UB2Q2_HUMAN
ID UB2Q2_HUMAN Reviewed; 375 AA.
AC Q8WVN8; B7Z3Q2; H3BRG2; Q8N4G6; Q96J08;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 Q2;
DE EC=2.3.2.23 {ECO:0000269|PubMed:20061386};
DE AltName: Full=E2 ubiquitin-conjugating enzyme Q2;
DE AltName: Full=Ubiquitin carrier protein Q2;
DE AltName: Full=Ubiquitin-protein ligase Q2;
GN Name=UBE2Q2;
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 [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Thalamus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 116-375 (ISOFORM 2).
RC TISSUE=Ovary, Placenta, and Uterus;
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 [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16300736; DOI=10.1016/j.bbrc.2005.11.026;
RA Seghatoleslam A., Zambrano A., Millon R., Ganguli G., Argentini M.,
RA Cromer A., Abecassis J., Wasylyk B.;
RT "Analysis of a novel human gene, LOC92912, over-expressed in hypopharyngeal
RT tumours.";
RL Biochem. Biophys. Res. Commun. 339:422-429(2006).
RN [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 197-363.
RG Structural genomics consortium (SGC);
RT "Structure of human ubiquitin-conjugating enzyme (UBCI) involved in embryo
RT attachment and implantation.";
RL Submitted (JAN-2006) to the PDB data bank.
RN [8] {ECO:0007744|PDB:1ZUO}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 197-363, AND AUTOUBIQUITINATION.
RX PubMed=22496338; DOI=10.1074/mcp.o111.013706;
RA Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J., Avvakumov G.V.,
RA Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K., Arrowsmith C.H.,
RA Raught B., Dhe-Paganon S.;
RT "A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-
RT function screen.";
RL Mol. Cell. Proteomics 11:329-341(2012).
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-
CC linked polyubiquitination. {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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- INTERACTION:
CC Q8WVN8; P62879: GNB2; NbExp=3; IntAct=EBI-2130157, EBI-356942;
CC Q8WVN8; P04792: HSPB1; NbExp=3; IntAct=EBI-2130157, EBI-352682;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16300736}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8WVN8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WVN8-2; Sequence=VSP_017298, VSP_017299;
CC Name=3;
CC IsoId=Q8WVN8-3; Sequence=VSP_044817;
CC Name=4;
CC IsoId=Q8WVN8-4; Sequence=VSP_055681;
CC -!- TISSUE SPECIFICITY: Detected in hypopharyngeal head and neck squamous
CC cell carcinoma, in tumor masses and invasive epithelium.
CC {ECO:0000269|PubMed:16300736}.
CC -!- PTM: Auto-ubiquitinated in vitro. {ECO:0000269|PubMed:22496338}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH34342.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK000617; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK296234; BAH12288.1; -; mRNA.
DR EMBL; AL832429; CAH10654.1; -; mRNA.
DR EMBL; AC019294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006827; AAH06827.1; -; mRNA.
DR EMBL; BC017708; AAH17708.1; -; mRNA.
DR EMBL; BC034342; AAH34342.1; ALT_INIT; mRNA.
DR CCDS; CCDS10286.1; -. [Q8WVN8-1]
DR CCDS; CCDS45309.1; -. [Q8WVN8-3]
DR CCDS; CCDS66839.1; -. [Q8WVN8-4]
DR RefSeq; NP_001138807.1; NM_001145335.1. [Q8WVN8-3]
DR RefSeq; NP_001271311.1; NM_001284382.1. [Q8WVN8-4]
DR RefSeq; NP_775740.1; NM_173469.3. [Q8WVN8-1]
DR PDB; 1ZUO; X-ray; 1.80 A; A/B=197-363.
DR PDBsum; 1ZUO; -.
DR AlphaFoldDB; Q8WVN8; -.
DR SMR; Q8WVN8; -.
DR BioGRID; 124986; 29.
DR IntAct; Q8WVN8; 10.
DR STRING; 9606.ENSP00000267938; -.
DR iPTMnet; Q8WVN8; -.
DR PhosphoSitePlus; Q8WVN8; -.
DR BioMuta; UBE2Q2; -.
DR DMDM; 74751557; -.
DR EPD; Q8WVN8; -.
DR jPOST; Q8WVN8; -.
DR MassIVE; Q8WVN8; -.
DR MaxQB; Q8WVN8; -.
DR PaxDb; Q8WVN8; -.
DR PeptideAtlas; Q8WVN8; -.
DR PRIDE; Q8WVN8; -.
DR ProteomicsDB; 42059; -.
DR ProteomicsDB; 74807; -. [Q8WVN8-1]
DR ProteomicsDB; 74808; -. [Q8WVN8-2]
DR Antibodypedia; 27387; 204 antibodies from 28 providers.
DR DNASU; 92912; -.
DR Ensembl; ENST00000267938.9; ENSP00000267938.4; ENSG00000140367.12. [Q8WVN8-1]
DR Ensembl; ENST00000561851.5; ENSP00000456229.1; ENSG00000140367.12. [Q8WVN8-3]
DR Ensembl; ENST00000569423.5; ENSP00000456324.1; ENSG00000140367.12. [Q8WVN8-4]
DR GeneID; 92912; -.
DR KEGG; hsa:92912; -.
DR MANE-Select; ENST00000267938.9; ENSP00000267938.4; NM_173469.4; NP_775740.1.
DR UCSC; uc002bbg.4; human. [Q8WVN8-1]
DR CTD; 92912; -.
DR DisGeNET; 92912; -.
DR GeneCards; UBE2Q2; -.
DR HGNC; HGNC:19248; UBE2Q2.
DR HPA; ENSG00000140367; Low tissue specificity.
DR MIM; 612501; gene.
DR neXtProt; NX_Q8WVN8; -.
DR OpenTargets; ENSG00000140367; -.
DR PharmGKB; PA142670652; -.
DR VEuPathDB; HostDB:ENSG00000140367; -.
DR eggNOG; KOG0897; Eukaryota.
DR GeneTree; ENSGT00940000155357; -.
DR HOGENOM; CLU_053863_0_0_1; -.
DR InParanoid; Q8WVN8; -.
DR OMA; LHCNITX; -.
DR OrthoDB; 1214134at2759; -.
DR PhylomeDB; Q8WVN8; -.
DR TreeFam; TF313338; -.
DR BRENDA; 2.3.2.23; 2681.
DR BRENDA; 2.3.2.24; 2681.
DR PathwayCommons; Q8WVN8; -.
DR Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q8WVN8; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 92912; 15 hits in 1079 CRISPR screens.
DR ChiTaRS; UBE2Q2; human.
DR EvolutionaryTrace; Q8WVN8; -.
DR GenomeRNAi; 92912; -.
DR Pharos; Q8WVN8; Tbio.
DR PRO; PR:Q8WVN8; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8WVN8; protein.
DR Bgee; ENSG00000140367; Expressed in secondary oocyte and 193 other tissues.
DR ExpressionAtlas; Q8WVN8; baseline and differential.
DR Genevisible; Q8WVN8; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 2.
DR IDEAL; IID00635; -.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 2.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm;
KW Nucleotide-binding; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..375
FT /note="Ubiquitin-conjugating enzyme E2 Q2"
FT /id="PRO_0000223879"
FT DOMAIN 204..368
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 123..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..157
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 304
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT VAR_SEQ 1..60
FT /note="MSVSGLKAELKFLASIFDKNHERFRIVSWKLDELHCQFLVPQQGSPHSLPPP
FT LTLHCNIT -> MRMDSLTEEKLECRLWCCLSDPSPPGLAARCCVLERSIVPSLRQ
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044817"
FT VAR_SEQ 95..129
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055681"
FT VAR_SEQ 296..314
FT /note="YVLGGGALCMELLTKQGWS -> LVHPSKGRWLNMLTVVCLD (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017298"
FT VAR_SEQ 315..375
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017299"
FT CONFLICT 161
FT /note="E -> K (in Ref. 1; BAH12288)"
FT /evidence="ECO:0000305"
FT HELIX 203..217
FT /evidence="ECO:0007829|PDB:1ZUO"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:1ZUO"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:1ZUO"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:1ZUO"
FT HELIX 251..263
FT /evidence="ECO:0007829|PDB:1ZUO"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:1ZUO"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:1ZUO"
FT STRAND 284..290
FT /evidence="ECO:0007829|PDB:1ZUO"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:1ZUO"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:1ZUO"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:1ZUO"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:1ZUO"
FT HELIX 319..332
FT /evidence="ECO:0007829|PDB:1ZUO"
FT HELIX 348..361
FT /evidence="ECO:0007829|PDB:1ZUO"
SQ SEQUENCE 375 AA; 42818 MW; 7DE07315E89178A3 CRC64;
MSVSGLKAEL KFLASIFDKN HERFRIVSWK LDELHCQFLV PQQGSPHSLP PPLTLHCNIT
ESYPSSSPIW FVDSEDPNLT SVLERLEDTK NNNLLRQQLK WLICELCSLY NLPKHLDVEM
LDQPLPTGQN GTTEEVTSEE EEEEEEMAED IEDLDHYEMK EEEPISGKKS EDEGIEKENL
AILEKIRKTQ RQDHLNGAVS GSVQASDRLM KELRDIYRSQ SYKTGIYSVE LINDSLYDWH
VKLQKVDPDS PLHSDLQILK EKEGIEYILL NFSFKDNFPF DPPFVRVVLP VLSGGYVLGG
GALCMELLTK QGWSSAYSIE SVIMQINATL VKGKARVQFG ANKNQYNLAR AQQSYNSIVQ
IHEKNGWYTP PKEDG
