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Q7Z6E9

- RBBP6_HUMAN

UniProt

Q7Z6E9 - RBBP6_HUMAN

Protein

E3 ubiquitin-protein ligase RBBP6

Gene

RBBP6

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 1 (01 Oct 2003)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase which promotes ubiquitination of YBX1, leading to its degradation by the proteasome. 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.

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri159 – 17618CCHC-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri259 – 30042RING-type; degeneratePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. ubiquitin-protein transferase activity Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

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

    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 Q protein 1
    Short name:
    RBQ-1
    Retinoblastoma-binding protein 6
    p53-associated cellular protein of testis
    Gene namesi
    Name:RBBP6
    Synonyms:P2PR, PACT, RBQ1
    ORF Names:My038
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:9889. RBBP6.

    Subcellular locationi

    Nucleusnucleolus. Chromosome. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
    Note: Colocalizes with mitotic chromosomes. Colocalizes with NEK6 in the centrosome.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34253.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17921792E3 ubiquitin-protein ligase RBBP6PRO_0000234354Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei130 – 1301N6-acetyllysineBy similarity
    Modified residuei244 – 2441Phosphoserine3 Publications
    Modified residuei245 – 2451Phosphoserine3 Publications
    Modified residuei246 – 2461Phosphoserine3 Publications
    Modified residuei247 – 2471Phosphoserine3 Publications
    Modified residuei360 – 3601Phosphoserine3 Publications
    Modified residuei516 – 5161Phosphoserine6 Publications
    Modified residuei770 – 7701Phosphoserine2 Publications
    Modified residuei772 – 7721Phosphoserine2 Publications
    Modified residuei780 – 7801Phosphoserine2 Publications
    Modified residuei861 – 8611Phosphoserine3 Publications
    Modified residuei984 – 9841PhosphothreonineBy similarity
    Modified residuei1179 – 11791Phosphoserine6 Publications
    Modified residuei1271 – 12711PhosphothreonineBy similarity
    Modified residuei1277 – 12771Phosphoserine2 Publications
    Modified residuei1328 – 13281Phosphoserine6 Publications
    Modified residuei1468 – 14681Phosphothreonine2 Publications
    Modified residuei1646 – 16461Phosphoserine2 Publications
    Modified residuei1648 – 16481Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated by NEK6.9 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ7Z6E9.
    PaxDbiQ7Z6E9.
    PRIDEiQ7Z6E9.

    PTM databases

    PhosphoSiteiQ7Z6E9.

    Miscellaneous databases

    PMAP-CutDBQ7Z6E9.

    Expressioni

    Tissue specificityi

    Highly expressed in the placenta and testis. Expressed at lower levels in the brain, heart, kidney, liver and lung. Overexpressed in esophageal cancer.1 Publication

    Gene expression databases

    ArrayExpressiQ7Z6E9.
    BgeeiQ7Z6E9.
    GenevestigatoriQ7Z6E9.

    Organism-specific databases

    HPAiCAB032866.
    HPA041725.
    HPA043544.

    Interactioni

    Subunit structurei

    Interacts with p53/TP53 and RB1 By similarity. Interacts also with MDM2 and YBX1. Interacts with NEK6.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SRSF7Q166293EBI-2117026,EBI-398885

    Protein-protein interaction databases

    BioGridi111865. 49 interactions.
    DIPiDIP-46897N.
    IntActiQ7Z6E9. 29 interactions.
    MINTiMINT-1181085.

    Structurei

    Secondary structure

    1792
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1 – 88
    Beta strandi12 – 2514
    Helixi26 – 3712
    Turni41 – 433
    Beta strandi44 – 5310
    Beta strandi63 – 653
    Beta strandi70 – 767
    Turni162 – 1643
    Helixi171 – 1733
    Helixi176 – 1783
    Beta strandi197 – 1993
    Helixi255 – 2573
    Beta strandi260 – 2623
    Beta strandi273 – 2753
    Helixi283 – 2908
    Beta strandi291 – 2944
    Beta strandi297 – 2993
    Turni306 – 3094
    Helixi313 – 32614

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C7HNMR-A1-81[»]
    2YSANMR-A159-206[»]
    2YURNMR-A249-309[»]
    3ZTGNMR-A/B249-335[»]
    ProteinModelPortaliQ7Z6E9.
    SMRiQ7Z6E9. Positions 1-81, 159-206, 249-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7Z6E9.

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni982 – 1139158Interaction with RB1By similarityAdd
    BLAST
    Regioni1433 – 1544112Interaction with p53By similarityAdd
    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 fingeri159 – 17618CCHC-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri259 – 30042RING-type; degeneratePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5222.
    HOVERGENiHBG061131.
    InParanoidiQ7Z6E9.
    KOiK10624.
    OMAiEREYFNR.
    OrthoDBiEOG74BJR8.
    PhylomeDBiQ7Z6E9.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7Z6E9-1) [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 AADCDLQITN     50
    AQTKEEYTDD NALIPKNSSV IVRRIPIGGV KSTSKTYVIS RTEPAMATTK 100
    AIDDSSASIS LAQLTKTANL AEANASEEDK IKAMMSQSGH EYDPINYMKK 150
    PLGPPPPSYT CFRCGKPGHY IKNCPTNGDK NFESGPRIKK STGIPRSFMM 200
    EVKDPNMKGA MLTNTGKYAI PTIDAEAYAI GKKEKPPFLP EEPSSSSEED 250
    DPIPDELLCL ICKDIMTDAV VIPCCGNSYC DECIRTALLE SDEHTCPTCH 300
    QNDVSPDALI ANKFLRQAVN NFKNETGYTK RLRKQLPPPP PPIPPPRPLI 350
    QRNLQPLMRS PISRQQDPLM IPVTSSSTHP APSISSLTSN QSSLAPPVSG 400
    NPSSAPAPVP DITATVSISV HSEKSDGPFR DSDNKILPAA ALASEHSKGT 450
    SSIAITALME EKGYQVPVLG TPSLLGQSLL HGQLIPTTGP VRINTARPGG 500
    GRPGWEHSNK LGYLVSPPQQ IRRGERSCYR SINRGRHHSE RSQRTQGPSL 550
    PATPVFVPVP PPPLYPPPPH TLPLPPGVPP PQFSPQFPPG QPPPAGYSVP 600
    PPGFPPAPAN LSTPWVSSGV QTAHSNTIPT TQAPPLSREE FYREQRRLKE 650
    EEKKKSKLDE FTNDFAKELM EYKKIQKERR RSFSRSKSPY SGSSYSRSSY 700
    TYSKSRSGST RSRSYSRSFS RSHSRSYSRS PPYPRRGRGK SRNYRSRSRS 750
    HGYHRSRSRS PPYRRYHSRS RSPQAFRGQS PNKRNVPQGE TEREYFNRYR 800
    EVPPPYDMKA YYGRSVDFRD PFEKERYREW ERKYREWYEK YYKGYAAGAQ 850
    PRPSANRENF SPERFLPLNI RNSPFTRGRR EDYVGGQSHR SRNIGSNYPE 900
    KLSARDGHNQ KDNTKSKEKE SENAPGDGKG NKHKKHRKRR KGEESEGFLN 950
    PELLETSRKS REPTGVEENK TDSLFVLPSR DDATPVRDEP MDAESITFKS 1000
    VSEKDKRERD KPKAKGDKTK RKNDGSAVSK KENIVKPAKG PQEKVDGERE 1050
    RSPRSEPPIK KAKEETPKTD NTKSSSSSQK DEKITGTPRK AHSKSAKEHQ 1100
    ETKPVKEEKV KKDYSKDVKS EKLTTKEEKA KKPNEKNKPL DNKGEKRKRK 1150
    TEEKGVDKDF ESSSMKISKL EVTEIVKPSP KRKMEPDTEK MDRTPEKDKI 1200
    SLSAPAKKIK LNRETGKKIG STENISNTKE PSEKLESTSS KVKQEKVKGK 1250
    VRRKVTGTEG SSSTLVDYTS TSSTGGSPVR KSEEKTDTKR TVIKTMEEYN 1300
    NDNTAPAEDV IIMIQVPQSK WDKDDFESEE EDVKSTQPIS SVGKPASVIK 1350
    NVSTKPSNIV KYPEKESEPS EKIQKFTKDV SHEIIQHEVK SSKNSASSEK 1400
    GKTKDRDYSV LEKENPEKRK NSTQPEKESN LDRLNEQGNF KSLSQSSKEA 1450
    RTSDKHDSTR ASSNKDFTPN RDKKTDYDTR EYSSSKRRDE KNELTRRKDS 1500
    PSRNKDSASG QKNKPREERD LPKKGTGDSK KSNSSPSRDR KPHDHKATYD 1550
    TKRPNEETKS VDKNPCKDRE KHVLEARNNK ESSGNKLLYI LNPPETQVEK 1600
    EQITGQIDKS TVKPKPQLSH SSRLSSDLTR ETDEAAFEPD YNESDSESNV 1650
    SVKEEESSGN ISKDLKDKIV EKAKESLDTA AVVQVGISRN QSHSSPSVSP 1700
    SRSHSPSGSQ TRSHSSSASS AESQDSKKKK KKKEKKKHKK HKKHKKHKKH 1750
    AGTEVELEKS QKHKHKKKKS KKNKDKEKEK EKDDQKVKSV TV 1792
    Length:1,792
    Mass (Da):201,564
    Last modified:October 1, 2003 - v1
    Checksum:i550F7BBA5125DA06
    GO
    Isoform 2 (identifier: Q7Z6E9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         652-685: Missing.

    Show »
    Length:1,758
    Mass (Da):197,287
    Checksum:i5062A3FBA5BB5255
    GO
    Isoform 3 (identifier: Q7Z6E9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         102-117: IDDSSASISLAQLTKT → VCKNTISHFFYTLLLPL
         118-1792: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:118
    Mass (Da):13,235
    Checksum:i18B6431D0D740828
    GO
    Isoform 4 (identifier: Q7Z6E9-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         431-1270: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:952
    Mass (Da):106,037
    Checksum:iBC28F8CCB1EED8E5
    GO

    Sequence cautioni

    The sequence AAG43155.1 differs from that shown. Reason: Intron retention.
    The sequence AAH63524.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAL68925.1 differs from that shown. Reason: Intron retention.
    The sequence AAL05625.1 differs from that shown. Reason: Frameshift at position 198.
    The sequence CAA59445.1 differs from that shown. Reason: Frameshift at positions 198, 1048 and 1098.
    The sequence BAB15600.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti223 – 2231I → T in AAL68925. 1 PublicationCurated
    Sequence conflicti1633 – 16331D → H in AAL68925. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti43 – 431D → H.
    Corresponds to variant rs16973796 [ dbSNP | Ensembl ].
    VAR_051306
    Natural varianti555 – 5551V → A.
    Corresponds to variant rs16973840 [ dbSNP | Ensembl ].
    VAR_026216
    Natural varianti1208 – 12081K → I.
    Corresponds to variant rs3743968 [ dbSNP | Ensembl ].
    VAR_051307

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei102 – 11716IDDSS…QLTKT → VCKNTISHFFYTLLLPL in isoform 3. 1 PublicationVSP_018281Add
    BLAST
    Alternative sequencei118 – 17921675Missing in isoform 3. 1 PublicationVSP_018282Add
    BLAST
    Alternative sequencei431 – 1270840Missing in isoform 4. 1 PublicationVSP_018283Add
    BLAST
    Alternative sequencei652 – 68534Missing in isoform 2. 2 PublicationsVSP_018284Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB112074 mRNA. Translation: BAC77636.1.
    AB112075 mRNA. Translation: BAC77637.1.
    CH471145 Genomic DNA. Translation: EAW55789.1.
    BC029352 mRNA. Translation: AAH29352.1.
    BC063524 mRNA. Translation: AAH63524.1. Sequence problems.
    BC073938 mRNA. Translation: AAH73938.1.
    BC101139 mRNA. Translation: AAI01140.1.
    BC101140 mRNA. Translation: AAI01141.1.
    BC101141 mRNA. Translation: AAI01142.1.
    BC101142 mRNA. Translation: AAI01143.1.
    BC114353 mRNA. Translation: AAI14354.1.
    BC114354 mRNA. Translation: AAI14355.1.
    BC118667 mRNA. Translation: AAI18668.1.
    BC139830 mRNA. Translation: AAI39831.1.
    AF063596 mRNA. Translation: AAG43155.1. Sequence problems.
    AY072922 mRNA. Translation: AAL68925.1. Sequence problems.
    AF352051 mRNA. Translation: AAL05625.1. Frameshift.
    X85133 mRNA. Translation: CAA59445.1. Frameshift.
    AK026954 mRNA. Translation: BAB15600.1. Different initiation.
    AL359564 mRNA. Translation: CAB94869.1.
    CCDSiCCDS10621.1. [Q7Z6E9-1]
    CCDS10622.1. [Q7Z6E9-2]
    CCDS45444.1. [Q7Z6E9-3]
    PIRiA57640.
    T50609.
    RefSeqiNP_008841.2. NM_006910.4. [Q7Z6E9-1]
    NP_061173.1. NM_018703.3. [Q7Z6E9-2]
    NP_116015.2. NM_032626.5. [Q7Z6E9-3]
    UniGeneiHs.188553.

    Genome annotation databases

    EnsembliENST00000319715; ENSP00000317872; ENSG00000122257. [Q7Z6E9-1]
    ENST00000348022; ENSP00000316291; ENSG00000122257. [Q7Z6E9-2]
    ENST00000381039; ENSP00000370427; ENSG00000122257. [Q7Z6E9-4]
    ENST00000452655; ENSP00000390537; ENSG00000122257. [Q7Z6E9-3]
    GeneIDi5930.
    KEGGihsa:5930.
    UCSCiuc002dmg.3. human. [Q7Z6E9-3]
    uc002dmh.3. human. [Q7Z6E9-1]
    uc002dmi.3. human. [Q7Z6E9-2]
    uc010bxr.3. human. [Q7Z6E9-4]

    Polymorphism databases

    DMDMi74762440.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB112074 mRNA. Translation: BAC77636.1 .
    AB112075 mRNA. Translation: BAC77637.1 .
    CH471145 Genomic DNA. Translation: EAW55789.1 .
    BC029352 mRNA. Translation: AAH29352.1 .
    BC063524 mRNA. Translation: AAH63524.1 . Sequence problems.
    BC073938 mRNA. Translation: AAH73938.1 .
    BC101139 mRNA. Translation: AAI01140.1 .
    BC101140 mRNA. Translation: AAI01141.1 .
    BC101141 mRNA. Translation: AAI01142.1 .
    BC101142 mRNA. Translation: AAI01143.1 .
    BC114353 mRNA. Translation: AAI14354.1 .
    BC114354 mRNA. Translation: AAI14355.1 .
    BC118667 mRNA. Translation: AAI18668.1 .
    BC139830 mRNA. Translation: AAI39831.1 .
    AF063596 mRNA. Translation: AAG43155.1 . Sequence problems.
    AY072922 mRNA. Translation: AAL68925.1 . Sequence problems.
    AF352051 mRNA. Translation: AAL05625.1 . Frameshift.
    X85133 mRNA. Translation: CAA59445.1 . Frameshift.
    AK026954 mRNA. Translation: BAB15600.1 . Different initiation.
    AL359564 mRNA. Translation: CAB94869.1 .
    CCDSi CCDS10621.1. [Q7Z6E9-1 ]
    CCDS10622.1. [Q7Z6E9-2 ]
    CCDS45444.1. [Q7Z6E9-3 ]
    PIRi A57640.
    T50609.
    RefSeqi NP_008841.2. NM_006910.4. [Q7Z6E9-1 ]
    NP_061173.1. NM_018703.3. [Q7Z6E9-2 ]
    NP_116015.2. NM_032626.5. [Q7Z6E9-3 ]
    UniGenei Hs.188553.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C7H NMR - A 1-81 [» ]
    2YSA NMR - A 159-206 [» ]
    2YUR NMR - A 249-309 [» ]
    3ZTG NMR - A/B 249-335 [» ]
    ProteinModelPortali Q7Z6E9.
    SMRi Q7Z6E9. Positions 1-81, 159-206, 249-335.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111865. 49 interactions.
    DIPi DIP-46897N.
    IntActi Q7Z6E9. 29 interactions.
    MINTi MINT-1181085.

    PTM databases

    PhosphoSitei Q7Z6E9.

    Polymorphism databases

    DMDMi 74762440.

    Proteomic databases

    MaxQBi Q7Z6E9.
    PaxDbi Q7Z6E9.
    PRIDEi Q7Z6E9.

    Protocols and materials databases

    DNASUi 5930.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000319715 ; ENSP00000317872 ; ENSG00000122257 . [Q7Z6E9-1 ]
    ENST00000348022 ; ENSP00000316291 ; ENSG00000122257 . [Q7Z6E9-2 ]
    ENST00000381039 ; ENSP00000370427 ; ENSG00000122257 . [Q7Z6E9-4 ]
    ENST00000452655 ; ENSP00000390537 ; ENSG00000122257 . [Q7Z6E9-3 ]
    GeneIDi 5930.
    KEGGi hsa:5930.
    UCSCi uc002dmg.3. human. [Q7Z6E9-3 ]
    uc002dmh.3. human. [Q7Z6E9-1 ]
    uc002dmi.3. human. [Q7Z6E9-2 ]
    uc010bxr.3. human. [Q7Z6E9-4 ]

    Organism-specific databases

    CTDi 5930.
    GeneCardsi GC16P024458.
    HGNCi HGNC:9889. RBBP6.
    HPAi CAB032866.
    HPA041725.
    HPA043544.
    MIMi 600938. gene.
    neXtProti NX_Q7Z6E9.
    PharmGKBi PA34253.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5222.
    HOVERGENi HBG061131.
    InParanoidi Q7Z6E9.
    KOi K10624.
    OMAi EREYFNR.
    OrthoDBi EOG74BJR8.
    PhylomeDBi Q7Z6E9.
    TreeFami TF350543.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi RBBP6. human.
    EvolutionaryTracei Q7Z6E9.
    GeneWikii RBBP6.
    GenomeRNAii 5930.
    NextBioi 23102.
    PMAP-CutDB Q7Z6E9.
    PROi Q7Z6E9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7Z6E9.
    Bgeei Q7Z6E9.
    Genevestigatori Q7Z6E9.

    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. "Retinoblastoma binding protein 6 (RBBP6), mRNA."
      Kudo E., Itakura M.
      Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1727 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1427-1792 (ISOFORMS 1/2/4).
      Tissue: Bone and Kidney.
    4. Mao Y.M., Xie Y., Zheng Z.H.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-55 (ISOFORMS 1/2/3/4).
      Tissue: Fetal brain.
    5. "The cDNA sequence for the human PACT gene."
      Ma X., Qu X., Sun L., Wu S., He F.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 117-1792 (ISOFORM 2).
      Tissue: Spleen.
    6. Camargo A.A., Moreira E.S., Simpson A.J.G.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 150-1792 (ISOFORM 1).
    7. "cDNA sequence and chromosomal localization of a novel human protein, RBQ-1 (RBBP6), that binds to the retinoblastoma gene product."
      Sakai Y., Saijo M., Coelho K., Kishino T., Niikawa N., Taya Y.
      Genomics 30:98-101(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 150-1146 (ISOFORM 1).
      Tissue: Lung carcinoma.
    8. "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] OF 1165-1792 (ISOFORMS 1/2).
      Tissue: Hepatoma.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1264-1792 (ISOFORMS 1/2).
      Tissue: Amygdala.
    10. "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.
    11. Erratum
      Gao S., Witte M.M., Scott R.E.
      J. Cell. Physiol. 192:359-360(2002)
    12. "Proliferation potential-related protein, an ideal esophageal cancer antigen for immunotherapy, identified using complementary DNA microarray analysis."
      Yoshitake Y., Nakatsura T., Monji M., Senju S., Matsuyoshi H., Tsukamoto H., Hosaka S., Komori H., Fukuma D., Ikuta Y., Katagiri T., Furukawa Y., Ito H., Shinohara M., Nakamura Y., Nishimura Y.
      Clin. Cancer Res. 10:6437-6448(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, OVEREXPRESSION IN ESOPHAGEAL CANCER.
    13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244; SER-245; SER-246; SER-247; SER-360; SER-770; SER-772; SER-861; SER-1179 AND SER-1328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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: INTERACTION WITH MDM2.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    17. "RBBP6 interacts with multifunctional protein YB-1 through its RING finger domain, leading to ubiquitination and proteosomal degradation of YB-1."
      Chibi M., Meyer M., Skepu A., Rees D.J.G., Moolman-Smook J.C., Pugh D.J.
      J. Mol. Biol. 384:908-916(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YBX1.
    18. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-516; SER-1179; THR-1468; SER-1646 AND SER-1648, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    21. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516; SER-1179; SER-1277; SER-1328 AND SER-1648, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    22. "Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome."
      Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J.
      J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK6, PHOSPHORYLATION.
    23. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244; SER-245; SER-246; SER-247; SER-516; SER-861; SER-1179 AND SER-1328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-780; SER-1179 AND SER-1328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways."
      Pugh D.J.R., Ab E., Faro A., Lutya P.T., Hoffmann E., Rees D.J.G.
      BMC Struct. Biol. 6:1-1(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-81.
    26. "Solution structure of the zinc finger CCHC domain and of the RING finger from the human retinoblastoma-binding protein 6 (retinoblastoma-binding Q protein 1, RBQ-1)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 159-309.

    Entry informationi

    Entry nameiRBBP6_HUMAN
    AccessioniPrimary (citable) accession number: Q7Z6E9
    Secondary accession number(s): Q147T5
    , Q15290, Q6DKH4, Q6P4C2, Q6YNC9, Q7Z6E8, Q8N0V2, Q96PH3, Q9H3I8, Q9H5M5, Q9NPX4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2006
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 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

    3D-structure, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

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