3SQVX-ray3.30C/D1-154[»]
3SY2X-ray3.27C/D1-154[»]
ProteinModelPortalP68036.
SMRP68036. Positions 4-147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113180. 99 interactions.
DIPDIP-6124N.
IntActP68036. 22 interactions.
MINTMINT-5002693.
STRING9606.ENSP00000344259.

PTM databases

PhosphoSiteP68036.

Polymorphism databases

DMDM54039805.

2D gel databases

OGPP51966.
UCD-2DPAGEP68036.

Proteomic databases

MaxQBP68036.
PaxDbP68036.
PRIDEP68036.

Protocols and materials databases

DNASU7332.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342192; ENSP00000344259; ENSG00000185651. [P68036-1]
ENST00000458578; ENSP00000400906; ENSG00000185651. [P68036-3]
ENST00000545681; ENSP00000445931; ENSG00000185651. [P68036-2]
GeneID7332.
KEGGhsa:7332.
UCSCuc002zuz.2. human. [P68036-1]
uc011aig.3. human.

Organism-specific databases

CTD7332.
GeneCardsGC22P021903.
HGNCHGNC:12488. UBE2L3.
HPAHPA045609.
MIM603721. gene.
neXtProtNX_P68036.
Orphanet536. Systemic lupus erythematosus.
PharmGKBPA37137.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5078.
HOGENOMHOG000233455.
HOVERGENHBG063308.
InParanoidP68036.
KOK04552.
OMAIALVNDX.
OrthoDBEOG7GXPD8.
PhylomeDBP68036.
TreeFamTF313043.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP68036.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressP68036.
BgeeP68036.
CleanExHS_UBE2L3.
GenevestigatorP68036.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBE2L3. human.
EvolutionaryTraceP68036.
GeneWikiUBE2L3.
GenomeRNAi7332.
NextBio28696.
PROP68036.
SOURCESearch...

Entry information

Entry nameUB2L3_HUMAN
AccessionPrimary (citable) accession number: P68036
Secondary accession number(s): B2R4A7 expand/collapse secondary AC list , B4DDG1, B4DSZ4, E7EWS7, P51966, P70653, Q9HAV1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 9, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM