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Protein

E3 ubiquitin-protein ligase BRE1B

Gene

Rnf40

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role in histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes (By similarity).By similarity

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri948 – 98740RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase BRE1B (EC:6.3.2.-)
Short name:
BRE1-B
Alternative name(s):
RING finger protein 40
Gene namesi
Name:Rnf40
Synonyms:Bre1b, Kiaa0661
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2142048. Rnf40.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10011001E3 ubiquitin-protein ligase BRE1BPRO_0000055841Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201N6-acetyllysineCombined sources
Modified residuei355 – 3551N6-acetyllysineBy similarity
Modified residuei517 – 5171N6-acetyllysineCombined sources
Modified residuei584 – 5841PhosphoserineCombined sources
Modified residuei585 – 5851PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ3U319.
MaxQBiQ3U319.
PaxDbiQ3U319.
PRIDEiQ3U319.

PTM databases

iPTMnetiQ3U319.
PhosphoSiteiQ3U319.

Expressioni

Gene expression databases

BgeeiQ3U319.
CleanExiMM_RNF40.
GenevisibleiQ3U319. MM.

Interactioni

Subunit structurei

Component of the RNF20/40 complex (also known as BRE1 complex) probably composed of 2 copies of RNF20/BRE1A and 2 copies of RNF40/BRE1B. Interacts with UBE2E1/UBCH6. Interacts with RB1 and WAC (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ3U319. 1 interaction.
MINTiMINT-4110865.
STRINGi10090.ENSMUSP00000033088.

Structurei

3D structure databases

ProteinModelPortaliQ3U319.
SMRiQ3U319. Positions 939-998.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili55 – 9137Sequence analysisAdd
BLAST
Coiled coili189 – 377189Sequence analysisAdd
BLAST
Coiled coili437 – 52589Sequence analysisAdd
BLAST
Coiled coili627 – 946320Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the BRE1 family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri948 – 98740RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG0978. Eukaryota.
ENOG410Y5C6. LUCA.
GeneTreeiENSGT00390000002866.
HOGENOMiHOG000231526.
HOVERGENiHBG080312.
InParanoidiQ3U319.
KOiK10696.
OMAiPNLGHPE.
OrthoDBiEOG7DVD99.
PhylomeDBiQ3U319.
TreeFamiTF323183.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3U319-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGLSNKRAA GDGGSGPPEK KMNREEKTTT TLIEPIRLGG ISSTEEMDSK
60 70 80 90 100
VLQFKNKKLA ERLEQRQACE DELRERIEKL EKRQATDDAT LLIVNRYWAQ
110 120 130 140 150
LDETVEALLQ CYENQRELSS GTEVPGCQEG LTRDVIPRPD PGTSDLREPL
160 170 180 190 200
PVQFRAPLSE PALAFVVALG ASSCEEVELQ LQGRMEFSKA AVSRVVEASD
210 220 230 240 250
RLQRQVEELC QRVYSRGDSE APGEVARVRT RELGRENRRL QDLATQLQEK
260 270 280 290 300
HHRISLEYSE LQDKVTSTET KVLEMETTVE DLQWDIEKLR KREQKLNKHL
310 320 330 340 350
AEALEQLNSG YYVSGSSTGF QGGQITLSMQ KFEMLNAELE ENQELANSRM
360 370 380 390 400
AELEKLQAEL QGAVRTNERL KVALRSLPEE VVRETGEYRM LQAQFSLLYN
410 420 430 440 450
ESLQVKTQLD EARGLLLASK NSHLRHIEHM ESDELGLQKK LRTEVIQLED
460 470 480 490 500
TLAQVRKEYE MLRIEFEQNL AANEQAGPIN REMRHLISSL QNHNHQLKGD
510 520 530 540 550
AQRYKRKLRE VQAEIGKLRA QASGSSHCIP TLSHPDDPGL NALAPGKEDS
560 570 580 590 600
GPGPGGTPDC KKEMALLAGA TSATSSIKKE ELVSSEDDAQ ALTPVTQGLP
610 620 630 640 650
SRGREPEARP KRELREREGP SLGPPPAAST LSRADREKAK VEEAKRKESE
660 670 680 690 700
LLKGLRAELK KAQESQKEMK LLLDMYKSAP KEQRDKVQLM AAERKAKAEV
710 720 730 740 750
DELRSRIREL EERDRRESKK IADEDALRRI RQAEEQIEHL QRKLGATKQE
760 770 780 790 800
EEALLSEMDV TGQAFEDMQE QNGRLLQQLR EKDDANFKLM SERIKANQIH
810 820 830 840 850
KLLREEKDEL GEQVLGLKSQ VDAQLLTVQK LEEKERALQG SLGGVEKELT
860 870 880 890 900
LRSQALELNK RKAVEAAQLA EDLKVQLEHV QTRLREIQPC LAESRAAREK
910 920 930 940 950
ESFNLKRAQE DISRLRRKLE KQRKVEVYAD ADEILQEEIK EYKARLTCPC
960 970 980 990 1000
CNTRKKDAVL TKCFHVFCFE CVRGRYEARQ RKCPKCNAAF GAHDFHRVYI

S
Length:1,001
Mass (Da):113,967
Last modified:December 20, 2005 - v2
Checksum:iF4368B7CA414BF01
GO

Sequence cautioni

The sequence BAC97994.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti385 – 3851T → A in BAE32971 (PubMed:16141072).Curated
Sequence conflicti493 – 4931H → Y in AAH38348 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129184 mRNA. Translation: BAC97994.1. Different initiation.
AK042654 mRNA. Translation: BAC31322.1.
AK089805 mRNA. Translation: BAC40966.1.
AK154982 mRNA. Translation: BAE32971.1.
AK171462 mRNA. Translation: BAE42468.1.
BC038348 mRNA. Translation: AAH38348.1.
CCDSiCCDS21871.1.
RefSeqiNP_758485.2. NM_172281.2.
UniGeneiMm.41122.

Genome annotation databases

EnsembliENSMUST00000205694; ENSMUSP00000146310; ENSMUSG00000030816.
GeneIDi233900.
KEGGimmu:233900.
UCSCiuc009jwe.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129184 mRNA. Translation: BAC97994.1. Different initiation.
AK042654 mRNA. Translation: BAC31322.1.
AK089805 mRNA. Translation: BAC40966.1.
AK154982 mRNA. Translation: BAE32971.1.
AK171462 mRNA. Translation: BAE42468.1.
BC038348 mRNA. Translation: AAH38348.1.
CCDSiCCDS21871.1.
RefSeqiNP_758485.2. NM_172281.2.
UniGeneiMm.41122.

3D structure databases

ProteinModelPortaliQ3U319.
SMRiQ3U319. Positions 939-998.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ3U319. 1 interaction.
MINTiMINT-4110865.
STRINGi10090.ENSMUSP00000033088.

PTM databases

iPTMnetiQ3U319.
PhosphoSiteiQ3U319.

Proteomic databases

EPDiQ3U319.
MaxQBiQ3U319.
PaxDbiQ3U319.
PRIDEiQ3U319.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000205694; ENSMUSP00000146310; ENSMUSG00000030816.
GeneIDi233900.
KEGGimmu:233900.
UCSCiuc009jwe.2. mouse.

Organism-specific databases

CTDi9810.
MGIiMGI:2142048. Rnf40.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0978. Eukaryota.
ENOG410Y5C6. LUCA.
GeneTreeiENSGT00390000002866.
HOGENOMiHOG000231526.
HOVERGENiHBG080312.
InParanoidiQ3U319.
KOiK10696.
OMAiPNLGHPE.
OrthoDBiEOG7DVD99.
PhylomeDBiQ3U319.
TreeFamiTF323183.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiQ3U319.
SOURCEiSearch...

Gene expression databases

BgeeiQ3U319.
CleanExiMM_RNF40.
GenevisibleiQ3U319. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic tail.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Cerebellum and Spleen.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Salivary gland.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-584 AND SER-585, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-20 AND LYS-517, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiBRE1B_MOUSE
AccessioniPrimary (citable) accession number: Q3U319
Secondary accession number(s): Q6ZQ75
, Q8BJA1, Q8BY03, Q8CHX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: June 8, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.