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Protein

Ubiquitin-conjugating enzyme E2 A

Gene

UBE2A

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

Functioni

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes 'Lys-11', as well as 'Lys-48'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA.2 Publications

Catalytic activityi

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

Pathway: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.PROSITE-ProRule annotation
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei88 – 881Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ligase activity Source: UniProtKB-KW
  • ubiquitin conjugating enzyme activity Source: MGI
  • ubiquitin protein ligase activity Source: GO_Central
  • ubiquitin protein ligase binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  • antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  • DNA repair Source: UniProtKB
  • histone H2A ubiquitination Source: UniProtKB
  • in utero embryonic development Source: Ensembl
  • maternal process involved in female pregnancy Source: Ensembl
  • positive regulation of cell proliferation Source: UniProtKB
  • postreplication repair Source: UniProtKB
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: GO_Central
  • protein autoubiquitination Source: UniProtKB
  • protein K11-linked ubiquitination Source: UniProtKB
  • protein K48-linked ubiquitination Source: UniProtKB
  • protein polyubiquitination Source: Reactome
  • response to UV Source: UniProtKB
  • ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.3.2.B6. 2681.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiP49459.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 A (EC:6.3.2.19)
Alternative name(s):
RAD6 homolog A
Short name:
HR6A
Short name:
hHR6A
Ubiquitin carrier protein A
Ubiquitin-protein ligase A
Gene namesi
Name:UBE2A
Synonyms:RAD6A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:12472. UBE2A.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: UniProtKB
  • cytoplasm Source: GO_Central
  • cytosol Source: Reactome
  • HULC complex Source: UniProtKB
  • nuclear chromatin Source: GO_Central
  • XY body Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Mental retardation, X-linked, syndromic, Nascimento-type (MRXSN)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXSN features include dysmorphic facies, hirsutism, skin and nails abnormalities, obesity, speech anomalies and seizures.

See also OMIM:300860
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111R → Q in MRXSN. 1 Publication
VAR_066627
Natural varianti23 – 231G → R in MRXSN. 1 Publication
VAR_066628

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi300860. phenotype.
Orphaneti163956. X-linked intellectual disability, Nascimento type.
PharmGKBiPA37122.

Polymorphism and mutation databases

DMDMi33518639.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Ubiquitin-conjugating enzyme E2 APRO_0000082445Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei120 – 1201Phosphoserine; by CDK91 Publication

Post-translational modificationi

Phosphorylation at Ser-120 by CDK9 increases activity towards histone H2B.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP49459.
PaxDbiP49459.
PRIDEiP49459.

PTM databases

PhosphoSiteiP49459.

Expressioni

Gene expression databases

BgeeiP49459.
CleanExiHS_UBE2A.
GenevisibleiP49459. HS.

Interactioni

Subunit structurei

Interacts with RAD18 and WAC.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SDCBPO005603EBI-2339348,EBI-727004

Protein-protein interaction databases

BioGridi113167. 50 interactions.
DIPiDIP-24260N.
IntActiP49459. 19 interactions.
MINTiMINT-267059.
STRINGi9606.ENSP00000360613.

Structurei

3D structure databases

ProteinModelPortaliP49459.
SMRiP49459. Positions 2-149.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110565.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiP49459.
KOiK10573.
OMAiSENNIMM.
OrthoDBiEOG7M0NTH.
PhylomeDBiP49459.
TreeFamiTF101128.

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. AlignAdd to basket

Isoform 1 (identifier: P49459-1) [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
MSTPARRRLM RDFKRLQEDP PAGVSGAPSE NNIMVWNAVI FGPEGTPFED
60 70 80 90 100
GTFKLTIEFT EEYPNKPPTV RFVSKMFHPN VYADGSICLD ILQNRWSPTY
110 120 130 140 150
DVSSILTSIQ SLLDEPNPNS PANSQAAQLY QENKREYEKR VSAIVEQSWR

DC
Length:152
Mass (Da):17,315
Last modified:August 4, 2003 - v2
Checksum:i0AAEB5B7770E47E2
GO
Isoform 2 (identifier: P49459-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     51-80: Missing.

Show »
Length:122
Mass (Da):13,777
Checksum:iFE5B4840CF115701
GO
Isoform 3 (identifier: P49459-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-75: Missing.

Note: No experimental confirmation available.
Show »
Length:77
Mass (Da):8,833
Checksum:iE947FEF59BB7F0AE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491E → G in AAA35981 (PubMed:1717990).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111R → Q in MRXSN. 1 Publication
VAR_066627
Natural varianti23 – 231G → R in MRXSN. 1 Publication
VAR_066628

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7575Missing in isoform 3. CuratedVSP_043851Add
BLAST
Alternative sequencei51 – 8030Missing in isoform 2. 1 PublicationVSP_043852Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74524 mRNA. Translation: AAA35981.1.
AK297696 mRNA. Translation: BAG60054.1.
AK313092 mRNA. Translation: BAG35916.1.
DQ068065 Genomic DNA. Translation: AAY46159.1.
AC004913 Genomic DNA. No translation available.
CH471161 Genomic DNA. Translation: EAW89861.1.
CH471161 Genomic DNA. Translation: EAW89862.1.
CH471161 Genomic DNA. Translation: EAW89863.1.
BC010175 mRNA. Translation: AAH10175.1.
CCDSiCCDS14580.1. [P49459-1]
CCDS14581.1. [P49459-2]
PIRiA41222.
RefSeqiNP_001269090.1. NM_001282161.1.
NP_003327.2. NM_003336.3. [P49459-1]
NP_861427.1. NM_181762.2. [P49459-2]
UniGeneiHs.379466.

Genome annotation databases

EnsembliENST00000371558; ENSP00000360613; ENSG00000077721. [P49459-1]
ENST00000625938; ENSP00000486599; ENSG00000077721. [P49459-2]
ENST00000630695; ENSP00000486550; ENSG00000077721. [P49459-3]
GeneIDi7319.
KEGGihsa:7319.
UCSCiuc004erl.3. human. [P49459-1]
uc004erm.3. human. [P49459-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74524 mRNA. Translation: AAA35981.1.
AK297696 mRNA. Translation: BAG60054.1.
AK313092 mRNA. Translation: BAG35916.1.
DQ068065 Genomic DNA. Translation: AAY46159.1.
AC004913 Genomic DNA. No translation available.
CH471161 Genomic DNA. Translation: EAW89861.1.
CH471161 Genomic DNA. Translation: EAW89862.1.
CH471161 Genomic DNA. Translation: EAW89863.1.
BC010175 mRNA. Translation: AAH10175.1.
CCDSiCCDS14580.1. [P49459-1]
CCDS14581.1. [P49459-2]
PIRiA41222.
RefSeqiNP_001269090.1. NM_001282161.1.
NP_003327.2. NM_003336.3. [P49459-1]
NP_861427.1. NM_181762.2. [P49459-2]
UniGeneiHs.379466.

3D structure databases

ProteinModelPortaliP49459.
SMRiP49459. Positions 2-149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113167. 50 interactions.
DIPiDIP-24260N.
IntActiP49459. 19 interactions.
MINTiMINT-267059.
STRINGi9606.ENSP00000360613.

PTM databases

PhosphoSiteiP49459.

Polymorphism and mutation databases

DMDMi33518639.

Proteomic databases

MaxQBiP49459.
PaxDbiP49459.
PRIDEiP49459.

Protocols and materials databases

DNASUi7319.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371558; ENSP00000360613; ENSG00000077721. [P49459-1]
ENST00000625938; ENSP00000486599; ENSG00000077721. [P49459-2]
ENST00000630695; ENSP00000486550; ENSG00000077721. [P49459-3]
GeneIDi7319.
KEGGihsa:7319.
UCSCiuc004erl.3. human. [P49459-1]
uc004erm.3. human. [P49459-2]

Organism-specific databases

CTDi7319.
GeneCardsiGC0XP118708.
HGNCiHGNC:12472. UBE2A.
MIMi300860. phenotype.
312180. gene.
neXtProtiNX_P49459.
Orphaneti163956. X-linked intellectual disability, Nascimento type.
PharmGKBiPA37122.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110565.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiP49459.
KOiK10573.
OMAiSENNIMM.
OrthoDBiEOG7M0NTH.
PhylomeDBiP49459.
TreeFamiTF101128.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B6. 2681.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiP49459.

Miscellaneous databases

ChiTaRSiUBE2A. human.
GeneWikiiUBE2A.
GenomeRNAii7319.
NextBioi28614.
PROiP49459.
SOURCEiSearch...

Gene expression databases

BgeeiP49459.
CleanExiHS_UBE2A.
GenevisibleiP49459. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6."
    Koken M.H.M., Reynolds P., Jaspers-Dekker I., Prakash L., Prakash S., Bootsma D., Hoeijmakers J.H.J.
    Proc. Natl. Acad. Sci. U.S.A. 88:8865-8869(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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 AND 2).
    Tissue: Subthalamic nucleus.
  3. NIEHS SNPs program
    Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Skin.
  7. "The human homolog of yeast BRE1 functions as a transcriptional coactivator through direct activator interactions."
    Kim J., Hake S.B., Roeder R.G.
    Mol. Cell 20:759-770(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "UBE2A, which encodes a ubiquitin-conjugating enzyme, is mutated in a novel X-linked mental retardation syndrome."
    Nascimento R.M., Otto P.A., de Brouwer A.P., Vianna-Morgante A.M.
    Am. J. Hum. Genet. 79:549-555(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MRXSN.
  9. "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.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "WAC, a functional partner of RNF20/40, regulates histone H2B ubiquitination and gene transcription."
    Zhang F., Yu X.
    Mol. Cell 41:384-397(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WAC.
  12. "Phosphorylation by cyclin-dependent kinase-9 controls ubiquitin-conjugating enzyme-2A function."
    Shchebet A., Karpiuk O., Kremmer E., Eick D., Johnsen S.A.
    Cell Cycle 11:2122-2127(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-120.
  13. "Novel missense mutations in the ubiquitination-related gene UBE2A cause a recognizable X-linked mental retardation syndrome."
    Budny B., Badura-Stronka M., Materna-Kiryluk A., Tzschach A., Raynaud M., Latos-Bielenska A., Ropers H.H.
    Clin. Genet. 77:541-551(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MRXSN GLN-11 AND ARG-23.

Entry informationi

Entry nameiUBE2A_HUMAN
AccessioniPrimary (citable) accession number: P49459
Secondary accession number(s): A6NFE9
, A6NGR2, A6NMF5, B2R7R9, D3DWI1, Q4TTG1, Q96FX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: August 4, 2003
Last modified: June 24, 2015
This is version 144 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.