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Database: UniProt
Entry: M7AMM4_CHEMY
LinkDB: M7AMM4_CHEMY
Original site: M7AMM4_CHEMY 
ID   M7AMM4_CHEMY            Unreviewed;       875 AA.
AC   M7AMM4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN   ORFNames=UY3_16448 {ECO:0000313|EMBL:EMP26461.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP26461.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
CC   -!- FUNCTION: Component of the RNF20/40 E3 ubiquitin-protein ligase complex
CC       that mediates monoubiquitination of 'Lys-120' of histone H2B
CC       (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic
CC       transcriptional activation and is also prerequisite for histone H3
CC       'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It
CC       thereby plays a central role in histone code and gene regulation. The
CC       RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation
CC       with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with
CC       UBE2E1/UBCH are contradictory. Required for transcriptional activation
CC       of Hox genes. {ECO:0000256|ARBA:ARBA00037123}.
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|RuleBase:RU365038};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU365038}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU365038}.
CC   -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000256|ARBA:ARBA00005555,
CC       ECO:0000256|RuleBase:RU365038}.
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DR   EMBL; KB579331; EMP26461.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7AMM4; -.
DR   STRING; 8469.M7AMM4; -.
DR   eggNOG; KOG0978; Eukaryota.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000031443; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16815; RING-HC_RNF40; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR23163:SF4; E3 UBIQUITIN-PROTEIN LIGASE BRE1B; 1.
DR   PANTHER; PTHR23163; RING FINGER PROTEIN-RELATED; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW   ECO:0000256|RuleBase:RU365038};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU365038};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU365038}; Nucleus {ECO:0000256|RuleBase:RU365038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW   Transferase {ECO:0000256|RuleBase:RU365038};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU365038};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365038};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          822..861
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          206..367
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          431..514
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          772..799
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        117..141
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..564
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   875 AA;  100243 MW;  C47DE3D08F3C4491 CRC64;
     MSGPGSKRAA GDGGSGPPEK KANREEKTTT TLIEPIRLGG ISSTEEMDLK VLQFKNKKLA
     ERLEQRQAFE DELRERIEKL EKRQATDDAT LLIVNRYWSQ LDENVQVLLR GYDGDCEPPP
     PAAPAVPSAE EPRPEPTGPD PENTASPSTE GPDRTALSFL ATLASSSSEE IELQLQERME
     FSKAAVSRVV EVSNKIHRRT EELCQKIHAR ADLDQLDEAL KSLNKELMRE NQRLQDLAMQ
     LQEKHHKISL EYTELQDKVT SSETKVLEME TTVEDLQWDI EKLRKREQKL NKHLAEALEQ
     LNSGYYVSGS SGGFQGGQIT LSMQKFEMLN AELEENQELA NSRMAELEKL QQELQQAVRT
     NEKLKVTRWR AVPPGARFGG GTWLQSQFSL LYNESLQVKT QLDEARALLL TTKNSHLRHI
     EHMESDELNL QKKLRTEVIQ LEDTLAQVRK EYEMLRIEFE QNLAANEQAG PINREMRHLI
     SSLQNHNHQL KGDVQRYKRK LREVQAEINK IRMQSSGFPC GSAVLPPAPG PEELVGVVPA
     VAVKEEEGGT PSVEKSSDDP KKKDSDLLKQ LRIELKKAQE SQKEMKLLLD MYKSAPKEQR
     DKVQLMAAEK KTKAEVEELR GRVRELEEKE KKESKKMADE DALRKIKLAE EQIEHLQKKL
     AATKQEEEAL LSEMDVTGQA FEDMQEQNMR LMQQLREKDD ANFKLMSERI KSNQIHKLLR
     EEKDELADQV LALKSQAVEA AQLAEDLKVQ QEHVQCKLKE IQACMAENRA AKEKESFNLK
     RAQEDISRLR RKLEKQKKVE VYADADEILQ EEIKEYKAKL TCPCCNTRKK DAVLTKCFHV
     FCFDCVKTRY DTRQRKCPKC NAAFGANDFH RIYIS
//
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