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Database: UniProt
Entry: H2P080_PONAB
LinkDB: H2P080_PONAB
Original site: H2P080_PONAB 
ID   H2P080_PONAB            Unreviewed;       222 AA.
AC   H2P080; A0A2J8R3E8;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=E2 ubiquitin-conjugating enzyme {ECO:0000256|ARBA:ARBA00012486};
DE            EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486};
GN   Name=UBE2S {ECO:0000313|Ensembl:ENSPPYP00000011677.3};
GN   ORFNames=CR201_G0054342 {ECO:0000313|EMBL:PNJ03050.1};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000011677.3, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000011677.3, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PNJ03050.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Susie {ECO:0000313|EMBL:PNJ03050.1};
RA   Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA   Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA   Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA   Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA   Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT   "High-resolution comparative analysis of great ape genomes.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPPYP00000011677.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000485};
CC   -!- PATHWAY: Protein modification. {ECO:0000256|ARBA:ARBA00043952}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000256|RuleBase:RU362109}.
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DR   EMBL; NDHI03003771; PNJ03050.1; -; Genomic_DNA.
DR   STRING; 9601.ENSPPYP00000011677; -.
DR   Ensembl; ENSPPYT00000012121.3; ENSPPYP00000011677.3; ENSPPYG00000010418.3.
DR   eggNOG; KOG0423; Eukaryota.
DR   GeneTree; ENSGT00940000157149; -.
DR   HOGENOM; CLU_030988_5_3_1; -.
DR   OMA; QPAKCGA; -.
DR   OrthoDB; 179223at2759; -.
DR   TreeFam; TF101120; -.
DR   Proteomes; UP000001595; Chromosome 19.
DR   GO; GO:0005680; C:anaphase-promoting complex; IEA:Ensembl.
DR   GO; GO:0010997; F:anaphase-promoting complex binding; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:Ensembl.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IEA:Ensembl.
DR   GO; GO:0010458; P:exit from mitosis; IEA:Ensembl.
DR   GO; GO:0010994; P:free ubiquitin chain polymerization; IEA:Ensembl.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; IEA:Ensembl.
DR   GO; GO:0044314; P:protein K27-linked ubiquitination; IEA:Ensembl.
DR   GO; GO:0035519; P:protein K29-linked ubiquitination; IEA:Ensembl.
DR   GO; GO:0085020; P:protein K6-linked ubiquitination; IEA:Ensembl.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:Ensembl.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24067:SF154; UBIQUITIN-CONJUGATING ENZYME E2 G2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362109};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU362109}.
FT   DOMAIN          11..157
FT                   /note="UBC core"
FT                   /evidence="ECO:0000259|PROSITE:PS50127"
FT   REGION          157..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        95
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   222 AA;  23815 MW;  35F31C3DCD2AEB7B CRC64;
     MNSNVENLPP HIIRLVYKEV TTLTADPPDG IKVFPNEEDL TDLQVTIEGP EGTPYAGGLF
     RMKLLLGKDF PASPPKGYFL TKIFHPNVGA NGEICVNVLK RDWTAELGIR HVLLTIKCLL
     IHPNPESALN EEAGRLLLEN YEEYAARARL LTEIHGGAGG PSGRAEAGRA LASGTAASST
     DPGAPGGPGG AEGPMAKKHA GERDKKLVAK KKTDKKRALR RL
//
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