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
//