Reviewed, UniProtKB/Swiss-Prot Q9H0D6 (XRN2_HUMAN)

Names and origin

Protein names

Recommended name:
    5'-3' exoribonuclease 2
    EC=3.1.13.-
Alternative name(s):
    DHM1-like protein
      Short name=DHP protein

Gene names

Name:

XRN2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	950 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
Catalytic activity	Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates.
Subcellular location	Nucleus › nucleolus. 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Transcription termination mRNA processing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Exonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	DNA catabolic process, exonucleolytic Ref.8 Inferred from direct assay. Source: UniProtKB RNA catabolic process Ref.1 Traceable author statement. 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-dependent Inferred from electronic annotation. Source: UniProtKB-KW spermatogenesis Ref.1 Inferred from expression pattern. Source: UniProtKB transcription termination Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleolus Ref.7 Inferred from direct assay. Source: UniProtKB
Molecular function	5'-3' exoribonuclease activity Ref.1 Traceable author statement. Source: UniProtKB nucleic acid binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
COMT	P21964	1	EBI-372110,EBI-372265
DOM3Z	O77932	1	EBI-372110,EBI-372173
EIF3L	Q9Y262	1	EBI-372110,EBI-373519
EIF5A	P63241	1	EBI-372110,EBI-373150
EIF6	P56537	1	EBI-372110,EBI-372243
EXOSC10	Q01780	1	EBI-372110,EBI-358236
EXOSC8	Q96B26	1	EBI-372110,EBI-371922
LSM3	P62310	1	EBI-372110,EBI-348239
MOCS3	O95396	1	EBI-372110,EBI-373206
PSMA3	P25788	1	EBI-372110,EBI-348380
TARDBP	Q13148	1	EBI-372110,EBI-372899
TIPARP	Q7Z3E1	1	EBI-372110,EBI-373532
TOLLIP	Q9H0E2	1	EBI-372110,EBI-74615
UPF2	Q9HAU5	1	EBI-372110,EBI-372073

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 950	950	5'-3' exoribonuclease 2		PRO_0000071396
Regions
	Zinc finger	262 – 278	17	CCHC-type
Amino acid modifications
	Modified residue	439	1	Phosphothreonine Ref.16
	Modified residue	448	1	Phosphoserine Ref.16 Ref.9 Ref.11 Ref.13 Ref.14 Ref.15
	Modified residue	455	1	Phosphoserine Ref.13
	Modified residue	499	1	Phosphoserine Ref.16 Ref.9 Ref.11 Ref.17
	Modified residue	501	1	Phosphoserine Ref.16 Ref.9 Ref.11 Ref.17 Ref.10
Natural variations
	Alternative sequence	1 – 76	76	Missing in isoform 2.		VSP_020596
	Natural variant	743	1	R → M: dbSNP rs6137324.		VAR_027516
	Natural variant	925	1	R → C: dbSNP rs6047420.		VAR_053002
Experimental info
	Sequence conflict	14	1	Y → C in AAQ13577. Ref.1
	Sequence conflict	109	1	A → V in AAD55138. Ref.1
	Sequence conflict	109	1	A → V in AAQ13577. Ref.1
	Sequence conflict	122 – 124	3	SKE → IKR in AAD55138. Ref.1
	Sequence conflict	240 – 245	6	GLATHE → AFPHMN in AAQ13577. Ref.1
	Sequence conflict	259	1	K → R in AAD55138. Ref.1
	Sequence conflict	259	1	K → R in AAQ13577. Ref.1
	Sequence conflict	280	1	P → S in AAD55138. Ref.1
	Sequence conflict	280	1	P → S in AAQ13577. Ref.1
	Sequence conflict	313	1	L → V in AAQ13577. Ref.1
	Sequence conflict	463	1	E → D in AAD55138. Ref.1
	Sequence conflict	582	1	P → S in AAQ13577. Ref.1
	Sequence conflict	584	1	D → E in AAD55138. Ref.1
	Sequence conflict	737	1	S → A in AAD55138. Ref.1
	Sequence conflict	760	1	F → L in AAR24369. Ref.2
	Sequence conflict	787	1	E → G in AAD55138. Ref.1
	Sequence conflict	874	1	P → L in AAR24369. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (XRN2a) [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 763B5E0E628F97A8	FASTA	950	108,582
	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
	Isoform 2 (XRN2b). Checksum: 85DBF4213F810AEC	FASTA	874	99,962
	10 20 30 40 50 60 MMVAIFEYID RLFSIVRPRR LLYMAIDGVA PRAKMNQQRS RRFRASKEGM EAAVEKQRVR 70 80 90 100 110 120 EEILAKGGFL PPEEIKERFD SNCITPGTEF MDNLAKCLRY YIADRLNNDP GWKNLTVILS 130 140 150 160 170 180 DASAPGEGEH KIMDYIRRQR AQPNHDPNTH HCLCGADADL IMLGLATHEP NFTIIREEFK 190 200 210 220 230 240 PNKPKPCGLC NQFGHEVKDC EGLPREKKGK HDELADSLPC AEGEFIFLRL NVLREYLERE 250 260 270 280 290 300 LTMASLPFTF DVERSIDDWV FMCFFVGNDF LPHLPSLEIR ENAIDRLVNI YKNVVHKTGG 310 320 330 340 350 360 YLTESGYVNL QRVQMIMLAV GEVEDSIFKK RKDDEDSFRR RQKEKRKRMK RDQPAFTPSG 370 380 390 400 410 420 ILTPHALGSR NSPGSQVASN PRQAAYEMRM QNNSSPSISP NTSFTSDGSP SPLGGIKRKA 430 440 450 460 470 480 EDSDSEPEPE DNVRLWEAGW KQRYYKNKFD VDAADEKFRR KVVQSYVEGL CWVLRYYYQG 490 500 510 520 530 540 CASWKWYYPF HYAPFASDFE GIADMPSDFE KGTKPFKPLE QLMGVFPAAS GNFLPPSWRK 550 560 570 580 590 600 LMSDPDSSII DFYPEDFAID LNGKKYAWQG VALLPFVDER RLRAALEEVY PDLTPEETRR 610 620 630 640 650 660 NSLGGDVLFV GKHHPLHDFI LELYQTGSTE PVEVPPELCH GIQGKFSLDE EAILPDQIVC 670 680 690 700 710 720 SPVPMLRDLT QNTVVSINFK DPQFAEDYIF KAVMLPGARK PAAVLKPSDW EKSSNGRQWK 730 740 750 760 770 780 PQLGFNRDRR PVHLDQAAFR TLGHVMPRGS GTGIYSNAAP PPVTYQGNLY RPLLRGQAQI 790 800 810 820 830 840 PKLMSNMRPQ DSWRGPPPLF QQQRFDRGVG AEPLLPWNRM LQTQNAAFQP NQYQMLAGPG 850 860 870 GYPPRRDDRG GRQGYPREGR KYPLPPPSGR YNWN

References

	« Hide 'large scale' referencesShow '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: 10409438] [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: 16147866] [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. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [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. , 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: 11780052] [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. , 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: 14702039] [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: 15489334] [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: 12429849] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[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: 15565158] [Abstract] Cited for: FUNCTION.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448; SER-499 AND SER-501, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, MASS SPECTROMETRY.
[11]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448; SER-499 AND SER-501, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"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: 16648491] [Abstract] Cited for: FUNCTION.
[13]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448 AND SER-455, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, MASS SPECTROMETRY. Tissue: Epithelium.
[15]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, MASS SPECTROMETRY.
[16]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-439; SER-448; SER-499 AND SER-501, MASS SPECTROMETRY.
[17]	"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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND SER-501, MASS SPECTROMETRY. Tissue: Liver.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00100151. IPI00788157.
RefSeq	NP_036387.2.
UniGene	Hs.255932
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H0D6. 15 interactions.
PTM databases
PhosphoSite	Q9H0D6.
2-D gel databases
SWISS-2DPAGE	Q9H0D6.
Proteomic databases
PeptideAtlas	Q9H0D6.
PRIDE	Q9H0D6.
Genome annotation databases
Ensembl	ENSG00000088930. Homo sapiens. [Contig view]
GeneID	22803.
KEGG	hsa:22803.
Organism-specific databases
GeneCards	GC20P021231.
H-InvDB	HIX0015683.
HGNC	HGNC:12836. XRN2.
MIM	608851. gene.
PharmGKB	PA37427.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q9H0D6.
OMA	Q9H0D6. RKRMKRD.
Gene expression databases
ArrayExpress	Q9H0D6.
Bgee	Q9H0D6.
CleanEx	HS_XRN2.
GermOnline	ENSG00000088930. Homo sapiens.
Family and domain databases
InterPro	IPR017151. 5_3_exoribonuclease_2. IPR004859. Put_53exo. IPR001878. Znf_CCHC. [Graphical view]
Pfam	PF03159. XRN_N. 1 hit. [Graphical view]
PIRSF	PIRSF037239. Exonuclease_Xrn2. 1 hit.
SMART	SM00343. ZnF_C2HC. 1 hit. [Graphical view]
PROSITE	PS50158. ZF_CCHC. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	43160.
PMAP-CutDB	Q9H0D6.
SOURCE	Search...

Entry information

Entry name

XRN2_HUMAN

Accession

Primary (citable) accession number: Q9H0D6
Secondary accession number(s): Q3L8N4 , Q6KGZ9, Q9BQL1, Q9NTW0, Q9NXS6, Q9UL53

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	March 1, 2001
Last modified:	June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)