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P68036

- UB2L3_HUMAN

UniProt

P68036 - UB2L3_HUMAN

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Protein

Ubiquitin-conjugating enzyme E2 L3

Gene

UBE2L3

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

Functioni

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.7 Publications

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei86 – 861Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. enzyme binding Source: UniProtKB
  4. poly(A) RNA binding Source: UniProtKB
  5. transcription coactivator activity Source: UniProtKB
  6. ubiquitin protein ligase binding Source: UniProtKB
  7. ubiquitin-protein transferase activator activity Source: ParkinsonsUK-UCL
  8. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. cell proliferation Source: UniProtKB
  2. cellular protein modification process Source: UniProtKB
  3. cellular response to glucocorticoid stimulus Source: UniProtKB
  4. cellular response to steroid hormone stimulus Source: UniProtKB
  5. positive regulation of protein ubiquitination Source: ParkinsonsUK-UCL
  6. positive regulation of ubiquitin-protein transferase activity Source: ParkinsonsUK-UCL
  7. protein K11-linked ubiquitination Source: UniProtKB
  8. protein polyubiquitination Source: UniProtKB
  9. protein ubiquitination Source: UniProtKB
  10. regulation of transcription, DNA-templated Source: UniProtKB
  11. transcription, DNA-templated Source: UniProtKB-KW
  12. ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiP68036.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:UBE2L3
Synonyms:UBCE7, UBCH7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:12488. UBE2L3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. nucleus Source: UniProtKB
  4. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi86 – 861C → S: Loss of catalytic activity. Prevents ubiquitin-dependent proteasomal degradation of UBE2L3. 2 Publications
Mutagenesisi88 – 881P → D: Does not convert into a lysine reactive E2; when associated with D-119. 1 Publication
Mutagenesisi119 – 1191H → D: Does not convert into a lysine reactive E2; when associated with D-88. 1 Publication

Organism-specific databases

Orphaneti536. Systemic lupus erythematosus.
PharmGKBiPA37137.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 154154Ubiquitin-conjugating enzyme E2 L3PRO_0000082476Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91N6-acetyllysine1 Publication
Modified residuei131 – 1311N6-acetyllysine1 Publication
Modified residuei138 – 1381N6-acetyllysine1 Publication

Post-translational modificationi

Ubiquitinated. The alteration of UBE2L3 protein levels during the S-phase of the cell cycle is due to ubiquitin-dependent proteasomal degradation.1 Publication

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiP68036.
PaxDbiP68036.
PRIDEiP68036.

2D gel databases

OGPiP51966.
UCD-2DPAGEP68036.

PTM databases

PhosphoSiteiP68036.

Expressioni

Tissue specificityi

Ubiquitous, with highest expression in testis.

Gene expression databases

BgeeiP68036.
CleanExiHS_UBE2L3.
GenevestigatoriP68036.

Organism-specific databases

HPAiHPA045609.

Interactioni

Subunit structurei

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 NR3C1.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARIH1Q9Y4X55EBI-711173,EBI-2514233
ARIH2O953768EBI-711173,EBI-711158
ospGQ99PZ63EBI-711173,EBI-9316527From a different organism.
RNF19BQ6ZMZ02EBI-711173,EBI-2466594

Protein-protein interaction databases

BioGridi113180. 103 interactions.
DIPiDIP-6124N.
IntActiP68036. 25 interactions.
MINTiMINT-5002693.
STRINGi9606.ENSP00000344259.

Structurei

Secondary structure

1
154
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 115Combined sources
Beta strandi15 – 173Combined sources
Beta strandi23 – 253Combined sources
Beta strandi30 – 3910Combined sources
Beta strandi43 – 453Combined sources
Beta strandi51 – 566Combined sources
Turni59 – 635Combined sources
Beta strandi67 – 726Combined sources
Beta strandi77 – 793Combined sources
Beta strandi81 – 844Combined sources
Turni88 – 903Combined sources
Beta strandi91 – 944Combined sources
Helixi101 – 11313Combined sources
Beta strandi117 – 1193Combined sources
Helixi123 – 1308Combined sources
Helixi137 – 1448Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C4ZX-ray2.60D1-154[»]
1FBVX-ray2.90C1-154[»]
3SQVX-ray3.30C/D1-154[»]
3SY2X-ray3.27C/D1-154[»]
4Q5EX-ray1.87C1-154[»]
4Q5HX-ray2.00C1-154[»]
ProteinModelPortaliP68036.
SMRiP68036. Positions 4-147.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68036.

Family & Domainsi

Domaini

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.1 Publication

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00760000119012.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiP68036.
KOiK04552.
OMAiIALVNDX.
OrthoDBiEOG7GXPD8.
PhylomeDBiP68036.
TreeFamiTF313043.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P68036-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAASRRLMKE LEEIRKCGMK NFRNIQVDEA NLLTWQGLIV PDNPPYDKGA
60 70 80 90 100
FRIEINFPAE YPFKPPKITF KTKIYHPNID EKGQVCLPVI SAENWKPATK
110 120 130 140 150
TDQVIQSLIA LVNDPQPEHP LRADLAEEYS KDRKKFCKNA EEFTKKYGEK

RPVD
Length:154
Mass (Da):17,862
Last modified:October 11, 2004 - v1
Checksum:iF5A30243BE3C9985
GO
Isoform 2 (identifier: P68036-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     10-41: Missing.

Show »
Length:122
Mass (Da):14,121
Checksum:iB6D14D8ABF26E365
GO
Isoform 3 (identifier: P68036-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: MAASRRLMK → MQVAAGTRGD...AGYRRAHGPE

Note: No experimental confirmation available.

Show »
Length:212
Mass (Da):24,004
Checksum:iFBA57DE90E19DA78
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151R → S in BAG61806. (PubMed:14702039)Curated
Sequence conflicti23 – 231R → C in AAG17922. 1 PublicationCurated
Sequence conflicti118 – 1181E → K in AAG17922. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 99MAASRRLMK → MQVAAGTRGDTRLQEVALLP QLFDLLVLGQRRARLLRQVP SALAGKDLAQLQAGATLAGY RRAHGPE in isoform 3. 1 PublicationVSP_047342
Alternative sequencei10 – 4132Missing in isoform 2. 1 PublicationVSP_045152Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13790.1. [P68036-1]
CCDS58795.1. [P68036-3]
CCDS58796.1. [P68036-2]
RefSeqiNP_001243284.1. NM_001256355.1. [P68036-3]
NP_001243285.1. NM_001256356.1. [P68036-2]
NP_003338.1. NM_003347.3. [P68036-1]
UniGeneiHs.108104.

Genome annotation databases

EnsembliENST00000342192; ENSP00000344259; ENSG00000185651. [P68036-1]
ENST00000458578; ENSP00000400906; ENSG00000185651. [P68036-3]
ENST00000545681; ENSP00000445931; ENSG00000185651. [P68036-2]
GeneIDi7332.
KEGGihsa:7332.
UCSCiuc002zuz.2. human. [P68036-1]
uc011aig.3. human.

Polymorphism databases

DMDMi54039805.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS13790.1. [P68036-1 ]
CCDS58795.1. [P68036-3 ]
CCDS58796.1. [P68036-2 ]
RefSeqi NP_001243284.1. NM_001256355.1. [P68036-3 ]
NP_001243285.1. NM_001256356.1. [P68036-2 ]
NP_003338.1. NM_003347.3. [P68036-1 ]
UniGenei Hs.108104.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C4Z X-ray 2.60 D 1-154 [» ]
1FBV X-ray 2.90 C 1-154 [» ]
3SQV X-ray 3.30 C/D 1-154 [» ]
3SY2 X-ray 3.27 C/D 1-154 [» ]
4Q5E X-ray 1.87 C 1-154 [» ]
4Q5H X-ray 2.00 C 1-154 [» ]
ProteinModelPortali P68036.
SMRi P68036. Positions 4-147.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113180. 103 interactions.
DIPi DIP-6124N.
IntActi P68036. 25 interactions.
MINTi MINT-5002693.
STRINGi 9606.ENSP00000344259.

PTM databases

PhosphoSitei P68036.

Polymorphism databases

DMDMi 54039805.

2D gel databases

OGPi P51966.
UCD-2DPAGE P68036.

Proteomic databases

MaxQBi P68036.
PaxDbi P68036.
PRIDEi P68036.

Protocols and materials databases

DNASUi 7332.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000342192 ; ENSP00000344259 ; ENSG00000185651 . [P68036-1 ]
ENST00000458578 ; ENSP00000400906 ; ENSG00000185651 . [P68036-3 ]
ENST00000545681 ; ENSP00000445931 ; ENSG00000185651 . [P68036-2 ]
GeneIDi 7332.
KEGGi hsa:7332.
UCSCi uc002zuz.2. human. [P68036-1 ]
uc011aig.3. human.

Organism-specific databases

CTDi 7332.
GeneCardsi GC22P021903.
HGNCi HGNC:12488. UBE2L3.
HPAi HPA045609.
MIMi 603721. gene.
neXtProti NX_P68036.
Orphaneti 536. Systemic lupus erythematosus.
PharmGKBi PA37137.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00760000119012.
HOGENOMi HOG000233455.
HOVERGENi HBG063308.
InParanoidi P68036.
KOi K04552.
OMAi IALVNDX.
OrthoDBi EOG7GXPD8.
PhylomeDBi P68036.
TreeFami TF313043.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinki P68036.

Miscellaneous databases

ChiTaRSi UBE2L3. human.
EvolutionaryTracei P68036.
GeneWikii UBE2L3.
GenomeRNAii 7332.
NextBioi 28696.
PROi P68036.
SOURCEi Search...

Gene expression databases

Bgeei P68036.
CleanExi HS_UBE2L3.
Genevestigatori P68036.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiUB2L3_HUMAN
AccessioniPrimary (citable) accession number: P68036
Secondary accession number(s): B2R4A7
, B4DDG1, B4DSZ4, E7EWS7, P51966, P70653, Q9HAV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: October 29, 2014
This is version 113 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

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