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Q6PR54 (RIF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Telomere-associated protein RIF1
Alternative name(s):
Rap1-interacting factor 1 homolog
Short name=mRif1
Gene names
Name:Rif1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2419 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Chromosometelomere. 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. 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.

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24192419Telomere-associated protein RIF1
PRO_0000097334

Regions

Region1882 – 2419538Interaction with condensed chromosomes in telophase By similarity

Amino acid modifications

Modified residue71Phosphoserine By similarity
Modified residue4011Phosphoserine By similarity
Modified residue4031Phosphotyrosine By similarity
Modified residue7791Phosphoserine By similarity
Modified residue9761Phosphoserine By similarity
Modified residue10441Phosphothreonine By similarity
Modified residue11531Phosphoserine By similarity
Modified residue12311Phosphoserine By similarity
Modified residue12331Phosphoserine By similarity
Modified residue12691N6-acetyllysine By similarity
Modified residue14071Phosphoserine By similarity
Modified residue14391Phosphoserine By similarity
Modified residue14981Phosphoserine By similarity
Modified residue15041Phosphothreonine By similarity
Modified residue15281Phosphoserine By similarity
Modified residue15381Phosphoserine By similarity
Modified residue15401Phosphoserine By similarity
Modified residue15621Phosphoserine By similarity
Modified residue15651Phosphoserine By similarity
Modified residue17801Phosphothreonine By similarity
Modified residue17841Phosphoserine By similarity
Modified residue18421Phosphoserine By similarity
Modified residue19311Phosphoserine By similarity
Modified residue20941Phosphoserine By similarity
Modified residue21091Phosphoserine By similarity
Modified residue21111Phosphoserine By similarity
Modified residue21211Phosphoserine By similarity
Modified residue21251Phosphoserine By similarity
Modified residue21381Phosphoserine By similarity
Modified residue21441Phosphoserine By similarity
Modified residue21531Phosphoserine By similarity
Modified residue21911Phosphoserine By similarity
Modified residue22081Phosphoserine By similarity
Modified residue22131Phosphoserine By similarity
Modified residue22871Phosphoserine By similarity
Modified residue23411Phosphoserine By similarity
Modified residue24131Phosphoserine By similarity
Modified residue24191Phosphoserine By similarity

Natural variations

Alternative sequence1671I → ISHWFLHC in isoform 3.
VSP_014432
Alternative sequence2198 – 222326Missing in isoform 2.
VSP_014433

Experimental info

Sequence conflict2111M → V in AAR87833. Ref.1
Sequence conflict5481M → V in AAR87833. Ref.1
Sequence conflict5861F → L in AAR87833. Ref.1
Sequence conflict5861F → L in BAC40506. Ref.3
Sequence conflict5921E → G in AAR87833. Ref.1
Sequence conflict5921E → G in BAC40506. Ref.3
Sequence conflict5961E → G in AAR87833. Ref.1
Sequence conflict5961E → G in BAC40506. Ref.3
Sequence conflict7171S → A in AAR87833. Ref.1
Sequence conflict7171S → A in BAC40506. Ref.3
Sequence conflict7431V → A in AAR87833. Ref.1
Sequence conflict7431V → A in BAC40506. Ref.3
Sequence conflict8021K → E in BAC40506. Ref.3
Sequence conflict9591I → S in AAR87833. Ref.1
Sequence conflict9591I → S in BAC40506. Ref.3
Sequence conflict10661K → R in BAB30843. Ref.3
Sequence conflict11221M → T in AAR87833. Ref.1
Sequence conflict11791L → M in AAR87833. Ref.1
Sequence conflict12381I → M in AAR87833. Ref.1
Sequence conflict15271A → R in BAB30843. Ref.3
Sequence conflict15841A → S in AAR87833. Ref.1
Sequence conflict16711N → T in AAR87833. Ref.1
Sequence conflict17721V → L in AAR87833. Ref.1
Sequence conflict17981P → S in AAR87833. Ref.1
Sequence conflict18971V → I in AAR87833. Ref.1
Sequence conflict19181E → D in AAR87833. Ref.1
Sequence conflict19971L → F in AAR87833. Ref.1
Sequence conflict20181F → L in AAR87833. Ref.1
Sequence conflict20241M → T in AAR87833. Ref.1
Sequence conflict20521N → K in AAR87833. Ref.1
Sequence conflict21141Missing in AAR87833. Ref.1
Sequence conflict23941E → G in AAR87833. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2005. Version 2.
Checksum: 016A1A4CEF25B8F9

FASTA2,419266,228
        10         20         30         40         50         60 
MTAPGRSPLE PLLETWEDPS VPPGEQTDAY LTLTSRMTGE EGKEVIAEIE KNLSRLYTVL 

        70         80         90        100        110        120 
KAHISSQNSE LSSAALQALG FCLYNPRITS GLSEANIQEL LLTLNGIIKS SDKNVCTRAL 

       130        140        150        160        170        180 
WVISKQTFPA ELVSKMVSSI IDSLEVILSK GEIHSAVVDF EALNVIIRLI EQAPVQMGEE 

       190        200        210        220        230        240 
SVRWAKLVIP LVVHSAQKVH LRGATALEMG MPLLLQKQQE IALITEHLMT TKLISELQKL 

       250        260        270        280        290        300 
FKNKNETYVL KLWPLFVKLL GKTLHRSGSF INSLLQLEEL GFRSGTPMIK KIAFIAWKSL 

       310        320        330        340        350        360 
IDNFALNPDI LCSAKRLKLL MQPLSSIHVR TETLALTKLE VWWYLLMRLG PQLPANFEQV 

       370        380        390        400        410        420 
CVPLIQSTIS VDSIPSPQGN SSRGSASPGL SPLTPGHKGA SPYGSPRGNL SSNTGGMAAI 

       430        440        450        460        470        480 
PSIQLLGLEM MLHFLLGPEV LSFAKQHKIV LSLEPLEHPL ISSPSFFSKY AHTLITAVHD 

       490        500        510        520        530        540 
SFVSVGKDAS DAVVSAIWKE LISLVKSVTE AGNRKEKSGS EVLTLLLKSL ENIVKSEVFP 

       550        560        570        580        590        600 
VSKTLVLMEI TVKGLPPKVL GSPAYQVANM DILNGTPALF LIQLIFNNNL LECGVEDEKF 

       610        620        630        640        650        660 
FLNLETLVGC VLSGPTSPLA FSDSVLTVIN QNAKQLVNKE HLWRMWSMIV SPLTDVIHQT 

       670        680        690        700        710        720 
NEVNQGDALE HNFSAIYGAL TLPINHIFSA QTFPTGTMKA LLKTWSELYR AFTRCASLVA 

       730        740        750        760        770        780 
TAEENLCCEE LSSKIMCSLE DEVLSDLLFL DRISHIIIVM VDCIDFSPYN KKYQPKIKSP 

       790        800        810        820        830        840 
QRSSDWSRKK KEPLGKLASL FKLIVKVIDT FHTLSLKETF SDTLLAIGNS IISMLSNVFG 

       850        860        870        880        890        900 
HISLPSMIRE IFATFTRPLA LLYENSKLDE APKVYTSLNN KLEKLLGEIV ACLQFSYLGA 

       910        920        930        940        950        960 
YDSELLEHLS PLLCVIFLHK NKQIRKQSAL LWNATFAKAT ALVYPEELKP ILRQAKQKIL 

       970        980        990       1000       1010       1020 
LLLPGLENVE MMDESSEPYS ESTENSQLNV KISGMERKSS GKRDSILAHT KDKKKKVKLS 

      1030       1040       1050       1060       1070       1080 
AKLKLESSSP KIKSGKLLEE EKSTDFVFIP PEGKETKARV LTEHQKEVLK TKRCDIPALY 

      1090       1100       1110       1120       1130       1140 
NNLDASQDTL FSAQFSQEES MESLTLTEKP KEDAKIIKEE QMESTIFIHQ DAPENCGIDE 

      1150       1160       1170       1180       1190       1200 
HSENASLPNC GGSVAETNPE TLITGFDARK EVLISSKILS AESSSSTETS VVSSSSVSNA 

      1210       1220       1230       1240       1250       1260 
TFSGTPPQPT SRRQTFITLE KFDGSETRPF SPSPLNNISS TVTVRNNQDN TTNTDMPPKA 

      1270       1280       1290       1300       1310       1320 
RKREVTNSKS DSENLANAGK KSSRRWSKAE QSVTKKSKPS LTSEQEEHSS ENNSPDLLSP 

      1330       1340       1350       1360       1370       1380 
TEHVSENDDH PSEATLEHKD GDPKPAVENA SLEDLTTEEK NVGINMESKE STASVVARTE 

      1390       1400       1410       1420       1430       1440 
QIVNEDSQAA ALAPNPKTLR RSSRRRSEAV DSCSDSQERE SGQQKKERRK EEEKIISKSP 

      1450       1460       1470       1480       1490       1500 
LRIKDDKLPT QKLTDESPIQ ENLTEKGNTL PERTSGEPSV NAEIDQNRRK PDLENVSSEG 

      1510       1520       1530       1540       1550       1560 
GGGTLDNLDK SSEKPLRGRT RYQTRRASQG LISAVENSES DSSEAKEEVS RKKRSGKWKN 

      1570       1580       1590       1600       1610       1620 
RSSDSVDIEE QEEKKAEEEV MKTANQTLDG QAVPDVDVNA AAQVCEKSTN NNRVILQDSA 

      1630       1640       1650       1660       1670       1680 
GPADSLQAPP KGEEKSKINK CVDSSFVSLP VPESNLRTRN ASKRLLYKQD NDSNVRVSDS 

      1690       1700       1710       1720       1730       1740 
SLSPEKFTQV ECQHKRSRRV RRSKSCDCCG EKSQSQEKSF IGLKNTESYA IKSVEKKKTD 

      1750       1760       1770       1780       1790       1800 
LQVPETAPET REARDHAETK LAGEEPLVNF HVGLKEENCT TGDSVKSEAE LQEASLPPEI 

      1810       1820       1830       1840       1850       1860 
VTVKEKTYDT DASEAVSEIQ GPCSENHSPA EDPGLSECKD ISQKQLSENG ELDISDVGKA 

      1870       1880       1890       1900       1910       1920 
CKVIAGSSPE GVETMELNVR NDAFVAADSE KSTQMDVSVD VATEEDNKKD ECEAVTTEVN 

      1930       1940       1950       1960       1970       1980 
VEGVATEDFN SGMDLSDTPI PVSKDVETEH AASGEIEGES NESDSGSCEE MNKEMGSHKA 

      1990       2000       2010       2020       2030       2040 
QMSTEIDSAR VKETDILASA SKSEEALIGR LDVNTQSFVS DIEMSSGERT VNCKTETSIE 

      2050       2060       2070       2080       2090       2100 
LNKLDEAKLS GNEATVGNDT LQEVCFTSEK VEKLPQCLLV QVASELGAES NTTSPEKLEL 

      2110       2120       2130       2140       2150       2160 
DSFGSVNESP SGMQQARCVW SPLASPSTSI LKRGLKRSQE DEISPVNKIR RVSFADPIYQ 

      2170       2180       2190       2200       2210       2220 
AGLADDIDRR CSVVRSHSSN SSPIIKSVKT SPTSHSKHNT TSAKGFLSPG SQSSKFKSPK 

      2230       2240       2250       2260       2270       2280 
KCLITEMAQE SMLSPTESVY PALVNCAASV DIILPQITSN MWARGLGQLI RAKNIKTIGD 

      2290       2300       2310       2320       2330       2340 
LSTLTASEIK TLPIRSPKVF NVKKALRVYH EQQMKSRGLE EIPIFDISEK AVNGVESRTV 

      2350       2360       2370       2380       2390       2400 
STDEERFASD LIEPVTLDTP LSKNLVAQIS ALALQLDSED LYSYTGSQLF EMHEKLGTMA 

      2410 
NSIIRNLQSR WRSPAHENS 

« Hide

Isoform 2 [UniParc].

Checksum: 97A1207A4F3AD637
Show »

FASTA2,393263,480
Isoform 3 [UniParc].

Checksum: 72C0C38EBD54A556
Show »

FASTA2,426267,139

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. expand/collapse author list , 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/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.
IPIIPI00408125.
IPI00421167.
IPI00626173.
RefSeqNP_780447.4. NM_175238.5.
UniGeneMm.254530.

3D structure databases

ProteinModelPortalQ6PR54.
SMRQ6PR54. Positions 271-301.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-54907N.
IntActQ6PR54. 4 interactions.

PTM databases

PhosphoSiteQ6PR54.

Proteomic databases

PaxDbQ6PR54.
PRIDEQ6PR54.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000069794; ENSMUSP00000064155; ENSMUSG00000036202.
ENSMUST00000112693; ENSMUSP00000108313; ENSMUSG00000036202.
GeneID51869.
KEGGmmu:51869.
UCSCuc008jqr.1. mouse.
uc008jqt.1. mouse.

Organism-specific databases

CTD55183.
MGIMGI:1098622. Rif1.

Phylogenomic databases

eggNOGNOG87885.
GeneTreeENSGT00390000012204.
HOGENOMHOG000231777.
HOVERGENHBG080431.
InParanoidQ6PR54.
KOK11138.
OMAPTESVYP.
OrthoDBEOG4XWFWW.

Gene expression databases

ArrayExpressQ6PR54.
BgeeQ6PR54.
CleanExMM_RIF1.
GenevestigatorQ6PR54.
GermOnlineENSMUSG00000036202. Mus musculus.

Family and domain databases

InterProIPR022031. Rif1_N.
[Graphical view]
PfamPF12231. Rif1_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRIF1. mouse.
NextBio308166.
SOURCESearch...

Entry information

Entry nameRIF1_MOUSE
AccessionPrimary (citable) accession number: Q6PR54
Secondary accession number(s): Q6T8D9 expand/collapse secondary AC list , Q7TPD8, Q8BTU2, Q8C408, Q9CS77
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: May 1, 2013
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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