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P28749

- RBL1_HUMAN

UniProt

P28749 - RBL1_HUMAN

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Protein

Retinoblastoma-like protein 1

Gene

RBL1

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

Functioni

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.

GO - Molecular functioni

  1. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. chromatin modification Source: UniProtKB-KW
  2. gene expression Source: Reactome
  3. mitotic cell cycle Source: Reactome
  4. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  5. positive regulation of transcription from RNA polymerase II promoter Source: Reactome
  6. regulation of cell cycle Source: InterPro
  7. regulation of lipid kinase activity Source: UniProtKB
  8. transcription, DNA-templated Source: Reactome
  9. transcription initiation from RNA polymerase II promoter Source: Reactome
  10. transforming growth factor beta receptor signaling pathway Source: Reactome
  11. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Cell cycle, Host-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_111214. G0 and Early G1.
REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
REACT_821. Cyclin D associated events in G1.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoblastoma-like protein 1
Alternative name(s):
107 kDa retinoblastoma-associated protein
Short name:
p107
pRb1
Gene namesi
Name:RBL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:9893. RBL1.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: HPA
  3. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi640 – 6401S → A: Strongly reduces phosphorylation by CDK2 and CDK4. 1 Publication
Mutagenesisi643 – 6431S → R: No effect on S-640 phosphorylation, but strongly increases S-640 phosphorylation; when associated with 657-A--A-660. 1 Publication
Mutagenesisi650 – 6501S → A: No effect on phosphorylation by CDK2. 1 Publication
Mutagenesisi657 – 6604KRRL → AAAA: Reduces S-640 phosphorylation by CDK2 and CDK4. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA34257.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10681068Retinoblastoma-like protein 1PRO_0000167839Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei332 – 3321Phosphothreonine; by CDK21 Publication
Modified residuei369 – 3691Phosphothreonine; by CDK42 Publications
Modified residuei385 – 3851Phosphothreonine; by CDK22 Publications
Modified residuei640 – 6401Phosphoserine; by CDK2 and CDK41 Publication
Modified residuei650 – 6501Phosphoserine1 Publication
Modified residuei749 – 7491Phosphoserine1 Publication
Modified residuei762 – 7621Phosphoserine; by CDK22 Publications
Modified residuei964 – 9641Phosphoserine; by CDK2 and CDK41 Publication
Modified residuei975 – 9751Phosphoserine; by CDK2 and CDK41 Publication
Modified residuei988 – 9881Phosphoserine; by CDK21 Publication
Modified residuei997 – 9971Phosphothreonine; by CDK21 Publication
Modified residuei1009 – 10091Phosphoserine; by CDK21 Publication
Modified residuei1041 – 10411PhosphoserineBy similarity

Post-translational modificationi

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 CDK4.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP28749.
PaxDbiP28749.
PRIDEiP28749.

PTM databases

PhosphoSiteiP28749.

Expressioni

Gene expression databases

BgeeiP28749.
CleanExiHS_RBL1.
ExpressionAtlasiP28749. baseline and differential.
GenevestigatoriP28749.

Organism-specific databases

HPAiHPA054962.
HPA056525.

Interactioni

Subunit structurei

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.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P032553EBI-971402,EBI-2603114From a different organism.
BEGAINQ9BUH82EBI-971402,EBI-742722
CDK4P118022EBI-971402,EBI-295644
DGKZQ13574-22EBI-971402,EBI-715527
DHX30Q7L2E34EBI-971402,EBI-1211456
DYRK1AQ136273EBI-971402,EBI-1053596
DYRK1BQ9Y4633EBI-971402,EBI-634187
IRF3Q146532EBI-971402,EBI-2650369
NR2E3Q9Y5X42EBI-971402,EBI-7216962
Pax3P246103EBI-971402,EBI-1208116From a different organism.
PPP2CAP677752EBI-971402,EBI-712311
Sirt1Q923E42EBI-971402,EBI-1802585From a different organism.

Protein-protein interaction databases

BioGridi111868. 73 interactions.
DIPiDIP-148N.
IntActiP28749. 35 interactions.
MINTiMINT-1353484.
STRINGi9606.ENSP00000362768.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H28X-ray2.80E/F653-663[»]
ProteinModelPortaliP28749.
SMRiP28749. Positions 86-587, 782-969.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28749.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni385 – 949565Pocket; binds T and E1AAdd
BLAST
Regioni385 – 584200Domain AAdd
BLAST
Regioni585 – 780196SpacerAdd
BLAST
Regioni781 – 949169Domain BAdd
BLAST

Sequence similaritiesi

Belongs to the retinoblastoma protein (RB) family.Curated

Phylogenomic databases

eggNOGiNOG296920.
GeneTreeiENSGT00530000063235.
HOGENOMiHOG000273892.
HOVERGENiHBG017710.
InParanoidiP28749.
KOiK04681.
OMAiRRDMQPL.
OrthoDBiEOG7P5T04.
PhylomeDBiP28749.
TreeFamiTF105568.

Family and domain databases

Gene3Di1.10.472.10. 3 hits.
InterProiIPR013763. Cyclin-like.
IPR002720. RB_A.
IPR002719. RB_B.
IPR015030. RB_C.
IPR028309. RB_fam.
IPR024599. RB_N.
IPR028310. RBL1.
[Graphical view]
PANTHERiPTHR13742. PTHR13742. 1 hit.
PTHR13742:SF20. PTHR13742:SF20. 1 hit.
PfamiPF11934. DUF3452. 1 hit.
PF01858. RB_A. 1 hit.
PF01857. RB_B. 1 hit.
PF08934. Rb_C. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 3 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P28749-1) [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
MFEDKPHAEG AAVVAAAGEA LQALCQELNL DEGSAAEALD DFTAIRGNYS
60 70 80 90 100
LEGEVTHWLA CSLYVACRKS IIPTVGKGIM EGNCVSLTRI LRSAKLSLIQ
110 120 130 140 150
FFSKMKKWMD MSNLPQEFRE RIERLERNFE VSTVIFKKYE PIFLDIFQNP
160 170 180 190 200
YEEPPKLPRS RKQRRIPCSV KDLFNFCWTL FVYTKGNFRM IGDDLVNSYH
210 220 230 240 250
LLLCCLDLIF ANAIMCPNRQ DLLNPSFKGL PSDFHTADFT ASEEPPCIIA
260 270 280 290 300
VLCELHDGLL VEAKGIKEHY FKPYISKLFD RKILKGECLL DLSSFTDNSK
310 320 330 340 350
AVNKEYEEYV LTVGDFDERI FLGADAEEEI GTPRKFTRDT PLGKLTAQAN
360 370 380 390 400
VEYNLQQHFE KKRSFAPSTP LTGRRYLREK EAVITPVASA TQSVSRLQSI
410 420 430 440 450
VAGLKNAPSD QLINIFESCV RNPVENIMKI LKGIGETFCQ HYTQSTDEQP
460 470 480 490 500
GSHIDFAVNR LKLAEILYYK ILETVMVQET RRLHGMDMSV LLEQDIFHRS
510 520 530 540 550
LMACCLEIVL FAYSSPRTFP WIIEVLNLQP FYFYKVIEVV IRSEEGLSRD
560 570 580 590 600
MVKHLNSIEE QILESLAWSH DSALWEALQV SANKVPTCEE VIFPNNFETG
610 620 630 640 650
NGGNVQGHLP LMPMSPLMHP RVKEVRTDSG SLRRDMQPLS PISVHERYSS
660 670 680 690 700
PTAGSAKRRL FGEDPPKEML MDKIITEGTK LKIAPSSSIT AENVSILPGQ
710 720 730 740 750
TLLTMATAPV TGTTGHKVTI PLHGVANDAG EITLIPLSMN TNQESKVKSP
760 770 780 790 800
VSLTAHSLIG ASPKQTNLTK AQEVHSTGIN RPKRTGSLAL FYRKVYHLAS
810 820 830 840 850
VRLRDLCLKL DVSNELRRKI WTCFEFTLVH CPDLMKDRHL DQLLLCAFYI
860 870 880 890 900
MAKVTKEERT FQEIMKSYRN QPQANSHVYR SVLLKSIPRE VVAYNKNIND
910 920 930 940 950
DFEMIDCDLE DATKTPDCSS GPVKEERGDL IKFYNTIYVG RVKSFALKYD
960 970 980 990 1000
LANQDHMMDA PPLSPFPHIK QQPGSPRRIS QQHSIYISPH KNGSGLTPRS
1010 1020 1030 1040 1050
ALLYKFNGSP SKSLKDINNM IRQGEQRTKK RVIAIDSDAE SPAKRVCQEN
1060
DDVLLKRLQD VVSERANH
Length:1,068
Mass (Da):120,847
Last modified:March 7, 2006 - v3
Checksum:i2BC4876EA04BDB31
GO
Isoform 2 (identifier: P28749-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,014
Mass (Da):114,688
Checksum:iCE1D47DBF365C4CB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti326 – 3261Missing AA sequence (PubMed:11884610)Curated
Sequence conflicti928 – 9281G → S(PubMed:8319904)Curated
Sequence conflicti928 – 9281G → S(PubMed:1833063)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1035 – 10351I → M.
Corresponds to variant rs8114297 [ dbSNP | Ensembl ].
VAR_034443

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1013 – 106856SLKDI…ERANH → VR in isoform 2. 1 PublicationVSP_017496Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13289.1. [P28749-1]
CCDS13290.1. [P28749-2]
PIRiA47319. A40265.
RefSeqiNP_002886.2. NM_002895.3. [P28749-1]
NP_899662.1. NM_183404.2. [P28749-2]
UniGeneiHs.207745.

Genome annotation databases

EnsembliENST00000344359; ENSP00000343646; ENSG00000080839. [P28749-2]
ENST00000373664; ENSP00000362768; ENSG00000080839. [P28749-1]
GeneIDi5933.
KEGGihsa:5933.
UCSCiuc002xgi.3. human. [P28749-1]
uc002xgj.1. human. [P28749-2]

Polymorphism databases

DMDMi90103515.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS13289.1. [P28749-1 ]
CCDS13290.1. [P28749-2 ]
PIRi A47319. A40265.
RefSeqi NP_002886.2. NM_002895.3. [P28749-1 ]
NP_899662.1. NM_183404.2. [P28749-2 ]
UniGenei Hs.207745.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1H28 X-ray 2.80 E/F 653-663 [» ]
ProteinModelPortali P28749.
SMRi P28749. Positions 86-587, 782-969.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111868. 73 interactions.
DIPi DIP-148N.
IntActi P28749. 35 interactions.
MINTi MINT-1353484.
STRINGi 9606.ENSP00000362768.

PTM databases

PhosphoSitei P28749.

Polymorphism databases

DMDMi 90103515.

Proteomic databases

MaxQBi P28749.
PaxDbi P28749.
PRIDEi P28749.

Protocols and materials databases

DNASUi 5933.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000344359 ; ENSP00000343646 ; ENSG00000080839 . [P28749-2 ]
ENST00000373664 ; ENSP00000362768 ; ENSG00000080839 . [P28749-1 ]
GeneIDi 5933.
KEGGi hsa:5933.
UCSCi uc002xgi.3. human. [P28749-1 ]
uc002xgj.1. human. [P28749-2 ]

Organism-specific databases

CTDi 5933.
GeneCardsi GC20M035624.
H-InvDB HIX0040570.
HGNCi HGNC:9893. RBL1.
HPAi HPA054962.
HPA056525.
MIMi 116957. gene.
neXtProti NX_P28749.
PharmGKBi PA34257.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG296920.
GeneTreei ENSGT00530000063235.
HOGENOMi HOG000273892.
HOVERGENi HBG017710.
InParanoidi P28749.
KOi K04681.
OMAi RRDMQPL.
OrthoDBi EOG7P5T04.
PhylomeDBi P28749.
TreeFami TF105568.

Enzyme and pathway databases

Reactomei REACT_111214. G0 and Early G1.
REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
REACT_821. Cyclin D associated events in G1.

Miscellaneous databases

ChiTaRSi RBL1. human.
EvolutionaryTracei P28749.
GeneWikii Retinoblastoma-like_protein_1.
GenomeRNAii 5933.
NextBioi 23126.
PROi P28749.
SOURCEi Search...

Gene expression databases

Bgeei P28749.
CleanExi HS_RBL1.
ExpressionAtlasi P28749. baseline and differential.
Genevestigatori P28749.

Family and domain databases

Gene3Di 1.10.472.10. 3 hits.
InterProi IPR013763. Cyclin-like.
IPR002720. RB_A.
IPR002719. RB_B.
IPR015030. RB_C.
IPR028309. RB_fam.
IPR024599. RB_N.
IPR028310. RBL1.
[Graphical view ]
PANTHERi PTHR13742. PTHR13742. 1 hit.
PTHR13742:SF20. PTHR13742:SF20. 1 hit.
Pfami PF11934. DUF3452. 1 hit.
PF01858. RB_A. 1 hit.
PF01857. RB_B. 1 hit.
PF08934. Rb_C. 1 hit.
[Graphical view ]
SMARTi SM00385. CYCLIN. 1 hit.
[Graphical view ]
SUPFAMi SSF47954. SSF47954. 3 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY 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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.

Entry informationi

Entry nameiRBL1_HUMAN
AccessioniPrimary (citable) accession number: P28749
Secondary accession number(s): A8K2W5
, Q4VXA0, Q8N5K6, Q9H1L5, Q9H1M1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: March 7, 2006
Last modified: November 26, 2014
This is version 156 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3