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Q5UIP0

- RIF1_HUMAN

UniProt

Q5UIP0 - RIF1_HUMAN

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Protein

Telomere-associated protein RIF1

Gene

RIF1

Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 Publication

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cellular response to DNA damage stimulus Source: UniProtKB-KW
  3. stem cell maintenance Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage

Names & Taxonomyi

Protein namesi
Recommended name:
Telomere-associated protein RIF1
Alternative name(s):
Rap1-interacting factor 1 homolog
Gene namesi
Name:RIF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:23207. RIF1.

Subcellular locationi

Nucleus. Chromosometelomere. Cytoplasmcytoskeletonspindle
Note: Exhibits ATM- and TP53BP1-dependent localization to uncapped or aberrant telomeres and to DNA double strand breaks (DSBs). Does not associate with normal telomere structures. Localizes to microtubules of the midzone of the mitotic spindle during anaphase, and to condensed chromosomes in telophase.

GO - Cellular componenti

  1. chromosome, telomeric region Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB-KW
  4. female pronucleus Source: Ensembl
  5. male pronucleus Source: Ensembl
  6. nucleolus Source: HPA
  7. nucleus Source: HPA
  8. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Nucleus, Telomere

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134933858.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24722472Telomere-associated protein RIF1PRO_0000097333Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei402 – 4021Phosphoserine1 Publication
Modified residuei409 – 4091Phosphothreonine2 Publications
Modified residuei782 – 7821Phosphoserine1 Publication
Modified residuei979 – 9791Phosphoserine1 Publication
Modified residuei1047 – 10471Phosphothreonine1 Publication
Modified residuei1162 – 11621Phosphoserine1 Publication
Modified residuei1236 – 12361Phosphoserine1 Publication
Modified residuei1238 – 12381Phosphoserine2 Publications
Modified residuei1422 – 14221Phosphoserine2 Publications
Modified residuei1454 – 14541Phosphoserine3 Publications
Modified residuei1513 – 15131Phosphoserine1 Publication
Modified residuei1518 – 15181Phosphothreonine1 Publication
Modified residuei1542 – 15421Phosphoserine2 Publications
Modified residuei1552 – 15521Phosphoserine1 Publication
Modified residuei1554 – 15541Phosphoserine3 Publications
Modified residuei1576 – 15761Phosphoserine1 Publication
Modified residuei1579 – 15791Phosphoserine4 Publications
Modified residuei1616 – 16161Phosphoserine1 Publication
Modified residuei1688 – 16881Phosphoserine5 Publications
Modified residuei1693 – 16931Phosphoserine1 Publication
Modified residuei1806 – 18061Phosphothreonine1 Publication
Modified residuei1810 – 18101Phosphoserine2 Publications
Modified residuei1873 – 18731Phosphoserine2 Publications
Modified residuei1876 – 18761Phosphoserine1 Publication
Modified residuei1971 – 19711Phosphoserine1 Publication
Modified residuei2144 – 21441Phosphoserine2 Publications
Modified residuei2161 – 21611Phosphoserine2 Publications
Modified residuei2167 – 21671Phosphothreonine1 Publication
Modified residuei2172 – 21721Phosphoserine2 Publications
Modified residuei2176 – 21761Phosphoserine1 Publication
Modified residuei2196 – 21961Phosphoserine3 Publications
Modified residuei2205 – 22051Phosphoserine2 Publications
Modified residuei2260 – 22601Phosphoserine1 Publication
Modified residuei2339 – 23391Phosphoserine1 Publication
Modified residuei2391 – 23911Phosphoserine1 Publication
Modified residuei2393 – 23931Phosphoserine3 Publications
Modified residuei2465 – 24651Phosphoserine1 Publication
Modified residuei2471 – 24711Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ5UIP0.
PaxDbiQ5UIP0.
PRIDEiQ5UIP0.

PTM databases

PhosphoSiteiQ5UIP0.

Expressioni

Tissue specificityi

Highly expressed in testis.1 Publication

Developmental stagei

Expression peaks in late G2/S phase of the cell cycle.1 Publication

Gene expression databases

BgeeiQ5UIP0.
CleanExiHS_RIF1.
ExpressionAtlasiQ5UIP0. baseline and differential.
GenevestigatoriQ5UIP0.

Organism-specific databases

HPAiHPA036887.
HPA036888.

Interactioni

Protein-protein interaction databases

BioGridi120482. 25 interactions.
IntActiQ5UIP0. 118 interactions.
MINTiMINT-3974483.

Structurei

3D structure databases

ProteinModelPortaliQ5UIP0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1924 – 2472549Interaction with condensed chromosomes in telophaseAdd
BLAST

Phylogenomic databases

eggNOGiNOG87885.
GeneTreeiENSGT00390000012204.
HOVERGENiHBG080431.
InParanoidiQ5UIP0.
KOiK11138.
OMAiPTESVYP.
OrthoDBiEOG70GMDW.
PhylomeDBiQ5UIP0.
TreeFamiTF323789.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR028566. Rif1.
IPR022031. Rif1_N.
[Graphical view]
PANTHERiPTHR22928. PTHR22928. 1 hit.
PfamiPF12231. Rif1_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 4 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5UIP0-1) [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
MTARGQSPLA PLLETLEDPS ASHGGQTDAY LTLTSRMTGE EGKEVITEIE
60 70 80 90 100
KKLPRLYKVL KTHISSQNSE LSSAALQALG FCLYNPKITS ELSEANALEL
110 120 130 140 150
LSKLNDTIKN SDKNVRTRAL WVISKQTFPS EVVGKMVSSI IDSLEILFNK
160 170 180 190 200
GETHSAVVDF EALNVIVRLI EQAPIQMGEE AVRWAKLVIP LVVHSAQKVH
210 220 230 240 250
LRGATALEMG MPLLLQKQQE IASITEQLMT TKLISELQKL FMSKNETYVL
260 270 280 290 300
KLWPLFVKLL GRTLHRSGSF INSLLQLEEL GFRSGAPMIK KIAFIAWKSL
310 320 330 340 350
IDNFALNPDI LCSAKRLKLL MQPLSSIHVR TETLALTKLE VWWYLLMRLG
360 370 380 390 400
PHLPANFEQV CVPLIQSTIS IDSNASPQGN SCHVATSPGL NPMTPVHKGA
410 420 430 440 450
SSPYGAPGTP RMNLSSNLGG MATIPSIQLL GLEMLLHFLL GPEALSFAKQ
460 470 480 490 500
NKLVLSLEPL EHPLISSPSF FSKHANTLIT AVHDSFVAVG KDAPDVVVSA
510 520 530 540 550
IWKELISLVK SVTESGNKKE KPGSEVLTLL LKSLESIVKS EVFPVSKTLV
560 570 580 590 600
LMEITIKGLP QKVLGSPAYQ VANMDILNGT PALFLIQLIF NNFLECGVSD
610 620 630 640 650
ERFFLSLESL VGCVLSGPTS PLAFSDSVLN VINQNAKQLE NKEHLWKMWS
660 670 680 690 700
VIVTPLTELI NQTNEVNQGD ALEHNFSAIY GALTLPVNHI FSEQRFPVAT
710 720 730 740 750
MKTLLRTWSE LYRAFARCAA LVATAEENLC CEELSSKIMS SLEDEGFSNL
760 770 780 790 800
LFVDRIIYII TVMVDCIDFS PYNIKYQPKV KSPQRPSDWS KKKNEPLGKL
810 820 830 840 850
TSLFKLIVKV IYSFHTLSFK EAHSDTLFTI GNSITGIISS VLGHISLPSM
860 870 880 890 900
IRKIFATLTR PLALFYENSK LDEVPKVYSC LNNKLEKLLG EIIACLQFSY
910 920 930 940 950
TGTYDSELLE QLSPLLCIIF LHKNKQIRKQ SAQFWNATFA KVMMLVYPEE
960 970 980 990 1000
LKPVLTQAKQ KFLLLLPGLE TVEMMEESSG PYSDGTENSQ LNVKISGMER
1010 1020 1030 1040 1050
KSNGKRDSFL AQTKNKKENM KPAAKLKLES SSLKVKGEIL LEEEKSTDFV
1060 1070 1080 1090 1100
FIPPEGKDAK ERILTDHQKE VLKTKRCDIP AMYNNLDVSQ DTLFTQYSQE
1110 1120 1130 1140 1150
EPMEIPTLTR KPKEDSKMMI TEEQMDSDIV IPQDVTEDCG MAEHLEKSSL
1160 1170 1180 1190 1200
SNNECGSLDK TSPEMSNSNN DERKKALISS RKTSTECASS TENSFVVSSS
1210 1220 1230 1240 1250
SVSNTTVAGT PPYPTSRRQT FITLEKFDGS ENRPFSPSPL NNISSTVTVK
1260 1270 1280 1290 1300
NNQETMIKTD FLPKAKQREG TFSKSDSEKI VNGTKRSSRR AGKAEQTGNK
1310 1320 1330 1340 1350
RSKPLMRSEP EKNTEESVEG IVVLENNPPG LLNQTECVSD NQVHLSESTM
1360 1370 1380 1390 1400
EHDNTKLKAA TVENAVLLET NTVEEKNVEI NLESKENTPP VVISADQMVN
1410 1420 1430 1440 1450
EDSQVQITPN QKTLRRSSRR RSEVVESTTE SQDKENSHQK KERRKEEEKP
1460 1470 1480 1490 1500
LQKSPLHIKD DVLPKQKLIA EQTLQENLIE KGSNLHEKTL GETSANAETE
1510 1520 1530 1540 1550
QNKKKADPEN IKSEGDGTQD IVDKSSEKLV RGRTRYQTRR ASQGLLSSIE
1560 1570 1580 1590 1600
NSESDSSEAK EEGSRKKRSG KWKNKSNESV DIQDQEEKVV KQECIKAENQ
1610 1620 1630 1640 1650
SHDYKATSEE DVSIKSPICE KQDESNTVIC QDSTVTSDLL QVPDDLPNVC
1660 1670 1680 1690 1700
EEKNETSKYA EYSFTSLPVP ESNLRTRNAI KRLHKRDSFD NCSLGESSKI
1710 1720 1730 1740 1750
GISDISSLSE KTFQTLECQH KRSRRVRRSK GCDCCGEKSQ PQEKSLIGLK
1760 1770 1780 1790 1800
NTENNDVEIS ETKKADVQAP VSPSETSQAN PYSEGQFLDE HHSVNFHLGL
1810 1820 1830 1840 1850
KEDNDTINDS LIVSETKSKE NTMQESLPSG IVNFREEICD MDSSEAMSLE
1860 1870 1880 1890 1900
SQESPNENFK TVGPCLGDSK NVSQESLETK EEKPEETPKM ELSLENVTVE
1910 1920 1930 1940 1950
GNACKVTESN LEKAKTMELN VGNEASFHGQ ERTKTGISEE AAIEENKRND
1960 1970 1980 1990 2000
DSEADTAKLN AKEVATEEFN SDISLSDNTT PVKLNAQTEI SEQTAAGELD
2010 2020 2030 2040 2050
GGNDVSDLHS SEETNTKMKN NEEMMIGEAM AETGHDGETE NEGITTKTSK
2060 2070 2080 2090 2100
PDEAETNMLT AEMDNFVCDT VEMSTEEGII DANKTETNTE YSKSEEKLDN
2110 2120 2130 2140 2150
NQMVMESDIL QEDHHTSQKV EEPSQCLASG TAISELIIED NNASPQKLRE
2160 2170 2180 2190 2200
LDPSLVSAND SPSGMQTRCV WSPLASPSTS ILKRGLKRSQ EDEISSPVNK
2210 2220 2230 2240 2250
VRRVSFADPI YQAGLADDID RRCSIVRSHS SNSSPIGKSV KTSPTTQSKH
2260 2270 2280 2290 2300
NTTSAKGFLS PGSRSPKFKS SKKCLISEMA KESIPCPTES VYPPLVNCVA
2310 2320 2330 2340 2350
PVDIILPQIT SNMWARGLGQ LIRAKNIKTI GDLSTLTASE IKTLPIRSPK
2360 2370 2380 2390 2400
VSNVKKALRI YHEQQVKTRG LEEIPVFDIS EKTVNGIENK SLSPDEERLV
2410 2420 2430 2440 2450
SDIIDPVALE IPLSKNLLAQ ISALALQLDS EDLHNYSGSQ LFEMHEKLSC
2460 2470
MANSVIKNLQ SRWRSPSHEN SI
Length:2,472
Mass (Da):274,466
Last modified:July 5, 2005 - v2
Checksum:iA45DCE3C5F9E052D
GO
Isoform 2 (identifier: Q5UIP0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2250-2275: Missing.

Show »
Length:2,446
Mass (Da):271,689
Checksum:i44D755C85EF23042
GO

Sequence cautioni

The sequence CAI45961.1 differs from that shown. Reason: Frameshift at position 470.
The sequence BAA91705.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAB14313.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAB14792.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAB85058.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961N → D in AAT40745. (PubMed:15342490)Curated
Sequence conflicti699 – 6991A → P in BAA91705. (PubMed:14702039)Curated
Sequence conflicti1256 – 12561M → V in BAA91705. (PubMed:14702039)Curated
Sequence conflicti2316 – 23161R → G in BAB85058. (PubMed:14702039)Curated
Sequence conflicti2392 – 23921L → F in BAB85058. (PubMed:14702039)Curated
Sequence conflicti2445 – 24462HE → RV in BAB85058. (PubMed:14702039)Curated
Sequence conflicti2464 – 24641R → G in BAB85058. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti836 – 8361G → S.2 Publications
Corresponds to variant rs2444263 [ dbSNP | Ensembl ].
VAR_022788
Natural varianti1362 – 13621V → M.2 Publications
Corresponds to variant rs2123465 [ dbSNP | Ensembl ].
VAR_022789
Natural varianti1686 – 16861R → G.
Corresponds to variant rs3732305 [ dbSNP | Ensembl ].
VAR_022790
Natural varianti1784 – 17841E → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_035983
Natural varianti1862 – 18621V → I.
Corresponds to variant rs2444258 [ dbSNP | Ensembl ].
VAR_022791
Natural varianti1955 – 19551D → H in a breast cancer sample; somatic mutation. 1 Publication
VAR_035984
Natural varianti2021 – 20211N → Y.3 Publications
Corresponds to variant rs2444257 [ dbSNP | Ensembl ].
VAR_022792
Natural varianti2165 – 21651M → R.
Corresponds to variant rs16830057 [ dbSNP | Ensembl ].
VAR_022793
Natural varianti2418 – 24181L → V.5 Publications
Corresponds to variant rs1065177 [ dbSNP | Ensembl ].
VAR_022794

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2250 – 227526Missing in isoform 2. 2 PublicationsVSP_014431Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY585745 mRNA. Translation: AAT40745.1.
AY727910 mRNA. Translation: AAV51401.1.
AY727911 mRNA. Translation: AAV51402.1.
AY727912 mRNA. Translation: AAV51403.1.
AY727913 mRNA. Translation: AAV51404.1.
AY584066 mRNA. Translation: AAS94233.1.
AC009311 Genomic DNA. No translation available.
AC009497 Genomic DNA. No translation available.
AL080129 mRNA. Translation: CAB45727.1.
CR933663 mRNA. Translation: CAI45961.1. Sequence problems.
AK001461 mRNA. Translation: BAA91705.1. Different initiation.
AK022932 mRNA. Translation: BAB14313.1. Different initiation.
AK024033 mRNA. Translation: BAB14792.1. Different initiation.
AK074349 mRNA. Translation: BAB85058.1. Different initiation.
U79263 mRNA. Translation: AAB50209.1.
CCDSiCCDS2194.1. [Q5UIP0-1]
CCDS54406.1. [Q5UIP0-2]
PIRiT12518.
RefSeqiNP_001171134.1. NM_001177663.1. [Q5UIP0-2]
NP_001171135.1. NM_001177664.1. [Q5UIP0-2]
NP_001171136.1. NM_001177665.1. [Q5UIP0-2]
NP_060621.3. NM_018151.4. [Q5UIP0-1]
XP_005246722.1. XM_005246665.1. [Q5UIP0-1]
UniGeneiHs.655671.
Hs.735592.

Genome annotation databases

EnsembliENST00000243326; ENSP00000243326; ENSG00000080345. [Q5UIP0-1]
ENST00000428287; ENSP00000415691; ENSG00000080345. [Q5UIP0-2]
ENST00000430328; ENSP00000416123; ENSG00000080345. [Q5UIP0-2]
ENST00000444746; ENSP00000390181; ENSG00000080345. [Q5UIP0-1]
ENST00000453091; ENSP00000414615; ENSG00000080345. [Q5UIP0-2]
GeneIDi55183.
KEGGihsa:55183.
UCSCiuc002txl.3. human. [Q5UIP0-2]
uc002txm.3. human. [Q5UIP0-1]

Polymorphism databases

DMDMi68565701.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY585745 mRNA. Translation: AAT40745.1 .
AY727910 mRNA. Translation: AAV51401.1 .
AY727911 mRNA. Translation: AAV51402.1 .
AY727912 mRNA. Translation: AAV51403.1 .
AY727913 mRNA. Translation: AAV51404.1 .
AY584066 mRNA. Translation: AAS94233.1 .
AC009311 Genomic DNA. No translation available.
AC009497 Genomic DNA. No translation available.
AL080129 mRNA. Translation: CAB45727.1 .
CR933663 mRNA. Translation: CAI45961.1 . Sequence problems.
AK001461 mRNA. Translation: BAA91705.1 . Different initiation.
AK022932 mRNA. Translation: BAB14313.1 . Different initiation.
AK024033 mRNA. Translation: BAB14792.1 . Different initiation.
AK074349 mRNA. Translation: BAB85058.1 . Different initiation.
U79263 mRNA. Translation: AAB50209.1 .
CCDSi CCDS2194.1. [Q5UIP0-1 ]
CCDS54406.1. [Q5UIP0-2 ]
PIRi T12518.
RefSeqi NP_001171134.1. NM_001177663.1. [Q5UIP0-2 ]
NP_001171135.1. NM_001177664.1. [Q5UIP0-2 ]
NP_001171136.1. NM_001177665.1. [Q5UIP0-2 ]
NP_060621.3. NM_018151.4. [Q5UIP0-1 ]
XP_005246722.1. XM_005246665.1. [Q5UIP0-1 ]
UniGenei Hs.655671.
Hs.735592.

3D structure databases

ProteinModelPortali Q5UIP0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120482. 25 interactions.
IntActi Q5UIP0. 118 interactions.
MINTi MINT-3974483.

PTM databases

PhosphoSitei Q5UIP0.

Polymorphism databases

DMDMi 68565701.

Proteomic databases

MaxQBi Q5UIP0.
PaxDbi Q5UIP0.
PRIDEi Q5UIP0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000243326 ; ENSP00000243326 ; ENSG00000080345 . [Q5UIP0-1 ]
ENST00000428287 ; ENSP00000415691 ; ENSG00000080345 . [Q5UIP0-2 ]
ENST00000430328 ; ENSP00000416123 ; ENSG00000080345 . [Q5UIP0-2 ]
ENST00000444746 ; ENSP00000390181 ; ENSG00000080345 . [Q5UIP0-1 ]
ENST00000453091 ; ENSP00000414615 ; ENSG00000080345 . [Q5UIP0-2 ]
GeneIDi 55183.
KEGGi hsa:55183.
UCSCi uc002txl.3. human. [Q5UIP0-2 ]
uc002txm.3. human. [Q5UIP0-1 ]

Organism-specific databases

CTDi 55183.
GeneCardsi GC02P152266.
HGNCi HGNC:23207. RIF1.
HPAi HPA036887.
HPA036888.
MIMi 608952. gene.
neXtProti NX_Q5UIP0.
PharmGKBi PA134933858.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG87885.
GeneTreei ENSGT00390000012204.
HOVERGENi HBG080431.
InParanoidi Q5UIP0.
KOi K11138.
OMAi PTESVYP.
OrthoDBi EOG70GMDW.
PhylomeDBi Q5UIP0.
TreeFami TF323789.

Miscellaneous databases

ChiTaRSi RIF1. human.
GeneWikii RIF1.
GenomeRNAii 55183.
NextBioi 59015.
PROi Q5UIP0.
SOURCEi Search...

Gene expression databases

Bgeei Q5UIP0.
CleanExi HS_RIF1.
ExpressionAtlasi Q5UIP0. baseline and differential.
Genevestigatori Q5UIP0.

Family and domain databases

Gene3Di 1.25.10.10. 3 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR028566. Rif1.
IPR022031. Rif1_N.
[Graphical view ]
PANTHERi PTHR22928. PTHR22928. 1 hit.
Pfami PF12231. Rif1_N. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 4 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human Rif1, ortholog of a yeast telomeric protein, is regulated by ATM and 53BP1 and functions in the S-phase checkpoint."
    Silverman J., Takai H., Buonomo S.B.C., Eisenhaber F., De Lange T.
    Genes Dev. 18:2108-2119(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, VARIANTS TYR-2021 AND VAL-2418.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Human Rif1 protein binds aberrant telomeres and aligns along anaphase midzone microtubules."
    Xu L., Blackburn E.H.
    J. Cell Biol. 167:819-830(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANTS SER-836; MET-1362; TYR-2021 AND VAL-2418.
  4. "Identification and characterization of human Rif1."
    Simonsson T.
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-853 AND 1728-2472 (ISOFORM 1), VARIANTS TYR-2021 AND VAL-2418.
    Tissue: Testis and Testis carcinoma.
  6. "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] OF 161-1499 AND 2217-2472 (ISOFORM 1), VARIANTS SER-836; MET-1362 AND VAL-2418.
  7. "Large-scale concatenation cDNA sequencing."
    Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
    Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2108-2472 (ISOFORM 2), VARIANT VAL-2418.
    Tissue: Brain.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1454 AND SER-1688, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-409 AND SER-1579, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1513; THR-1518 AND SER-1542, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402; THR-409; SER-1162; SER-1236; SER-1238; SER-1422; SER-1554; SER-1616; SER-1688; SER-1693; SER-1810; SER-2144; SER-2172; SER-2196; SER-2205; SER-2260; SER-2339; SER-2391; SER-2393; SER-2465 AND SER-2471, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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 SER-979; THR-1047; SER-1552; SER-1554; SER-1579; SER-1688; THR-1806; SER-1971 AND SER-2196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1238; SER-1454; SER-1579; SER-1688; SER-1810; SER-1873; SER-1876; SER-2161; SER-2172; SER-2176; SER-2196; SER-2205 AND SER-2393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782; SER-1422; SER-1454; SER-1542; SER-1554; SER-1576; SER-1579; SER-1688; SER-1873; SER-2144; SER-2161; THR-2167 AND SER-2393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-1784 AND HIS-1955.

Entry informationi

Entry nameiRIF1_HUMAN
AccessioniPrimary (citable) accession number: Q5UIP0
Secondary accession number(s): A6NC27
, C9JBR1, Q5H9R3, Q5UIP2, Q66YK6, Q6PRU2, Q8TE94, Q99772, Q9H830, Q9H9B9, Q9NVP5, Q9Y4R4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: October 29, 2014
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
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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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

External Data

Dasty 3