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Q9H0D6 (XRN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5'-3' exoribonuclease 2

EC=3.1.13.-
Alternative name(s):
DHM1-like protein
Short name=DHP protein
Gene names
Name:XRN2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length950 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Possesses 5'->3' exoribonuclease activity By similarity. May promote the termination of transcription by RNA polymerase II. During transcription termination, cleavage at the polyadenylation site liberates a 5' fragment which is subsequently processed to form the mature mRNA and a 3' fragment which remains attached to the elongating polymerase. The processive degradation of this 3' fragment by this protein may promote termination of transcription. Ref.8 Ref.10

Catalytic activity

Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates.

Subcellular location

Nucleusnucleolus Ref.7.

Tissue specificity

Expressed in the spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocytes, heart, brain, placenta, lung, liver, skeletal muscle, kidney, and pancreas. Isoform 2 is expressed predominantly in peripheral blood leukocytes. Ref.1 Ref.2

Sequence similarities

Belongs to the 5'-3' exonuclease family. XRN2/RAT1 subfamily.

Contains 1 CCHC-type zinc finger.

Sequence caution

The sequence AAR24369.1 differs from that shown. Reason: Frameshift at position 73.

The sequence BAA90934.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processmRNA processing
Transcription
Transcription regulation
Transcription termination
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionExonuclease
Hydrolase
Nuclease
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, exonucleolytic

Inferred from direct assay Ref.8. Source: UniProtKB

DNA-templated transcription, termination

Inferred from electronic annotation. Source: UniProtKB-KW

RNA catabolic process

Traceable author statement Ref.1. Source: ProtInc

RNA metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

RNA phosphodiester bond hydrolysis, exonucleolytic

Traceable author statement Ref.1. Source: GOC

RNA processing

Traceable author statement Ref.1. Source: ProtInc

cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

spermatogenesis

Inferred from expression pattern Ref.1. Source: UniProtKB

   Cellular_componentaggresome

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay Ref.7. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

   Molecular_function5'-3' exonuclease activity

Inferred from direct assay Ref.8. Source: UniProtKB

5'-3' exoribonuclease activity

Traceable author statement Ref.1. Source: UniProtKB

nuclease activity

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H0D6-1)

Also known as: XRN2a;

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: Q9H0D6-2)

Also known as: XRN2b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-76: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9509505'-3' exoribonuclease 2
PRO_0000071396

Regions

Zinc finger262 – 27817CCHC-type

Amino acid modifications

Modified residue2861N6-acetyllysine By similarity
Modified residue4391Phosphothreonine Ref.14
Modified residue4481Phosphoserine Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17 Ref.18 Ref.19 Ref.21
Modified residue4711Phosphoserine Ref.18
Modified residue4731Phosphoserine Ref.18
Modified residue4751Phosphoserine Ref.18
Modified residue4991Phosphoserine Ref.9 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21
Modified residue5011Phosphoserine Ref.9 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21

Natural variations

Alternative sequence1 – 7676Missing in isoform 2.
VSP_020596
Natural variant7431R → M.
Corresponds to variant rs6137324 [ dbSNP | Ensembl ].
VAR_027516
Natural variant9251R → C.
Corresponds to variant rs6047420 [ dbSNP | Ensembl ].
VAR_053002

Experimental info

Sequence conflict141Y → C in AAQ13577. Ref.1
Sequence conflict1091A → V in AAD55138. Ref.1
Sequence conflict1091A → V in AAQ13577. Ref.1
Sequence conflict122 – 1243SKE → IKR in AAD55138. Ref.1
Sequence conflict240 – 2456GLATHE → AFPHMN in AAQ13577. Ref.1
Sequence conflict2591K → R in AAD55138. Ref.1
Sequence conflict2591K → R in AAQ13577. Ref.1
Sequence conflict2801P → S in AAD55138. Ref.1
Sequence conflict2801P → S in AAQ13577. Ref.1
Sequence conflict3131L → V in AAQ13577. Ref.1
Sequence conflict4631E → D in AAD55138. Ref.1
Sequence conflict5821P → S in AAQ13577. Ref.1
Sequence conflict5841D → E in AAD55138. Ref.1
Sequence conflict7371S → A in AAD55138. Ref.1
Sequence conflict7601F → L in AAR24369. Ref.2
Sequence conflict7871E → G in AAD55138. Ref.1
Sequence conflict8741P → L in AAR24369. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (XRN2a) [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 763B5E0E628F97A8

FASTA950108,582
        10         20         30         40         50         60 
MGVPAFFRWL SRKYPSIIVN CVEEKPKECN GVKIPVDASK PNPNDVEFDN LYLDMNGIIH 

        70         80         90        100        110        120 
PCTHPEDKPA PKNEDEMMVA IFEYIDRLFS IVRPRRLLYM AIDGVAPRAK MNQQRSRRFR 

       130        140        150        160        170        180 
ASKEGMEAAV EKQRVREEIL AKGGFLPPEE IKERFDSNCI TPGTEFMDNL AKCLRYYIAD 

       190        200        210        220        230        240 
RLNNDPGWKN LTVILSDASA PGEGEHKIMD YIRRQRAQPN HDPNTHHCLC GADADLIMLG 

       250        260        270        280        290        300 
LATHEPNFTI IREEFKPNKP KPCGLCNQFG HEVKDCEGLP REKKGKHDEL ADSLPCAEGE 

       310        320        330        340        350        360 
FIFLRLNVLR EYLERELTMA SLPFTFDVER SIDDWVFMCF FVGNDFLPHL PSLEIRENAI 

       370        380        390        400        410        420 
DRLVNIYKNV VHKTGGYLTE SGYVNLQRVQ MIMLAVGEVE DSIFKKRKDD EDSFRRRQKE 

       430        440        450        460        470        480 
KRKRMKRDQP AFTPSGILTP HALGSRNSPG SQVASNPRQA AYEMRMQNNS SPSISPNTSF 

       490        500        510        520        530        540 
TSDGSPSPLG GIKRKAEDSD SEPEPEDNVR LWEAGWKQRY YKNKFDVDAA DEKFRRKVVQ 

       550        560        570        580        590        600 
SYVEGLCWVL RYYYQGCASW KWYYPFHYAP FASDFEGIAD MPSDFEKGTK PFKPLEQLMG 

       610        620        630        640        650        660 
VFPAASGNFL PPSWRKLMSD PDSSIIDFYP EDFAIDLNGK KYAWQGVALL PFVDERRLRA 

       670        680        690        700        710        720 
ALEEVYPDLT PEETRRNSLG GDVLFVGKHH PLHDFILELY QTGSTEPVEV PPELCHGIQG 

       730        740        750        760        770        780 
KFSLDEEAIL PDQIVCSPVP MLRDLTQNTV VSINFKDPQF AEDYIFKAVM LPGARKPAAV 

       790        800        810        820        830        840 
LKPSDWEKSS NGRQWKPQLG FNRDRRPVHL DQAAFRTLGH VMPRGSGTGI YSNAAPPPVT 

       850        860        870        880        890        900 
YQGNLYRPLL RGQAQIPKLM SNMRPQDSWR GPPPLFQQQR FDRGVGAEPL LPWNRMLQTQ 

       910        920        930        940        950 
NAAFQPNQYQ MLAGPGGYPP RRDDRGGRQG YPREGRKYPL PPPSGRYNWN 

« Hide

Isoform 2 (XRN2b) [UniParc].

Checksum: 85DBF4213F810AEC
Show »

FASTA87499,962

References

« Hide 'large scale' references
[1]"Cloning and mapping of the XRN2 gene to human chromosome 20p11.1-p11.2."
Zhang M., Yu L., Xin Y., Hu P., Fu Q., Yu C., Zhao S.Y.
Genomics 59:252-254(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"A novel splice variant of human XRN2 gene is mainly expressed in blood leukocyte."
Li J., Zheng H., Ji C., Fei X., Zheng M., Gao Y., Ren Y., Gu S., Xie Y., Mao Y.
DNA Seq. 16:143-146(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[4]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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. expand/collapse author list , 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 358-950 (ISOFORMS 1/2).
Tissue: Colon.
[6]"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 371-950 (ISOFORMS 1/2).
Tissue: Colon.
[7]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Human 5' -> 3' exonuclease Xrn2 promotes transcription termination at co-transcriptional cleavage sites."
West S., Gromak N., Proudfoot N.J.
Nature 432:522-525(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"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-448; SER-499 AND SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Pause sites promote transcriptional termination of mammalian RNA polymerase II."
Gromak N., West S., Proudfoot N.J.
Mol. Cell. Biol. 26:3986-3996(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"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 SER-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-439 AND SER-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[16]"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].
[17]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448; SER-499 AND SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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-448; SER-471; SER-473; SER-475; SER-499 AND SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"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-448; SER-499 AND SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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-448; SER-499 AND SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF064257 mRNA. Translation: AAD55138.1.
AF152169 mRNA. Translation: AAQ13577.1.
AY382900 mRNA. Translation: AAR24369.1. Frameshift.
AL136841 mRNA. Translation: CAB66775.1.
AL117332, AL158013 Genomic DNA. Translation: CAI19756.1.
AL158013, AL117332 Genomic DNA. Translation: CAH71495.1.
AK000084 mRNA. Translation: BAA90934.1. Different initiation.
BC006417 mRNA. Translation: AAH06417.2.
CCDSCCDS13144.1. [Q9H0D6-1]
RefSeqNP_036387.2. NM_012255.3. [Q9H0D6-1]
UniGeneHs.255932.

3D structure databases

ProteinModelPortalQ9H0D6.
SMRQ9H0D6. Positions 1-430, 502-785.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116483. 49 interactions.
IntActQ9H0D6. 30 interactions.
MINTMINT-3065664.
STRING9606.ENSP00000366396.

PTM databases

PhosphoSiteQ9H0D6.

Polymorphism databases

DMDM30173484.

2D gel databases

SWISS-2DPAGEQ9H0D6.

Proteomic databases

MaxQBQ9H0D6.
PaxDbQ9H0D6.
PeptideAtlasQ9H0D6.
PRIDEQ9H0D6.

Protocols and materials databases

DNASU22803.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377191; ENSP00000366396; ENSG00000088930. [Q9H0D6-1]
ENST00000430571; ENSP00000413548; ENSG00000088930. [Q9H0D6-2]
GeneID22803.
KEGGhsa:22803.
UCSCuc002wsf.1. human. [Q9H0D6-1]

Organism-specific databases

CTD22803.
GeneCardsGC20P021283.
HGNCHGNC:12836. XRN2.
HPAHPA047118.
HPA050485.
MIM608851. gene.
neXtProtNX_Q9H0D6.
PharmGKBPA37427.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5049.
HOVERGENHBG036677.
InParanoidQ9H0D6.
KOK12619.
OMAGFSRDRR.
OrthoDBEOG7S7SCW.
PhylomeDBQ9H0D6.
TreeFamTF105977.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ9H0D6.
BgeeQ9H0D6.
CleanExHS_XRN2.
GenevestigatorQ9H0D6.

Family and domain databases

InterProIPR027073. 5_3_exoribonuclease.
IPR017151. 5_3_exoribonuclease_2.
IPR004859. Put_53exo.
IPR001878. Znf_CCHC.
[Graphical view]
PANTHERPTHR12341. PTHR12341. 1 hit.
PfamPF03159. XRN_N. 1 hit.
[Graphical view]
PIRSFPIRSF037239. Exonuclease_Xrn2. 1 hit.
SMARTSM00343. ZnF_C2HC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSXRN2. human.
GeneWiki5%27-3%27_exoribonuclease_2.
GenomeRNAi22803.
NextBio43160.
PMAP-CutDBQ9H0D6.
PROQ9H0D6.
SOURCESearch...

Entry information

Entry nameXRN2_HUMAN
AccessionPrimary (citable) accession number: Q9H0D6
Secondary accession number(s): Q3L8N4 expand/collapse secondary AC list , Q6KGZ9, Q9BQL1, Q9NTW0, Q9NXS6, Q9UL53
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM