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Q9H0D6

- XRN2_HUMAN

UniProt

Q9H0D6 - XRN2_HUMAN

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Protein
5'-3' exoribonuclease 2
Gene
XRN2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri262 – 27817CCHC-type
Add
BLAST

GO - Molecular functioni

  1. 5'-3' exonuclease activity Source: UniProtKB
  2. 5'-3' exoribonuclease activity Source: UniProtKB
  3. nuclease activity Source: ProtInc
  4. poly(A) RNA binding Source: UniProtKB
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. DNA catabolic process, exonucleolytic Source: UniProtKB
  2. DNA-templated transcription, termination Source: UniProtKB-KW
  3. RNA catabolic process Source: ProtInc
  4. RNA metabolic process Source: UniProtKB
  5. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
  6. RNA processing Source: ProtInc
  7. cell growth Source: UniProtKB
  8. mRNA processing Source: UniProtKB-KW
  9. regulation of transcription, DNA-templated Source: UniProtKB-KW
  10. spermatogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

mRNA processing, Transcription, Transcription regulation, Transcription termination

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_16907. Association of TriC/CCT with target proteins during biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-3' exoribonuclease 2 (EC:3.1.13.-)
Alternative name(s):
DHM1-like protein
Short name:
DHP protein
Gene namesi
Name:XRN2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:12836. XRN2.

Subcellular locationi

Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. aggresome Source: HPA
  2. nucleolus Source: UniProtKB
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37427.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9509505'-3' exoribonuclease 2
PRO_0000071396Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei286 – 2861N6-acetyllysine By similarity
Modified residuei439 – 4391Phosphothreonine1 Publication
Modified residuei448 – 4481Phosphoserine9 Publications
Modified residuei471 – 4711Phosphoserine1 Publication
Modified residuei473 – 4731Phosphoserine1 Publication
Modified residuei475 – 4751Phosphoserine1 Publication
Modified residuei499 – 4991Phosphoserine6 Publications
Modified residuei501 – 5011Phosphoserine6 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H0D6.
PaxDbiQ9H0D6.
PeptideAtlasiQ9H0D6.
PRIDEiQ9H0D6.

2D gel databases

SWISS-2DPAGEQ9H0D6.

PTM databases

PhosphoSiteiQ9H0D6.

Miscellaneous databases

PMAP-CutDBQ9H0D6.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

ArrayExpressiQ9H0D6.
BgeeiQ9H0D6.
CleanExiHS_XRN2.
GenevestigatoriQ9H0D6.

Organism-specific databases

HPAiHPA047118.
HPA050485.

Interactioni

Protein-protein interaction databases

BioGridi116483. 58 interactions.
IntActiQ9H0D6. 30 interactions.
MINTiMINT-3065664.
STRINGi9606.ENSP00000366396.

Structurei

3D structure databases

ProteinModelPortaliQ9H0D6.
SMRiQ9H0D6. Positions 1-430, 502-785.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5049.
HOVERGENiHBG036677.
InParanoidiQ9H0D6.
KOiK12619.
OMAiGFSRDRR.
OrthoDBiEOG7S7SCW.
PhylomeDBiQ9H0D6.
TreeFamiTF105977.

Family and domain databases

InterProiIPR027073. 5_3_exoribonuclease.
IPR017151. 5_3_exoribonuclease_2.
IPR004859. Put_53exo.
IPR001878. Znf_CCHC.
[Graphical view]
PANTHERiPTHR12341. PTHR12341. 1 hit.
PfamiPF03159. XRN_N. 1 hit.
[Graphical view]
PIRSFiPIRSF037239. Exonuclease_Xrn2. 1 hit.
SMARTiSM00343. ZnF_C2HC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H0D6-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MGVPAFFRWL SRKYPSIIVN CVEEKPKECN GVKIPVDASK PNPNDVEFDN    50
LYLDMNGIIH PCTHPEDKPA PKNEDEMMVA IFEYIDRLFS IVRPRRLLYM 100
AIDGVAPRAK MNQQRSRRFR ASKEGMEAAV EKQRVREEIL AKGGFLPPEE 150
IKERFDSNCI TPGTEFMDNL AKCLRYYIAD RLNNDPGWKN LTVILSDASA 200
PGEGEHKIMD YIRRQRAQPN HDPNTHHCLC GADADLIMLG LATHEPNFTI 250
IREEFKPNKP KPCGLCNQFG HEVKDCEGLP REKKGKHDEL ADSLPCAEGE 300
FIFLRLNVLR EYLERELTMA SLPFTFDVER SIDDWVFMCF FVGNDFLPHL 350
PSLEIRENAI DRLVNIYKNV VHKTGGYLTE SGYVNLQRVQ MIMLAVGEVE 400
DSIFKKRKDD EDSFRRRQKE KRKRMKRDQP AFTPSGILTP HALGSRNSPG 450
SQVASNPRQA AYEMRMQNNS SPSISPNTSF TSDGSPSPLG GIKRKAEDSD 500
SEPEPEDNVR LWEAGWKQRY YKNKFDVDAA DEKFRRKVVQ SYVEGLCWVL 550
RYYYQGCASW KWYYPFHYAP FASDFEGIAD MPSDFEKGTK PFKPLEQLMG 600
VFPAASGNFL PPSWRKLMSD PDSSIIDFYP EDFAIDLNGK KYAWQGVALL 650
PFVDERRLRA ALEEVYPDLT PEETRRNSLG GDVLFVGKHH PLHDFILELY 700
QTGSTEPVEV PPELCHGIQG KFSLDEEAIL PDQIVCSPVP MLRDLTQNTV 750
VSINFKDPQF AEDYIFKAVM LPGARKPAAV LKPSDWEKSS NGRQWKPQLG 800
FNRDRRPVHL DQAAFRTLGH VMPRGSGTGI YSNAAPPPVT YQGNLYRPLL 850
RGQAQIPKLM SNMRPQDSWR GPPPLFQQQR FDRGVGAEPL LPWNRMLQTQ 900
NAAFQPNQYQ MLAGPGGYPP RRDDRGGRQG YPREGRKYPL PPPSGRYNWN 950
Length:950
Mass (Da):108,582
Last modified:March 1, 2001 - v1
Checksum:i763B5E0E628F97A8
GO
Isoform 2 (identifier: Q9H0D6-2) [UniParc]FASTAAdd to Basket

Also known as: XRN2b

The sequence of this isoform differs from the canonical sequence as follows:
     1-76: Missing.

Note: No experimental confirmation available.

Show »
Length:874
Mass (Da):99,962
Checksum:i85DBF4213F810AEC
GO

Sequence cautioni

The sequence AAR24369.1 differs from that shown. Reason: Frameshift at position 73.
The sequence BAA90934.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti743 – 7431R → M.
Corresponds to variant rs6137324 [ dbSNP | Ensembl ].
VAR_027516
Natural varianti925 – 9251R → C.
Corresponds to variant rs6047420 [ dbSNP | Ensembl ].
VAR_053002

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7676Missing in isoform 2.
VSP_020596Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141Y → C in AAQ13577. 1 Publication
Sequence conflicti109 – 1091A → V in AAD55138. 1 Publication
Sequence conflicti109 – 1091A → V in AAQ13577. 1 Publication
Sequence conflicti122 – 1243SKE → IKR in AAD55138. 1 Publication
Sequence conflicti240 – 2456GLATHE → AFPHMN in AAQ13577. 1 Publication
Sequence conflicti259 – 2591K → R in AAD55138. 1 Publication
Sequence conflicti259 – 2591K → R in AAQ13577. 1 Publication
Sequence conflicti280 – 2801P → S in AAD55138. 1 Publication
Sequence conflicti280 – 2801P → S in AAQ13577. 1 Publication
Sequence conflicti313 – 3131L → V in AAQ13577. 1 Publication
Sequence conflicti463 – 4631E → D in AAD55138. 1 Publication
Sequence conflicti582 – 5821P → S in AAQ13577. 1 Publication
Sequence conflicti584 – 5841D → E in AAD55138. 1 Publication
Sequence conflicti737 – 7371S → A in AAD55138. 1 Publication
Sequence conflicti760 – 7601F → L in AAR24369. 1 Publication
Sequence conflicti787 – 7871E → G in AAD55138. 1 Publication
Sequence conflicti874 – 8741P → L in AAR24369. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13144.1. [Q9H0D6-1]
RefSeqiNP_036387.2. NM_012255.3. [Q9H0D6-1]
UniGeneiHs.255932.

Genome annotation databases

EnsembliENST00000377191; ENSP00000366396; ENSG00000088930. [Q9H0D6-1]
ENST00000430571; ENSP00000413548; ENSG00000088930. [Q9H0D6-2]
GeneIDi22803.
KEGGihsa:22803.
UCSCiuc002wsf.1. human. [Q9H0D6-1]

Polymorphism databases

DMDMi30173484.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS13144.1. [Q9H0D6-1 ]
RefSeqi NP_036387.2. NM_012255.3. [Q9H0D6-1 ]
UniGenei Hs.255932.

3D structure databases

ProteinModelPortali Q9H0D6.
SMRi Q9H0D6. Positions 1-430, 502-785.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116483. 58 interactions.
IntActi Q9H0D6. 30 interactions.
MINTi MINT-3065664.
STRINGi 9606.ENSP00000366396.

PTM databases

PhosphoSitei Q9H0D6.

Polymorphism databases

DMDMi 30173484.

2D gel databases

SWISS-2DPAGE Q9H0D6.

Proteomic databases

MaxQBi Q9H0D6.
PaxDbi Q9H0D6.
PeptideAtlasi Q9H0D6.
PRIDEi Q9H0D6.

Protocols and materials databases

DNASUi 22803.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000377191 ; ENSP00000366396 ; ENSG00000088930 . [Q9H0D6-1 ]
ENST00000430571 ; ENSP00000413548 ; ENSG00000088930 . [Q9H0D6-2 ]
GeneIDi 22803.
KEGGi hsa:22803.
UCSCi uc002wsf.1. human. [Q9H0D6-1 ]

Organism-specific databases

CTDi 22803.
GeneCardsi GC20P021283.
HGNCi HGNC:12836. XRN2.
HPAi HPA047118.
HPA050485.
MIMi 608851. gene.
neXtProti NX_Q9H0D6.
PharmGKBi PA37427.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5049.
HOVERGENi HBG036677.
InParanoidi Q9H0D6.
KOi K12619.
OMAi GFSRDRR.
OrthoDBi EOG7S7SCW.
PhylomeDBi Q9H0D6.
TreeFami TF105977.

Enzyme and pathway databases

Reactomei REACT_16907. Association of TriC/CCT with target proteins during biosynthesis.

Miscellaneous databases

ChiTaRSi XRN2. human.
GeneWikii 5%27-3%27_exoribonuclease_2.
GenomeRNAii 22803.
NextBioi 43160.
PMAP-CutDB Q9H0D6.
PROi Q9H0D6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9H0D6.
Bgeei Q9H0D6.
CleanExi HS_XRN2.
Genevestigatori Q9H0D6.

Family and domain databases

InterProi IPR027073. 5_3_exoribonuclease.
IPR017151. 5_3_exoribonuclease_2.
IPR004859. Put_53exo.
IPR001878. Znf_CCHC.
[Graphical view ]
PANTHERi PTHR12341. PTHR12341. 1 hit.
Pfami PF03159. XRN_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF037239. Exonuclease_Xrn2. 1 hit.
SMARTi SM00343. ZnF_C2HC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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] [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.
    , 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. 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. 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. 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. 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].

Entry informationi

Entry nameiXRN2_HUMAN
AccessioniPrimary (citable) accession number: Q9H0D6
Secondary accession number(s): Q3L8N4
, Q6KGZ9, Q9BQL1, Q9NTW0, Q9NXS6, Q9UL53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2001
Last modified: September 3, 2014
This is version 126 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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

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