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MKRN2_DANRE
ID   MKRN2_DANRE             Reviewed;         414 AA.
AC   Q9DFG8; Q6P0Z6;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=E3 ubiquitin-protein ligase makorin-2;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9ERV1};
DE   AltName: Full=RING-type E3 ubiquitin transferase makorin-2 {ECO:0000305};
GN   Name=mkrn2;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11597136; DOI=10.1006/geno.2001.6627;
RA   Gray T.A., Azama K., Whitmore K., Min A., Abe S., Nicholls R.D.;
RT   "Phylogenetic conservation of the makorin-2 gene, encoding a multiple zinc-
RT   finger protein, antisense to the raf1 proto-oncogene.";
RL   Genomics 77:119-126(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of
CC       ubiquitin moieties onto substrate proteins (By similarity). Inhibits
CC       neurogenesis and axis formation during embryonic development by
CC       modulating the phosphatidylinositol 3-kinase (PI3K) pathway (By
CC       similarity). Acts downstream of PI3K and akt1 to up-regulate gsk3b mRNA
CC       expression (By similarity). {ECO:0000250|UniProtKB:B0F0H3,
CC       ECO:0000250|UniProtKB:Q9ERV1}.
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:0000250|UniProtKB:Q9ERV1};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ERV1}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9ERV1}.
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DR   EMBL; AF277172; AAG27597.1; -; mRNA.
DR   EMBL; BC065352; AAH65352.1; -; mRNA.
DR   RefSeq; NP_694511.1; NM_152979.2.
DR   RefSeq; XP_005155725.1; XM_005155668.3.
DR   AlphaFoldDB; Q9DFG8; -.
DR   STRING; 7955.ENSDARP00000016210; -.
DR   PaxDb; Q9DFG8; -.
DR   GeneID; 170783; -.
DR   KEGG; dre:170783; -.
DR   CTD; 23609; -.
DR   ZFIN; ZDB-GENE-020213-2; mkrn2.
DR   eggNOG; KOG1039; Eukaryota.
DR   InParanoid; Q9DFG8; -.
DR   OrthoDB; 1388677at2759; -.
DR   PhylomeDB; Q9DFG8; -.
DR   TreeFam; TF315108; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9DFG8; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0030274; F:LIM domain binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; ISS:UniProtKB.
DR   GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:1901485; P:positive regulation of transcription factor catabolic process; ISS:UniProtKB.
DR   GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0006351; P:transcription, DNA-templated; ISS:UniProtKB.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR026293; Makorin_2.
DR   InterPro; IPR045072; MKRN-like.
DR   InterPro; IPR041367; Znf-CCCH_4.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11224; PTHR11224; 1.
DR   PANTHER; PTHR11224:SF17; PTHR11224:SF17; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   Pfam; PF18044; zf-CCCH_4; 2.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 4.
DR   SUPFAM; SSF90229; SSF90229; 3.
DR   PROSITE; PS50103; ZF_C3H1; 4.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Developmental protein; Differentiation; Metal-binding;
KW   Neurogenesis; Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..414
FT                   /note="E3 ubiquitin-protein ligase makorin-2"
FT                   /id="PRO_0000055957"
FT   ZN_FING         2..29
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         31..58
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         164..191
FT                   /note="C3H1-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         237..291
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         320..349
FT                   /note="C3H1-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          57..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..221
FT                   /note="Makorin-type Cys-His"
FT   CONFLICT        89
FT                   /note="N -> H (in Ref. 2; AAH65352)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="N -> S (in Ref. 1; AAG27597)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155
FT                   /note="T -> A (in Ref. 2; AAH65352)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   414 AA;  46480 MW;  8D4BB66047A3B3D6 CRC64;
     MSTKQVTCRY FLHGVCREGS RCLFSHDLTT SKPSTICKYY QRGACAYGDR CRYDHIKPPG
     RGSGAPADHS NRSSSSAGAS APGPGPPANT SKHLKKPLVL RDKALCSDSR PRVFSAESSE
     LNECWEQRDD GAQKPHSYLE AIRSGLDASA AAAATAGTFP ELQQTSPQIC PFLAAGQCQY
     GESCPYLHGE MCEICRQHVL HPHDPEQRAA HEKKCMVAFE MDMERAFAVQ QSQDKVCKIC
     LDVVYEKSSP SERRFGILSS CAHTYCLNCI RQWRCVEQLH NQIRKSCPEC RVVSEFVIPS
     IYWVEDQEQK NLLIEEFKSG VSKKACKYFD QGRGTCPFGG KCFYMHAYAD GRRAEPDKPR
     KQLSAEGNVR FQNSVRLWDF IEEREHRSVP QLEDEVNDLG ELFMQLSGAS DAPH
 
 
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