Q7Z6E9 (RBBP6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	RBBP6
Synonyms:	P2PR, PACT, RBQ1
ORF Names:	My038

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1792 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Nucleus › nucleolus. Chromosome. Cytoplasm › cytoskeleton › centrosome. Note: Colocalizes with mitotic chromosomes. Co-localizes 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.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Chromosome Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.17. Source: UniProtKB
Cellular_component	chromosome Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	nucleic acid binding Inferred from electronic annotation. Source: InterPro ubiquitin-protein ligase activity Inferred from direct assay Ref.17. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SRSF7	Q16629	3	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1792

1792

E3 ubiquitin-protein ligase RBBP6

PRO_0000234354

Regions

Domain

4 – 76

73

DWNN

Zinc finger

159 – 176

18

CCHC-type

Zinc finger

259 – 300

42

RING-type; degenerate

Region

982 – 1139

158

Interaction with RB1 By similarity

Region

1433 – 1544

112

Interaction with p53 By similarity

Amino acid modifications

Modified residue

244

1

Phosphoserine Ref.13 Ref.23

Modified residue

245

1

Phosphoserine Ref.13 Ref.23

Modified residue

246

1

Phosphoserine Ref.13 Ref.23

Modified residue

247

1

Phosphoserine Ref.13 Ref.23

Modified residue

360

1

Phosphoserine Ref.13 Ref.19

Modified residue

516

1

Phosphoserine Ref.14 Ref.18 Ref.19 Ref.21 Ref.23

Modified residue

770

1

Phosphoserine Ref.13

Modified residue

772

1

Phosphoserine Ref.13

Modified residue

780

1

Phosphoserine Ref.24

Modified residue

861

1

Phosphoserine Ref.13 Ref.23

Modified residue

1179

1

Phosphoserine Ref.13 Ref.19 Ref.21 Ref.23 Ref.24

Modified residue

1271

1

Phosphothreonine By similarity

Modified residue

1277

1

Phosphoserine Ref.21

Modified residue

1328

1

Phosphoserine Ref.13 Ref.20 Ref.21 Ref.23 Ref.24

Modified residue

1468

1

Phosphothreonine Ref.19

Modified residue

1646

1

Phosphoserine Ref.19

Modified residue

1648

1

Phosphoserine Ref.19 Ref.21

Natural variations

Alternative sequence

102 – 117

16

IDDSS…QLTKT → VCKNTISHFFYTLLLPL in isoform 3.

VSP_018281

Alternative sequence

118 – 1792

1675

Missing in isoform 3.

VSP_018282

Alternative sequence

431 – 1270

840

Missing in isoform 4.

VSP_018283

Alternative sequence

652 – 685

34

Missing in isoform 2.

VSP_018284

Natural variant

43

1

D → H.
Corresponds to variant rs16973796 [ dbSNP | Ensembl ].

VAR_051306

Natural variant

555

1

V → A.
Corresponds to variant rs16973840 [ dbSNP | Ensembl ].

VAR_026216

Natural variant

1208

1

K → I.
Corresponds to variant rs3743968 [ dbSNP | Ensembl ].

VAR_051307

Experimental info

Sequence conflict

223

1

I → T in AAL68925. Ref.5

Sequence conflict

1633

1

D → H in AAL68925. Ref.5

Secondary structure

1

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1792

Helix Strand Turn

Details...

Beta strand

1 – 8

8

Beta strand

12 – 25

14

Helix

26 – 37

12

Turn

41 – 43

3

Beta strand

44 – 53

10

Beta strand

63 – 65

3

Beta strand

70 – 76

7

Turn

162 – 164

3

Helix

171 – 173

3

Helix

176 – 178

3

Beta strand

197 – 199

3

Helix

255 – 257

3

Beta strand

260 – 262

3

Beta strand

273 – 275

3

Helix

283 – 290

8

Beta strand

291 – 294

4

Beta strand

297 – 299

3

Turn

306 – 309

4

Helix

313 – 326

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 550F7BBA5125DA06	FASTA	1,792	201,564
	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
	Isoform 2 [UniParc]. Checksum: 5062A3FBA5BB5255	FASTA	1,758	197,287
	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 ESKSPYSGSS 670 680 690 700 710 720 YSRSSYTYSK SRSGSTRSRS YSRSFSRSHS RSYSRSPPYP RRGRGKSRNY RSRSRSHGYH 730 740 750 760 770 780 RSRSRSPPYR RYHSRSRSPQ AFRGQSPNKR NVPQGETERE YFNRYREVPP PYDMKAYYGR 790 800 810 820 830 840 SVDFRDPFEK ERYREWERKY REWYEKYYKG YAAGAQPRPS ANRENFSPER FLPLNIRNSP 850 860 870 880 890 900 FTRGRREDYV GGQSHRSRNI GSNYPEKLSA RDGHNQKDNT KSKEKESENA PGDGKGNKHK 910 920 930 940 950 960 KHRKRRKGEE SEGFLNPELL ETSRKSREPT GVEENKTDSL FVLPSRDDAT PVRDEPMDAE 970 980 990 1000 1010 1020 SITFKSVSEK DKRERDKPKA KGDKTKRKND GSAVSKKENI VKPAKGPQEK VDGERERSPR 1030 1040 1050 1060 1070 1080 SEPPIKKAKE ETPKTDNTKS SSSSQKDEKI TGTPRKAHSK SAKEHQETKP VKEEKVKKDY 1090 1100 1110 1120 1130 1140 SKDVKSEKLT TKEEKAKKPN EKNKPLDNKG EKRKRKTEEK GVDKDFESSS MKISKLEVTE 1150 1160 1170 1180 1190 1200 IVKPSPKRKM EPDTEKMDRT PEKDKISLSA PAKKIKLNRE TGKKIGSTEN ISNTKEPSEK 1210 1220 1230 1240 1250 1260 LESTSSKVKQ EKVKGKVRRK VTGTEGSSST LVDYTSTSST GGSPVRKSEE KTDTKRTVIK 1270 1280 1290 1300 1310 1320 TMEEYNNDNT APAEDVIIMI QVPQSKWDKD DFESEEEDVK STQPISSVGK PASVIKNVST 1330 1340 1350 1360 1370 1380 KPSNIVKYPE KESEPSEKIQ KFTKDVSHEI IQHEVKSSKN SASSEKGKTK DRDYSVLEKE 1390 1400 1410 1420 1430 1440 NPEKRKNSTQ PEKESNLDRL NEQGNFKSLS QSSKEARTSD KHDSTRASSN KDFTPNRDKK 1450 1460 1470 1480 1490 1500 TDYDTREYSS SKRRDEKNEL TRRKDSPSRN KDSASGQKNK PREERDLPKK GTGDSKKSNS 1510 1520 1530 1540 1550 1560 SPSRDRKPHD HKATYDTKRP NEETKSVDKN PCKDREKHVL EARNNKESSG NKLLYILNPP 1570 1580 1590 1600 1610 1620 ETQVEKEQIT GQIDKSTVKP KPQLSHSSRL SSDLTRETDE AAFEPDYNES DSESNVSVKE 1630 1640 1650 1660 1670 1680 EESSGNISKD LKDKIVEKAK ESLDTAAVVQ VGISRNQSHS SPSVSPSRSH SPSGSQTRSH 1690 1700 1710 1720 1730 1740 SSSASSAESQ DSKKKKKKKE KKKHKKHKKH KKHKKHAGTE VELEKSQKHK HKKKKSKKNK 1750 DKEKEKEKDD QKVKSVTV
	Isoform 3 [UniParc]. Checksum: 18B6431D0D740828	FASTA	118	13,235
	10 20 30 40 50 60 MSCVHYKFSS KLNYDTVTFD GLHISLCDLK KQIMGREKLK AADCDLQITN AQTKEEYTDD 70 80 90 100 110 NALIPKNSSV IVRRIPIGGV KSTSKTYVIS RTEPAMATTK AVCKNTISHF FYTLLLPL
	Isoform 4 [UniParc]. Checksum: BC28F8CCB1EED8E5	FASTA	952	106,037
	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 TSSTGGSPVR KSEEKTDTKR TVIKTMEEYN NDNTAPAEDV IIMIQVPQSK 490 500 510 520 530 540 WDKDDFESEE EDVKSTQPIS SVGKPASVIK NVSTKPSNIV KYPEKESEPS EKIQKFTKDV 550 560 570 580 590 600 SHEIIQHEVK SSKNSASSEK GKTKDRDYSV LEKENPEKRK NSTQPEKESN LDRLNEQGNF 610 620 630 640 650 660 KSLSQSSKEA RTSDKHDSTR ASSNKDFTPN RDKKTDYDTR EYSSSKRRDE KNELTRRKDS 670 680 690 700 710 720 PSRNKDSASG QKNKPREERD LPKKGTGDSK KSNSSPSRDR KPHDHKATYD TKRPNEETKS 730 740 750 760 770 780 VDKNPCKDRE KHVLEARNNK ESSGNKLLYI LNPPETQVEK EQITGQIDKS TVKPKPQLSH 790 800 810 820 830 840 SSRLSSDLTR ETDEAAFEPD YNESDSESNV SVKEEESSGN ISKDLKDKIV EKAKESLDTA 850 860 870 880 890 900 AVVQVGISRN QSHSSPSVSP SRSHSPSGSQ TRSHSSSASS AESQDSKKKK KKKEKKKHKK 910 920 930 940 950 HKKHKKHKKH AGTEVELEKS QKHKHKKKKS KKNKDKEKEK EKDDQKVKSV TV

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.

IPI

IPI00166084.
IPI00337315.
IPI00376283.
IPI00744671.

PIR

A57640.
T50609.

RefSeq

NP_008841.2. NM_006910.4.
NP_061173.1. NM_018703.3.
NP_116015.2. NM_032626.5.

UniGene

Hs.188553.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C7H	NMR	-	A	1-81	[»]
2YSA	NMR	-	A	159-206	[»]
2YUR	NMR	-	A	246-309	[»]
3ZTG	NMR	-	A/B	249-335	[»]

ProteinModelPortal

Q7Z6E9.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q7Z6E9. 24 interactions.

MINT

MINT-1181085.

PTM databases

PhosphoSite

Q7Z6E9.

Polymorphism databases

DMDM

74762440.

Proteomic databases

PaxDb

Q7Z6E9.

PRIDE

Q7Z6E9.

Protocols and materials databases

DNASU

5930.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000319715; ENSP00000317872; ENSG00000122257.
ENST00000348022; ENSP00000316291; ENSG00000122257.
ENST00000381039; ENSP00000370427; ENSG00000122257.
ENST00000452655; ENSP00000390537; ENSG00000122257.

GeneID

5930.

KEGG

hsa:5930.

UCSC

uc002dmg.3. human.
uc002dmh.3. human.
uc002dmi.3. human.
uc010bxr.3. human.

Organism-specific databases

CTD

5930.

GeneCards

GC16P024458.

HGNC

HGNC:9889. RBBP6.

HPA

CAB032866.

MIM

600938. gene.

neXtProt

NX_Q7Z6E9.

PharmGKB

PA34253.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5222.

HOVERGEN

HBG061131.

InParanoid

Q7Z6E9.

KO

K10624.

OMA

HSNTIPT.

OrthoDB

EOG44TP8G.

PhylomeDB

Q7Z6E9.

Enzyme and pathway databases

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q7Z6E9.

Bgee

Q7Z6E9.

Genevestigator

Q7Z6E9.

GermOnline

ENSG00000122257. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.
4.10.60.10. 1 hit.

InterPro

IPR014891. DWNN_domain.
IPR001878. Znf_CCHC.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

Pfam

PF08783. DWNN. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view]

SMART

SM00184. RING. 1 hit.
SM00343. ZnF_C2HC. 1 hit.
[Graphical view]

SUPFAM

SSF57756. SSF57756. 1 hit.

PROSITE

PS51282. DWNN. 1 hit.
PS50158. ZF_CCHC. 1 hit.
PS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RBBP6. human.

EvolutionaryTrace

Q7Z6E9.

GenomeRNAi

5930.

NextBio

23102.

PMAP-CutDB

Q7Z6E9.

SOURCE

Search...

Entry information

Entry name

RBBP6_HUMAN

Accession

Primary (citable) accession number: Q7Z6E9
Secondary accession number(s): Q147T5 , 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:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.