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Protein

Telomere-associated protein RIF1

Gene

Rif1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cellular response to DNA damage stimulus Source: UniProtKB-KW
  • positive regulation of double-strand break repair via nonhomologous end joining Source: CACAO
  • stem cell population maintenance Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage

Enzyme and pathway databases

ReactomeiR-MMU-5693571. Nonhomologous End-Joining (NHEJ).

Names & Taxonomyi

Protein namesi
Recommended name:
Telomere-associated protein RIF1
Alternative name(s):
Rap1-interacting factor 1 homolog
Short name:
mRif1
Gene namesi
Name:Rif1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1098622. Rif1.

Subcellular locationi

  • Nucleus 1 Publication
  • Chromosometelomere 1 Publication
  • Cytoplasmcytoskeletonspindle 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.By similarity

GO - Cellular componenti

  • chromosome, telomeric region Source: MGI
  • cytoplasm Source: UniProtKB-KW
  • female pronucleus Source: MGI
  • male pronucleus Source: MGI
  • nucleus Source: MGI
  • plasma membrane Source: MGI
  • spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Nucleus, Telomere

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24192419Telomere-associated protein RIF1PRO_0000097334Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei385 – 3851PhosphoserineCombined sources
Modified residuei391 – 3911PhosphoserineCombined sources
Modified residuei779 – 7791PhosphoserineBy similarity
Modified residuei976 – 9761PhosphoserineBy similarity
Modified residuei1044 – 10441PhosphothreonineBy similarity
Modified residuei1231 – 12311PhosphoserineBy similarity
Modified residuei1233 – 12331PhosphoserineBy similarity
Modified residuei1407 – 14071PhosphoserineCombined sources
Modified residuei1439 – 14391PhosphoserineBy similarity
Modified residuei1457 – 14571PhosphoserineCombined sources
Modified residuei1498 – 14981PhosphoserineBy similarity
Modified residuei1504 – 15041PhosphothreonineBy similarity
Modified residuei1528 – 15281PhosphoserineCombined sources
Modified residuei1538 – 15381PhosphoserineCombined sources
Modified residuei1540 – 15401PhosphoserineCombined sources
Modified residuei1550 – 15501PhosphoserineCombined sources
Modified residuei1562 – 15621PhosphoserineBy similarity
Modified residuei1565 – 15651PhosphoserineCombined sources
Modified residuei1683 – 16831PhosphoserineCombined sources
Modified residuei1780 – 17801PhosphothreonineBy similarity
Modified residuei1784 – 17841PhosphoserineBy similarity
Modified residuei1842 – 18421PhosphoserineBy similarity
Modified residuei1931 – 19311PhosphoserineBy similarity
Modified residuei2094 – 20941PhosphoserineBy similarity
Modified residuei2109 – 21091PhosphoserineBy similarity
Modified residuei2121 – 21211PhosphoserineBy similarity
Modified residuei2125 – 21251PhosphoserineBy similarity
Modified residuei2144 – 21441PhosphoserineCombined sources
Modified residuei2153 – 21531PhosphoserineBy similarity
Modified residuei2208 – 22081PhosphoserineBy similarity
Modified residuei2287 – 22871PhosphoserineBy similarity
Modified residuei2341 – 23411PhosphoserineBy similarity
Modified residuei2413 – 24131PhosphoserineBy similarity
Modified residuei2419 – 24191PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6PR54.
MaxQBiQ6PR54.
PaxDbiQ6PR54.
PRIDEiQ6PR54.

PTM databases

iPTMnetiQ6PR54.
PhosphoSiteiQ6PR54.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

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 E17.5.1 Publication

Gene expression databases

BgeeiQ6PR54.
CleanExiMM_RIF1.
GenevisibleiQ6PR54. MM.

Interactioni

Subunit structurei

A fraction of the protein may interact with TRF2.

Binary interactionsi

WithEntry#Exp.IntActNotes
NanogQ80Z645EBI-2312621,EBI-2312517
Nr0b1Q610662EBI-2312621,EBI-2312665

Protein-protein interaction databases

BioGridi206234. 9 interactions.
DIPiDIP-54907N.
IntActiQ6PR54. 4 interactions.
STRINGi10090.ENSMUSP00000064155.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1882 – 2419538Interaction with condensed chromosomes in telophaseBy similarityAdd
BLAST

Phylogenomic databases

eggNOGiENOG410IJ7R. Eukaryota.
ENOG410YNMC. LUCA.
GeneTreeiENSGT00390000012204.
HOGENOMiHOG000231777.
HOVERGENiHBG080431.
InParanoidiQ6PR54.
KOiK11138.
OMAiPTESVYP.
OrthoDBiEOG70GMDW.
TreeFamiTF323789.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR028566. Rif1.
IPR022031. Rif1_N.
[Graphical view]
PANTHERiPTHR22928. PTHR22928. 3 hits.
PfamiPF12231. Rif1_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6PR54-1) [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
MTAPGRSPLE PLLETWEDPS VPPGEQTDAY LTLTSRMTGE EGKEVIAEIE
60 70 80 90 100
KNLSRLYTVL KAHISSQNSE LSSAALQALG FCLYNPRITS GLSEANIQEL
110 120 130 140 150
LLTLNGIIKS SDKNVCTRAL WVISKQTFPA ELVSKMVSSI IDSLEVILSK
160 170 180 190 200
GEIHSAVVDF EALNVIIRLI EQAPVQMGEE SVRWAKLVIP LVVHSAQKVH
210 220 230 240 250
LRGATALEMG MPLLLQKQQE IALITEHLMT TKLISELQKL FKNKNETYVL
260 270 280 290 300
KLWPLFVKLL GKTLHRSGSF INSLLQLEEL GFRSGTPMIK KIAFIAWKSL
310 320 330 340 350
IDNFALNPDI LCSAKRLKLL MQPLSSIHVR TETLALTKLE VWWYLLMRLG
360 370 380 390 400
PQLPANFEQV CVPLIQSTIS VDSIPSPQGN SSRGSASPGL SPLTPGHKGA
410 420 430 440 450
SPYGSPRGNL SSNTGGMAAI PSIQLLGLEM MLHFLLGPEV LSFAKQHKIV
460 470 480 490 500
LSLEPLEHPL ISSPSFFSKY AHTLITAVHD SFVSVGKDAS DAVVSAIWKE
510 520 530 540 550
LISLVKSVTE AGNRKEKSGS EVLTLLLKSL ENIVKSEVFP VSKTLVLMEI
560 570 580 590 600
TVKGLPPKVL GSPAYQVANM DILNGTPALF LIQLIFNNNL LECGVEDEKF
610 620 630 640 650
FLNLETLVGC VLSGPTSPLA FSDSVLTVIN QNAKQLVNKE HLWRMWSMIV
660 670 680 690 700
SPLTDVIHQT NEVNQGDALE HNFSAIYGAL TLPINHIFSA QTFPTGTMKA
710 720 730 740 750
LLKTWSELYR AFTRCASLVA TAEENLCCEE LSSKIMCSLE DEVLSDLLFL
760 770 780 790 800
DRISHIIIVM VDCIDFSPYN KKYQPKIKSP QRSSDWSRKK KEPLGKLASL
810 820 830 840 850
FKLIVKVIDT FHTLSLKETF SDTLLAIGNS IISMLSNVFG HISLPSMIRE
860 870 880 890 900
IFATFTRPLA LLYENSKLDE APKVYTSLNN KLEKLLGEIV ACLQFSYLGA
910 920 930 940 950
YDSELLEHLS PLLCVIFLHK NKQIRKQSAL LWNATFAKAT ALVYPEELKP
960 970 980 990 1000
ILRQAKQKIL LLLPGLENVE MMDESSEPYS ESTENSQLNV KISGMERKSS
1010 1020 1030 1040 1050
GKRDSILAHT KDKKKKVKLS AKLKLESSSP KIKSGKLLEE EKSTDFVFIP
1060 1070 1080 1090 1100
PEGKETKARV LTEHQKEVLK TKRCDIPALY NNLDASQDTL FSAQFSQEES
1110 1120 1130 1140 1150
MESLTLTEKP KEDAKIIKEE QMESTIFIHQ DAPENCGIDE HSENASLPNC
1160 1170 1180 1190 1200
GGSVAETNPE TLITGFDARK EVLISSKILS AESSSSTETS VVSSSSVSNA
1210 1220 1230 1240 1250
TFSGTPPQPT SRRQTFITLE KFDGSETRPF SPSPLNNISS TVTVRNNQDN
1260 1270 1280 1290 1300
TTNTDMPPKA RKREVTNSKS DSENLANAGK KSSRRWSKAE QSVTKKSKPS
1310 1320 1330 1340 1350
LTSEQEEHSS ENNSPDLLSP TEHVSENDDH PSEATLEHKD GDPKPAVENA
1360 1370 1380 1390 1400
SLEDLTTEEK NVGINMESKE STASVVARTE QIVNEDSQAA ALAPNPKTLR
1410 1420 1430 1440 1450
RSSRRRSEAV DSCSDSQERE SGQQKKERRK EEEKIISKSP LRIKDDKLPT
1460 1470 1480 1490 1500
QKLTDESPIQ ENLTEKGNTL PERTSGEPSV NAEIDQNRRK PDLENVSSEG
1510 1520 1530 1540 1550
GGGTLDNLDK SSEKPLRGRT RYQTRRASQG LISAVENSES DSSEAKEEVS
1560 1570 1580 1590 1600
RKKRSGKWKN RSSDSVDIEE QEEKKAEEEV MKTANQTLDG QAVPDVDVNA
1610 1620 1630 1640 1650
AAQVCEKSTN NNRVILQDSA GPADSLQAPP KGEEKSKINK CVDSSFVSLP
1660 1670 1680 1690 1700
VPESNLRTRN ASKRLLYKQD NDSNVRVSDS SLSPEKFTQV ECQHKRSRRV
1710 1720 1730 1740 1750
RRSKSCDCCG EKSQSQEKSF IGLKNTESYA IKSVEKKKTD LQVPETAPET
1760 1770 1780 1790 1800
REARDHAETK LAGEEPLVNF HVGLKEENCT TGDSVKSEAE LQEASLPPEI
1810 1820 1830 1840 1850
VTVKEKTYDT DASEAVSEIQ GPCSENHSPA EDPGLSECKD ISQKQLSENG
1860 1870 1880 1890 1900
ELDISDVGKA CKVIAGSSPE GVETMELNVR NDAFVAADSE KSTQMDVSVD
1910 1920 1930 1940 1950
VATEEDNKKD ECEAVTTEVN VEGVATEDFN SGMDLSDTPI PVSKDVETEH
1960 1970 1980 1990 2000
AASGEIEGES NESDSGSCEE MNKEMGSHKA QMSTEIDSAR VKETDILASA
2010 2020 2030 2040 2050
SKSEEALIGR LDVNTQSFVS DIEMSSGERT VNCKTETSIE LNKLDEAKLS
2060 2070 2080 2090 2100
GNEATVGNDT LQEVCFTSEK VEKLPQCLLV QVASELGAES NTTSPEKLEL
2110 2120 2130 2140 2150
DSFGSVNESP SGMQQARCVW SPLASPSTSI LKRGLKRSQE DEISPVNKIR
2160 2170 2180 2190 2200
RVSFADPIYQ AGLADDIDRR CSVVRSHSSN SSPIIKSVKT SPTSHSKHNT
2210 2220 2230 2240 2250
TSAKGFLSPG SQSSKFKSPK KCLITEMAQE SMLSPTESVY PALVNCAASV
2260 2270 2280 2290 2300
DIILPQITSN MWARGLGQLI RAKNIKTIGD LSTLTASEIK TLPIRSPKVF
2310 2320 2330 2340 2350
NVKKALRVYH EQQMKSRGLE EIPIFDISEK AVNGVESRTV STDEERFASD
2360 2370 2380 2390 2400
LIEPVTLDTP LSKNLVAQIS ALALQLDSED LYSYTGSQLF EMHEKLGTMA
2410
NSIIRNLQSR WRSPAHENS
Length:2,419
Mass (Da):266,228
Last modified:July 5, 2005 - v2
Checksum:i016A1A4CEF25B8F9
GO
Isoform 2 (identifier: Q6PR54-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2198-2223: Missing.

Show »
Length:2,393
Mass (Da):263,480
Checksum:i97A1207A4F3AD637
GO
Isoform 3 (identifier: Q6PR54-3) [UniParc]FASTAAdd to basket

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.
Show »
Length:2,426
Mass (Da):267,139
Checksum:i72C0C38EBD54A556
GO

Sequence cautioni

The sequence BAB30843.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC38846.1 differs from that shown.Chimeric cDNA.Curated
The sequence BAC40506.1 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti211 – 2111M → V in AAR87833 (PubMed:15042697).Curated
Sequence conflicti548 – 5481M → V in AAR87833 (PubMed:15042697).Curated
Sequence conflicti586 – 5861F → L in AAR87833 (PubMed:15042697).Curated
Sequence conflicti586 – 5861F → L in BAC40506 (PubMed:16141072).Curated
Sequence conflicti592 – 5921E → G in AAR87833 (PubMed:15042697).Curated
Sequence conflicti592 – 5921E → G in BAC40506 (PubMed:16141072).Curated
Sequence conflicti596 – 5961E → G in AAR87833 (PubMed:15042697).Curated
Sequence conflicti596 – 5961E → G in BAC40506 (PubMed:16141072).Curated
Sequence conflicti717 – 7171S → A in AAR87833 (PubMed:15042697).Curated
Sequence conflicti717 – 7171S → A in BAC40506 (PubMed:16141072).Curated
Sequence conflicti743 – 7431V → A in AAR87833 (PubMed:15042697).Curated
Sequence conflicti743 – 7431V → A in BAC40506 (PubMed:16141072).Curated
Sequence conflicti802 – 8021K → E in BAC40506 (PubMed:16141072).Curated
Sequence conflicti959 – 9591I → S in AAR87833 (PubMed:15042697).Curated
Sequence conflicti959 – 9591I → S in BAC40506 (PubMed:16141072).Curated
Sequence conflicti1066 – 10661K → R in BAB30843 (PubMed:16141072).Curated
Sequence conflicti1122 – 11221M → T in AAR87833 (PubMed:15042697).Curated
Sequence conflicti1179 – 11791L → M in AAR87833 (PubMed:15042697).Curated
Sequence conflicti1238 – 12381I → M in AAR87833 (PubMed:15042697).Curated
Sequence conflicti1527 – 15271A → R in BAB30843 (PubMed:16141072).Curated
Sequence conflicti1584 – 15841A → S in AAR87833 (PubMed:15042697).Curated
Sequence conflicti1671 – 16711N → T in AAR87833 (PubMed:15042697).Curated
Sequence conflicti1772 – 17721V → L in AAR87833 (PubMed:15042697).Curated
Sequence conflicti1798 – 17981P → S in AAR87833 (PubMed:15042697).Curated
Sequence conflicti1897 – 18971V → I in AAR87833 (PubMed:15042697).Curated
Sequence conflicti1918 – 19181E → D in AAR87833 (PubMed:15042697).Curated
Sequence conflicti1997 – 19971L → F in AAR87833 (PubMed:15042697).Curated
Sequence conflicti2018 – 20181F → L in AAR87833 (PubMed:15042697).Curated
Sequence conflicti2024 – 20241M → T in AAR87833 (PubMed:15042697).Curated
Sequence conflicti2052 – 20521N → K in AAR87833 (PubMed:15042697).Curated
Sequence conflicti2114 – 21141Missing in AAR87833 (PubMed:15042697).Curated
Sequence conflicti2394 – 23941E → G in AAR87833 (PubMed:15042697).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei167 – 1671I → ISHWFLHC in isoform 3. 1 PublicationVSP_014432
Alternative sequencei2198 – 222326Missing in isoform 2. CuratedVSP_014433Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS50583.1. [Q6PR54-3]
RefSeqiNP_780447.4. NM_175238.5. [Q6PR54-3]
XP_006498240.1. XM_006498177.2. [Q6PR54-1]
XP_011237438.1. XM_011239136.1. [Q6PR54-2]
UniGeneiMm.254530.
Mm.389247.

Genome annotation databases

EnsembliENSMUST00000069794; ENSMUSP00000064155; ENSMUSG00000036202. [Q6PR54-3]
ENSMUST00000112693; ENSMUSP00000108313; ENSMUSG00000036202. [Q6PR54-3]
GeneIDi51869.
KEGGimmu:51869.
UCSCiuc008jqq.1. mouse. [Q6PR54-3]
uc008jqr.1. mouse. [Q6PR54-1]
uc008jqt.1. mouse. [Q6PR54-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS50583.1. [Q6PR54-3]
RefSeqiNP_780447.4. NM_175238.5. [Q6PR54-3]
XP_006498240.1. XM_006498177.2. [Q6PR54-1]
XP_011237438.1. XM_011239136.1. [Q6PR54-2]
UniGeneiMm.254530.
Mm.389247.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206234. 9 interactions.
DIPiDIP-54907N.
IntActiQ6PR54. 4 interactions.
STRINGi10090.ENSMUSP00000064155.

PTM databases

iPTMnetiQ6PR54.
PhosphoSiteiQ6PR54.

Proteomic databases

EPDiQ6PR54.
MaxQBiQ6PR54.
PaxDbiQ6PR54.
PRIDEiQ6PR54.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000069794; ENSMUSP00000064155; ENSMUSG00000036202. [Q6PR54-3]
ENSMUST00000112693; ENSMUSP00000108313; ENSMUSG00000036202. [Q6PR54-3]
GeneIDi51869.
KEGGimmu:51869.
UCSCiuc008jqq.1. mouse. [Q6PR54-3]
uc008jqr.1. mouse. [Q6PR54-1]
uc008jqt.1. mouse. [Q6PR54-2]

Organism-specific databases

CTDi55183.
MGIiMGI:1098622. Rif1.

Phylogenomic databases

eggNOGiENOG410IJ7R. Eukaryota.
ENOG410YNMC. LUCA.
GeneTreeiENSGT00390000012204.
HOGENOMiHOG000231777.
HOVERGENiHBG080431.
InParanoidiQ6PR54.
KOiK11138.
OMAiPTESVYP.
OrthoDBiEOG70GMDW.
TreeFamiTF323789.

Enzyme and pathway databases

ReactomeiR-MMU-5693571. Nonhomologous End-Joining (NHEJ).

Miscellaneous databases

ChiTaRSiRif1. mouse.
PROiQ6PR54.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PR54.
CleanExiMM_RIF1.
GenevisibleiQ6PR54. MM.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR028566. Rif1.
IPR022031. Rif1_N.
[Graphical view]
PANTHERiPTHR22928. PTHR22928. 3 hits.
PfamiPF12231. Rif1_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] 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/6J.
    Tissue: Brain.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385; SER-391; SER-1407; SER-1457; SER-1528; SER-1538; SER-1540; SER-1550; SER-1565; SER-1683 AND SER-2144, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Lung, Spleen and Testis.

Entry informationi

Entry nameiRIF1_MOUSE
AccessioniPrimary (citable) accession number: Q6PR54
Secondary accession number(s): Q6T8D9
, Q7TPD8, Q8BTU2, Q8C408, Q9CS77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: June 8, 2016
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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.