Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q7Z6E9

- RBBP6_HUMAN

UniProt

Q7Z6E9 - RBBP6_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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. ubiquitin-protein transferase activity Source: UniProtKB
  4. 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
Complete GO annotation...

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-KW
  2. cytoplasm Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB-KW
  4. nucleus Source: HPA
Complete GO annotation...

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 – 2441Phosphoserine2 Publications
Modified residuei245 – 2451Phosphoserine2 Publications
Modified residuei246 – 2461Phosphoserine2 Publications
Modified residuei247 – 2471Phosphoserine2 Publications
Modified residuei360 – 3601Phosphoserine2 Publications
Modified residuei516 – 5161Phosphoserine5 Publications
Modified residuei770 – 7701Phosphoserine1 Publication
Modified residuei772 – 7721Phosphoserine1 Publication
Modified residuei780 – 7801Phosphoserine1 Publication
Modified residuei861 – 8611Phosphoserine2 Publications
Modified residuei984 – 9841PhosphothreonineBy similarity
Modified residuei1179 – 11791Phosphoserine5 Publications
Modified residuei1271 – 12711PhosphothreonineBy similarity
Modified residuei1277 – 12771Phosphoserine1 Publication
Modified residuei1328 – 13281Phosphoserine5 Publications
Modified residuei1468 – 14681Phosphothreonine1 Publication
Modified residuei1646 – 16461Phosphoserine1 Publication
Modified residuei1648 – 16481Phosphoserine2 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

BgeeiQ7Z6E9.
ExpressionAtlasiQ7Z6E9. baseline and differential.
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. 52 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.
GeneTreeiENSGT00610000086096.
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

        10         20         30         40         50
MSCVHYKFSS KLNYDTVTFD GLHISLCDLK KQIMGREKLK AADCDLQITN
60 70 80 90 100
AQTKEEYTDD NALIPKNSSV IVRRIPIGGV KSTSKTYVIS RTEPAMATTK
110 120 130 140 150
AIDDSSASIS LAQLTKTANL AEANASEEDK IKAMMSQSGH EYDPINYMKK
160 170 180 190 200
PLGPPPPSYT CFRCGKPGHY IKNCPTNGDK NFESGPRIKK STGIPRSFMM
210 220 230 240 250
EVKDPNMKGA MLTNTGKYAI PTIDAEAYAI GKKEKPPFLP EEPSSSSEED
260 270 280 290 300
DPIPDELLCL ICKDIMTDAV VIPCCGNSYC DECIRTALLE SDEHTCPTCH
310 320 330 340 350
QNDVSPDALI ANKFLRQAVN NFKNETGYTK RLRKQLPPPP PPIPPPRPLI
360 370 380 390 400
QRNLQPLMRS PISRQQDPLM IPVTSSSTHP APSISSLTSN QSSLAPPVSG
410 420 430 440 450
NPSSAPAPVP DITATVSISV HSEKSDGPFR DSDNKILPAA ALASEHSKGT
460 470 480 490 500
SSIAITALME EKGYQVPVLG TPSLLGQSLL HGQLIPTTGP VRINTARPGG
510 520 530 540 550
GRPGWEHSNK LGYLVSPPQQ IRRGERSCYR SINRGRHHSE RSQRTQGPSL
560 570 580 590 600
PATPVFVPVP PPPLYPPPPH TLPLPPGVPP PQFSPQFPPG QPPPAGYSVP
610 620 630 640 650
PPGFPPAPAN LSTPWVSSGV QTAHSNTIPT TQAPPLSREE FYREQRRLKE
660 670 680 690 700
EEKKKSKLDE FTNDFAKELM EYKKIQKERR RSFSRSKSPY SGSSYSRSSY
710 720 730 740 750
TYSKSRSGST RSRSYSRSFS RSHSRSYSRS PPYPRRGRGK SRNYRSRSRS
760 770 780 790 800
HGYHRSRSRS PPYRRYHSRS RSPQAFRGQS PNKRNVPQGE TEREYFNRYR
810 820 830 840 850
EVPPPYDMKA YYGRSVDFRD PFEKERYREW ERKYREWYEK YYKGYAAGAQ
860 870 880 890 900
PRPSANRENF SPERFLPLNI RNSPFTRGRR EDYVGGQSHR SRNIGSNYPE
910 920 930 940 950
KLSARDGHNQ KDNTKSKEKE SENAPGDGKG NKHKKHRKRR KGEESEGFLN
960 970 980 990 1000
PELLETSRKS REPTGVEENK TDSLFVLPSR DDATPVRDEP MDAESITFKS
1010 1020 1030 1040 1050
VSEKDKRERD KPKAKGDKTK RKNDGSAVSK KENIVKPAKG PQEKVDGERE
1060 1070 1080 1090 1100
RSPRSEPPIK KAKEETPKTD NTKSSSSSQK DEKITGTPRK AHSKSAKEHQ
1110 1120 1130 1140 1150
ETKPVKEEKV KKDYSKDVKS EKLTTKEEKA KKPNEKNKPL DNKGEKRKRK
1160 1170 1180 1190 1200
TEEKGVDKDF ESSSMKISKL EVTEIVKPSP KRKMEPDTEK MDRTPEKDKI
1210 1220 1230 1240 1250
SLSAPAKKIK LNRETGKKIG STENISNTKE PSEKLESTSS KVKQEKVKGK
1260 1270 1280 1290 1300
VRRKVTGTEG SSSTLVDYTS TSSTGGSPVR KSEEKTDTKR TVIKTMEEYN
1310 1320 1330 1340 1350
NDNTAPAEDV IIMIQVPQSK WDKDDFESEE EDVKSTQPIS SVGKPASVIK
1360 1370 1380 1390 1400
NVSTKPSNIV KYPEKESEPS EKIQKFTKDV SHEIIQHEVK SSKNSASSEK
1410 1420 1430 1440 1450
GKTKDRDYSV LEKENPEKRK NSTQPEKESN LDRLNEQGNF KSLSQSSKEA
1460 1470 1480 1490 1500
RTSDKHDSTR ASSNKDFTPN RDKKTDYDTR EYSSSKRRDE KNELTRRKDS
1510 1520 1530 1540 1550
PSRNKDSASG QKNKPREERD LPKKGTGDSK KSNSSPSRDR KPHDHKATYD
1560 1570 1580 1590 1600
TKRPNEETKS VDKNPCKDRE KHVLEARNNK ESSGNKLLYI LNPPETQVEK
1610 1620 1630 1640 1650
EQITGQIDKS TVKPKPQLSH SSRLSSDLTR ETDEAAFEPD YNESDSESNV
1660 1670 1680 1690 1700
SVKEEESSGN ISKDLKDKIV EKAKESLDTA AVVQVGISRN QSHSSPSVSP
1710 1720 1730 1740 1750
SRSHSPSGSQ TRSHSSSASS AESQDSKKKK KKKEKKKHKK HKKHKKHKKH
1760 1770 1780 1790
AGTEVELEKS QKHKHKKKKS KKNKDKEKEK EKDDQKVKSV TV
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. 52 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.
GeneTreei ENSGT00610000086096.
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

Bgeei Q7Z6E9.
ExpressionAtlasi Q7Z6E9. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 120 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

Dasty 3