UB2L5_HUMAN
ID UB2L5_HUMAN Reviewed; 154 AA.
AC A0A1B0GUS4;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 L5 {ECO:0000305};
DE EC=2.3.2.23 {ECO:0000255|PROSITE-ProRule:PRU10133};
DE AltName: Full=Ubiquitin-protein ligase L5 {ECO:0000255|PROSITE-ProRule:PRU10133};
GN Name=UBE2L5 {ECO:0000312|HGNC:HGNC:13477};
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 GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [2]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. {ECO:0000255|PROSITE-ProRule:PRU00388}.
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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AL161893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08456.1; -; Genomic_DNA.
DR EMBL; BQ438552; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS86346.1; -.
DR AlphaFoldDB; A0A1B0GUS4; -.
DR SMR; A0A1B0GUS4; -.
DR iPTMnet; A0A1B0GUS4; -.
DR PhosphoSitePlus; A0A1B0GUS4; -.
DR BioMuta; UBE2L5; -.
DR EPD; A0A1B0GUS4; -.
DR jPOST; A0A1B0GUS4; -.
DR MassIVE; A0A1B0GUS4; -.
DR PeptideAtlas; A0A1B0GUS4; -.
DR Ensembl; ENST00000436446.1; ENSP00000490834.1; ENSG00000236444.5.
DR Ensembl; ENST00000635918.2; ENSP00000490225.1; ENSG00000236444.5.
DR Ensembl; ENST00000638137.1; ENSP00000490931.1; ENSG00000236444.5.
DR MANE-Select; ENST00000635918.2; ENSP00000490225.1; NM_001355247.2; NP_001342176.1.
DR GeneCards; UBE2L5; -.
DR HGNC; HGNC:13477; UBE2L5.
DR HPA; ENSG00000236444; Tissue enriched (testis).
DR neXtProt; NX_A0A1B0GUS4; -.
DR OpenTargets; ENSG00000236444; -.
DR VEuPathDB; HostDB:ENSG00000236444; -.
DR GeneTree; ENSGT00940000153654; -.
DR OMA; NILTWHG; -.
DR SignaLink; A0A1B0GUS4; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; UBE2L5P; human.
DR Pharos; A0A1B0GUS4; Tdark.
DR PRO; PR:A0A1B0GUS4; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; A0A1B0GUS4; protein.
DR Bgee; ENSG00000236444; Expressed in left testis and 81 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..154
FT /note="Ubiquitin-conjugating enzyme E2 L5"
FT /id="PRO_0000443500"
FT DOMAIN 2..149
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 86
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 154 AA; 17875 MW; 378E48A28B89B4A5 CRC64;
MAASRRLMKE LEEIRKCGME NFRNIQVDEA NLLTWQGLIV PDNPPYNKGA FRIEINFPAE
YPFKPPRITF KTKIYHPNID EKGQVCLPVI SAENWKPATK TDQVIQSLIA LVNDPQPEHP
LRADLAEEYS NDRKKFCKNA EEFTKKYGEK RPVD
