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   27-MAR-2024, entry version 180.
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; 30.
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; 9606-ENSP00000267938; -.
DR   PeptideAtlas; Q8WVN8; -.
DR   ProteomicsDB; 42059; -.
DR   ProteomicsDB; 74807; -. [Q8WVN8-1]
DR   ProteomicsDB; 74808; -. [Q8WVN8-2]
DR   Pumba; Q8WVN8; -.
DR   Antibodypedia; 27387; 228 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   AGR; HGNC:19248; -.
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; XDIEDLD; -.
DR   OrthoDB; 37924at2759; -.
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   SIGNOR; Q8WVN8; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 92912; 17 hits in 1156 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 195 other cell types or tissues.
DR   ExpressionAtlas; Q8WVN8; baseline and differential.
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   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 2.
DR   IDEAL; IID00635; -.
DR   InterPro; IPR006575; RWD_dom.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF05773; RWD; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 2.
DR   PROSITE; PS50127; UBC_2; 1.
DR   Genevisible; Q8WVN8; HS.
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
//