Q9H0D6 (XRN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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.
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. Ref.8 Ref.12
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. The sequence BAA90934.1 differs from that shown. Reason: Erroneous initiation.

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	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA catabolic process, exonucleolytic Inferred from direct assay Ref.8. Source: UniProtKB RNA catabolic process 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 Inferred from expression pattern Ref.1. Source: UniProtKB transcription termination, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleolus Inferred from direct assay Ref.7. Source: UniProtKB
Molecular function	5'-3' exoribonuclease activity Traceable author statement Ref.1. Source: UniProtKB nucleic acid binding Inferred from electronic annotation. Source: InterPro 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 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.17
	Modified residue	448	1	Phosphoserine Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21
	Modified residue	455	1	Phosphoserine Ref.13
	Modified residue	471	1	Phosphoserine Ref.21
	Modified residue	473	1	Phosphoserine Ref.19 Ref.21
	Modified residue	475	1	Phosphoserine Ref.19 Ref.21
	Modified residue	499	1	Phosphoserine Ref.9 Ref.11 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21
	Modified residue	501	1	Phosphoserine Ref.9 Ref.10 Ref.11 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21
	Modified residue	796	1	N6-acetyllysine Ref.22
Natural variations
	Alternative sequence	1 – 76	76	Missing in isoform 2.		VSP_020596
	Natural variant	743	1	R → M. Corresponds to variant rs6137324 [ dbSNP | Ensembl ].		VAR_027516
	Natural variant	925	1	R → C. Corresponds to variant rs6047420 [ dbSNP | Ensembl ].		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) [UniParc]. 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]. 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: 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: Cervix carcinoma.
[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. Tissue: Colon adenocarcinoma.
[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: Cervix carcinoma.
[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: Cervix carcinoma.
[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: Cervix carcinoma.
[15]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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. Tissue: Cervix carcinoma.
[17]	"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. Tissue: Cervix carcinoma.
[18]	"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.
[19]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448; SER-473; SER-475; SER-499 AND SER-501, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[20]	"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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448; SER-499 AND SER-501, MASS SPECTROMETRY.
[21]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448; SER-471; SER-473; SER-475; SER-499 AND SER-501, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[22]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-796, MASS SPECTROMETRY.
[23]	"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: 21269460] [Abstract] Cited for: 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.
IPI	IPI00100151. IPI00788157.
RefSeq	NP_036387.2. NM_012255.3.
UniGene	Hs.255932.
3D structure databases
ProteinModelPortal	Q9H0D6.
SMR	Q9H0D6. Positions 1-793.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H0D6. 20 interactions.
MINT	MINT-3065664.
STRING	Q9H0D6.
PTM databases
PhosphoSite	Q9H0D6.
Polymorphism databases
DMDM	30173484.
2D gel databases
SWISS-2DPAGE	Q9H0D6.
Proteomic databases
PeptideAtlas	Q9H0D6.
PRIDE	Q9H0D6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000377191; ENSP00000366396; ENSG00000088930.
GeneID	22803.
KEGG	hsa:22803.
UCSC	uc002wsf.1. human. uc002wsg.1. human.
Organism-specific databases
CTD	22803.
GeneCards	GC20P021283.
H-InvDB	HIX0015683.
HGNC	HGNC:12836. XRN2.
MIM	608851. gene.
neXtProt	NX_Q9H0D6.
PharmGKB	PA37427.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG09774.
GeneTree	ENSGT00600000084422.
HOVERGEN	HBG036677.
InParanoid	Q9H0D6.
OMA	RKRMKRD.
OrthoDB	EOG4M0F0Z.
PhylomeDB	Q9H0D6.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	Q9H0D6.
Bgee	Q9H0D6.
CleanEx	HS_XRN2.
Genevestigator	Q9H0D6.
GermOnline	ENSG00000088930. Homo sapiens.
Family and domain databases
InterPro	IPR017151. 5_3_exoribonuclease_2. IPR004859. Put_53exo. IPR001878. Znf_CCHC. [Graphical view]
KO	K12619.
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
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:	December 14, 2011
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.