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P97868

- RBBP6_MOUSE

UniProt

P97868 - RBBP6_MOUSE

Protein

E3 ubiquitin-protein ligase RBBP6

Gene

Rbbp6

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 5 (16 May 2006)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase which promotes ubiquitination of YBX1, leading to its degradation by the proteasome By similarity. May play a role as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in increase of MDM2-mediated ubiquitination and degradation of p53/TP53; may function as negative regulator of p53/TP53, leading to both apoptosis and cell growth retardation.By similarity1 Publication

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri160 – 17718CCHC-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri260 – 30142RING-type; degeneratePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. nucleic acid binding Source: InterPro
    3. ubiquitin-protein transferase activity Source: UniProtKB
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. embryonic organ development Source: MGI
    2. in utero embryonic development Source: MGI
    3. multicellular organism growth Source: MGI
    4. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
    5. somite development Source: MGI

    Keywords - Molecular functioni

    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 RBBP6 (EC:6.3.2.-)
    Alternative name(s):
    Proliferation potential-related protein
    Protein P2P-R
    Retinoblastoma-binding protein 6
    p53-associated cellular protein of testis
    Gene namesi
    Name:Rbbp6
    Synonyms:P2pr, Pact
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:894835. Rbbp6.

    Subcellular locationi

    Nucleusnucleolus. Chromosome. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
    Note: Colocalizes with mitotic chromosomes. Co-localizes with NEK6 in the centrosome By similarity.By similarity

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. cytoplasm Source: UniProtKB-KW
    3. microtubule organizing center Source: UniProtKB-SubCell
    4. nucleolus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Early embryonic lethality before E7.5, accompanied by accumulation of p53 and widespread apoptosis.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17901790E3 ubiquitin-protein ligase RBBP6PRO_0000234355Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei130 – 1301N6-acetyllysine1 Publication
    Modified residuei245 – 2451PhosphoserineBy similarity
    Modified residuei246 – 2461PhosphoserineBy similarity
    Modified residuei247 – 2471PhosphoserineBy similarity
    Modified residuei248 – 2481PhosphoserineBy similarity
    Modified residuei361 – 3611PhosphoserineBy similarity
    Modified residuei517 – 5171PhosphoserineBy similarity
    Modified residuei771 – 7711PhosphoserineBy similarity
    Modified residuei773 – 7731PhosphoserineBy similarity
    Modified residuei781 – 7811PhosphoserineBy similarity
    Modified residuei862 – 8621PhosphoserineBy similarity
    Modified residuei985 – 9851Phosphothreonine1 Publication
    Modified residuei1179 – 11791Phosphoserine2 Publications
    Modified residuei1272 – 12721Phosphothreonine1 Publication
    Modified residuei1278 – 12781PhosphoserineBy similarity
    Modified residuei1329 – 13291Phosphoserine2 Publications
    Modified residuei1469 – 14691PhosphothreonineBy similarity
    Modified residuei1646 – 16461PhosphoserineBy similarity
    Modified residuei1648 – 16481PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by NEK6.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP97868.
    PaxDbiP97868.
    PRIDEiP97868.

    PTM databases

    PhosphoSiteiP97868.

    Expressioni

    Tissue specificityi

    Highly expressed in testis. Expressed at lower levels in brain, heart, kidney, liver, lung, skeletal muscle, spleen, thymus and tongue.2 Publications

    Developmental stagei

    Expression is reduced during terminal differentiation. Expression is induced in the G2/M phase of the cell cycle (at protein level).2 Publications

    Gene expression databases

    ArrayExpressiP97868.
    BgeeiP97868.
    CleanExiMM_RBBP6.
    GenevestigatoriP97868.

    Interactioni

    Subunit structurei

    Interacts with MDM2 and YBX1 By similarity. Interacts also with p53/TP53 and RB1. Interacts with NEK6 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi202817. 1 interaction.
    IntActiP97868. 1 interaction.
    MINTiMINT-4106375.
    STRINGi10090.ENSMUSP00000049528.

    Structurei

    3D structure databases

    ProteinModelPortaliP97868.
    SMRiP97868. Positions 1-81, 160-207, 250-336.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 7673DWNNPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni983 – 1139157Interaction with RB1Add
    BLAST
    Regioni1434 – 1544111Interaction with p53Add
    BLAST

    Sequence similaritiesi

    Contains 1 CCHC-type zinc finger.PROSITE-ProRule annotation
    Contains 1 DWNN domain.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri160 – 17718CCHC-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri260 – 30142RING-type; degeneratePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5222.
    GeneTreeiENSGT00610000086096.
    HOVERGENiHBG093889.
    InParanoidiP97868.
    KOiK10624.
    OMAiEREYFNR.
    OrthoDBiEOG74BJR8.
    PhylomeDBiP97868.
    TreeFamiTF350543.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    4.10.60.10. 1 hit.
    InterProiIPR014891. DWNN_domain.
    IPR001878. Znf_CCHC.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF08783. DWNN. 1 hit.
    PF00098. zf-CCHC. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    SM00343. ZnF_C2HC. 1 hit.
    [Graphical view]
    SUPFAMiSSF57756. SSF57756. 1 hit.
    PROSITEiPS51282. DWNN. 1 hit.
    PS50158. ZF_CCHC. 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: P97868-1) [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

    MSCVHYKFSS KLNYDTVTFD GLHISLCDLK KQIMGREKLK AADSDLQITN     50
    AQTKEEYTDD NALIPKNSSV IVRRIPIGGV KSTSKTYVIS RTEPVMGTTK 100
    AIDDASASIS LAQLTKTANL AEANASEEDK IKAMMSQSGH EYDPINYMKK 150
    TLVGPPPPSY TCFRCGKPGH YIKNCPTNGD KNFESGPRIK KSTGIPRSFM 200
    MEVKDPNMKG AMLTNTGKYA IPTIDAEAYA IGKKEKPPFL PEEPSSSSEE 250
    DDPIPDELLC LICKDIMTDA VVIPCCGNSY CDECIRTALL ESDEHTCPTC 300
    HQNDVSPDAL IANKFLRQAV NNFKNETGYT KRLRKQLPPP PPPVPPPRPL 350
    MQRNLQPLMR SPISRQQDPL MIPVTSSSAH SAPSISSLTS NPSALAPSVS 400
    GNPSSAPAPV PDITATVSIS VHSEKSDGPF RDSDNKLLPA AALTSEHSKG 450
    ASSIAITALM EEKGYQVPVL GTPSLLGQSL LHGQLIPTTG PVRINAARPG 500
    GGRPGWEHSN KLGYLVSPPQ QIRRGERSCY RSINRGRHHS ERSQRTQGPS 550
    LPATPVFVPV PPPPLYPPPP HTLPLPPGVP PPQFSPQFPP GQPPPAGYSV 600
    PPPGFPPAPA NISTPWVSSG VQTAHSNTIP TTQAPPLSRE EFYREQRRLK 650
    EEEKKKSKLD EFTNDFAKEL MEYKKIQKER RRSFSRSKSP YSGSSYSRSS 700
    YTYSKSRSGS TRSRSYSRSF SRSHSRSYSR SPPYPRRGRG KSRNYRSRSR 750
    SHGYHRSRSR SPPYRRYHSR SRSPQAFRGQ SPTKRNVPQG ETEREYFNRY 800
    REVPPPYDIK AYYGRSVDFR DPFEKERYRE WERKYREWYE KYYKGYAVGA 850
    QPRPSANRED FSPERLLPLN IRNSPFTRGR REDYAAGQSH RNRNLGGNYP 900
    EKLSTRDSHN AKDNPKSKEK ESENVPGDGK GNKHKKHRKR RKGEESESFL 950
    NPELLETSRK CRESSGIDET KTDTLFVLPS RDDATPVRDE PMDAESITFK 1000
    SVSDKDKREK DKPKVKSDKT KRKSDGSATA KKDNVLKPSK GPQEKVDGDR 1050
    EKSPRSEPPL KKAKEEATKI DSVKPSSSSQ KDEKVTGTPR KAHSKSAKEH 1100
    QEAKPAKDEK VKKDCSKDIK SEKPASKDEK AKKPEKNKLL DSKGEKRKRK 1150
    TEEKSVDKDF ESSSMKISKV EGTEIVKPSP KRKMEGDVEK LERTPEKDKI 1200
    ASSTTPAKKI KLNRETGKKI GNAENASTTK EPSEKLESTS SKIKQEKVKG 1250
    KAKRKVAGSE GSSSTLVDYT STSSTGGSPV RKSEEKTDTK RTVIKTMEEY 1300
    NNDNTAPAED VIIMIQVPQS KWDKDDFESE EEDVKTTQPI QSVGKPSSII 1350
    KNVTTKPSAT AKYTEKESEQ PEKLQKLPKE ASHELMQHEL RSSKGSASSE 1400
    KGRAKDREHS GSEKDNPDKR KSGAQPDKES TVDRLSEQGH FKTLSQSSKE 1450
    TRTSEKHESV RGSSNKDFTP GRDKKVDYDS RDYSSSKRRD ERGELARRKD 1500
    SPPRGKESLS GQKSKLREER DLPKKGAESK KSNSSPPRDK KPHDHKAPYE 1550
    TKRPCEETKP VDKNSGKERE KHAAEARNGK ESSGGKLPCI PNPPDPPMEK 1600
    ELAAGQVEKS AVKPKPQLSH SSRLSSDLTR ETDEAAFEPD YNESDSESNV 1650
    SVKEEEAVAS ISKDLKEKTT EKAKESLTVA TASQPGADRS QSQSSPSVSP 1700
    SRSHSPSGSQ TRSHSSSASS AGSQDSKKKK KKKEKKKHKK HKKHKKHKKH 1750
    AGADGDVEKS QKHKHKKKKA KKNKDKEKEK DDQKVRSVTV 1790
    Length:1,790
    Mass (Da):199,587
    Last modified:May 16, 2006 - v5
    Checksum:i3909C30EB9DD2CE3
    GO
    Isoform 2 (identifier: P97868-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         653-686: Missing.

    Show »
    Length:1,756
    Mass (Da):195,310
    Checksum:iE3C0F009CC28107E
    GO
    Isoform 3 (identifier: P97868-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         102-123: IDDASASISLAQLTKTANLAEA → VCKNTITLFLHNCFYLYNVSVT
         124-1756: Missing.

    Show »
    Length:157
    Mass (Da):17,888
    Checksum:i39B749141C9B2FA6
    GO

    Sequence cautioni

    The sequence AAC72432.1 differs from that shown. Reason: Frameshift at position 176.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti254 – 2541I → F in AAB49620. (PubMed:9010216)Curated
    Sequence conflicti317 – 3182RQ → GR in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti341 – 3411P → H in AAB49620. (PubMed:9010216)Curated
    Sequence conflicti418 – 4181S → F in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti421 – 4211V → S in AAB49620. (PubMed:9010216)Curated
    Sequence conflicti580 – 5801P → L in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti595 – 5951P → T in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti615 – 6228PWVSSGVQ → ACFSPGVP in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti629 – 6291I → M in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti636 – 6361P → L in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti647 – 6471R → K in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti689 – 6891S → F in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti703 – 7031Y → D in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti789 – 7891Q → R in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti940 – 9401R → Q in BAE36255. (PubMed:16141072)Curated
    Sequence conflicti941 – 9411R → RNEE in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti956 – 9583ETS → GKF in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti963 – 9631E → G in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti978 – 9781L → F in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti982 – 9821D → E in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti1012 – 10121K → N in AAB49620. (PubMed:9010216)Curated
    Sequence conflicti1290 – 12901K → T in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti1316 – 13161Q → H in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti1564 – 15641N → I in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti1581 – 15811E → D in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti1591 – 15911P → L in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti1596 – 15961P → L in AAC72432. (PubMed:9037032)Curated
    Sequence conflicti1604 – 16041A → V in AAC72432. (PubMed:9037032)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei102 – 12322IDDAS…NLAEA → VCKNTITLFLHNCFYLYNVS VT in isoform 3. 2 PublicationsVSP_018285Add
    BLAST
    Alternative sequencei124 – 17561633Missing in isoform 3. 2 PublicationsVSP_018286Add
    BLAST
    Alternative sequencei653 – 68634Missing in isoform 2. 2 PublicationsVSP_018287Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK045635 mRNA. Translation: BAC32441.1.
    AK079129 mRNA. Translation: BAC37553.1.
    AK081261 mRNA. Translation: BAC38179.1.
    AK144758 mRNA. Translation: BAE26051.1.
    AK160656 mRNA. Translation: BAE35944.1.
    AK161231 mRNA. Translation: BAE36255.1.
    AC125221 Genomic DNA. No translation available.
    BC025874 mRNA. Translation: AAH25874.1.
    U83913 mRNA. Translation: AAC72432.1. Frameshift.
    U28789 mRNA. Translation: AAB49620.1.
    CCDSiCCDS52387.1. [P97868-1]
    PIRiT42727.
    RefSeqiNP_035377.2. NM_011247.2. [P97868-1]
    NP_778188.1. NM_175023.3.
    XP_006507533.1. XM_006507470.1. [P97868-2]
    UniGeneiMm.4480.

    Genome annotation databases

    EnsembliENSMUST00000052135; ENSMUSP00000049528; ENSMUSG00000030779. [P97868-1]
    ENSMUST00000071590; ENSMUSP00000071519; ENSMUSG00000030779. [P97868-2]
    ENSMUST00000098062; ENSMUSP00000095670; ENSMUSG00000030779.
    GeneIDi19647.
    KEGGimmu:19647.
    UCSCiuc009jow.2. mouse. [P97868-3]
    uc009joy.2. mouse. [P97868-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK045635 mRNA. Translation: BAC32441.1 .
    AK079129 mRNA. Translation: BAC37553.1 .
    AK081261 mRNA. Translation: BAC38179.1 .
    AK144758 mRNA. Translation: BAE26051.1 .
    AK160656 mRNA. Translation: BAE35944.1 .
    AK161231 mRNA. Translation: BAE36255.1 .
    AC125221 Genomic DNA. No translation available.
    BC025874 mRNA. Translation: AAH25874.1 .
    U83913 mRNA. Translation: AAC72432.1 . Frameshift.
    U28789 mRNA. Translation: AAB49620.1 .
    CCDSi CCDS52387.1. [P97868-1 ]
    PIRi T42727.
    RefSeqi NP_035377.2. NM_011247.2. [P97868-1 ]
    NP_778188.1. NM_175023.3.
    XP_006507533.1. XM_006507470.1. [P97868-2 ]
    UniGenei Mm.4480.

    3D structure databases

    ProteinModelPortali P97868.
    SMRi P97868. Positions 1-81, 160-207, 250-336.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202817. 1 interaction.
    IntActi P97868. 1 interaction.
    MINTi MINT-4106375.
    STRINGi 10090.ENSMUSP00000049528.

    PTM databases

    PhosphoSitei P97868.

    Proteomic databases

    MaxQBi P97868.
    PaxDbi P97868.
    PRIDEi P97868.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000052135 ; ENSMUSP00000049528 ; ENSMUSG00000030779 . [P97868-1 ]
    ENSMUST00000071590 ; ENSMUSP00000071519 ; ENSMUSG00000030779 . [P97868-2 ]
    ENSMUST00000098062 ; ENSMUSP00000095670 ; ENSMUSG00000030779 .
    GeneIDi 19647.
    KEGGi mmu:19647.
    UCSCi uc009jow.2. mouse. [P97868-3 ]
    uc009joy.2. mouse. [P97868-1 ]

    Organism-specific databases

    CTDi 5930.
    MGIi MGI:894835. Rbbp6.

    Phylogenomic databases

    eggNOGi COG5222.
    GeneTreei ENSGT00610000086096.
    HOVERGENi HBG093889.
    InParanoidi P97868.
    KOi K10624.
    OMAi EREYFNR.
    OrthoDBi EOG74BJR8.
    PhylomeDBi P97868.
    TreeFami TF350543.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi RBBP6. mouse.
    NextBioi 296898.
    PROi P97868.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P97868.
    Bgeei P97868.
    CleanExi MM_RBBP6.
    Genevestigatori P97868.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    4.10.60.10. 1 hit.
    InterProi IPR014891. DWNN_domain.
    IPR001878. Znf_CCHC.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF08783. DWNN. 1 hit.
    PF00098. zf-CCHC. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    SM00343. ZnF_C2HC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57756. SSF57756. 1 hit.
    PROSITEi PS51282. DWNN. 1 hit.
    PS50158. ZF_CCHC. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 546-1148 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1356-1790 (ISOFORMS 1/2).
      Strain: C57BL/6J.
      Tissue: Corpora quadrigemina, Corpus striatum, Embryo, Head and Lung.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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] (ISOFORM 3).
      Strain: FVB/N-3.
      Tissue: Mammary tumor.
    4. "The proliferation potential protein-related (P2P-R) gene with domains encoding heterogeneous nuclear ribonucleoprotein association and Rb1 binding shows repressed expression during terminal differentiation."
      Witte M.M., Scott R.E.
      Proc. Natl. Acad. Sci. U.S.A. 94:1212-1217(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 154-1790 (ISOFORM 2), INTERACTION WITH RB1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: BALB/c.
    5. "PACT: cloning and characterization of a cellular p53 binding protein that interacts with Rb."
      Simons A., Melamed-Bessudo C., Wolkowicz R., Sperling J., Sperling R., Eisenbach L., Rotter V.
      Oncogene 14:145-155(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 204-1790 (ISOFORM 1), INTERACTION WITH TP53 AND RB1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Strain: BALB/c.
      Tissue: Testis.
    6. "P2P-R protein localizes to the nucleolus of interphase cells and the periphery of chromosomes in mitotic cells which show maximum P2P-R immunoreactivity."
      Gao S., Witte M.M., Scott R.E.
      J. Cell. Physiol. 191:145-154(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    7. Erratum
      Gao S., Witte M.M., Scott R.E.
      J. Cell. Physiol. 192:359-360(2002)
    8. "P2P-R protein overexpression restricts mitotic progression at prometaphase and promotes mitotic apoptosis."
      Gao S., Scott R.E.
      J. Cell. Physiol. 193:199-207(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "Stable overexpression of specific segments of the P2P-R protein in human MCF-7 cells promotes camptothecin-induced apoptosis."
      Gao S., Scott R.E.
      J. Cell. Physiol. 197:445-452(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TP53.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-985; SER-1179; THR-1272 AND SER-1329, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. "PACT is a negative regulator of p53 and essential for cell growth and embryonic development."
      Li L., Deng B., Xing G., Teng Y., Tian C., Cheng X., Yin X., Yang J., Gao X., Zhu Y., Sun Q., Zhang L., Yang X., He F.
      Proc. Natl. Acad. Sci. U.S.A. 104:7951-7956(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    12. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1179 AND SER-1329, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiRBBP6_MOUSE
    AccessioniPrimary (citable) accession number: P97868
    Secondary accession number(s): P70287
    , Q3TTR9, Q3TUM7, Q3UMP7, Q4U217, Q7TT06, Q8BNY8, Q8R399
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2006
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 116 of the entry and version 5 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

    External Data

    Dasty 3