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Q05086 (UBE3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-protein ligase E3A

EC=6.3.2.-
Alternative name(s):
E6AP ubiquitin-protein ligase
Human papillomavirus E6-associated protein
Oncogenic protein-associated protein E6-AP
Renal carcinoma antigen NY-REN-54
Gene names
Name:UBE3A
Synonyms:E6AP, EPVE6AP, HPVE6A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length875 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and transfers it to its substrates. Several substrates have been identified including the RAD23A and RAD23B, MCM7 (which is involved in DNA replication), annexin A1, the PML tumor suppressor, and the cell cycle regulator CDKN1B. Catalyzes the high-risk human papilloma virus E6-mediated ubiquitination of p53/TP53, contributing to the neoplastic progression of cells infected by these viruses. Additionally, may function as a cellular quality control ubiquitin ligase by helping the degradation of the cytoplasmic misfolded proteins. Finally, UBE3A also promotes its own degradation in vivo. Ref.11 Ref.17 Ref.18 Ref.19 Ref.20 Ref.23

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Binds UBQLN1 and UBQLN2. Interacts with the 26S proteasome. Interacts with HCV core protein and targets it to degradation. Interacts with the E6 protein of the cancer-associated human papillomavirus types 16 and 18. The E6/E6-AP complex binds to and targets the p53/TP53 tumor-suppressor protein for ubiquitin-mediated proteolysis. Interacts with BPY2. Interacts with HIF1AN, MAPK6 AND NEURL4; interaction with MAPK6 may be mediated by NEURL4. Interacts with the proteasomal subunit PSMD4. Ref.12 Ref.13 Ref.15 Ref.23

Subcellular location

Nucleus Probable.

Involvement in disease

Angelman syndrome (AS) [MIM:105830]: A neurodevelopmental disorder characterized by severe motor and intellectual retardation, ataxia, frequent jerky limb movements and flapping of the arms and hands, hypotonia, seizures, absence of speech, frequent smiling and episodes of paroxysmal laughter, open-mouthed expression revealing the tongue.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.26

Miscellaneous

A cysteine residue is required for ubiquitin-thioester formation.

Sequence similarities

Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.

Sequence caution

The sequence AAA35542.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processHost-virus interaction
Ubl conjugation pathway
   Cellular componentNucleus
Proteasome
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   Molecular functionLigase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

brain development

Traceable author statement Ref.2. Source: ProtInc

ovarian follicle development

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

prostate gland growth

Inferred from electronic annotation. Source: Ensembl

protein K48-linked ubiquitination

Inferred from direct assay PubMed 12890688. Source: UniProtKB

protein autoubiquitination

Inferred from direct assay PubMed 24105792. Source: FlyBase

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

proteolysis

Traceable author statement PubMed 8221889. Source: ProtInc

sperm entry

Inferred from electronic annotation. Source: Ensembl

ubiquitin-dependent protein catabolic process

Traceable author statement PubMed 8221889. Source: ProtInc

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosol

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from Biological aspect of Ancestor. Source: RefGenome

proteasome complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 12620801PubMed 16493710PubMed 17023019PubMed 17166906PubMed 7624774PubMed 9467941. Source: IntAct

transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

ubiquitin-protein transferase activity

Inferred from direct assay PubMed 12890688. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

E6P031262EBI-954357,EBI-1177242From a different organism.
E6P040193EBI-954357,EBI-1177232From a different organism.
E6P064633EBI-954357,EBI-1186926From a different organism.
E6P069312EBI-954357,EBI-7281937From a different organism.
E6Q77E163EBI-954357,EBI-7011359From a different organism.
TP53P046373EBI-954357,EBI-366083

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform II (identifier: Q05086-1)

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 I (identifier: Q05086-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.
Isoform III (identifier: Q05086-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-10: MEKLHQCYWK → MATACKR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 875875Ubiquitin-protein ligase E3A
PRO_0000194980

Regions

Domain776 – 875100HECT
Region401 – 41818E6-binding
Region418 – 517100Interaction with HCV core protein
Compositional bias394 – 3996Asp/Glu-rich (acidic)

Sites

Active site8431Glycyl thioester intermediate

Amino acid modifications

Modified residue2181Phosphoserine Ref.16 Ref.21

Natural variations

Alternative sequence1 – 2323Missing in isoform I.
VSP_006705
Alternative sequence1 – 1010MEKLHQCYWK → MATACKR in isoform III.
VSP_006706
Natural variant441C → Y Probable polymorphism. Ref.3
VAR_007852
Natural variant621R → H. Ref.26
VAR_008142
Natural variant2011A → T. Ref.3 Ref.26
Corresponds to variant rs147145506 [ dbSNP | Ensembl ].
VAR_007853
Natural variant2901V → G. Ref.1 Ref.7 Ref.9
Corresponds to variant rs1059383 [ dbSNP | Ensembl ].
VAR_047516
Natural variant3721S → P. Ref.26
VAR_008143
Natural variant8261I → II in AS. Ref.26
VAR_008144

Experimental info

Sequence conflict3591R → RNLVNEFNSR AA sequence Ref.7
Sequence conflict4231P → L in AAA35542. Ref.7
Sequence conflict647 – 6493TFR → LFV in AAA35542. Ref.7
Sequence conflict6691E → V in AAA35542. Ref.7
Sequence conflict6861D → N in AAA35542. Ref.7

Secondary structure

....................................................................... 875
Helix Strand Turn

Details...

Sequences

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

Last modified November 25, 2008. Version 4.
Checksum: F80F0502B3B3838A

FASTA875100,688
        10         20         30         40         50         60 
MEKLHQCYWK SGEPQSDDIE ASRMKRAAAK HLIERYYHQL TEGCGNEACT NEFCASCPTF 

        70         80         90        100        110        120 
LRMDNNAAAI KALELYKINA KLCDPHPSKK GASSAYLENS KGAPNNSCSE IKMNKKGARI 

       130        140        150        160        170        180 
DFKDVTYLTE EKVYEILELC REREDYSPLI RVIGRVFSSA EALVQSFRKV KQHTKEELKS 

       190        200        210        220        230        240 
LQAKDEDKDE DEKEKAACSA AAMEEDSEAS SSRIGDSSQG DNNLQKLGPD DVSVDIDAIR 

       250        260        270        280        290        300 
RVYTRLLSNE KIETAFLNAL VYLSPNVECD LTYHNVYSRD PNYLNLFIIV MENRNLHSPE 

       310        320        330        340        350        360 
YLEMALPLFC KAMSKLPLAA QGKLIRLWSK YNADQIRRMM ETFQQLITYK VISNEFNSRN 

       370        380        390        400        410        420 
LVNDDDAIVA ASKCLKMVYY ANVVGGEVDT NHNEEDDEEP IPESSELTLQ ELLGEERRNK 

       430        440        450        460        470        480 
KGPRVDPLET ELGVKTLDCR KPLIPFEEFI NEPLNEVLEM DKDYTFFKVE TENKFSFMTC 

       490        500        510        520        530        540 
PFILNAVTKN LGLYYDNRIR MYSERRITVL YSLVQGQQLN PYLRLKVRRD HIIDDALVRL 

       550        560        570        580        590        600 
EMIAMENPAD LKKQLYVEFE GEQGVDEGGV SKEFFQLVVE EIFNPDIGMF TYDESTKLFW 

       610        620        630        640        650        660 
FNPSSFETEG QFTLIGIVLG LAIYNNCILD VHFPMVVYRK LMGKKGTFRD LGDSHPVLYQ 

       670        680        690        700        710        720 
SLKDLLEYEG NVEDDMMITF QISQTDLFGN PMMYDLKENG DKIPITNENR KEFVNLYSDY 

       730        740        750        760        770        780 
ILNKSVEKQF KAFRRGFHMV TNESPLKYLF RPEEIELLIC GSRNLDFQAL EETTEYDGGY 

       790        800        810        820        830        840 
TRDSVLIREF WEIVHSFTDE QKRLFLQFTT GTDRAPVGGL GKLKMIIAKN GPDTERLPTS 

       850        860        870 
HTCFNVLLLP EYSSKEKLKE RLLKAITYAK GFGML 

« Hide

Isoform I [UniParc].

Checksum: 3C061DA8D216055A
Show »

FASTA85297,968
Isoform III [UniParc].

Checksum: AB4C9B22356C9556
Show »

FASTA872100,102

References

« Hide 'large scale' references
[1]"The human E6-AP gene (UBE3A) encodes three potential protein isoforms generated by differential splicing."
Yamamoto Y., Huibregtse J.M., Howley P.M.
Genomics 41:263-266(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS I; II AND III), VARIANT GLY-290.
Tissue: Keratinocyte.
[2]"UBE3A/E6-AP mutations cause Angelman syndrome."
Kishino T., Lalande M., Wagstaff J.
Nat. Genet. 15:70-73(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I).
Tissue: Fetal brain.
[3]"De novo truncating mutations in E6-AP ubiquitin-protein ligase gene (UBE3A) in Angelman syndrome."
Matsuura T., Sutcliffe J.S., Fang P., Galjaard R.-J., Jiang Y.-H., Benton C.S., Rommens J.M., Beaudet A.L.
Nat. Genet. 15:74-77(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM I), VARIANTS TYR-44 AND THR-201.
[4]"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] (ISOFORM III).
Tissue: Testis.
[5]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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].
[7]"Cloning and expression of the cDNA for E6-AP, a protein that mediates the interaction of the human papillomavirus E6 oncoprotein with p53."
Huibregtse J.M., Scheffner M., Howley P.M.
Mol. Cell. Biol. 13:775-784(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-875, PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION, VARIANT GLY-290.
Tissue: Keratinocyte.
[8]"The ubiquitin-protein ligase E6-associated protein (E6-AP) serves as its own substrate."
Nuber U., Schwarz S.E., Scheffner M.
Eur. J. Biochem. 254:643-649(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[9]"Mutations in the E6-AP gene (UBE3A) in patients with Angelman syndrome."
Hennies H.C., Buerger J., Sperling K., Reis A.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-787, VARIANT GLY-290.
[10]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.
Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
Tissue: Renal cell carcinoma.
[11]"Identification of HHR23A as a substrate for E6-associated protein-mediated ubiquitination."
Kumar S., Talis A.L., Howley P.M.
J. Biol. Chem. 274:18785-18792(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome."
Kleijnen M.F., Shih A.H., Zhou P., Kumar S., Soccio R.E., Kedersha N.L., Gill G., Howley P.M.
Mol. Cell 6:409-419(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBQLN1 AND UBQLN2.
[13]"VCY2 protein interacts with the HECT domain of ubiquitin-protein ligase E3A."
Wong E.Y., Tse J.Y., Yao K.M., Tam P.C., Yeung W.S.
Biochem. Biophys. Res. Commun. 296:1104-1111(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BPY2.
[14]"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[15]"E6AP ubiquitin ligase mediates ubiquitylation and degradation of hepatitis C virus core protein."
Shirakura M., Murakami K., Ichimura T., Suzuki R., Shimoji T., Fukuda K., Abe K., Sato S., Fukasawa M., Yamakawa Y., Nishijima M., Moriishi K., Matsuura Y., Wakita T., Suzuki T., Howley P.M., Miyamura T., Shoji I.
J. Virol. 81:1174-1185(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCV CORE PROTEIN.
[16]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[17]"E6AP promotes the degradation of the PML tumor suppressor."
Louria-Hayon I., Alsheich-Bartok O., Levav-Cohen Y., Silberman I., Berger M., Grossman T., Matentzoglu K., Jiang Y.H., Muller S., Scheffner M., Haupt S., Haupt Y.
Cell Death Differ. 16:1156-1166(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"The ubiquitin ligase E6-AP is induced and recruited to aggresomes in response to proteasome inhibition and may be involved in the ubiquitination of Hsp70-bound misfolded proteins."
Mishra A., Godavarthi S.K., Maheshwari M., Goswami A., Jana N.R.
J. Biol. Chem. 284:10537-10545(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"Identification of annexin A1 as a novel substrate for E6AP-mediated ubiquitylation."
Shimoji T., Murakami K., Sugiyama Y., Matsuda M., Inubushi S., Nasu J., Shirakura M., Suzuki T., Wakita T., Kishino T., Hotta H., Miyamura T., Shoji I.
J. Cell. Biochem. 106:1123-1135(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[20]"UBE3A/E6-AP regulates cell proliferation by promoting proteasomal degrADation of p27."
Mishra A., Godavarthi S.K., Jana N.R.
Neurobiol. Dis. 36:26-34(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[22]"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].
[23]"Identification and proteomic analysis of distinct UBE3A/E6AP protein complexes."
Martinez-Noel G., Galligan J.T., Sowa M.E., Arndt V., Overton T.M., Harper J.W., Howley P.M.
Mol. Cell. Biol. 32:3095-3106(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HIF1AN; MAPK6; NEURL4 AND PSMD4.
[24]"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) OF 495-852 IN COMPLEX WITH UBE2L3.
[25]"Solution structure determination and mutational analysis of the papillomavirus E6 interacting peptide of E6AP."
Be X., Hong Y., Wei J., Androphy E.J., Chen J.J., Baleja J.D.
Biochemistry 40:1293-1299(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 401-418.
[26]"Mutation analysis of UBE3A in Angelman syndrome patients."
Malzac P., Webber H., Moncla A., Graham J.M. Jr., Kukolich M., Williams C., Pagon R.A., Ramsdell L.A., Kishino T., Wagstaff J.
Am. J. Hum. Genet. 62:1353-1360(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AS ILE-826 INS, VARIANTS HIS-62; THR-201 AND PRO-372.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98021 expand/collapse EMBL AC list , X98027, X98022, X98023, X98024, X98025, X98026, X98028, X98029, X98030 Genomic DNA. Translation: CAA66653.1.
X98031 mRNA. Translation: CAA66654.1.
X98032 mRNA. Translation: CAA66655.1.
X98033 mRNA. Translation: CAA66656.1.
AC100774 Genomic DNA. No translation available.
AK292514 mRNA. Translation: BAF85203.1.
AC124997 Genomic DNA. No translation available.
CH471151 Genomic DNA. Translation: EAW57645.1.
L07557 mRNA. Translation: AAA35542.1. Different initiation.
AF016708 expand/collapse EMBL AC list , AF016703, AF016704, AF016705, AF016706, AF016707 Genomic DNA. Translation: AAB69154.1.
U84404 mRNA. Translation: AAB49301.1.
AJ001107 Genomic DNA. Translation: CAA04534.1.
AJ001108 Genomic DNA. Translation: CAA04535.1.
AJ001109 Genomic DNA. Translation: CAA04536.1.
AJ001110 Genomic DNA. Translation: CAA04537.1.
AJ001111 Genomic DNA. Translation: CAA04538.1.
AJ001112 Genomic DNA. Translation: CAA04539.1.
CCDSCCDS32177.1. [Q05086-2]
CCDS45191.1. [Q05086-3]
CCDS45192.1. [Q05086-1]
RefSeqNP_000453.2. NM_000462.3. [Q05086-1]
NP_570853.1. NM_130838.1. [Q05086-2]
NP_570854.1. NM_130839.2. [Q05086-3]
XP_005268324.1. XM_005268267.2. [Q05086-2]
XP_005268325.1. XM_005268268.2. [Q05086-2]
XP_005268326.1. XM_005268269.2. [Q05086-2]
XP_005268327.1. XM_005268270.2. [Q05086-2]
XP_005268328.1. XM_005268271.2. [Q05086-2]
XP_006720736.1. XM_006720673.1. [Q05086-3]
XP_006720737.1. XM_006720674.1. [Q05086-3]
XP_006720738.1. XM_006720675.1. [Q05086-2]
XP_006720739.1. XM_006720676.1. [Q05086-2]
UniGeneHs.598862.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C4ZX-ray2.60A/B/C518-875[»]
1D5FX-ray2.80A/B/C518-875[»]
1EQXNMR-A401-418[»]
2KR1NMR-A24-87[»]
4GIZX-ray2.55A/B403-414[»]
ProteinModelPortalQ05086.
SMRQ05086. Positions 24-87, 520-869.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113185. 116 interactions.
DIPDIP-6002N.
IntActQ05086. 39 interactions.
MINTMINT-147444.

PTM databases

PhosphoSiteQ05086.

Polymorphism databases

DMDM215274240.

Proteomic databases

MaxQBQ05086.
PaxDbQ05086.
PRIDEQ05086.

Protocols and materials databases

DNASU7337.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000232165; ENSP00000232165; ENSG00000114062. [Q05086-3]
ENST00000397954; ENSP00000381045; ENSG00000114062. [Q05086-1]
ENST00000428984; ENSP00000401265; ENSG00000114062. [Q05086-2]
ENST00000438097; ENSP00000411258; ENSG00000114062. [Q05086-2]
ENST00000566215; ENSP00000457771; ENSG00000114062. [Q05086-2]
GeneID7337.
KEGGhsa:7337.
UCSCuc001zaq.3. human. [Q05086-1]
uc001zas.3. human. [Q05086-3]

Organism-specific databases

CTD7337.
GeneCardsGC15M025582.
GeneReviewsUBE3A.
HGNCHGNC:12496. UBE3A.
HPAHPA039410.
MIM105830. phenotype.
601623. gene.
neXtProtNX_Q05086.
Orphanet72. Angelman syndrome.
PharmGKBPA37144.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5021.
HOVERGENHBG059326.
InParanoidQ05086.
KOK10587.
OMANEPLNDV.
OrthoDBEOG7NKKJP.
PhylomeDBQ05086.
TreeFamTF315189.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ05086.
BgeeQ05086.
GenevestigatorQ05086.

Family and domain databases

InterProIPR000569. HECT.
IPR017134. Ubiquitin-protein_ligase_E6-AP.
[Graphical view]
PfamPF00632. HECT. 1 hit.
[Graphical view]
PIRSFPIRSF037201. Ubiquitin-protein_ligase_E6-AP. 1 hit.
SMARTSM00119. HECTc. 1 hit.
[Graphical view]
SUPFAMSSF56204. SSF56204. 1 hit.
PROSITEPS50237. HECT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBE3A. human.
EvolutionaryTraceQ05086.
GeneWikiUBE3A.
GenomeRNAi7337.
NextBio28722.
PROQ05086.
SOURCESearch...

Entry information

Entry nameUBE3A_HUMAN
AccessionPrimary (citable) accession number: Q05086
Secondary accession number(s): A8K8Z9 expand/collapse secondary AC list , P78355, Q93066, Q9UEP4, Q9UEP5, Q9UEP6, Q9UEP7, Q9UEP8, Q9UEP9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 148 of the entry and version 4 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM