Q6PR54 (RIF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 73.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Telomere-associated protein RIF1 Alternative name(s): Rap1-interacting factor 1 homolog Short name=mRif1 | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 2419 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Required for checkpoint mediated arrest of cell cycle progression in response to DNA damage during S-phase (the intra-S-phase checkpoint). This checkpoint requires activation of at least 2 parallel pathways by the ATM kinase: one involves the MRN (MRE11A-RAD50-NBS1) complex, while the second requires CHEK2. RIF1 seems to act independently of both these pathways. Seems to play no role in either the G1/S or G2/M DNA damage checkpoints By similarity. |
| Subunit structure | A fraction of the protein may interact with TRF2. |
| Subcellular location | Nucleus. Chromosome › telomere. Cytoplasm › cytoskeleton › spindle By similarity. Note: Exhibits ATM- and TP53BP1-dependent localization to uncapped or aberrant telomeres and to DNA double strand breaks (DSBs). Localizes to microtubules of the midzone of the mitotic spindle during anaphase, and to condensed chromosomes in telophase By similarity. While the majority of the protein appears nuclear and distinct from normal telomere structures, a small fraction may bind to telomeres in embryonic stem cells. Ref.1 |
| Tissue specificity | Expressed in Sertoli cells, prospermatagonia, early primary spermatocytes, and in oocytes at all stages of their growth. Expressed in embryonic stem (ES) and embryonic germ (EG) cells: expression is lost upon differentiation. Ref.1 |
| Developmental stage | Found in the nucleus of germinal-vesicle (GV) stage oocytes prior to fertilization. Accumulates in the male and female pronucleus after fertilization. Expressed in the nuclei of all blastomeres from the two cell stage to the compacted morula stage, although absent from the polar body and inner cell mass (ICM). Found in the nuclei of polar and mural trophectoderm cells from E3.5, and at high levels in the epiblast from E5.5 to E7.5. Expressed by primitive germ cells (PGCs) in both male and female from E9.5 to E13.5, at which point expression declines. A low level is observed in Sertoli cells of the testis at E17.5. Ref.1 |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR By similarity. |
| Sequence caution | The sequence BAB30843.1 differs from that shown. Reason: Erroneous initiation. The sequence BAC38846.1 differs from that shown. Reason: Chimeric cDNA. The sequence BAC40506.1 differs from that shown. Reason: Intron retention. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell cycle DNA damage |
| Cellular component | Chromosome Cytoplasm Cytoskeleton Nucleus Telomere |
| Coding sequence diversity | Alternative splicing |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cell cycle Inferred from electronic annotation. Source: UniProtKB-KW response to DNA damage stimulusInferred from electronic annotation. Source: UniProtKB-KW stem cell maintenanceInferred from mutant phenotype PubMed 16518401. Source: MGI |
| Cellular_component | chromosome, telomeric region Inferred from direct assay Ref.1. Source: MGI cytoplasmInferred from electronic annotation. Source: UniProtKB-KW female pronucleusInferred from direct assay Ref.1. Source: MGI male pronucleusInferred from direct assay Ref.1. Source: MGI spindleInferred from electronic annotation. Source: UniProtKB-SubCell |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Nanog | Q80Z64 | 5 | EBI-2312621,EBI-2312517 | |
| Nr0b1 | Q61066 | 2 | EBI-2312621,EBI-2312665 |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q6PR54-1) 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: Q6PR54-2) The sequence of this isoform differs from the canonical sequence as follows: 2198-2223: Missing. | ||||||
| Isoform 3 (identifier: Q6PR54-3) The sequence of this isoform differs from the canonical sequence as follows: 167-167: I → ISHWFLHC | ||||||
| Note: May be due to a competing acceptor splice site. No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2419 | 2419 | Telomere-associated protein RIF1 | PRO_0000097334 | |||||
Regions | |||||||||
| Region | 1882 – 2419 | 538 | Interaction with condensed chromosomes in telophase By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 7 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 401 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 403 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 779 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 976 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1044 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1153 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1231 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1233 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1269 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 1407 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1439 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1498 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1504 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1528 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1538 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1540 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1562 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1565 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1780 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1784 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1842 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1931 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2094 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2109 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2111 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2121 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2125 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2138 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2144 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2153 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2191 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2208 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2213 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2287 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2341 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2413 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2419 | 1 | Phosphoserine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 167 | 1 | I → ISHWFLHC in isoform 3. | VSP_014432 | |||||
| Alternative sequence | 2198 – 2223 | 26 | Missing in isoform 2. | VSP_014433 | |||||
Experimental info | |||||||||
| Sequence conflict | 211 | 1 | M → V in AAR87833. Ref.1 | ||||||
| Sequence conflict | 548 | 1 | M → V in AAR87833. Ref.1 | ||||||
| Sequence conflict | 586 | 1 | F → L in AAR87833. Ref.1 | ||||||
| Sequence conflict | 586 | 1 | F → L in BAC40506. Ref.3 | ||||||
| Sequence conflict | 592 | 1 | E → G in AAR87833. Ref.1 | ||||||
| Sequence conflict | 592 | 1 | E → G in BAC40506. Ref.3 | ||||||
| Sequence conflict | 596 | 1 | E → G in AAR87833. Ref.1 | ||||||
| Sequence conflict | 596 | 1 | E → G in BAC40506. Ref.3 | ||||||
| Sequence conflict | 717 | 1 | S → A in AAR87833. Ref.1 | ||||||
| Sequence conflict | 717 | 1 | S → A in BAC40506. Ref.3 | ||||||
| Sequence conflict | 743 | 1 | V → A in AAR87833. Ref.1 | ||||||
| Sequence conflict | 743 | 1 | V → A in BAC40506. Ref.3 | ||||||
| Sequence conflict | 802 | 1 | K → E in BAC40506. Ref.3 | ||||||
| Sequence conflict | 959 | 1 | I → S in AAR87833. Ref.1 | ||||||
| Sequence conflict | 959 | 1 | I → S in BAC40506. Ref.3 | ||||||
| Sequence conflict | 1066 | 1 | K → R in BAB30843. Ref.3 | ||||||
| Sequence conflict | 1122 | 1 | M → T in AAR87833. Ref.1 | ||||||
| Sequence conflict | 1179 | 1 | L → M in AAR87833. Ref.1 | ||||||
| Sequence conflict | 1238 | 1 | I → M in AAR87833. Ref.1 | ||||||
| Sequence conflict | 1527 | 1 | A → R in BAB30843. Ref.3 | ||||||
| Sequence conflict | 1584 | 1 | A → S in AAR87833. Ref.1 | ||||||
| Sequence conflict | 1671 | 1 | N → T in AAR87833. Ref.1 | ||||||
| Sequence conflict | 1772 | 1 | V → L in AAR87833. Ref.1 | ||||||
| Sequence conflict | 1798 | 1 | P → S in AAR87833. Ref.1 | ||||||
| Sequence conflict | 1897 | 1 | V → I in AAR87833. Ref.1 | ||||||
| Sequence conflict | 1918 | 1 | E → D in AAR87833. Ref.1 | ||||||
| Sequence conflict | 1997 | 1 | L → F in AAR87833. Ref.1 | ||||||
| Sequence conflict | 2018 | 1 | F → L in AAR87833. Ref.1 | ||||||
| Sequence conflict | 2024 | 1 | M → T in AAR87833. Ref.1 | ||||||
| Sequence conflict | 2052 | 1 | N → K in AAR87833. Ref.1 | ||||||
| Sequence conflict | 2114 | 1 | Missing in AAR87833. Ref.1 | ||||||
| Sequence conflict | 2394 | 1 | E → G in AAR87833. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification and characterisation of mRif1: a mouse telomere-associated protein highly expressed in germ cells and embryo-derived pluripotent stem cells." Adams I.R., McLaren A. Dev. Dyn. 229:733-744(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TRF2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: 129/Sv. |
| [2] | "ATM-mediated S-phase checkpoint function for hRif1." Silvermann J., Takai H., Buonomo S.B.C., Eisenhaber F., de Lange T. Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). |
| [3] | "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. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 416-1011; 1061-1556 AND 1859-2419. Strain: C57BL/6J. Tissue: Liver and Thymus. |
| [4] | "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] OF 1860-2419. Strain: C57BL/6. Tissue: Brain. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY428571 mRNA. Translation: AAR87833.2. AY585206 mRNA. Translation: AAS94124.1. AK017618 mRNA. Translation: BAB30843.1. Different initiation. AK083291 mRNA. Translation: BAC38846.1. Sequence problems. AK088688 mRNA. Translation: BAC40506.1. Sequence problems. BC055320 mRNA. Translation: AAH55320.1. |
| IPI | IPI00408125. IPI00421167. IPI00626173. |
| RefSeq | NP_780447.4. NM_175238.5. |
| UniGene | Mm.254530. |
3D structure databases | |
| ProteinModelPortal | Q6PR54. |
| SMR | Q6PR54. Positions 271-301. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-54907N. |
| IntAct | Q6PR54. 4 interactions. |
PTM databases | |
| PhosphoSite | Q6PR54. |
Proteomic databases | |
| PaxDb | Q6PR54. |
| PRIDE | Q6PR54. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000069794; ENSMUSP00000064155; ENSMUSG00000036202. ENSMUST00000112693; ENSMUSP00000108313; ENSMUSG00000036202. |
| GeneID | 51869. |
| KEGG | mmu:51869. |
| UCSC | uc008jqr.1. mouse. uc008jqt.1. mouse. |
Organism-specific databases | |
| CTD | 55183. |
| MGI | MGI:1098622. Rif1. |
Phylogenomic databases | |
| eggNOG | NOG87885. |
| GeneTree | ENSGT00390000012204. |
| HOGENOM | HOG000231777. |
| HOVERGEN | HBG080431. |
| InParanoid | Q6PR54. |
| KO | K11138. |
| OMA | PTESVYP. |
| OrthoDB | EOG4XWFWW. |
Gene expression databases | |
| ArrayExpress | Q6PR54. |
| Bgee | Q6PR54. |
| CleanEx | MM_RIF1. |
| Genevestigator | Q6PR54. |
| GermOnline | ENSMUSG00000036202. Mus musculus. |
Family and domain databases | |
| InterPro | IPR022031. Rif1_N. [Graphical view] |
| Pfam | PF12231. Rif1_N. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | RIF1. mouse. |
| NextBio | 308166. |
| SOURCE | Search... |
Entry information
| Entry name | RIF1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q6PR54 Secondary accession number(s): Q6T8D9 Q9CS77 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |

Clusters with
