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Q9H0D6

- XRN2_HUMAN

UniProt

Q9H0D6 - XRN2_HUMAN

Protein

5'-3' exoribonuclease 2

Gene

XRN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    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.By similarity2 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-typeAdd
    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. cell growth Source: UniProtKB
    2. DNA catabolic process, exonucleolytic Source: UniProtKB
    3. DNA-templated transcription, termination Source: UniProtKB-KW
    4. mRNA processing Source: UniProtKB-KW
    5. regulation of transcription, DNA-templated Source: UniProtKB-KW
    6. RNA catabolic process Source: ProtInc
    7. RNA metabolic process Source: UniProtKB
    8. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
    9. RNA processing Source: ProtInc
    10. spermatogenesis Source: UniProtKB

    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. membrane Source: UniProtKB
    3. nucleolus Source: UniProtKB
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37427.

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei286 – 2861N6-acetyllysineBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Contains 1 CCHC-type zinc finger.Curated

    Zinc finger

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

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141Y → C in AAQ13577. (PubMed:10409438)Curated
    Sequence conflicti109 – 1091A → V in AAD55138. (PubMed:10409438)Curated
    Sequence conflicti109 – 1091A → V in AAQ13577. (PubMed:10409438)Curated
    Sequence conflicti122 – 1243SKE → IKR in AAD55138. (PubMed:10409438)Curated
    Sequence conflicti240 – 2456GLATHE → AFPHMN in AAQ13577. (PubMed:10409438)Curated
    Sequence conflicti259 – 2591K → R in AAD55138. (PubMed:10409438)Curated
    Sequence conflicti259 – 2591K → R in AAQ13577. (PubMed:10409438)Curated
    Sequence conflicti280 – 2801P → S in AAD55138. (PubMed:10409438)Curated
    Sequence conflicti280 – 2801P → S in AAQ13577. (PubMed:10409438)Curated
    Sequence conflicti313 – 3131L → V in AAQ13577. (PubMed:10409438)Curated
    Sequence conflicti463 – 4631E → D in AAD55138. (PubMed:10409438)Curated
    Sequence conflicti582 – 5821P → S in AAQ13577. (PubMed:10409438)Curated
    Sequence conflicti584 – 5841D → E in AAD55138. (PubMed:10409438)Curated
    Sequence conflicti737 – 7371S → A in AAD55138. (PubMed:10409438)Curated
    Sequence conflicti760 – 7601F → L in AAR24369. (PubMed:16147866)Curated
    Sequence conflicti787 – 7871E → G in AAD55138. (PubMed:10409438)Curated
    Sequence conflicti874 – 8741P → L in AAR24369. (PubMed:16147866)Curated

    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. 1 PublicationVSP_020596Add
    BLAST

    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]
    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 ]
    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

    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: October 1, 2014
    This is version 127 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