位置:首页 > 蛋白库 > TRIM2_CALJA
TRIM2_CALJA
ID   TRIM2_CALJA             Reviewed;         744 AA.
AC   F7H9X2;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Tripartite motif-containing protein 2;
DE            EC=2.3.2.27;
DE   AltName: Full=E3 ubiquitin-protein ligase TRIM2;
DE   AltName: Full=RING-type E3 ubiquitin transferase TRIM2 {ECO:0000305};
GN   Name=TRIM2;
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates the ubiquitination
CC       of phosphorylated BCL2L11. Also mediates the UBE2D1-dependent
CC       ubiquitination of NEFL. Plays a neuroprotective function. May play a
CC       role in neuronal rapid ischemic tolerance.
CC       {ECO:0000250|UniProtKB:Q9ESN6}.
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;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with myosin V; myosin V may not be a substrate for
CC       ubiquitination. Interacts with NEFL. Interacts with phosphorylated
CC       BCL2L11. {ECO:0000250|UniProtKB:Q9ESN6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ESN6}.
CC   -!- DOMAIN: The interaction with myosin V is dependent upon its NHL
CC       repeats, which form a beta-propeller (NHL) domain containing six
CC       blades. {ECO:0000250|UniProtKB:Q9ESN6}.
CC   -!- PTM: RING-type zinc finger-dependent and UBE2D1-dependent
CC       autoubiquitination. {ECO:0000250|UniProtKB:Q9ESN6}.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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; ACFV01002178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01002179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01002180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01002181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01002182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01002183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01002184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01002185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01002186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01002187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01002188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01002189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01002190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01002191; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01002192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01002193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01002194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01002195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01002196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F7H9X2; -.
DR   SMR; F7H9X2; -.
DR   STRING; 9483.ENSCJAP00000003623; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   HOGENOM; CLU_008645_5_0_1; -.
DR   InParanoid; F7H9X2; -.
DR   OMA; CTSGEHR; -.
DR   TreeFam; TF331018; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008225; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
DR   Gene3D; 2.120.10.30; -; 2.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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; IPR001258; NHL_repeat.
DR   InterPro; IPR027370; Znf-RING_LisH.
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   Pfam; PF00630; Filamin; 1.
DR   Pfam; PF01436; NHL; 6.
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; SSF81296; SSF81296; 1.
DR   PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR   PROSITE; PS51125; NHL; 6.
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   Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW   Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..744
FT                   /note="Tripartite motif-containing protein 2"
FT                   /id="PRO_0000413607"
FT   REPEAT          320..421
FT                   /note="Filamin"
FT   REPEAT          473..516
FT                   /note="NHL 1"
FT   REPEAT          520..563
FT                   /note="NHL 2"
FT   REPEAT          564..605
FT                   /note="NHL 3"
FT   REPEAT          609..652
FT                   /note="NHL 4"
FT   REPEAT          656..699
FT                   /note="NHL 5"
FT   REPEAT          700..743
FT                   /note="NHL 6"
FT   ZN_FING         23..64
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         113..154
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   REGION          432..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:D3ZQG6"
FT   MOD_RES         371
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ESN6"
FT   MOD_RES         375
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ESN6"
FT   MOD_RES         424
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ESN6"
FT   MOD_RES         428
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ESN6"
SQ   SEQUENCE   744 AA;  81517 MW;  113ACDB1EFF52C7D CRC64;
     MASEGTNIPS PVVRQIDKQF LICSICLERY KNPKVLPCLH TFCERCLQNY IPAHSLTLSC
     PVCRQTSILP EKGVAALQNN FFITNLMDVL QRTPGSNVEE SSILETVTAV AAGKPLSCPN
     HDGNVMEFYC QSCETAMCRE CTEGEHAEHP TVPLKDVVEQ HKASLQVQLD AVNKRLPEID
     SALQFISEII HQLTNQKASI VDDIHSTFDE LQKTLNVRKS VLLMELEVNY GVKHKVLQSQ
     LDTLLQGQES IKSCSNFTAQ ALNHGTETEV LLVKKQMSEK LNELADQDFP LHPRENDQLD
     FIVETEGLKK SIHNLGTILT TNAVASETVA TGEGLRQTII GQPMSVTITT KDKDGELCKT
     GNAYLTAELS TPDGSVADGE ILDNKNGTYE FLYTVQKEGD FTLSLRLYDQ HIRGSPFKLK
     VIRSADVSPT TEGVKRRVKS PGSGHVKQKA VKRPASMYST GKRKENPIED DLIFRVGTKG
     RNKGEFTNLQ GVAASTSGKI LIADSNNQCV QIFSNDGQFK SRFGIRGRSP GQLQRPTGVA
     VHPSGDIIIA DYDNKWVSIF SSDGKFKTKI GSGKLMGPKG VSVDRNGHII VVDNKACCVF
     IFQPNGKIVT RFGSRGNGDR QFAGPHFAAV NSNNEIIITD FHNHSVKVFN QEGEFMLKFG
     SNGEGNGQFN APTGVAVDSN GNIIVADWGN SRIQVFDGSG SFLSYINTSA DPLYGPQGLA
     LTSDGHVVVA DSGNHCFKVY RYLQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024