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O75150

- BRE1B_HUMAN

UniProt

O75150 - BRE1B_HUMAN

Protein

E3 ubiquitin-protein ligase BRE1B

Gene

RNF40

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 4 (30 Nov 2010)
      Previous versions | rss
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    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. protein 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. ubiquitin-dependent protein catabolic process Source: UniProtKB

    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: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:16867. RNF40.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. HULC complex Source: UniProtKB
    2. membrane Source: UniProtKB
    3. neuron projection Source: UniProtKB
    4. nucleus Source: UniProtKB
    5. ubiquitin ligase complex Source: UniProtKB

    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.

    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

    ArrayExpressiO75150.
    BgeeiO75150.
    CleanExiHS_RNF40.
    GenevestigatoriO75150.

    Organism-specific databases

    HPAiHPA041330.

    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
    HTTP428583EBI-744408,EBI-466029
    RB1P064003EBI-744408,EBI-491274
    RNF20Q5VTR210EBI-744408,EBI-2372238

    Protein-protein interaction databases

    BioGridi115149. 44 interactions.
    IntActiO75150. 13 interactions.
    MINTiMINT-1466706.
    STRINGi9606.ENSP00000325677.

    Structurei

    3D structure databases

    ProteinModelPortaliO75150.
    SMRiO75150. Positions 943-993.
    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.
    OMAiYSELQDK.
    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. Align

    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

    MSGPGNKRAA GDGGSGPPEK KLSREEKTTT TLIEPIRLGG ISSTEEMDLK     50
    VLQFKNKKLA ERLEQRQACE DELRERIEKL EKRQATDDAT LLIVNRYWAQ 100
    LDETVEALLR CHESQGELSS APEAPGTQEG PTCDGTPLPE PGTSELRDPL 150
    LMQLRPPLSE PALAFVVALG ASSSEEVELE LQGRMEFSKA AVSRVVEASD 200
    RLQRRVEELC QRVYSRGDSE PLSEAAQAHT RELGRENRRL QDLATQLQEK 250
    HHRISLEYSE LQDKVTSAET KVLEMETTVE DLQWDIEKLR KREQKLNKHL 300
    AEALEQLNSG YYVSGSSSGF QGGQITLSMQ KFEMLNAELE ENQELANSRM 350
    AELEKLQAEL QGAVRTNERL KVALRSLPEE VVRETGEYRM LQAQFSLLYN 400
    ESLQVKTQLD EARGLLLATK NSHLRHIEHM ESDELGLQKK LRTEVIQLED 450
    TLAQVRKEYE MLRIEFEQNL AANEQAGPIN REMRHLISSL QNHNHQLKGD 500
    AQRYKRKLRE VQAEIGKLRA QASGSAHSTP NLGHPEDSGV SAPAPGKEEG 550
    GPGPVSTPDN RKEMAPVPGT TTTTTSVKKE ELVPSEEDFQ GITPGAQGPS 600
    SRGREPEARP KRELQEREGP SLGPPPVASA LSRADREKAK VEETKRKESE 650
    LLKGLRAELK KAQESQKEMK LLLDMYKSAP KEQRDKVQLM AAERKAKAEV 700
    DELRSRIREL EERDRRESKK IADEDALRRI RQAEEQIEHL QRKLGATKQE 750
    EEALLSEMDV TGQAFEDMQE QNGRLLQQLR EKDDANFKLM SERIKANQIH 800
    KLLREEKDEL GEQVLGLKSQ VDAQLLTVQK LEEKERALQG SLGGVEKELT 850
    LRSQALELNK RKAVEAAQLA EDLKVQLEHV QTRLREIQPC LAESRAAREK 900
    ESFNLKRAQE DISRLRRKLE KQRKVEVYAD ADEILQEEIK EYKARLTCPC 950
    CNTRKKDAVL TKCFHVFCFE CVRGRYEARQ RKCPKCNAAF GAHDFHRIYI 1000
    S 1001
    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 CAE45869.1 differs from that shown. Reason: Aberrant splicing.
    The sequence BAA31636.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    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:
    EMBL
    GenBank
    DDBJ
    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. [O75150-1]
    ENST00000357890; ENSP00000350563; ENSG00000103549. [O75150-4]
    GeneIDi9810.
    KEGGihsa:9810.
    UCSCiuc002dzq.3. human. [O75150-1]
    uc010cab.3. human. [O75150-4]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS10691.1. [O75150-1 ]
    CCDS55994.1. [O75150-4 ]
    PIRi JC7363.
    RefSeqi NP_001193962.1. NM_001207033.1.
    NP_001193963.1. NM_001207034.1.
    NP_001273501.1. NM_001286572.2.
    NP_055586.1. NM_014771.3.
    UniGenei Hs.65238.

    3D structure databases

    ProteinModelPortali O75150.
    SMRi O75150. Positions 943-993.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115149. 44 interactions.
    IntActi O75150. 13 interactions.
    MINTi MINT-1466706.
    STRINGi 9606.ENSP00000325677.

    PTM databases

    PhosphoSitei O75150.

    Proteomic databases

    MaxQBi O75150.
    PaxDbi O75150.
    PRIDEi O75150.

    Protocols and materials databases

    DNASUi 9810.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000324685 ; ENSP00000325677 ; ENSG00000103549 . [O75150-1 ]
    ENST00000357890 ; ENSP00000350563 ; ENSG00000103549 . [O75150-4 ]
    GeneIDi 9810.
    KEGGi hsa:9810.
    UCSCi uc002dzq.3. human. [O75150-1 ]
    uc010cab.3. human. [O75150-4 ]

    Organism-specific databases

    CTDi 9810.
    GeneCardsi GC16P030775.
    HGNCi HGNC:16867. RNF40.
    HPAi HPA041330.
    MIMi 607700. gene.
    neXtProti NX_O75150.
    PharmGKBi PA34440.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG263074.
    HOVERGENi HBG080312.
    InParanoidi O75150.
    KOi K10696.
    OMAi YSELQDK.
    OrthoDBi EOG7DVD99.
    PhylomeDBi O75150.
    TreeFami TF323183.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    GeneWikii RNF40.
    GenomeRNAii 9810.
    NextBioi 36932.
    PROi O75150.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75150.
    Bgeei O75150.
    CleanExi HS_RNF40.
    Genevestigatori O75150.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF00097. zf-C3HC4. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 119 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