UBC9_ICTTR
ID UBC9_ICTTR Reviewed; 158 AA.
AC Q2EF73;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=SUMO-conjugating enzyme UBC9;
DE EC=2.3.2.- {ECO:0000250|UniProtKB:P63279};
DE AltName: Full=RING-type E3 SUMO transferase UBC9;
DE AltName: Full=SUMO-protein ligase;
DE AltName: Full=Ubiquitin carrier protein 9;
DE AltName: Full=Ubiquitin carrier protein I;
DE AltName: Full=Ubiquitin-conjugating enzyme E2 I;
DE AltName: Full=Ubiquitin-protein ligase I;
GN Name=UBE2I; Synonyms=UBC9;
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=16955077; DOI=10.1038/sj.jcbfm.9600395;
RA Lee Y.J., Miyake S., Wakita H., McMullen D.C., Azuma Y., Auh S.,
RA Hallenbeck J.M.;
RT "Protein SUMOylation is massively increased in hibernation torpor and is
RT critical for the cytoprotection provided by ischemic preconditioning and
RT hypothermia in SHSY5Y cells.";
RL J. Cereb. Blood Flow Metab. 27:950-962(2007).
CC -!- FUNCTION: Accepts the ubiquitin-like proteins SUMO1, SUMO2 and SUMO3
CC from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent
CC attachment to other proteins with the help of an E3 ligase such as
CC RANBP2, CBX4 and ZNF451. Can catalyze the formation of poly-SUMO
CC chains. Essential for nuclear architecture and chromosome segregation
CC (By similarity). Necessary for sumoylation of FOXL2 and KAT5.
CC Sumoylates p53/TP53 at 'Lys-386'. {ECO:0000250|UniProtKB:P63279}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000250|UniProtKB:P63279}.
CC -!- SUBUNIT: Forms a complex with SENP6 and UBE2I in response to UV
CC irradiation (By similarity). Forms a tight complex with RANGAP1 and
CC RANBP2 (By similarity). Identified in a complex with SUMO2 and UBE2I,
CC where one ZNF451 interacts with one UBE2I and two SUMO2 chains, one
CC bound to the UBE2I active site and the other to another region of the
CC same UBE2I molecule (By similarity). Interacts with SETX (By
CC similarity). Interacts with HIPK1 and HIPK2 (By similarity). Interacts
CC with PPM1J (By similarity). Interacts with RASD2 (By similarity).
CC Interacts with TCF3 (By similarity). Interacts with NR2C1; the
CC interaction promotes its sumoylation (By similarity). Interacts with
CC SIAH1 (By similarity). Interacts with PARP (By similarity). Interacts
CC with various transcription factors such as TFAP2A, TFAP2B, and TFAP2C
CC (By similarity). Interacts with AR (By similarity). Interacts with ETS1
CC (By similarity). Interacts with SOX4 (By similarity). Interacts with
CC RWDD3; the interaction enhances the sumoylation of a number of proteins
CC such as HIF1A and I-kappa-B (By similarity). Interacts with FOXL2 (By
CC similarity). Interacts with DNM1l (via its GTPase and B domains); the
CC interaction promotes sumoylation of DNM1L, mainly in its B domain (By
CC similarity). Interacts with NFATC2IP; this inhibits formation of poly-
CC SUMO chains (By similarity). Interacts with FHIT (By similarity).
CC Interacts with PRKRA and p53/TP53 (By similarity). Interacts with UHRF2
CC (By similarity). Interacts with NR3C1 and this interaction is enhanced
CC in the presence of RWDD3 (By similarity). Interacts with MTA1 (By
CC similarity). Interacts with ZNF451 (By similarity). Interacts with
CC CPEB3 (By similarity). Interacts with SUMO1, SUMO2, and SUMO3 (By
CC similarity). Interacts with IPO13 (By similarity). Interacts with DNMT1
CC (By similarity). {ECO:0000250|UniProtKB:P63279,
CC ECO:0000250|UniProtKB:P63280, ECO:0000250|UniProtKB:P63281}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P63280}. Cytoplasm
CC {ECO:0000250|UniProtKB:P63280}. Note=Mainly nuclear (By similarity). In
CC spermatocytes, localizes in synaptonemal complexes (By similarity).
CC Recruited by BCL11A into the nuclear body (By similarity).
CC {ECO:0000250|UniProtKB:P63279, ECO:0000250|UniProtKB:P63280}.
CC -!- INDUCTION: In brain and kidney, during hibernation torpor (at protein
CC level). {ECO:0000269|PubMed:16955077}.
CC -!- PTM: Phosphorylation at Ser-71 significantly enhances SUMOylation
CC activity. {ECO:0000250|UniProtKB:P63279}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ385871; ABD39323.1; -; mRNA.
DR RefSeq; NP_001269197.1; NM_001282268.1.
DR RefSeq; XP_013219438.1; XM_013363984.1.
DR AlphaFoldDB; Q2EF73; -.
DR SMR; Q2EF73; -.
DR STRING; 43179.ENSSTOP00000009175; -.
DR PRIDE; Q2EF73; -.
DR Ensembl; ENSSTOT00000010227; ENSSTOP00000009175; ENSSTOG00000010233.
DR GeneID; 101955823; -.
DR CTD; 7329; -.
DR eggNOG; KOG0424; Eukaryota.
DR GeneTree; ENSGT00550000075088; -.
DR HOGENOM; CLU_030988_12_0_1; -.
DR InParanoid; Q2EF73; -.
DR OMA; QEPAWRA; -.
DR OrthoDB; 1522509at2759; -.
DR TreeFam; TF101122; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
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 Acetylation; ATP-binding; Cell cycle; Cell division; Chromosome partition;
KW Cytoplasm; Isopeptide bond; Mitosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P63279"
FT CHAIN 2..158
FT /note="SUMO-conjugating enzyme UBC9"
FT /id="PRO_0000250519"
FT DOMAIN 4..157
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 13..18
FT /note="Interaction with SUMO1"
FT /evidence="ECO:0000250"
FT ACT_SITE 93
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT SITE 4
FT /note="Interaction with RANBP2"
FT /evidence="ECO:0000250"
FT SITE 25
FT /note="Interaction with RANBP2"
FT /evidence="ECO:0000250"
FT SITE 57
FT /note="Interaction with RANBP2"
FT /evidence="ECO:0000250"
FT SITE 100..101
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P63279"
FT MOD_RES 65
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63279"
FT MOD_RES 71
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P63279"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63279"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63279"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P63279"
FT CROSSLNK 49
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63279"
FT CROSSLNK 49
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63279"
FT CROSSLNK 101
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P63279"
SQ SEQUENCE 158 AA; 18007 MW; E2C826E9C8D0683D CRC64;
MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG TPWEGGLFKL
RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED KDWRPAITIK QILLGIQELL
NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA QAKKFAPS
