ID A0A2I3S7I0_PANTR Unreviewed; 526 AA.
AC A0A2I3S7I0; A0A2J8MUN0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=TRIM2 {ECO:0000313|Ensembl:ENSPTRP00000072498.1,
GN ECO:0000313|VGNC:VGNC:57073};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000072498.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000072498.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000072498.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC {ECO:0000256|ARBA:ARBA00008518}.
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; AACZ04005056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04005057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3S7I0; -.
DR Ensembl; ENSPTRT00000084667.1; ENSPTRP00000072498.1; ENSPTRG00000016522.6.
DR VGNC; VGNC:57073; TRIM2.
DR GeneTree; ENSGT00940000155905; -.
DR Proteomes; UP000002277; Chromosome 4.
DR Bgee; ENSPTRG00000016522; Expressed in temporal lobe and 21 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19824; Bbox2_TRIM2_C-VII; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR047153; TRIM45/56/19.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR25462; BONUS, ISOFORM C-RELATED; 1.
DR PANTHER; PTHR25462:SF304; E3 UBIQUITIN-PROTEIN LIGASE TRIM56; 1.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00557; IG_FLMN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 23..64
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 113..154
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 320..421
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REGION 430..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 526 AA; 58469 MW; D7E2AB85D0B851B9 CRC64;
MASEGTNIPS PVVRQIDKQF LICSICLERY KNPKVLPCLH TFCERCLQNY IPAHSLTLSC
PVCRQTSILP EKGVAALQNN FFITNLMDVL QRTPGSNVEE SSILETVTAV AAGKPLSCPN
HDGNVMEFYC QSCETAMCRE CTEGEHAEHP TVPLKDVVEQ HKASLQVQLD AVNKRLPEID
SALQFISEII HQLTNQKASI VDDIHSTFDE LQKTLNVRKS VLLMELEVNY GLKHKVLQSQ
LDTLLQGQES IKSCSNFTAQ ALNHGTETEV LLVKKQMSEK LNELADQDFP LHPRENDQLD
FIVETEGLKK SIHNLGTILT TNAVASETVA TGEGLRQTII GQPMSVTITT KDKDGELCKT
GNAYLTAELS TPDGSVADGE ILDNKNGTYE FLYTVQKEGD FTLSLRLYDQ HIRGSPFKLK
VVRSADVSPT TEGVKRRVKS PGSGHVKQKA VKRPASMYST GKRKENPIED DLIFRVDGVL
QAEVQWHDLS PLQPLPPGFK QFSCLGLLSS WDYRHAPPCS ANFLYF
//
