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Protein

Retinoblastoma-binding protein 5

Gene

RBBP5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid (By similarity). As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation.By similarity1 Publication

GO - Molecular functioni

  • histone-lysine N-methyltransferase activity Source: Reactome
  • methylated histone binding Source: UniProtKB
  • transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  • beta-catenin-TCF complex assembly Source: Reactome
  • cellular response to DNA damage stimulus Source: MGI
  • histone H3-K4 methylation Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • response to estrogen Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SignaLinkiQ15291.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoblastoma-binding protein 5
Short name:
RBBP-5
Alternative name(s):
Retinoblastoma-binding protein RBQ-3
Gene namesi
Name:RBBP5
Synonyms:RBQ3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9888. RBBP5.

Subcellular locationi

GO - Cellular componenti

  • histone methyltransferase complex Source: UniProtKB
  • MLL1 complex Source: UniProtKB
  • MLL3/4 complex Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • Set1C/COMPASS complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34252.

Chemistry

ChEMBLiCHEMBL3137282.

Polymorphism and mutation databases

BioMutaiRBBP5.
DMDMi209572664.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 538538Retinoblastoma-binding protein 5PRO_0000051194Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei252 – 2521Phosphothreonine; by CDK11 Publication
Modified residuei350 – 3501PhosphoserineCombined sources
Modified residuei388 – 3881PhosphoserineCombined sources
Modified residuei389 – 3891PhosphoserineCombined sources
Modified residuei497 – 4971Phosphoserine; by CDK11 Publication
Modified residuei525 – 5251PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ15291.
MaxQBiQ15291.
PaxDbiQ15291.
PRIDEiQ15291.

PTM databases

iPTMnetiQ15291.
PhosphoSiteiQ15291.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiQ15291.
CleanExiHS_RBBP5.
ExpressionAtlasiQ15291. baseline and differential.
GenevisibleiQ15291. HS.

Organism-specific databases

HPAiHPA049042.
HPA058085.

Interactioni

Subunit structurei

Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7. Each complex is at least composed of ASH2L, RBBP5, WDR5, DPY30, one or more specific histone methyltransferases (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and KMT2B/MLL4), and the facultative components PAGR1, BAP18, CHD8, E2F6, HCFC1, HCFC2, HSP70, INO80C, KDM6A, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, MYST1/MOF, NCOA6, PAXIP1/PTIP, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9, TEX10 and alpha- and beta-tubulin. Interacts with WDR5 and ASH2L; the interaction is direct. Interacts with WDR82 and SETD1A. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ASH2LQ9UBL326EBI-592823,EBI-540797
CHD8Q9HCK82EBI-592823,EBI-1169146
CUL4AQ136193EBI-592823,EBI-456106
CXXC1Q9P0U46EBI-592823,EBI-949911
KMT2AQ031646EBI-592823,EBI-591370
PAXIP1Q6ZW4911EBI-592823,EBI-743225
SETD1AO150473EBI-592823,EBI-540779
WDR5P6196411EBI-592823,EBI-540834

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111864. 76 interactions.
DIPiDIP-29224N.
IntActiQ15291. 39 interactions.
MINTiMINT-3031197.
STRINGi9606.ENSP00000264515.

Structurei

Secondary structure

1
538
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni349 – 3524Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P4FX-ray2.35B371-381[»]
4X8NX-ray2.10B347-356[»]
4X8PX-ray2.20B344-355[»]
5F6KX-ray2.41D/F330-356[»]
5F6LX-ray1.90J330-356[»]
ProteinModelPortaliQ15291.
SMRiQ15291. Positions 30-320.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati22 – 6342WD 1Add
BLAST
Repeati64 – 10340WD 2Add
BLAST
Repeati148 – 18841WD 3Add
BLAST
Repeati196 – 23540WD 4Add
BLAST
Repeati249 – 29143WD 5Add
BLAST
Repeati293 – 33139WD 6Add
BLAST

Sequence similaritiesi

Contains 6 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG1273. Eukaryota.
ENOG410XTA2. LUCA.
GeneTreeiENSGT00530000064100.
HOVERGENiHBG054324.
InParanoidiQ15291.
KOiK14961.
OMAiEQGVIEW.
OrthoDBiEOG7S21X6.
PhylomeDBiQ15291.
TreeFamiTF313289.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 1 hit.
[Graphical view]
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
PROSITEiPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15291-1) [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
MNLELLESFG QNYPEEADGT LDCISMALTC TFNRWGTLLA VGCNDGRIVI
60 70 80 90 100
WDFLTRGIAK IISAHIHPVC SLCWSRDGHK LVSASTDNIV SQWDVLSGDC
110 120 130 140 150
DQRFRFPSPI LKVQYHPRDQ NKVLVCPMKS APVMLTLSDS KHVVLPVDDD
160 170 180 190 200
SDLNVVASFD RRGEYIYTGN AKGKILVLKT DSQDLVASFR VTTGTSNTTA
210 220 230 240 250
IKSIEFARKG SCFLINTADR IIRVYDGREI LTCGRDGEPE PMQKLQDLVN
260 270 280 290 300
RTPWKKCCFS GDGEYIVAGS ARQHALYIWE KSIGNLVKIL HGTRGELLLD
310 320 330 340 350
VAWHPVRPII ASISSGVVSI WAQNQVENWS AFAPDFKELD ENVEYEERES
360 370 380 390 400
EFDIEDEDKS EPEQTGADAA EDEEVDVTSV DPIAAFCSSD EELEDSKALL
410 420 430 440 450
YLPIAPEVED PEENPYGPPP DAVQTSLMDE GASSEKKRQS SADGSQPPKK
460 470 480 490 500
KPKTTNIELQ GVPNDEVHPL LGVKGDGKSK KKQAGRPKGS KGKEKDSPFK
510 520 530
PKLYKGDRGL PLEGSAKGKV QAELSQPLTA GGAISELL
Length:538
Mass (Da):59,153
Last modified:October 14, 2008 - v2
Checksum:i095CCB41613CBED9
GO
Isoform 2 (identifier: Q15291-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     492-529: Missing.

Show »
Length:500
Mass (Da):55,072
Checksum:i45E9CCD4E2448FA5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti206 – 2061F → Y in BAF82826 (PubMed:14702039).Curated
Sequence conflicti244 – 2441K → E in CAA59446 (PubMed:7558034).Curated
Sequence conflicti351 – 3511E → G in CAA59446 (PubMed:7558034).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei492 – 52938Missing in isoform 2. 2 PublicationsVSP_035583Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85134 mRNA. Translation: CAA59446.1.
AK290137 mRNA. Translation: BAF82826.1.
AL583832, AC093422 Genomic DNA. Translation: CAI15286.1.
AL583832, AC093422 Genomic DNA. Translation: CAI15287.1.
CH471067 Genomic DNA. Translation: EAW91537.1.
CH471067 Genomic DNA. Translation: EAW91538.1.
BC037284 mRNA. Translation: AAH37284.1.
BC053856 mRNA. Translation: AAH53856.1.
BC075059 mRNA. Translation: AAH75059.1.
BC075060 mRNA. Translation: AAH75060.1.
CCDSiCCDS30983.1. [Q15291-1]
CCDS53463.1. [Q15291-2]
PIRiA57624.
RefSeqiNP_001180201.1. NM_001193272.1. [Q15291-2]
NP_001180202.1. NM_001193273.1.
NP_005048.2. NM_005057.3. [Q15291-1]
UniGeneiHs.519230.

Genome annotation databases

EnsembliENST00000264515; ENSP00000264515; ENSG00000117222. [Q15291-1]
ENST00000367164; ENSP00000356132; ENSG00000117222. [Q15291-2]
GeneIDi5929.
KEGGihsa:5929.
UCSCiuc001hbu.3. human. [Q15291-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85134 mRNA. Translation: CAA59446.1.
AK290137 mRNA. Translation: BAF82826.1.
AL583832, AC093422 Genomic DNA. Translation: CAI15286.1.
AL583832, AC093422 Genomic DNA. Translation: CAI15287.1.
CH471067 Genomic DNA. Translation: EAW91537.1.
CH471067 Genomic DNA. Translation: EAW91538.1.
BC037284 mRNA. Translation: AAH37284.1.
BC053856 mRNA. Translation: AAH53856.1.
BC075059 mRNA. Translation: AAH75059.1.
BC075060 mRNA. Translation: AAH75060.1.
CCDSiCCDS30983.1. [Q15291-1]
CCDS53463.1. [Q15291-2]
PIRiA57624.
RefSeqiNP_001180201.1. NM_001193272.1. [Q15291-2]
NP_001180202.1. NM_001193273.1.
NP_005048.2. NM_005057.3. [Q15291-1]
UniGeneiHs.519230.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P4FX-ray2.35B371-381[»]
4X8NX-ray2.10B347-356[»]
4X8PX-ray2.20B344-355[»]
5F6KX-ray2.41D/F330-356[»]
5F6LX-ray1.90J330-356[»]
ProteinModelPortaliQ15291.
SMRiQ15291. Positions 30-320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111864. 76 interactions.
DIPiDIP-29224N.
IntActiQ15291. 39 interactions.
MINTiMINT-3031197.
STRINGi9606.ENSP00000264515.

Chemistry

ChEMBLiCHEMBL3137282.

PTM databases

iPTMnetiQ15291.
PhosphoSiteiQ15291.

Polymorphism and mutation databases

BioMutaiRBBP5.
DMDMi209572664.

Proteomic databases

EPDiQ15291.
MaxQBiQ15291.
PaxDbiQ15291.
PRIDEiQ15291.

Protocols and materials databases

DNASUi5929.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264515; ENSP00000264515; ENSG00000117222. [Q15291-1]
ENST00000367164; ENSP00000356132; ENSG00000117222. [Q15291-2]
GeneIDi5929.
KEGGihsa:5929.
UCSCiuc001hbu.3. human. [Q15291-1]

Organism-specific databases

CTDi5929.
GeneCardsiRBBP5.
H-InvDBHIX0023636.
HGNCiHGNC:9888. RBBP5.
HPAiHPA049042.
HPA058085.
MIMi600697. gene.
neXtProtiNX_Q15291.
PharmGKBiPA34252.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1273. Eukaryota.
ENOG410XTA2. LUCA.
GeneTreeiENSGT00530000064100.
HOVERGENiHBG054324.
InParanoidiQ15291.
KOiK14961.
OMAiEQGVIEW.
OrthoDBiEOG7S21X6.
PhylomeDBiQ15291.
TreeFamiTF313289.

Enzyme and pathway databases

ReactomeiR-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SignaLinkiQ15291.

Miscellaneous databases

GeneWikiiRBBP5.
GenomeRNAii5929.
PROiQ15291.
SOURCEiSearch...

Gene expression databases

BgeeiQ15291.
CleanExiHS_RBBP5.
ExpressionAtlasiQ15291. baseline and differential.
GenevisibleiQ15291. HS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 1 hit.
[Graphical view]
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
PROSITEiPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a human protein that binds to the retinoblastoma protein and chromosomal mapping."
    Saijo M., Sakai Y., Kishino T., Niikawa N., Matsuura Y., Morino K., Tamai K., Taya Y.
    Genomics 27:511-519(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT THR-252 AND SER-497, CHARACTERIZATION.
    Tissue: Lung carcinoma and Testis.
  2. "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] (ISOFORM 2).
    Tissue: Thalamus.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 1 AND 2).
    Tissue: Brain and Testis.
  6. Cited for: IDENTIFICATION IN THE MEN1-ASSOCIATED HISTONE METHYLTRANSFERASE COMPLEX.
  7. "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression."
    Yokoyama A., Wang Z., Wysocka J., Sanyal M., Aufiero D.J., Kitabayashi I., Herr W., Cleary M.L.
    Mol. Cell. Biol. 24:5639-5649(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL-LIKE COMPLEX.
  8. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
    Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
    Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
  9. "CpG-binding protein (CXXC finger protein 1) is a component of the mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of the yeast Set1/COMPASS complex."
    Lee J.-H., Skalnik D.G.
    J. Biol. Chem. 280:41725-41731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SET1 COMPLEX.
  10. "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-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Identification and characterization of the human Set1B histone H3-Lys4 methyltransferase complex."
    Lee J.-H., Tate C.M., You J.-S., Skalnik D.G.
    J. Biol. Chem. 282:13419-13428(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE SET1 COMPLEX.
  12. "PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex."
    Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T., Dressler G.R., Copeland T.D., Kalkum M., Ge K.
    J. Biol. Chem. 282:20395-20406(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MLL2/3 COMPLEX.
  13. "Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A Histone H3-Lys4 methyltransferase complex to transcription start sites of transcribed human genes."
    Lee J.H., Skalnik D.G.
    Mol. Cell. Biol. 28:609-618(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN SET1 COMPLEX, INTERACTION WITH SETD1A.
  14. "Molecular regulation of H3K4 trimethylation by Wdr82, a component of human Set1/COMPASS."
    Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M., Shilatifard A.
    Mol. Cell. Biol. 28:7337-7344(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN SET1 COMPLEX, INTERACTION WITH WDR82.
  15. "Identification and characterization of a novel nuclear protein complex involved in nuclear hormone receptor-mediated gene regulation."
    Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.
    J. Biol. Chem. 284:7542-7552(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH HCFC1; MKI67; EMSY; MATR3; HSPA8; ZNF335; CCAR2; ASCL2; ZNF335 AND WDR5.
  16. "On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex."
    Patel A., Dharmarajan V., Vought V.E., Cosgrove M.S.
    J. Biol. Chem. 284:24242-24256(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION OF THE MLL1/MLL COMPLEX, INTERACTION WITH WDR5 AND ASH2L.
  17. "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-388 AND SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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-525, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: INTERACTION WITH ZNF335.

Entry informationi

Entry nameiRBBP5_HUMAN
AccessioniPrimary (citable) accession number: Q15291
Secondary accession number(s): A8K272, Q7Z6D8, Q8NDZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: October 14, 2008
Last modified: June 8, 2016
This is version 154 of the entry and version 2 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.