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P97868 (RBBP6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·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 protein 6
p53-associated cellular protein of testis
Gene names
Name:Rbbp6
Synonyms:P2pr, Pact
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1790 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 By similarity. May play a role as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in increase of MDM2-mediated ubiquitination and degradation of p53/TP53; may function as negative regulator of p53/TP53, leading to both apoptosis and cell growth retardation. Ref.11

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with MDM2 and YBX1 By similarity. Interacts also with p53/TP53 and RB1. Interacts with NEK6 By similarity. Ref.4 Ref.5 Ref.9

Subcellular location

Nucleus › nucleolus. Chromosome. Cytoplasm › cytoskeleton › centrosome By similarity. Note: Colocalizes with mitotic chromosomes. Co-localizes with NEK6 in the centrosome By similarity. Ref.5 Ref.6 Ref.8

Tissue specificity

Highly expressed in testis. Expressed at lower levels in brain, heart, kidney, liver, lung, skeletal muscle, spleen, thymus and tongue. Ref.4 Ref.5

Developmental stage

Expression is reduced during terminal differentiation. Expression is induced in the G2/M phase of the cell cycle (at protein level). Ref.4 Ref.6

Post-translational modification

Phosphorylated by NEK6 By similarity.

Disruption phenotype

Early embryonic lethality before E7.5, accompanied by accumulation of p53 and widespread apoptosis. Ref.11

Sequence similarities

Contains 1 CCHC-type zinc finger.

Contains 1 DWNN domain.

Contains 1 RING-type zinc finger.

Sequence caution

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P97868-1)

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: P97868-2)

The sequence of this isoform differs from the canonical sequence as follows:
     653-686: Missing.
Isoform 3 (identifier: P97868-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17901790E3 ubiquitin-protein ligase RBBP6
PRO_0000234355

Regions

Domain4 – 7673DWNN
Zinc finger160 – 17718CCHC-type
Zinc finger260 – 30142RING-type; degenerate
Region983 – 1139157Interaction with RB1
Region1434 – 1544111Interaction with p53

Amino acid modifications

Modified residue2451Phosphoserine By similarity
Modified residue2461Phosphoserine By similarity
Modified residue2471Phosphoserine By similarity
Modified residue2481Phosphoserine By similarity
Modified residue3611Phosphoserine By similarity
Modified residue5171Phosphoserine By similarity
Modified residue7711Phosphoserine Ref.12
Modified residue7731Phosphoserine Ref.12 Ref.13
Modified residue7811Phosphoserine By similarity
Modified residue8621Phosphoserine Ref.12
Modified residue11791Phosphoserine Ref.12 Ref.13
Modified residue12721Phosphothreonine Ref.10
Modified residue12781Phosphoserine Ref.10
Modified residue13291Phosphoserine Ref.13
Modified residue14691Phosphothreonine By similarity
Modified residue16461Phosphoserine By similarity
Modified residue16481Phosphoserine By similarity

Natural variations

Alternative sequence102 – 12322IDDAS…NLAEA → VCKNTITLFLHNCFYLYNVS VT in isoform 3.
VSP_018285
Alternative sequence124 – 17561633Missing in isoform 3.
VSP_018286
Alternative sequence653 – 68634Missing in isoform 2.
VSP_018287

Experimental info

Sequence conflict2541I → F in AAB49620. Ref.5
Sequence conflict317 – 3182RQ → GR in AAC72432. Ref.4
Sequence conflict3411P → H in AAB49620. Ref.5
Sequence conflict4181S → F in AAC72432. Ref.4
Sequence conflict4211V → S in AAB49620. Ref.5
Sequence conflict5801P → L in AAC72432. Ref.4
Sequence conflict5951P → T in AAC72432. Ref.4
Sequence conflict615 – 6228PWVSSGVQ → ACFSPGVP in AAC72432. Ref.4
Sequence conflict6291I → M in AAC72432. Ref.4
Sequence conflict6361P → L in AAC72432. Ref.4
Sequence conflict6471R → K in AAC72432. Ref.4
Sequence conflict6891S → F in AAC72432. Ref.4
Sequence conflict7031Y → D in AAC72432. Ref.4
Sequence conflict7891Q → R in AAC72432. Ref.4
Sequence conflict9401R → Q in BAE36255. Ref.1
Sequence conflict9411R → RNEE in AAC72432. Ref.4
Sequence conflict956 – 9583ETS → GKF in AAC72432. Ref.4
Sequence conflict9631E → G in AAC72432. Ref.4
Sequence conflict9781L → F in AAC72432. Ref.4
Sequence conflict9821D → E in AAC72432. Ref.4
Sequence conflict10121K → N in AAB49620. Ref.5
Sequence conflict12901K → T in AAC72432. Ref.4
Sequence conflict13161Q → H in AAC72432. Ref.4
Sequence conflict15641N → I in AAC72432. Ref.4
Sequence conflict15811E → D in AAC72432. Ref.4
Sequence conflict15911P → L in AAC72432. Ref.4
Sequence conflict15961P → L in AAC72432. Ref.4
Sequence conflict16041A → V in AAC72432. Ref.4

Sequences

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

Last modified May 16, 2006. Version 5.
Checksum: 3909C30EB9DD2CE3

FASTA1,790199,587
        10         20         30         40         50         60 
MSCVHYKFSS KLNYDTVTFD GLHISLCDLK KQIMGREKLK AADSDLQITN AQTKEEYTDD 

        70         80         90        100        110        120 
NALIPKNSSV IVRRIPIGGV KSTSKTYVIS RTEPVMGTTK AIDDASASIS LAQLTKTANL 

       130        140        150        160        170        180 
AEANASEEDK IKAMMSQSGH EYDPINYMKK TLVGPPPPSY TCFRCGKPGH YIKNCPTNGD 

       190        200        210        220        230        240 
KNFESGPRIK KSTGIPRSFM MEVKDPNMKG AMLTNTGKYA IPTIDAEAYA IGKKEKPPFL 

       250        260        270        280        290        300 
PEEPSSSSEE DDPIPDELLC LICKDIMTDA VVIPCCGNSY CDECIRTALL ESDEHTCPTC 

       310        320        330        340        350        360 
HQNDVSPDAL IANKFLRQAV NNFKNETGYT KRLRKQLPPP PPPVPPPRPL MQRNLQPLMR 

       370        380        390        400        410        420 
SPISRQQDPL MIPVTSSSAH SAPSISSLTS NPSALAPSVS GNPSSAPAPV PDITATVSIS 

       430        440        450        460        470        480 
VHSEKSDGPF RDSDNKLLPA AALTSEHSKG ASSIAITALM EEKGYQVPVL GTPSLLGQSL 

       490        500        510        520        530        540 
LHGQLIPTTG PVRINAARPG GGRPGWEHSN KLGYLVSPPQ QIRRGERSCY RSINRGRHHS 

       550        560        570        580        590        600 
ERSQRTQGPS LPATPVFVPV PPPPLYPPPP HTLPLPPGVP PPQFSPQFPP GQPPPAGYSV 

       610        620        630        640        650        660 
PPPGFPPAPA NISTPWVSSG VQTAHSNTIP TTQAPPLSRE EFYREQRRLK EEEKKKSKLD 

       670        680        690        700        710        720 
EFTNDFAKEL MEYKKIQKER RRSFSRSKSP YSGSSYSRSS YTYSKSRSGS TRSRSYSRSF 

       730        740        750        760        770        780 
SRSHSRSYSR SPPYPRRGRG KSRNYRSRSR SHGYHRSRSR SPPYRRYHSR SRSPQAFRGQ 

       790        800        810        820        830        840 
SPTKRNVPQG ETEREYFNRY REVPPPYDIK AYYGRSVDFR DPFEKERYRE WERKYREWYE 

       850        860        870        880        890        900 
KYYKGYAVGA QPRPSANRED FSPERLLPLN IRNSPFTRGR REDYAAGQSH RNRNLGGNYP 

       910        920        930        940        950        960 
EKLSTRDSHN AKDNPKSKEK ESENVPGDGK GNKHKKHRKR RKGEESESFL NPELLETSRK 

       970        980        990       1000       1010       1020 
CRESSGIDET KTDTLFVLPS RDDATPVRDE PMDAESITFK SVSDKDKREK DKPKVKSDKT 

      1030       1040       1050       1060       1070       1080 
KRKSDGSATA KKDNVLKPSK GPQEKVDGDR EKSPRSEPPL KKAKEEATKI DSVKPSSSSQ 

      1090       1100       1110       1120       1130       1140 
KDEKVTGTPR KAHSKSAKEH QEAKPAKDEK VKKDCSKDIK SEKPASKDEK AKKPEKNKLL 

      1150       1160       1170       1180       1190       1200 
DSKGEKRKRK TEEKSVDKDF ESSSMKISKV EGTEIVKPSP KRKMEGDVEK LERTPEKDKI 

      1210       1220       1230       1240       1250       1260 
ASSTTPAKKI KLNRETGKKI GNAENASTTK EPSEKLESTS SKIKQEKVKG KAKRKVAGSE 

      1270       1280       1290       1300       1310       1320 
GSSSTLVDYT STSSTGGSPV RKSEEKTDTK RTVIKTMEEY NNDNTAPAED VIIMIQVPQS 

      1330       1340       1350       1360       1370       1380 
KWDKDDFESE EEDVKTTQPI QSVGKPSSII KNVTTKPSAT AKYTEKESEQ PEKLQKLPKE 

      1390       1400       1410       1420       1430       1440 
ASHELMQHEL RSSKGSASSE KGRAKDREHS GSEKDNPDKR KSGAQPDKES TVDRLSEQGH 

      1450       1460       1470       1480       1490       1500 
FKTLSQSSKE TRTSEKHESV RGSSNKDFTP GRDKKVDYDS RDYSSSKRRD ERGELARRKD 

      1510       1520       1530       1540       1550       1560 
SPPRGKESLS GQKSKLREER DLPKKGAESK KSNSSPPRDK KPHDHKAPYE TKRPCEETKP 

      1570       1580       1590       1600       1610       1620 
VDKNSGKERE KHAAEARNGK ESSGGKLPCI PNPPDPPMEK ELAAGQVEKS AVKPKPQLSH 

      1630       1640       1650       1660       1670       1680 
SSRLSSDLTR ETDEAAFEPD YNESDSESNV SVKEEEAVAS ISKDLKEKTT EKAKESLTVA 

      1690       1700       1710       1720       1730       1740 
TASQPGADRS QSQSSPSVSP SRSHSPSGSQ TRSHSSSASS AGSQDSKKKK KKKEKKKHKK 

      1750       1760       1770       1780       1790 
HKKHKKHKKH AGADGDVEKS QKHKHKKKKA KKNKDKEKEK DDQKVRSVTV

« Hide

Isoform 2 [UniParc].

Checksum: E3C0F009CC28107E
Show »

FASTA1,756195,310
Isoform 3 [UniParc].

Checksum: 39B749141C9B2FA6
Show »

FASTA15717,888

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 546-1148 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1356-1790 (ISOFORMS 1/2).
Strain: C57BL/6J.
Tissue: Corpora quadrigemina, Corpus striatum, Embryo, Head and Lung.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Strain: FVB/N-3.
Tissue: Mammary tumor.
[4]"The proliferation potential protein-related (P2P-R) gene with domains encoding heterogeneous nuclear ribonucleoprotein association and Rb1 binding shows repressed expression during terminal differentiation."
Witte M.M., Scott R.E.
Proc. Natl. Acad. Sci. U.S.A. 94:1212-1217(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 154-1790 (ISOFORM 2), INTERACTION WITH RB1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: BALB/c.
[5]"PACT: cloning and characterization of a cellular p53 binding protein that interacts with Rb."
Simons A., Melamed-Bessudo C., Wolkowicz R., Sperling J., Sperling R., Eisenbach L., Rotter V.
Oncogene 14:145-155(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 204-1790 (ISOFORM 1), INTERACTION WITH TP53 AND RB1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: BALB/c.
Tissue: Testis.
[6]"P2P-R protein localizes to the nucleolus of interphase cells and the periphery of chromosomes in mitotic cells which show maximum P2P-R immunoreactivity."
Gao S., Witte M.M., Scott R.E.
J. Cell. Physiol. 191:145-154(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[7]Erratum
Gao S., Witte M.M., Scott R.E.
J. Cell. Physiol. 192:359-360(2002)
[8]"P2P-R protein overexpression restricts mitotic progression at prometaphase and promotes mitotic apoptosis."
Gao S., Scott R.E.
J. Cell. Physiol. 193:199-207(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Stable overexpression of specific segments of the P2P-R protein in human MCF-7 cells promotes camptothecin-induced apoptosis."
Gao S., Scott R.E.
J. Cell. Physiol. 197:445-452(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TP53.
[10]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1272 AND SER-1278, MASS SPECTROMETRY.
Tissue: Liver.
[11]"PACT is a negative regulator of p53 and essential for cell growth and embryonic development."
Li L., Deng B., Xing G., Teng Y., Tian C., Cheng X., Yin X., Yang J., Gao X., Zhu Y., Sun Q., Zhang L., Yang X., He F.
Proc. Natl. Acad. Sci. U.S.A. 104:7951-7956(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[12]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-771; SER-773; SER-862 AND SER-1179, MASS SPECTROMETRY.
Tissue: Melanoma.
[13]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-773; SER-1179 AND SER-1329, MASS SPECTROMETRY.
Tissue: Macrophage.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK045635 mRNA. Translation: BAC32441.1.
AK079129 mRNA. Translation: BAC37553.1.
AK081261 mRNA. Translation: BAC38179.1.
AK144758 mRNA. Translation: BAE26051.1.
AK160656 mRNA. Translation: BAE35944.1.
AK161231 mRNA. Translation: BAE36255.1.
AC125221 Genomic DNA. No translation available.
BC025874 mRNA. Translation: AAH25874.1.
U83913 mRNA. Translation: AAC72432.1. Frameshift.
U28789 mRNA. Translation: AAB49620.1.
IPIIPI00153709.
IPI00551082.
IPI00551482.
PIRT42727.
RefSeqNP_035377.2. NM_011247.2.
NP_778188.1. NM_175023.3.
UniGeneMm.4480.

3D structure databases

ProteinModelPortalP97868.
SMRP97868. Positions 1-81, 160-207, 250-336.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000049528.

PTM databases

PhosphoSiteP97868.

Proteomic databases

PaxDbP97868.
PRIDEP97868.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000052135; ENSMUSP00000049528; ENSMUSG00000030779.
ENSMUST00000071590; ENSMUSP00000071519; ENSMUSG00000030779.
ENSMUST00000098062; ENSMUSP00000095670; ENSMUSG00000030779.
GeneID19647.
KEGGmmu:19647.
UCSCuc009jow.2. mouse.
uc009joy.2. mouse.

Organism-specific databases

CTD5930.
MGIMGI:894835. Rbbp6.

Phylogenomic databases

eggNOGCOG5222.
GeneTreeENSGT00610000086096.
HOVERGENHBG093889.
InParanoidP97868.
KOK10624.
OMAHSNTIPT.
OrthoDBEOG44TP8G.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressP97868.
BgeeP97868.
CleanExMM_RBBP6.
GenevestigatorP97868.
GermOnlineENSMUSG00000030779. Mus musculus.

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]
PROSITEPS51282. DWNN. 1 hit.
PS50158. ZF_CCHC. 1 hit.
PS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRBBP6. mouse.
NextBio296898.
SOURCESearch...

Entry information

Entry nameRBBP6_MOUSE
AccessionPrimary (citable) accession number: P97868
Secondary accession number(s): P70287 expand/collapse secondary AC list , Q3TTR9, Q3TUM7, Q3UMP7, Q4U217, Q7TT06, Q8BNY8, Q8R399
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: April 3, 2013
This is version 104 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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