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Protein

E3 ubiquitin-protein ligase BRE1B

Gene

RNF40

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.2 Publications

Pathwayi

Regions

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

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. mRNA 3'-UTR binding Source: UniProtKB
  3. protein homodimerization activity Source: UniProtKB
  4. ubiquitin protein ligase binding Source: UniProtKB
  5. ubiquitin-protein transferase activity Source: Ensembl
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. histone H2B ubiquitination Source: UniProtKB
  2. histone monoubiquitination Source: UniProtKB
  3. negative regulation of mRNA polyadenylation Source: UniProtKB
  4. positive regulation of histone H2B ubiquitination Source: UniProtKB
  5. ubiquitin-dependent protein catabolic process Source: UniProtKB
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):
95 kDa retinoblastoma-associated protein
Short name:
RBP95
RING finger protein 40
Gene namesi
Name:RNF40
Synonyms:BRE1B, KIAA0661
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:16867. RNF40.

Subcellular locationi

  1. Nucleus 1 Publication

GO - Cellular componenti

  1. HULC complex Source: UniProtKB
  2. membrane Source: UniProtKB
  3. neuron projection Source: UniProtKB
  4. nucleoplasm Source: HPA
  5. nucleus Source: UniProtKB
  6. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi109 – 1091L → S: Abolishes interaction with RB1. 1 Publication
Mutagenesisi111 – 1111C → M: Abolishes interaction with RB1. 1 Publication
Mutagenesisi113 – 1131E → Q: Abolishes interaction with RB1. 1 Publication

Organism-specific databases

PharmGKBiPA34440.

Polymorphism and mutation databases

BioMutaiRNF40.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10011001E3 ubiquitin-protein ligase BRE1BPRO_0000055839Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201N6-acetyllysineBy similarity
Modified residuei517 – 5171N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO75150.
PaxDbiO75150.
PRIDEiO75150.

PTM databases

PhosphoSiteiO75150.

Expressioni

Tissue specificityi

Ubiquitously expressed. Expressed at higher level in testis, heart and pancreas, while it is only weakly expressed in lung, skeletal muscle and small intestine.1 Publication

Gene expression databases

BgeeiO75150.
CleanExiHS_RNF40.
ExpressionAtlasiO75150. baseline and differential.
GenevestigatoriO75150.

Organism-specific databases

HPAiHPA041330.
HPA054227.

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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AMOTL2Q9Y2J4-43EBI-744408,EBI-10187270
CCDC146Q8IYE0-23EBI-744408,EBI-10247802
HTTP428583EBI-744408,EBI-466029
RB1P064003EBI-744408,EBI-491274
RNF20Q5VTR210EBI-744408,EBI-2372238
SFR1Q86XK33EBI-744408,EBI-1104535
UBE2IQ7KZS03EBI-744408,EBI-10180829

Protein-protein interaction databases

BioGridi115149. 48 interactions.
IntActiO75150. 17 interactions.
MINTiMINT-1466706.
STRINGi9606.ENSP00000325677.

Structurei

3D structure databases

ProteinModelPortaliO75150.
SMRiO75150. Positions 938-998.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili44 – 9148Sequence 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

eggNOGiNOG263074.
HOVERGENiHBG080312.
InParanoidiO75150.
KOiK10696.
OMAiHHESQGE.
OrthoDBiEOG7DVD99.
PhylomeDBiO75150.
TreeFamiTF323183.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75150-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSGPGNKRAA GDGGSGPPEK KLSREEKTTT TLIEPIRLGG ISSTEEMDLK
60 70 80 90 100
VLQFKNKKLA ERLEQRQACE DELRERIEKL EKRQATDDAT LLIVNRYWAQ
110 120 130 140 150
LDETVEALLR CHESQGELSS APEAPGTQEG PTCDGTPLPE PGTSELRDPL
160 170 180 190 200
LMQLRPPLSE PALAFVVALG ASSSEEVELE LQGRMEFSKA AVSRVVEASD
210 220 230 240 250
RLQRRVEELC QRVYSRGDSE PLSEAAQAHT RELGRENRRL QDLATQLQEK
260 270 280 290 300
HHRISLEYSE LQDKVTSAET KVLEMETTVE DLQWDIEKLR KREQKLNKHL
310 320 330 340 350
AEALEQLNSG YYVSGSSSGF QGGQITLSMQ KFEMLNAELE ENQELANSRM
360 370 380 390 400
AELEKLQAEL QGAVRTNERL KVALRSLPEE VVRETGEYRM LQAQFSLLYN
410 420 430 440 450
ESLQVKTQLD EARGLLLATK NSHLRHIEHM ESDELGLQKK LRTEVIQLED
460 470 480 490 500
TLAQVRKEYE MLRIEFEQNL AANEQAGPIN REMRHLISSL QNHNHQLKGD
510 520 530 540 550
AQRYKRKLRE VQAEIGKLRA QASGSAHSTP NLGHPEDSGV SAPAPGKEEG
560 570 580 590 600
GPGPVSTPDN RKEMAPVPGT TTTTTSVKKE ELVPSEEDFQ GITPGAQGPS
610 620 630 640 650
SRGREPEARP KRELQEREGP SLGPPPVASA LSRADREKAK VEETKRKESE
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 GAHDFHRIYI

S
Length:1,001
Mass (Da):113,650
Last modified:November 30, 2010 - v4
Checksum:i82D7CD183EDD5EFC
GO
Isoform 3 (identifier: O75150-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     822-838: DAQLLTVQKLEEKERAL → WPPPACRLELERWGSWP
     839-1001: Missing.

Note: No experimental confirmation available.

Show »
Length:838
Mass (Da):94,796
Checksum:i87B68E08B358A730
GO
Isoform 4 (identifier: O75150-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     332-431: Missing.

Note: No experimental confirmation available.

Show »
Length:901
Mass (Da):102,046
Checksum:i445DD31CF7511205
GO

Sequence cautioni

The sequence BAA31636.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAE45869.1 differs from that shown.Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561N → D in BAB55092 (PubMed:14702039).Curated
Sequence conflicti96 – 961R → L in AAG13723 (PubMed:10944455).Curated
Sequence conflicti108 – 1081L → P in BAB55092 (PubMed:14702039).Curated
Sequence conflicti172 – 1721S → G in BAB55092 (PubMed:14702039).Curated
Sequence conflicti387 – 3871E → K in CAH10518 (PubMed:17974005).Curated
Sequence conflicti562 – 5621K → E in CAE45869 (PubMed:17974005).Curated
Sequence conflicti600 – 6001S → F in CAE45869 (PubMed:17974005).Curated
Sequence conflicti714 – 7141D → N in BAB55092 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti463 – 4631R → H.
Corresponds to variant rs11556801 [ dbSNP | Ensembl ].
VAR_055021
Natural varianti615 – 6151Q → R.5 Publications
Corresponds to variant rs7195142 [ dbSNP | Ensembl ].
VAR_055022

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei332 – 431100Missing in isoform 4. 1 PublicationVSP_016681Add
BLAST
Alternative sequencei822 – 83817DAQLL…KERAL → WPPPACRLELERWGSWP in isoform 3. 1 PublicationVSP_016682Add
BLAST
Alternative sequencei839 – 1001163Missing in isoform 3. 1 PublicationVSP_016683Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF122819 mRNA. Translation: AAG13723.1.
AB014561 mRNA. Translation: BAA31636.2. Different initiation.
AK027406 mRNA. Translation: BAB55092.1.
BX640763 mRNA. Translation: CAE45869.1. Sequence problems.
CR627431 mRNA. Translation: CAH10518.1.
AC106886 Genomic DNA. No translation available.
BC004527 mRNA. Translation: AAH04527.2.
BC006133 mRNA. Translation: AAH06133.1.
BC011769 mRNA. Translation: AAH11769.1.
BC018647 mRNA. Translation: AAH18647.1.
BC030802 mRNA. Translation: AAH30802.2.
CCDSiCCDS10691.1. [O75150-1]
CCDS55994.1. [O75150-4]
PIRiJC7363.
RefSeqiNP_001193962.1. NM_001207033.1.
NP_001193963.1. NM_001207034.1.
NP_001273501.1. NM_001286572.2.
NP_055586.1. NM_014771.3.
UniGeneiHs.65238.

Genome annotation databases

EnsembliENST00000324685; ENSP00000325677; ENSG00000103549.
ENST00000357890; ENSP00000350563; ENSG00000103549.
GeneIDi9810.
KEGGihsa:9810.
UCSCiuc002dzq.3. human. [O75150-1]
uc010cab.3. human. [O75150-4]

Polymorphism and mutation databases

BioMutaiRNF40.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF122819 mRNA. Translation: AAG13723.1.
AB014561 mRNA. Translation: BAA31636.2. Different initiation.
AK027406 mRNA. Translation: BAB55092.1.
BX640763 mRNA. Translation: CAE45869.1. Sequence problems.
CR627431 mRNA. Translation: CAH10518.1.
AC106886 Genomic DNA. No translation available.
BC004527 mRNA. Translation: AAH04527.2.
BC006133 mRNA. Translation: AAH06133.1.
BC011769 mRNA. Translation: AAH11769.1.
BC018647 mRNA. Translation: AAH18647.1.
BC030802 mRNA. Translation: AAH30802.2.
CCDSiCCDS10691.1. [O75150-1]
CCDS55994.1. [O75150-4]
PIRiJC7363.
RefSeqiNP_001193962.1. NM_001207033.1.
NP_001193963.1. NM_001207034.1.
NP_001273501.1. NM_001286572.2.
NP_055586.1. NM_014771.3.
UniGeneiHs.65238.

3D structure databases

ProteinModelPortaliO75150.
SMRiO75150. Positions 938-998.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115149. 48 interactions.
IntActiO75150. 17 interactions.
MINTiMINT-1466706.
STRINGi9606.ENSP00000325677.

PTM databases

PhosphoSiteiO75150.

Polymorphism and mutation databases

BioMutaiRNF40.

Proteomic databases

MaxQBiO75150.
PaxDbiO75150.
PRIDEiO75150.

Protocols and materials databases

DNASUi9810.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000324685; ENSP00000325677; ENSG00000103549.
ENST00000357890; ENSP00000350563; ENSG00000103549.
GeneIDi9810.
KEGGihsa:9810.
UCSCiuc002dzq.3. human. [O75150-1]
uc010cab.3. human. [O75150-4]

Organism-specific databases

CTDi9810.
GeneCardsiGC16P030775.
HGNCiHGNC:16867. RNF40.
HPAiHPA041330.
HPA054227.
MIMi607700. gene.
neXtProtiNX_O75150.
PharmGKBiPA34440.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG263074.
HOVERGENiHBG080312.
InParanoidiO75150.
KOiK10696.
OMAiHHESQGE.
OrthoDBiEOG7DVD99.
PhylomeDBiO75150.
TreeFamiTF323183.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiRNF40. human.
GeneWikiiRNF40.
GenomeRNAii9810.
NextBioi36932.
PROiO75150.
SOURCEiSearch...

Gene expression databases

BgeeiO75150.
CleanExiHS_RNF40.
ExpressionAtlasiO75150. baseline and differential.
GenevestigatoriO75150.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "RBP95, a novel leucine zipper protein, binds to the retinoblastoma protein."
    Wen H., Ao S.
    Biochem. Biophys. Res. Commun. 275:141-148(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT, INTERACTION WITH RB1, MUTAGENESIS OF LEU-109; CYS-111 AND GLU-113, VARIANT ARG-615.
    Tissue: Fetal brain.
  2. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-615.
    Tissue: Brain.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT ARG-615.
    Tissue: Teratocarcinoma.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-615.
    Tissue: Cervix and Rectum tumor.
  5. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1), VARIANT ARG-615.
    Tissue: Brain, Mammary gland, Skin and Uterus.
  7. "Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation."
    Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P., Reinberg D.
    Mol. Cell 20:601-611(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH RNF20 AND UBE2E1.
  8. "RAD6-mediated transcription-coupled H2B ubiquitylation directly stimulates H3K4 methylation in human cells."
    Kim J., Guermah M., McGinty R.K., Lee J.S., Tang Z., Milne T.A., Shilatifard A., Muir T.W., Roeder R.G.
    Cell 137:459-471(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "WAC, a functional partner of RNF20/40, regulates histone H2B ubiquitination and gene transcription."
    Zhang F., Yu X.
    Mol. Cell 41:384-397(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WAC.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiBRE1B_HUMAN
AccessioniPrimary (citable) accession number: O75150
Secondary accession number(s): Q6AHZ6
, Q6N005, Q7L3T6, Q8N615, Q96T18, Q9BSV9, Q9HC82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: November 30, 2010
Last modified: April 29, 2015
This is version 126 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.