UBE2A_HUMAN
ID UBE2A_HUMAN Reviewed; 152 AA.
AC P49459; A6NFE9; A6NGR2; A6NMF5; B2R7R9; D3DWI1; Q4TTG1; Q96FX4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 A;
DE EC=2.3.2.23 {ECO:0000269|PubMed:20061386};
DE AltName: Full=E2 ubiquitin-conjugating enzyme A;
DE AltName: Full=RAD6 homolog A;
DE Short=HR6A;
DE Short=hHR6A;
DE AltName: Full=Ubiquitin carrier protein A;
DE AltName: Full=Ubiquitin-protein ligase A;
GN Name=UBE2A; Synonyms=RAD6A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1717990; DOI=10.1073/pnas.88.20.8865;
RA Koken M.H.M., Reynolds P., Jaspers-Dekker I., Prakash L., Prakash S.,
RA Bootsma D., Hoeijmakers J.H.J.;
RT "Structural and functional conservation of two human homologs of the yeast
RT DNA repair gene RAD6.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8865-8869(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Subthalamic nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION.
RX PubMed=16337599; DOI=10.1016/j.molcel.2005.11.012;
RA Kim J., Hake S.B., Roeder R.G.;
RT "The human homolog of yeast BRE1 functions as a transcriptional coactivator
RT through direct activator interactions.";
RL Mol. Cell 20:759-770(2005).
RN [8]
RP INVOLVEMENT IN MRXSN.
RX PubMed=16909393; DOI=10.1086/507047;
RA Nascimento R.M., Otto P.A., de Brouwer A.P., Vianna-Morgante A.M.;
RT "UBE2A, which encodes a ubiquitin-conjugating enzyme, is mutated in a novel
RT X-linked mental retardation syndrome.";
RL Am. J. Hum. Genet. 79:549-555(2006).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20061386; DOI=10.1074/jbc.m109.089003;
RA David Y., Ziv T., Admon A., Navon A.;
RT "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
RT preferred lysines.";
RL J. Biol. Chem. 285:8595-8604(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP INTERACTION WITH WAC.
RX PubMed=21329877; DOI=10.1016/j.molcel.2011.01.024;
RA Zhang F., Yu X.;
RT "WAC, a functional partner of RNF20/40, regulates histone H2B
RT ubiquitination and gene transcription.";
RL Mol. Cell 41:384-397(2011).
RN [12]
RP PHOSPHORYLATION AT SER-120.
RX PubMed=22592529; DOI=10.4161/cc.20548;
RA Shchebet A., Karpiuk O., Kremmer E., Eick D., Johnsen S.A.;
RT "Phosphorylation by cyclin-dependent kinase-9 controls ubiquitin-
RT conjugating enzyme-2A function.";
RL Cell Cycle 11:2122-2127(2012).
RN [13]
RP VARIANTS MRXSN GLN-11 AND ARG-23.
RX PubMed=20412111; DOI=10.1111/j.1399-0004.2010.01429.x;
RA Budny B., Badura-Stronka M., Materna-Kiryluk A., Tzschach A., Raynaud M.,
RA Latos-Bielenska A., Ropers H.H.;
RT "Novel missense mutations in the ubiquitination-related gene UBE2A cause a
RT recognizable X-linked mental retardation syndrome.";
RL Clin. Genet. 77:541-551(2010).
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. In association with the E3
CC enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription
CC regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-
CC 120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic
CC transcriptional activation, elongation by RNA polymerase II, telomeric
CC silencing, and is also a prerequisite for H3K4me and H3K79me formation.
CC In vitro catalyzes 'Lys-11', as well as 'Lys-48'-linked
CC polyubiquitination. Required for postreplication repair of UV-damaged
CC DNA. {ECO:0000269|PubMed:16337599, ECO:0000269|PubMed:20061386}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC ProRule:PRU10133, ECO:0000269|PubMed:20061386};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Interacts with RAD18 and WAC (PubMed:21329877). Interacts with
CC RFPL4A and CCNB1 (By similarity). {ECO:0000250|UniProtKB:Q9Z255,
CC ECO:0000269|PubMed:21329877}.
CC -!- INTERACTION:
CC P49459; P55212: CASP6; NbExp=3; IntAct=EBI-2339348, EBI-718729;
CC P49459; P28329-3: CHAT; NbExp=3; IntAct=EBI-2339348, EBI-25837549;
CC P49459; O14645: DNALI1; NbExp=3; IntAct=EBI-2339348, EBI-395638;
CC P49459; P41091: EIF2S3; NbExp=3; IntAct=EBI-2339348, EBI-1054228;
CC P49459; O75460-2: ERN1; NbExp=3; IntAct=EBI-2339348, EBI-25852368;
CC P49459; P22607: FGFR3; NbExp=3; IntAct=EBI-2339348, EBI-348399;
CC P49459; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-2339348, EBI-10226858;
CC P49459; Q14957: GRIN2C; NbExp=3; IntAct=EBI-2339348, EBI-8285963;
CC P49459; P06396: GSN; NbExp=3; IntAct=EBI-2339348, EBI-351506;
CC P49459; P30519: HMOX2; NbExp=3; IntAct=EBI-2339348, EBI-712096;
CC P49459; P54652: HSPA2; NbExp=3; IntAct=EBI-2339348, EBI-356991;
CC P49459; O14901: KLF11; NbExp=3; IntAct=EBI-2339348, EBI-948266;
CC P49459; P13473-2: LAMP2; NbExp=3; IntAct=EBI-2339348, EBI-21591415;
CC P49459; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-2339348, EBI-2811583;
CC P49459; Q96CV9: OPTN; NbExp=3; IntAct=EBI-2339348, EBI-748974;
CC P49459; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-2339348, EBI-5280197;
CC P49459; Q9NS91: RAD18; NbExp=4; IntAct=EBI-2339348, EBI-2339393;
CC P49459; P62826: RAN; NbExp=3; IntAct=EBI-2339348, EBI-286642;
CC P49459; Q8WZA2: RAPGEF4; NbExp=3; IntAct=EBI-2339348, EBI-948476;
CC P49459; O00560: SDCBP; NbExp=9; IntAct=EBI-2339348, EBI-727004;
CC P49459; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-2339348, EBI-741480;
CC P49459; Q9Y649; NbExp=3; IntAct=EBI-2339348, EBI-25900580;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P49459-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49459-2; Sequence=VSP_043852;
CC Name=3;
CC IsoId=P49459-3; Sequence=VSP_043851;
CC -!- PTM: Phosphorylation at Ser-120 by CDK9 increases activity towards
CC histone H2B. {ECO:0000269|PubMed:22592529}.
CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic,
CC Nascimento-type (MRXSN) [MIM:300860]: A disorder characterized by
CC significantly below average general intellectual functioning associated
CC with impairments in adaptive behavior and manifested during the
CC developmental period. MRXSN features include dysmorphic facies,
CC hirsutism, skin and nails abnormalities, obesity, speech anomalies and
CC seizures. {ECO:0000269|PubMed:16909393, ECO:0000269|PubMed:20412111}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ube2a/";
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DR EMBL; M74524; AAA35981.1; -; mRNA.
DR EMBL; AK297696; BAG60054.1; -; mRNA.
DR EMBL; AK313092; BAG35916.1; -; mRNA.
DR EMBL; DQ068065; AAY46159.1; -; Genomic_DNA.
DR EMBL; AC004913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471161; EAW89861.1; -; Genomic_DNA.
DR EMBL; CH471161; EAW89862.1; -; Genomic_DNA.
DR EMBL; CH471161; EAW89863.1; -; Genomic_DNA.
DR EMBL; BC010175; AAH10175.1; -; mRNA.
DR CCDS; CCDS14580.1; -. [P49459-1]
DR CCDS; CCDS14581.1; -. [P49459-2]
DR PIR; A41222; A41222.
DR RefSeq; NP_001269090.1; NM_001282161.1.
DR RefSeq; NP_003327.2; NM_003336.3. [P49459-1]
DR RefSeq; NP_861427.1; NM_181762.2. [P49459-2]
DR PDB; 6CYO; X-ray; 1.85 A; A=1-152.
DR PDB; 6CYR; X-ray; 2.20 A; A=1-152.
DR PDBsum; 6CYO; -.
DR PDBsum; 6CYR; -.
DR AlphaFoldDB; P49459; -.
DR SMR; P49459; -.
DR BioGRID; 113167; 227.
DR CORUM; P49459; -.
DR DIP; DIP-24260N; -.
DR IntAct; P49459; 50.
DR MINT; P49459; -.
DR STRING; 9606.ENSP00000360613; -.
DR iPTMnet; P49459; -.
DR PhosphoSitePlus; P49459; -.
DR SwissPalm; P49459; -.
DR BioMuta; UBE2A; -.
DR DMDM; 33518639; -.
DR EPD; P49459; -.
DR jPOST; P49459; -.
DR MassIVE; P49459; -.
DR MaxQB; P49459; -.
DR PaxDb; P49459; -.
DR PeptideAtlas; P49459; -.
DR PRIDE; P49459; -.
DR ProteomicsDB; 56018; -. [P49459-1]
DR ProteomicsDB; 56019; -. [P49459-2]
DR ProteomicsDB; 56020; -. [P49459-3]
DR TopDownProteomics; P49459-1; -. [P49459-1]
DR TopDownProteomics; P49459-2; -. [P49459-2]
DR Antibodypedia; 29799; 209 antibodies from 28 providers.
DR DNASU; 7319; -.
DR Ensembl; ENST00000371558.7; ENSP00000360613.2; ENSG00000077721.16. [P49459-1]
DR Ensembl; ENST00000625938.2; ENSP00000486599.1; ENSG00000077721.16. [P49459-2]
DR Ensembl; ENST00000630695.2; ENSP00000486550.1; ENSG00000077721.16. [P49459-3]
DR GeneID; 7319; -.
DR KEGG; hsa:7319; -.
DR MANE-Select; ENST00000371558.7; ENSP00000360613.2; NM_003336.4; NP_003327.2.
DR UCSC; uc004erl.5; human. [P49459-1]
DR CTD; 7319; -.
DR DisGeNET; 7319; -.
DR GeneCards; UBE2A; -.
DR HGNC; HGNC:12472; UBE2A.
DR HPA; ENSG00000077721; Low tissue specificity.
DR MalaCards; UBE2A; -.
DR MIM; 300860; phenotype.
DR MIM; 312180; gene.
DR neXtProt; NX_P49459; -.
DR OpenTargets; ENSG00000077721; -.
DR Orphanet; 163956; X-linked intellectual disability, Nascimento type.
DR PharmGKB; PA37122; -.
DR VEuPathDB; HostDB:ENSG00000077721; -.
DR eggNOG; KOG0419; Eukaryota.
DR GeneTree; ENSGT00940000155075; -.
DR HOGENOM; CLU_030988_10_2_1; -.
DR InParanoid; P49459; -.
DR OMA; DHKSQYI; -.
DR OrthoDB; 1292821at2759; -.
DR PhylomeDB; P49459; -.
DR TreeFam; TF101128; -.
DR BRENDA; 2.3.2.23; 2681.
DR BRENDA; 2.3.2.24; 2681.
DR PathwayCommons; P49459; -.
DR Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P49459; -.
DR SIGNOR; P49459; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 7319; 41 hits in 717 CRISPR screens.
DR ChiTaRS; UBE2A; human.
DR GeneWiki; UBE2A; -.
DR GenomeRNAi; 7319; -.
DR Pharos; P49459; Tbio.
DR PRO; PR:P49459; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P49459; protein.
DR Bgee; ENSG00000077721; Expressed in endothelial cell and 206 other tissues.
DR ExpressionAtlas; P49459; baseline and differential.
DR Genevisible; P49459; HS.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0033503; C:HULC complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; TAS:Reactome.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IGI:UniProtKB.
DR GO; GO:0033522; P:histone H2A ubiquitination; IDA:UniProtKB.
DR GO; GO:0016574; P:histone ubiquitination; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0006301; P:postreplication repair; NAS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0009411; P:response to UV; IGI:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; NAS:UniProtKB.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Chromatin regulator;
KW Disease variant; DNA damage; DNA repair; Intellectual disability;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..152
FT /note="Ubiquitin-conjugating enzyme E2 A"
FT /id="PRO_0000082445"
FT DOMAIN 4..150
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 88
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT MOD_RES 120
FT /note="Phosphoserine; by CDK9"
FT /evidence="ECO:0000269|PubMed:22592529"
FT VAR_SEQ 1..75
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_043851"
FT VAR_SEQ 51..80
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043852"
FT VARIANT 11
FT /note="R -> Q (in MRXSN; dbSNP:rs387906728)"
FT /evidence="ECO:0000269|PubMed:20412111"
FT /id="VAR_066627"
FT VARIANT 23
FT /note="G -> R (in MRXSN; dbSNP:rs1556235551)"
FT /evidence="ECO:0000269|PubMed:20412111"
FT /id="VAR_066628"
FT CONFLICT 49
FT /note="E -> G (in Ref. 1; AAA35981)"
FT /evidence="ECO:0000305"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:6CYO"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:6CYO"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:6CYO"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:6CYO"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:6CYO"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:6CYO"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6CYO"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:6CYO"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:6CYO"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:6CYO"
FT HELIX 134..148
FT /evidence="ECO:0007829|PDB:6CYO"
SQ SEQUENCE 152 AA; 17315 MW; 0AAEB5B7770E47E2 CRC64;
MSTPARRRLM RDFKRLQEDP PAGVSGAPSE NNIMVWNAVI FGPEGTPFED GTFKLTIEFT
EEYPNKPPTV RFVSKMFHPN VYADGSICLD ILQNRWSPTY DVSSILTSIQ SLLDEPNPNS
PANSQAAQLY QENKREYEKR VSAIVEQSWR DC
