Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8IZH2

- XRN1_HUMAN

UniProt

Q8IZH2 - XRN1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

5'-3' exoribonuclease 1

Gene

XRN1

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

Functioni

Major 5'-3' exoribonuclease involved in mRNA decay. Required for the 5'-3'-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA (By similarity). Plays a role in replication-dependent histone mRNA degradation. May act as a tumor suppressor protein in osteogenic sarcoma (OGS).By similarity1 Publication

GO - Molecular functioni

  1. 5'-3' exonuclease activity Source: InterPro
  2. DNA binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
  2. gene expression Source: Reactome
  3. histone mRNA catabolic process Source: UniProtKB
  4. mRNA metabolic process Source: Reactome
  5. nuclear mRNA surveillance Source: UniProtKB
  6. nuclear-transcribed mRNA catabolic process Source: UniProtKB
  7. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  8. RNA metabolic process Source: Reactome
  9. rRNA catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_20518. mRNA decay by 5' to 3' exoribonuclease.
REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-3' exoribonuclease 1 (EC:3.1.13.-)
Alternative name(s):
Strand-exchange protein 1 homolog
Gene namesi
Name:XRN1
Synonyms:SEP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:30654. XRN1.

Subcellular locationi

Cytoplasm 3 Publications
Note: Discrete foci at the inner surface of the cell membrane.

GO - Cellular componenti

  1. cytoplasmic mRNA processing body Source: Ensembl
  2. cytosol Source: Reactome
  3. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA134878471.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 170617065'-3' exoribonuclease 1PRO_0000071392Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1348 – 13481PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8IZH2.
PaxDbiQ8IZH2.
PRIDEiQ8IZH2.

PTM databases

PhosphoSiteiQ8IZH2.

Expressioni

Tissue specificityi

Expressed in heart, brain, pancreas, spleen, testis, osteogenic sarcoma (OGS) biopsy and primary cell lines.1 Publication

Inductioni

By GDNF/glial cell line-derived neurotrophic factor.1 Publication

Gene expression databases

BgeeiQ8IZH2.
CleanExiHS_XRN1.
ExpressionAtlasiQ8IZH2. baseline and differential.
GenevestigatoriQ8IZH2.

Organism-specific databases

HPAiHPA035005.
HPA035006.

Interactioni

Subunit structurei

Associates with alpha and beta tubulins (By similarity). Found in a mRNP complex with UPF1, UPF2, UPF3B and XRN1. Interacts with ZC3HAV1 in an RNA-dependent manner. Interacts with DIS3L2.By similarity3 Publications

Protein-protein interaction databases

BioGridi119970. 73 interactions.
DIPiDIP-31174N.
IntActiQ8IZH2. 25 interactions.
STRINGi9606.ENSP00000264951.

Structurei

3D structure databases

ProteinModelPortaliQ8IZH2.
SMRiQ8IZH2. Positions 1-600.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 5'-3' exonuclease family.Curated

Phylogenomic databases

eggNOGiCOG5049.
GeneTreeiENSGT00670000098080.
HOVERGENiHBG094164.
KOiK12618.
OMAiCKQRKSN.
OrthoDBiEOG7S7SCW.
PhylomeDBiQ8IZH2.
TreeFamiTF105757.

Family and domain databases

InterProiIPR027073. 5_3_exoribonuclease.
IPR016494. 5_3_exoribonuclease_1.
IPR004859. Put_53exo.
[Graphical view]
PANTHERiPTHR12341. PTHR12341. 1 hit.
PfamiPF03159. XRN_N. 1 hit.
[Graphical view]
PIRSFiPIRSF006743. Exonuclease_Xnr1. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8IZH2-1) [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
MGVPKFYRWI SERYPCLSEV VKEHQIPEFD NLYLDMNGII HQCSHPNDDD
60 70 80 90 100
VHFRISDDKI FTDIFHYLEV LFRIIKPRKV FFMAVDGVAP RAKMNQQRGR
110 120 130 140 150
RFRSAKEAED KIKKAIEKGE TLPTEARFDS NCITPGTEFM ARLHEHLKYF
160 170 180 190 200
VNMKISTDKS WQGVTIYFSG HETPGEGEHK IMEFIRSEKA KPDHDPNTRH
210 220 230 240 250
CLYGLDADLI MLGLTSHEAH FSLLREEVRF GGKKTQRVCA PEETTFHLLH
260 270 280 290 300
LSLMREYIDY EFSVLKEKIT FKYDIERIID DWILMGFLVG NDFIPHLPHL
310 320 330 340 350
HINHDALPLL YGTYVTILPE LGGYINESGH LNLPRFEKYL VKLSDFDREH
360 370 380 390 400
FSEVFVDLKW FESKVGNKYL NEAAGVAAEE ARNYKEKKKL KGQENSLCWT
410 420 430 440 450
ALDKNEGEMI TSKDNLEDET EDDDLFETEF RQYKRTYYMT KMGVDVVSDD
460 470 480 490 500
FLADQAACYV QAIQWILHYY YHGVQSWSWY YPYHYAPFLS DIHNISTLKI
510 520 530 540 550
HFELGKPFKP FEQLLAVLPA ASKNLLPACY QHLMTNEDSP IIEYYPPDFK
560 570 580 590 600
TDLNGKQQEW EAVVLIPFID EKRLLEAMET CNHSLKKEER KRNQHSECLM
610 620 630 640 650
CWYDRDTEFI YPSPWPEKFP AIERCCTRYK IISLDAWRVD INKNKITRID
660 670 680 690 700
QKALYFCGFP TLKHIRHKFF LKKSGVQVFQ QSSRGENMML EILVDAESDE
710 720 730 740 750
LTVENVASSV LGKSVFVNWP HLEEARVVAV SDGETKFYLE EPPGTQKLYS
760 770 780 790 800
GRTAPPSKVV HLGDKEQSNW AKEVQGISEH YLRRKGIIIN ETSAVVYAQL
810 820 830 840 850
LTGRKYQINQ NGEVRLEKQW SKQVVPFVYQ TIVKDIRAFD SRFSNIKTLD
860 870 880 890 900
DLFPLRSMVF MLGTPYYGCT GEVQDSGDVI TEGRIRVIFS IPCEPNLDAL
910 920 930 940 950
IQNQHKYSIK YNPGYVLASR LGVSGYLVSR FTGSIFIGRG SRRNPHGDHK
960 970 980 990 1000
ANVGLNLKFN KKNEEVPGYT KKVGSEWMYS SAAEQLLAEY LERAPELFSY
1010 1020 1030 1040 1050
IAKNSQEDVF YEDDIWPGEN ENGAEKVQEI ITWLKGHPVS TLSRSSCDLQ
1060 1070 1080 1090 1100
ILDAAIVEKI EEEVEKCKQR KNNKKVRVTV KPHLLYRPLE QQHGVIPDRD
1110 1120 1130 1140 1150
AEFCLFDRVV NVRENFSVPV GLRGTIIGIK GANREADVLF EVLFDEEFPG
1160 1170 1180 1190 1200
GLTIRCSPGR GYRLPTSALV NLSHGSRSET GNQKLTAIVK PQPAVHQHSS
1210 1220 1230 1240 1250
SSSVSSGHLG ALNHSPQSLF VPTQVPTKDD DEFCNIWQSL QGSGKMQYFQ
1260 1270 1280 1290 1300
PTIQEKGAVL PQEISQVNQH HKSGFNDNSV KYQQRKHDPH RKFKEECKSP
1310 1320 1330 1340 1350
KAECWSQKMS NKQPNSGIEN FLASLNISKE NEVQSSHHGE PPSEEHLSPQ
1360 1370 1380 1390 1400
SFAMGTRMLK EILKIDGSNT VDHKNEIKQI ANEIPVSSNR RDEYGLPSQP
1410 1420 1430 1440 1450
KQNKKLASYM NKPHSANEYH NVQSMDNMCW PAPSQIPPVS TPVTELSRIC
1460 1470 1480 1490 1500
SLVGMPQPDF SFLRMPQTMT VCQVKLSNGL LVHGPQCHSE NEAKEKAALF
1510 1520 1530 1540 1550
ALQQLGSLGM NFPLPSQVFA NYPSAVPPGT IPPAFPPPTG WDHYGSNYAL
1560 1570 1580 1590 1600
GAANIMPSSS HLFGSMPWGP SVPVPGKPFH HTLYSGTMPM AGGIPGGVHN
1610 1620 1630 1640 1650
QFIPLQVTKK RVANKKNFEN KEAQSSQATP VQTSQPDSSN IVKVSPRESS
1660 1670 1680 1690 1700
SASLKSSPIA QPASSFQVET ASQGHSISHH KSTPISSSRR KSRKLAVNFG

VSKPSE
Length:1,706
Mass (Da):194,107
Last modified:March 1, 2003 - v1
Checksum:iD06A76208DE78698
GO
Isoform 2 (identifier: Q8IZH2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1354-1354: M → MK
     1540-1552: Missing.

Show »
Length:1,694
Mass (Da):192,843
Checksum:i25AD7CD0191A4E05
GO
Isoform 3 (identifier: Q8IZH2-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     449-459: DDFLADQAACY → EYVFANAFILK
     460-1706: Missing.

Show »
Length:459
Mass (Da):53,818
Checksum:i2C546FA5EDB81BC3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481D → G in CAE45950. (PubMed:17974005)Curated
Sequence conflicti55 – 551I → T in BAC04718. (PubMed:14702039)Curated
Sequence conflicti113 – 1131K → E in CAH18332. (PubMed:17974005)Curated
Sequence conflicti142 – 1421R → K in AAH48104. (PubMed:15489334)Curated
Sequence conflicti148 – 1481K → E in CAH18332. (PubMed:17974005)Curated
Sequence conflicti572 – 5721Missing in CAB63749. (PubMed:17974005)Curated
Sequence conflicti722 – 7221L → I in CAE45950. (PubMed:17974005)Curated
Sequence conflicti834 – 8341K → R in CAH18332. (PubMed:17974005)Curated
Sequence conflicti1250 – 12501Q → R in CAH18332. (PubMed:17974005)Curated
Sequence conflicti1463 – 14631L → F in CAE45950. (PubMed:17974005)Curated
Sequence conflicti1686 – 16861S → P in CAH18332. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti674 – 6741S → G.
Corresponds to variant rs35214510 [ dbSNP | Ensembl ].
VAR_053000
Natural varianti1259 – 12591V → A.
Corresponds to variant rs35902661 [ dbSNP | Ensembl ].
VAR_053001

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei449 – 45911DDFLADQAACY → EYVFANAFILK in isoform 3. 1 PublicationVSP_016692Add
BLAST
Alternative sequencei460 – 17061247Missing in isoform 3. 1 PublicationVSP_016693Add
BLAST
Alternative sequencei1354 – 13541M → MK in isoform 2. 1 PublicationVSP_016694
Alternative sequencei1540 – 155213Missing in isoform 2. 1 PublicationVSP_016695Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY137776 mRNA. Translation: AAN11306.1.
AL133623 mRNA. Translation: CAB63749.1.
BX640905 mRNA. Translation: CAE45950.1.
CR627396 mRNA. Translation: CAH10490.1.
CR749518 mRNA. Translation: CAH18332.1.
BC039314 mRNA. Translation: AAH39314.1.
BC048104 mRNA. Translation: AAH48104.1.
AK096177 mRNA. Translation: BAC04718.1.
CCDSiCCDS3123.1. [Q8IZH2-1]
CCDS63801.1. [Q8IZH2-2]
CCDS75028.1. [Q8IZH2-3]
PIRiT43461.
RefSeqiNP_001269786.1. NM_001282857.1. [Q8IZH2-2]
NP_001269788.1. NM_001282859.1. [Q8IZH2-3]
NP_061874.3. NM_019001.4. [Q8IZH2-1]
UniGeneiHs.435103.

Genome annotation databases

EnsembliENST00000264951; ENSP00000264951; ENSG00000114127. [Q8IZH2-1]
ENST00000392981; ENSP00000376707; ENSG00000114127. [Q8IZH2-2]
ENST00000463916; ENSP00000418404; ENSG00000114127. [Q8IZH2-3]
GeneIDi54464.
KEGGihsa:54464.
UCSCiuc003eus.3. human. [Q8IZH2-1]
uc003euu.3. human. [Q8IZH2-2]
uc003euw.3. human. [Q8IZH2-3]

Polymorphism databases

DMDMi74714582.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY137776 mRNA. Translation: AAN11306.1 .
AL133623 mRNA. Translation: CAB63749.1 .
BX640905 mRNA. Translation: CAE45950.1 .
CR627396 mRNA. Translation: CAH10490.1 .
CR749518 mRNA. Translation: CAH18332.1 .
BC039314 mRNA. Translation: AAH39314.1 .
BC048104 mRNA. Translation: AAH48104.1 .
AK096177 mRNA. Translation: BAC04718.1 .
CCDSi CCDS3123.1. [Q8IZH2-1 ]
CCDS63801.1. [Q8IZH2-2 ]
CCDS75028.1. [Q8IZH2-3 ]
PIRi T43461.
RefSeqi NP_001269786.1. NM_001282857.1. [Q8IZH2-2 ]
NP_001269788.1. NM_001282859.1. [Q8IZH2-3 ]
NP_061874.3. NM_019001.4. [Q8IZH2-1 ]
UniGenei Hs.435103.

3D structure databases

ProteinModelPortali Q8IZH2.
SMRi Q8IZH2. Positions 1-600.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119970. 73 interactions.
DIPi DIP-31174N.
IntActi Q8IZH2. 25 interactions.
STRINGi 9606.ENSP00000264951.

PTM databases

PhosphoSitei Q8IZH2.

Polymorphism databases

DMDMi 74714582.

Proteomic databases

MaxQBi Q8IZH2.
PaxDbi Q8IZH2.
PRIDEi Q8IZH2.

Protocols and materials databases

DNASUi 54464.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264951 ; ENSP00000264951 ; ENSG00000114127 . [Q8IZH2-1 ]
ENST00000392981 ; ENSP00000376707 ; ENSG00000114127 . [Q8IZH2-2 ]
ENST00000463916 ; ENSP00000418404 ; ENSG00000114127 . [Q8IZH2-3 ]
GeneIDi 54464.
KEGGi hsa:54464.
UCSCi uc003eus.3. human. [Q8IZH2-1 ]
uc003euu.3. human. [Q8IZH2-2 ]
uc003euw.3. human. [Q8IZH2-3 ]

Organism-specific databases

CTDi 54464.
GeneCardsi GC03M142025.
HGNCi HGNC:30654. XRN1.
HPAi HPA035005.
HPA035006.
MIMi 607994. gene.
neXtProti NX_Q8IZH2.
PharmGKBi PA134878471.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5049.
GeneTreei ENSGT00670000098080.
HOVERGENi HBG094164.
KOi K12618.
OMAi CKQRKSN.
OrthoDBi EOG7S7SCW.
PhylomeDBi Q8IZH2.
TreeFami TF105757.

Enzyme and pathway databases

Reactomei REACT_20518. mRNA decay by 5' to 3' exoribonuclease.
REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

Miscellaneous databases

ChiTaRSi XRN1. human.
GenomeRNAii 54464.
NextBioi 56731.
PROi Q8IZH2.
SOURCEi Search...

Gene expression databases

Bgeei Q8IZH2.
CleanExi HS_XRN1.
ExpressionAtlasi Q8IZH2. baseline and differential.
Genevestigatori Q8IZH2.

Family and domain databases

InterProi IPR027073. 5_3_exoribonuclease.
IPR016494. 5_3_exoribonuclease_1.
IPR004859. Put_53exo.
[Graphical view ]
PANTHERi PTHR12341. PTHR12341. 1 hit.
Pfami PF03159. XRN_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF006743. Exonuclease_Xnr1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of human SEP1 as a glial cell line-derived neurotrophic factor-inducible protein and its expression in the nervous system."
    Shimoyama Y., Morikawa Y., Ichihara M., Kodama Y., Fukuda N., Hayashi H., Morinaga T., Iwashita T., Murakumo Y., Takahashi M.
    Neuroscience 121:899-906(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION BY GDNF, SUBCELLULAR LOCATION.
    Tissue: Neuroblastoma.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Fetal kidney, Small intestine and Testis.
  3. "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 3).
    Tissue: Brain and Testis.
  4. "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 1-473 (ISOFORMS 1/2).
    Tissue: Mesangial cell.
  5. "Cloning and characterization of human Sep1 (hSEP1) gene and cytoplasmic localization of its product."
    Sato Y., Shimamoto A., Shobuike T., Sugimoto M., Ikeda H., Kuroda S., Furuichi Y.
    DNA Res. 5:241-246(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORM 2), SUBCELLULAR LOCATION.
  6. "Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities."
    Lejeune F., Li X., Maquat L.E.
    Mol. Cell 12:675-687(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH UPF1; UPF2 AND UPF3B.
  7. "The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci."
    Ingelfinger D., Arndt-Jovin D.J., Luehrmann R., Achsel T.
    RNA 8:1489-1501(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "The human homolog of yeast SEP1 is a novel candidate tumor suppressor gene in osteogenic sarcoma."
    Zhang K., Dion N., Fuchs B., Damron T., Gitelis S., Irwin R., O'Connor M., Schwartz H., Scully S.P., Rock M.G., Bolander M.E., Sarkar G.
    Gene 298:121-127(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: POTENTIAL TUMOR SUPPRESSION ROLE IN OSTEOGENIC SARCOMA, TISSUE SPECIFICITY.
  9. "Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'."
    Mullen T.E., Marzluff W.F.
    Genes Dev. 22:50-65(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation."
    Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T., Gao G.
    Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZC3HAV1.
  13. "Exonuclease hDIS3L2 specifies an exosome-independent 3'-5' degradation pathway of human cytoplasmic mRNA."
    Lubas M., Damgaard C.K., Tomecki R., Cysewski D., Jensen T.H., Dziembowski A.
    EMBO J. 32:1855-1868(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DIS3L2.

Entry informationi

Entry nameiXRN1_HUMAN
AccessioniPrimary (citable) accession number: Q8IZH2
Secondary accession number(s): Q4G0S3
, Q68D88, Q6AI24, Q6MZS8, Q86WS7, Q8N8U4, Q9UF39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2003
Last modified: October 29, 2014
This is version 104 of the entry and version 1 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

Miscellaneous

Down-regulated in OGS biopsy.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3