P28749 (RBL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Retinoblastoma-like protein 1

Alternative name(s):
107 kDa retinoblastoma-associated protein
Short name=p107
pRb1

Gene names

Name:

RBL1

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	1068 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Key regulator of entry into cell division. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. Potent inhibitor of E2F-mediated trans-activation. Forms a complex with adenovirus E1A and with SV40 large T antigen. May bind and modulate functionally certain cellular proteins with which T and E1A compete for pocket binding. May act as a tumor suppressor.
Subunit structure	Interacts with SUV420H1, SUV420H2 and USP4 By similarity. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2. Interacts with AATF. Interacts with KDM5A. Interacts with SV40 and JC virus large T antigens. Ref.9 Ref.10 Ref.11 Ref.13 Ref.14
Subcellular location	Nucleus Potential.
Post-translational modification	Exists in both phosphorylated and unphosphorylated forms, and T, but not E1A, binds only to the unphosphorylated form. Cell-cycle arrest properties are inactivated by phosphorylation on Thr-332, Ser-640, Ser-964 and Ser-975 by CDK4. Ref.8 Ref.12
Sequence similarities	Belongs to the retinoblastoma protein (RB) family.

Ontologies

Keywords
Biological process	Cell cycle Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Tumor suppressor
Molecular function	Chromatin regulator Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G1 phase of mitotic cell cycle Traceable author statement. Source: Reactome chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: Reactome regulation of cell cycle Inferred from electronic annotation. Source: InterPro regulation of lipid kinase activity Inferred from direct assay PubMed 16286473. Source: UniProtKB transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome transcription factor complex Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BEGAIN	Q9BUH8	2	EBI-971402,EBI-742722
CDK4	P11802	2	EBI-971402,EBI-295644
DGKZ	Q13574-2	2	EBI-971402,EBI-715527
IRF3	Q14653	2	EBI-971402,EBI-2650369
Pax3	P24610	3	EBI-971402,EBI-1208116	From a different organism.
Sirt1	Q923E4	2	EBI-971402,EBI-1802585	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P28749-1)

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: P28749-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1013-1068: SLKDINNMIRQGEQRTKKRVIAIDSDAESPAKRVCQENDDVLLKRLQDVVSERANH → VR

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1068	1068	Retinoblastoma-like protein 1		PRO_0000167839
Regions
	Region	385 – 949	565	Pocket; binds T and E1A
	Region	385 – 584	200	Domain A
	Region	585 – 780	196	Spacer
	Region	781 – 949	169	Domain B
Amino acid modifications
	Modified residue	332	1	Phosphothreonine; by CDK2 Ref.8
	Modified residue	369	1	Phosphothreonine; by CDK4 Ref.8 Ref.12
	Modified residue	385	1	Phosphothreonine; by CDK2 Ref.8 Ref.15
	Modified residue	640	1	Phosphoserine; by CDK2 and CDK4 Ref.8
	Modified residue	650	1	Phosphoserine Ref.12
	Modified residue	749	1	Phosphoserine Ref.15
	Modified residue	762	1	Phosphoserine; by CDK2 Ref.8 Ref.15
	Modified residue	964	1	Phosphoserine; by CDK2 and CDK4 Ref.8
	Modified residue	975	1	Phosphoserine; by CDK2 and CDK4 Ref.8
	Modified residue	988	1	Phosphoserine; by CDK2 Ref.8
	Modified residue	997	1	Phosphothreonine; by CDK2 Ref.8
	Modified residue	1009	1	Phosphoserine; by CDK2 Ref.8
Natural variations
	Alternative sequence	1013 – 1068	56	SLKDI…ERANH → VR in isoform 2.		VSP_017496
	Natural variant	1035	1	I → M. Corresponds to variant rs8114297 [ dbSNP | Ensembl ].		VAR_034443
Experimental info
	Mutagenesis	640	1	S → A: Strongly reduces phosphorylation by CDK2 and CDK4. Ref.8
	Mutagenesis	643	1	S → R: No effect on S-640 phosphorylation, but strongly increases S-640 phosphorylation; when associated with 657-A--A-660. Ref.8
	Mutagenesis	650	1	S → A: No effect on phosphorylation by CDK2. Ref.8
	Mutagenesis	657 – 660	4	KRRL → AAAA: Reduces S-640 phosphorylation by CDK2 and CDK4. Ref.8
	Sequence conflict	326	1	Missing AA sequence Ref.8
	Sequence conflict	928	1	G → S Ref.1
	Sequence conflict	928	1	G → S Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 7, 2006. Version 3. Checksum: 2BC4876EA04BDB31	FASTA	1,068	120,847
	10 20 30 40 50 60 MFEDKPHAEG AAVVAAAGEA LQALCQELNL DEGSAAEALD DFTAIRGNYS LEGEVTHWLA 70 80 90 100 110 120 CSLYVACRKS IIPTVGKGIM EGNCVSLTRI LRSAKLSLIQ FFSKMKKWMD MSNLPQEFRE 130 140 150 160 170 180 RIERLERNFE VSTVIFKKYE PIFLDIFQNP YEEPPKLPRS RKQRRIPCSV KDLFNFCWTL 190 200 210 220 230 240 FVYTKGNFRM IGDDLVNSYH LLLCCLDLIF ANAIMCPNRQ DLLNPSFKGL PSDFHTADFT 250 260 270 280 290 300 ASEEPPCIIA VLCELHDGLL VEAKGIKEHY FKPYISKLFD RKILKGECLL DLSSFTDNSK 310 320 330 340 350 360 AVNKEYEEYV LTVGDFDERI FLGADAEEEI GTPRKFTRDT PLGKLTAQAN VEYNLQQHFE 370 380 390 400 410 420 KKRSFAPSTP LTGRRYLREK EAVITPVASA TQSVSRLQSI VAGLKNAPSD QLINIFESCV 430 440 450 460 470 480 RNPVENIMKI LKGIGETFCQ HYTQSTDEQP GSHIDFAVNR LKLAEILYYK ILETVMVQET 490 500 510 520 530 540 RRLHGMDMSV LLEQDIFHRS LMACCLEIVL FAYSSPRTFP WIIEVLNLQP FYFYKVIEVV 550 560 570 580 590 600 IRSEEGLSRD MVKHLNSIEE QILESLAWSH DSALWEALQV SANKVPTCEE VIFPNNFETG 610 620 630 640 650 660 NGGNVQGHLP LMPMSPLMHP RVKEVRTDSG SLRRDMQPLS PISVHERYSS PTAGSAKRRL 670 680 690 700 710 720 FGEDPPKEML MDKIITEGTK LKIAPSSSIT AENVSILPGQ TLLTMATAPV TGTTGHKVTI 730 740 750 760 770 780 PLHGVANDAG EITLIPLSMN TNQESKVKSP VSLTAHSLIG ASPKQTNLTK AQEVHSTGIN 790 800 810 820 830 840 RPKRTGSLAL FYRKVYHLAS VRLRDLCLKL DVSNELRRKI WTCFEFTLVH CPDLMKDRHL 850 860 870 880 890 900 DQLLLCAFYI MAKVTKEERT FQEIMKSYRN QPQANSHVYR SVLLKSIPRE VVAYNKNIND 910 920 930 940 950 960 DFEMIDCDLE DATKTPDCSS GPVKEERGDL IKFYNTIYVG RVKSFALKYD LANQDHMMDA 970 980 990 1000 1010 1020 PPLSPFPHIK QQPGSPRRIS QQHSIYISPH KNGSGLTPRS ALLYKFNGSP SKSLKDINNM 1030 1040 1050 1060 IRQGEQRTKK RVIAIDSDAE SPAKRVCQEN DDVLLKRLQD VVSERANH
	Isoform 2 [UniParc]. Checksum: CE1D47DBF365C4CB	FASTA	1,014	114,688
	10 20 30 40 50 60 MFEDKPHAEG AAVVAAAGEA LQALCQELNL DEGSAAEALD DFTAIRGNYS LEGEVTHWLA 70 80 90 100 110 120 CSLYVACRKS IIPTVGKGIM EGNCVSLTRI LRSAKLSLIQ FFSKMKKWMD MSNLPQEFRE 130 140 150 160 170 180 RIERLERNFE VSTVIFKKYE PIFLDIFQNP YEEPPKLPRS RKQRRIPCSV KDLFNFCWTL 190 200 210 220 230 240 FVYTKGNFRM IGDDLVNSYH LLLCCLDLIF ANAIMCPNRQ DLLNPSFKGL PSDFHTADFT 250 260 270 280 290 300 ASEEPPCIIA VLCELHDGLL VEAKGIKEHY FKPYISKLFD RKILKGECLL DLSSFTDNSK 310 320 330 340 350 360 AVNKEYEEYV LTVGDFDERI FLGADAEEEI GTPRKFTRDT PLGKLTAQAN VEYNLQQHFE 370 380 390 400 410 420 KKRSFAPSTP LTGRRYLREK EAVITPVASA TQSVSRLQSI VAGLKNAPSD QLINIFESCV 430 440 450 460 470 480 RNPVENIMKI LKGIGETFCQ HYTQSTDEQP GSHIDFAVNR LKLAEILYYK ILETVMVQET 490 500 510 520 530 540 RRLHGMDMSV LLEQDIFHRS LMACCLEIVL FAYSSPRTFP WIIEVLNLQP FYFYKVIEVV 550 560 570 580 590 600 IRSEEGLSRD MVKHLNSIEE QILESLAWSH DSALWEALQV SANKVPTCEE VIFPNNFETG 610 620 630 640 650 660 NGGNVQGHLP LMPMSPLMHP RVKEVRTDSG SLRRDMQPLS PISVHERYSS PTAGSAKRRL 670 680 690 700 710 720 FGEDPPKEML MDKIITEGTK LKIAPSSSIT AENVSILPGQ TLLTMATAPV TGTTGHKVTI 730 740 750 760 770 780 PLHGVANDAG EITLIPLSMN TNQESKVKSP VSLTAHSLIG ASPKQTNLTK AQEVHSTGIN 790 800 810 820 830 840 RPKRTGSLAL FYRKVYHLAS VRLRDLCLKL DVSNELRRKI WTCFEFTLVH CPDLMKDRHL 850 860 870 880 890 900 DQLLLCAFYI MAKVTKEERT FQEIMKSYRN QPQANSHVYR SVLLKSIPRE VVAYNKNIND 910 920 930 940 950 960 DFEMIDCDLE DATKTPDCSS GPVKEERGDL IKFYNTIYVG RVKSFALKYD LANQDHMMDA 970 980 990 1000 1010 PPLSPFPHIK QQPGSPRRIS QQHSIYISPH KNGSGLTPRS ALLYKFNGSP SKVR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Inhibition of cell proliferation by p107, a relative of the retinoblastoma protein." Zhu L., van den Heuvel S., Helin K., Fattaey A., Ewen M., Livingston D., Dyson N., Harlow E. Genes Dev. 7:1111-1125(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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 1). Tissue: Tongue.
[3]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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].
[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] (ISOFORM 2). Tissue: Testis.
[6]	"Molecular cloning, chromosomal mapping, and expression of the cDNA for p107, a retinoblastoma gene product-related protein." Ewen M.E., Xing Y., Lawrence J.B., Livingston D.M. Cell 66:1155-1164(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 134-1068 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[7]	"Differential roles of two tandem E2F sites in repression of the human p107 promoter by retinoblastoma and p107 proteins." Zhu L., Zhu L., Xie E., Chang L.S. Mol. Cell. Biol. 15:3552-3562(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
[8]	"Reversal of growth suppression by p107 via direct phosphorylation by cyclin D1/cyclin-dependent kinase 4." Leng X., Noble M., Adams P.D., Qin J., Harper J.W. Mol. Cell. Biol. 22:2242-2254(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 320-334; 364-374; 635-657; 949-977 AND 1006-1012, PHOSPHORYLATION AT THR-332; THR-369; THR-385; SER-640; SER-762; SER-964; SER-975; SER-988; THR-997 AND SER-1009, MUTAGENESIS OF SER-640; SER-643; SER-650 AND 657-LYS--LEU-660, MASS SPECTROMETRY.
[9]	"The cellular 107K protein that binds to adenovirus E1A also associates with the large T antigens of SV40 and JC virus." Dyson N., Buchkovich K., Whyte P., Harlow E. Cell 58:249-255(1989) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SV40 AND JC VIRUS LARGE T ANTIGEN.
[10]	"Differential specificity for binding of retinoblastoma binding protein 2 to RB, p107, and TATA-binding protein." Kim Y.W., Otterson G.A., Kratzke R.A., Coxon A.B., Kaye F.J. Mol. Cell. Biol. 14:7256-7264(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KDM5A.
[11]	"Che-1 affects cell growth by interfering with the recruitment of HDAC1 by Rb." Bruno T., De Angelis R., De Nicola F., Barbato C., Di Padova M., Corbi N., Libri V., Benassi B., Mattei E., Chersi A., Soddu S., Floridi A., Passananti C., Fanciulli M. Cancer Cell 2:387-399(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AATF.
[12]	"Distinct phosphorylation events regulate p130- and p107-mediated repression of E2F-4." Farkas T., Hansen K., Holm K., Lukas J., Bartek J. J. Biol. Chem. 277:26741-26752(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-369 AND SER-650.
[13]	"Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release." Rubin S.M., Gall A.-L., Zheng N., Pavletich N.P. Cell 123:1093-1106(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WITH E2F4 AND TFDP1.
[14]	"LINC, a human complex that is related to pRB-containing complexes in invertebrates regulates the expression of G2/M genes." Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C., von Eyss B., Gagrica S., Haenel F., Brehm A., Gaubatz S. Cell Cycle 6:1903-1913(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
[15]	"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 THR-385; SER-749 AND SER-762, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L14812 mRNA. Translation: AAA02489.1.
AK290380 mRNA. Translation: BAF83069.1.
AL136172, AL365505, AL391114 Genomic DNA. Translation: CAI95716.1.
AL365505, AL136172, AL391114 Genomic DNA. Translation: CAI95177.1.
AL391114, AL136172, AL365505 Genomic DNA. Translation: CAI95151.1.
AL365505, AL136172, AL391114 Genomic DNA. Translation: CAI95178.1.
AL391114, AL136172, AL365505 Genomic DNA. Translation: CAI95152.1.
AL136172, AL365505, AL391114 Genomic DNA. Translation: CAI95717.1.
CH471077 Genomic DNA. Translation: EAW76088.1.
BC032247 mRNA. Translation: AAH32247.1.
M74547 mRNA. Translation: AAA36397.1.
S78664 Genomic DNA. Translation: AAD14290.1.

IPI

IPI00005139.
IPI00375494.

PIR

A40265. A47319.

RefSeq

NP_002886.2. NM_002895.2.
NP_899662.1. NM_183404.1.

UniGene

Hs.207745.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H28	X-ray	2.80	E/F	653-663	[»]

ProteinModelPortal

P28749.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-148N.

IntAct

P28749. 22 interactions.

MINT

MINT-1353484.

STRING

9606.ENSP00000362768.

PTM databases

PhosphoSite

P28749.

Polymorphism databases

DMDM

90103515.

Proteomic databases

PaxDb

P28749.

PRIDE

P28749.

Protocols and materials databases

DNASU

5933.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000344359; ENSP00000343646; ENSG00000080839.
ENST00000373664; ENSP00000362768; ENSG00000080839.

GeneID

5933.

KEGG

hsa:5933.

UCSC

uc002xgi.3. human.
uc002xgj.1. human.

Organism-specific databases

CTD

5933.

GeneCards

GC20M035624.

H-InvDB

HIX0040570.

HGNC

HGNC:9893. RBL1.

MIM

116957. gene.

neXtProt

NX_P28749.

PharmGKB

PA34257.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG296920.

HOGENOM

HOG000273892.

HOVERGEN

HBG017710.

InParanoid

P28749.

KO

K04681.

OMA

RRDMQPL.

OrthoDB

EOG4QZ7KB.

PhylomeDB

P28749.

Enzyme and pathway databases

Pathway_Interaction_DB

smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P28749.

Bgee

P28749.

CleanEx

HS_RBL1.

Genevestigator

P28749.

GermOnline

ENSG00000080839. Homo sapiens.

Family and domain databases

Gene3D

1.10.472.10. 3 hits.

InterPro

IPR013763. Cyclin-like.
IPR024599. DUF3452_retinoblatoma-assoc.
IPR002720. RB_A.
IPR002719. RB_B.
IPR015030. Rb_C.
[Graphical view]

Pfam

PF11934. DUF3452. 1 hit.
PF01858. RB_A. 1 hit.
PF01857. RB_B. 1 hit.
PF08934. Rb_C. 1 hit.
[Graphical view]

SMART

SM00385. CYCLIN. 1 hit.
[Graphical view]

SUPFAM

SSF47954. Cyclin_like. 2 hits.

ProtoNet

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Other

EvolutionaryTrace

P28749.

GenomeRNAi

5933.

NextBio

23126.

SOURCE

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Entry information

Entry name

RBL1_HUMAN

Accession

Primary (citable) accession number: P28749
Secondary accession number(s): A8K2W5 , Q4VXA0, Q8N5K6, Q9H1L5, Q9H1M1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	March 7, 2006
Last modified:	May 1, 2013
This is version 140 of the entry and version 3 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.