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Q7Z6E9 (RBBP6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RBBP6
Synonyms:P2PR, PACT, RBQ1
ORF Names:My038
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1792 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with p53/TP53 and RB1 By similarity. Interacts also with MDM2 and YBX1. Interacts with NEK6. Ref.15 Ref.17 Ref.22

Subcellular location

Nucleusnucleolus. Chromosome. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Colocalizes with mitotic chromosomes. Colocalizes with NEK6 in the centrosome. Ref.10 Ref.12 Ref.22

Tissue specificity

Highly expressed in the placenta and testis. Expressed at lower levels in the brain, heart, kidney, liver and lung. Overexpressed in esophageal cancer. Ref.12

Post-translational modification

Phosphorylated by NEK6. Ref.22

Sequence similarities

Contains 1 CCHC-type zinc finger.

Contains 1 DWNN domain.

Contains 1 RING-type zinc finger.

Sequence caution

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 AAL05625.1 differs from that shown. Reason: Frameshift at position 198.

The sequence AAL68925.1 differs from that shown. Reason: Intron retention.

The sequence BAB15600.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA59445.1 differs from that shown. Reason: Frameshift at positions 198, 1048 and 1098.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SRSF7Q166293EBI-2117026,EBI-398885

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7Z6E9-1)

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.
Isoform 2 (identifier: Q7Z6E9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     652-685: Missing.
Isoform 3 (identifier: Q7Z6E9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     102-117: IDDSSASISLAQLTKT → VCKNTISHFFYTLLLPL
     118-1792: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q7Z6E9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     431-1270: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17921792E3 ubiquitin-protein ligase RBBP6
PRO_0000234354

Regions

Domain4 – 7673DWNN
Zinc finger159 – 17618CCHC-type
Zinc finger259 – 30042RING-type; degenerate
Region982 – 1139158Interaction with RB1 By similarity
Region1433 – 1544112Interaction with p53 By similarity

Amino acid modifications

Modified residue1301N6-acetyllysine By similarity
Modified residue2441Phosphoserine Ref.13 Ref.23
Modified residue2451Phosphoserine Ref.13 Ref.23
Modified residue2461Phosphoserine Ref.13 Ref.23
Modified residue2471Phosphoserine Ref.13 Ref.23
Modified residue3601Phosphoserine Ref.13 Ref.19
Modified residue5161Phosphoserine Ref.14 Ref.18 Ref.19 Ref.21 Ref.23
Modified residue7701Phosphoserine Ref.13
Modified residue7721Phosphoserine Ref.13
Modified residue7801Phosphoserine Ref.24
Modified residue8611Phosphoserine Ref.13 Ref.23
Modified residue9841Phosphothreonine By similarity
Modified residue11791Phosphoserine Ref.13 Ref.19 Ref.21 Ref.23 Ref.24
Modified residue12711Phosphothreonine By similarity
Modified residue12771Phosphoserine Ref.21
Modified residue13281Phosphoserine Ref.13 Ref.20 Ref.21 Ref.23 Ref.24
Modified residue14681Phosphothreonine Ref.19
Modified residue16461Phosphoserine Ref.19
Modified residue16481Phosphoserine Ref.19 Ref.21

Natural variations

Alternative sequence102 – 11716IDDSS…QLTKT → VCKNTISHFFYTLLLPL in isoform 3.
VSP_018281
Alternative sequence118 – 17921675Missing in isoform 3.
VSP_018282
Alternative sequence431 – 1270840Missing in isoform 4.
VSP_018283
Alternative sequence652 – 68534Missing in isoform 2.
VSP_018284
Natural variant431D → H.
Corresponds to variant rs16973796 [ dbSNP | Ensembl ].
VAR_051306
Natural variant5551V → A.
Corresponds to variant rs16973840 [ dbSNP | Ensembl ].
VAR_026216
Natural variant12081K → I.
Corresponds to variant rs3743968 [ dbSNP | Ensembl ].
VAR_051307

Experimental info

Sequence conflict2231I → T in AAL68925. Ref.5
Sequence conflict16331D → H in AAL68925. Ref.5

Secondary structure

................................... 1792
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 550F7BBA5125DA06

FASTA1,792201,564
        10         20         30         40         50         60 
MSCVHYKFSS KLNYDTVTFD GLHISLCDLK KQIMGREKLK AADCDLQITN AQTKEEYTDD 

        70         80         90        100        110        120 
NALIPKNSSV IVRRIPIGGV KSTSKTYVIS RTEPAMATTK AIDDSSASIS LAQLTKTANL 

       130        140        150        160        170        180 
AEANASEEDK IKAMMSQSGH EYDPINYMKK PLGPPPPSYT CFRCGKPGHY IKNCPTNGDK 

       190        200        210        220        230        240 
NFESGPRIKK STGIPRSFMM EVKDPNMKGA MLTNTGKYAI PTIDAEAYAI GKKEKPPFLP 

       250        260        270        280        290        300 
EEPSSSSEED DPIPDELLCL ICKDIMTDAV VIPCCGNSYC DECIRTALLE SDEHTCPTCH 

       310        320        330        340        350        360 
QNDVSPDALI ANKFLRQAVN NFKNETGYTK RLRKQLPPPP PPIPPPRPLI QRNLQPLMRS 

       370        380        390        400        410        420 
PISRQQDPLM IPVTSSSTHP APSISSLTSN QSSLAPPVSG NPSSAPAPVP DITATVSISV 

       430        440        450        460        470        480 
HSEKSDGPFR DSDNKILPAA ALASEHSKGT SSIAITALME EKGYQVPVLG TPSLLGQSLL 

       490        500        510        520        530        540 
HGQLIPTTGP VRINTARPGG GRPGWEHSNK LGYLVSPPQQ IRRGERSCYR SINRGRHHSE 

       550        560        570        580        590        600 
RSQRTQGPSL PATPVFVPVP PPPLYPPPPH TLPLPPGVPP PQFSPQFPPG QPPPAGYSVP 

       610        620        630        640        650        660 
PPGFPPAPAN LSTPWVSSGV QTAHSNTIPT TQAPPLSREE FYREQRRLKE EEKKKSKLDE 

       670        680        690        700        710        720 
FTNDFAKELM EYKKIQKERR RSFSRSKSPY SGSSYSRSSY TYSKSRSGST RSRSYSRSFS 

       730        740        750        760        770        780 
RSHSRSYSRS PPYPRRGRGK SRNYRSRSRS HGYHRSRSRS PPYRRYHSRS RSPQAFRGQS 

       790        800        810        820        830        840 
PNKRNVPQGE TEREYFNRYR EVPPPYDMKA YYGRSVDFRD PFEKERYREW ERKYREWYEK 

       850        860        870        880        890        900 
YYKGYAAGAQ PRPSANRENF SPERFLPLNI RNSPFTRGRR EDYVGGQSHR SRNIGSNYPE 

       910        920        930        940        950        960 
KLSARDGHNQ KDNTKSKEKE SENAPGDGKG NKHKKHRKRR KGEESEGFLN PELLETSRKS 

       970        980        990       1000       1010       1020 
REPTGVEENK TDSLFVLPSR DDATPVRDEP MDAESITFKS VSEKDKRERD KPKAKGDKTK 

      1030       1040       1050       1060       1070       1080 
RKNDGSAVSK KENIVKPAKG PQEKVDGERE RSPRSEPPIK KAKEETPKTD NTKSSSSSQK 

      1090       1100       1110       1120       1130       1140 
DEKITGTPRK AHSKSAKEHQ ETKPVKEEKV KKDYSKDVKS EKLTTKEEKA KKPNEKNKPL 

      1150       1160       1170       1180       1190       1200 
DNKGEKRKRK TEEKGVDKDF ESSSMKISKL EVTEIVKPSP KRKMEPDTEK MDRTPEKDKI 

      1210       1220       1230       1240       1250       1260 
SLSAPAKKIK LNRETGKKIG STENISNTKE PSEKLESTSS KVKQEKVKGK VRRKVTGTEG 

      1270       1280       1290       1300       1310       1320 
SSSTLVDYTS TSSTGGSPVR KSEEKTDTKR TVIKTMEEYN NDNTAPAEDV IIMIQVPQSK 

      1330       1340       1350       1360       1370       1380 
WDKDDFESEE EDVKSTQPIS SVGKPASVIK NVSTKPSNIV KYPEKESEPS EKIQKFTKDV 

      1390       1400       1410       1420       1430       1440 
SHEIIQHEVK SSKNSASSEK GKTKDRDYSV LEKENPEKRK NSTQPEKESN LDRLNEQGNF 

      1450       1460       1470       1480       1490       1500 
KSLSQSSKEA RTSDKHDSTR ASSNKDFTPN RDKKTDYDTR EYSSSKRRDE KNELTRRKDS 

      1510       1520       1530       1540       1550       1560 
PSRNKDSASG QKNKPREERD LPKKGTGDSK KSNSSPSRDR KPHDHKATYD TKRPNEETKS 

      1570       1580       1590       1600       1610       1620 
VDKNPCKDRE KHVLEARNNK ESSGNKLLYI LNPPETQVEK EQITGQIDKS TVKPKPQLSH 

      1630       1640       1650       1660       1670       1680 
SSRLSSDLTR ETDEAAFEPD YNESDSESNV SVKEEESSGN ISKDLKDKIV EKAKESLDTA 

      1690       1700       1710       1720       1730       1740 
AVVQVGISRN QSHSSPSVSP SRSHSPSGSQ TRSHSSSASS AESQDSKKKK KKKEKKKHKK 

      1750       1760       1770       1780       1790 
HKKHKKHKKH AGTEVELEKS QKHKHKKKKS KKNKDKEKEK EKDDQKVKSV TV 

« Hide

Isoform 2 [UniParc].

Checksum: 5062A3FBA5BB5255
Show »

FASTA1,758197,287
Isoform 3 [UniParc].

Checksum: 18B6431D0D740828
Show »

FASTA11813,235
Isoform 4 [UniParc].

Checksum: BC28F8CCB1EED8E5
Show »

FASTA952106,037

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA57640.
T50609.
RefSeqNP_008841.2. NM_006910.4.
NP_061173.1. NM_018703.3.
NP_116015.2. NM_032626.5.
UniGeneHs.188553.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C7HNMR-A1-81[»]
2YSANMR-A159-206[»]
2YURNMR-A246-309[»]
3ZTGNMR-A/B249-335[»]
ProteinModelPortalQ7Z6E9.
SMRQ7Z6E9. Positions 1-81, 159-206, 249-335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111865. 49 interactions.
IntActQ7Z6E9. 29 interactions.
MINTMINT-1181085.

PTM databases

PhosphoSiteQ7Z6E9.

Polymorphism databases

DMDM74762440.

Proteomic databases

PaxDbQ7Z6E9.
PRIDEQ7Z6E9.

Protocols and materials databases

DNASU5930.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319715; ENSP00000317872; ENSG00000122257. [Q7Z6E9-1]
ENST00000348022; ENSP00000316291; ENSG00000122257. [Q7Z6E9-2]
ENST00000381039; ENSP00000370427; ENSG00000122257. [Q7Z6E9-4]
ENST00000452655; ENSP00000390537; ENSG00000122257. [Q7Z6E9-3]
GeneID5930.
KEGGhsa:5930.
UCSCuc002dmg.3. human. [Q7Z6E9-3]
uc002dmh.3. human. [Q7Z6E9-1]
uc002dmi.3. human. [Q7Z6E9-2]
uc010bxr.3. human. [Q7Z6E9-4]

Organism-specific databases

CTD5930.
GeneCardsGC16P024458.
HGNCHGNC:9889. RBBP6.
HPACAB032866.
HPA041725.
HPA043544.
MIM600938. gene.
neXtProtNX_Q7Z6E9.
PharmGKBPA34253.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5222.
HOVERGENHBG061131.
InParanoidQ7Z6E9.
KOK10624.
OMAEREYFNR.
OrthoDBEOG74BJR8.
PhylomeDBQ7Z6E9.
TreeFamTF350543.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ7Z6E9.
BgeeQ7Z6E9.
GenevestigatorQ7Z6E9.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
4.10.60.10. 1 hit.
InterProIPR014891. DWNN_domain.
IPR001878. Znf_CCHC.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF08783. DWNN. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
SM00343. ZnF_C2HC. 1 hit.
[Graphical view]
SUPFAMSSF57756. SSF57756. 1 hit.
PROSITEPS51282. DWNN. 1 hit.
PS50158. ZF_CCHC. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRBBP6. human.
EvolutionaryTraceQ7Z6E9.
GeneWikiRBBP6.
GenomeRNAi5930.
NextBio23102.
PMAP-CutDBQ7Z6E9.
PROQ7Z6E9.
SOURCESearch...

Entry information

Entry nameRBBP6_HUMAN
AccessionPrimary (citable) accession number: Q7Z6E9
Secondary accession number(s): Q147T5 expand/collapse secondary AC list , Q15290, Q6DKH4, Q6P4C2, Q6YNC9, Q7Z6E8, Q8N0V2, Q96PH3, Q9H3I8, Q9H5M5, Q9NPX4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: October 1, 2003
Last modified: April 16, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM