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Q5QJE6

- TDIF2_HUMAN

UniProt

Q5QJE6 - TDIF2_HUMAN

Protein

Deoxynucleotidyltransferase terminal-interacting protein 2

Gene

DNTTIP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 2 (05 Feb 2008)
      Previous versions | rss
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    Functioni

    Regulates the transcriptional activity of DNTT and ESR1. May function as a chromatin remodeling protein.2 Publications

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxynucleotidyltransferase terminal-interacting protein 2
    Alternative name(s):
    Estrogen receptor-binding protein
    LPTS-interacting protein 2
    Short name:
    LPTS-RP2
    Terminal deoxynucleotidyltransferase-interacting factor 2
    Short name:
    TdIF2
    Short name:
    TdT-interacting factor 2
    Gene namesi
    Name:DNTTIP2
    Synonyms:ERBP, TDIF2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:24013. DNTTIP2.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. nucleolus Source: HPA
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671963.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 756756Deoxynucleotidyltransferase terminal-interacting protein 2PRO_0000318505Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211Phosphoserine2 Publications
    Modified residuei117 – 1171Phosphoserine4 Publications
    Modified residuei129 – 1291Phosphothreonine1 Publication
    Modified residuei141 – 1411Phosphoserine5 Publications
    Modified residuei145 – 1451Phosphoserine1 Publication
    Modified residuei148 – 1481Phosphoserine1 Publication
    Modified residuei184 – 1841Phosphoserine2 Publications
    Modified residuei194 – 1941Phosphoserine1 Publication
    Modified residuei232 – 2321Phosphothreonine4 Publications
    Modified residuei251 – 2511Phosphoserine1 Publication
    Modified residuei324 – 3241Phosphoserine1 Publication
    Modified residuei330 – 3301Phosphoserine1 Publication
    Modified residuei381 – 3811Phosphoserine1 Publication
    Modified residuei434 – 4341Phosphoserine2 Publications
    Modified residuei512 – 5121Phosphoserine2 Publications
    Modified residuei610 – 6101Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ5QJE6.
    PaxDbiQ5QJE6.
    PRIDEiQ5QJE6.

    PTM databases

    PhosphoSiteiQ5QJE6.

    Expressioni

    Tissue specificityi

    Widely expressed with higher levels in testis.2 Publications

    Gene expression databases

    ArrayExpressiQ5QJE6.
    BgeeiQ5QJE6.
    CleanExiHS_DNTTIP2.
    GenevestigatoriQ5QJE6.

    Organism-specific databases

    HPAiHPA044502.

    Interactioni

    Subunit structurei

    Forms a ternary complex with DNTT and core histone; interaction with PCNA releases DNTT and H2A/H2B histones from this ternary complex. Interacts with ESR1, ESR2, PPARG and RXRA.2 Publications

    Protein-protein interaction databases

    BioGridi119052. 17 interactions.
    IntActiQ5QJE6. 3 interactions.
    MINTiMINT-3026940.
    STRINGi9606.ENSP00000352137.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5QJE6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni548 – 60558TdBR region; mediates interaction with DNTTAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili505 – 54238Sequence AnalysisAdd
    BLAST

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG273245.
    HOVERGENiHBG106308.
    InParanoidiQ5QJE6.
    OMAiEAESHVS.
    OrthoDBiEOG76T9SJ.
    PhylomeDBiQ5QJE6.
    TreeFamiTF105964.

    Family and domain databases

    InterProiIPR014810. Fcf2.
    [Graphical view]
    PfamiPF08698. Fcf2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5QJE6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVVTRSARAK ASIQAASAES SGQKSFAANG IQAHPESSTG SDARTTAESQ    50
    TTGKQSLIPR TPKARKRKSR TTGSLPKGTE PSTDGETSEA ESNYSVSEHH 100
    DTILRVTRRR QILIACSPVS SVRKKPKVTP TKESYTEEIV SEAESHVSGI 150
    SRIVLPTEKT TGARRSKAKS LTDPSQESHT EAISDAETSS SDISFSGIAT 200
    RRTRSMQRKL KAQTEKKDSK IVPGNEKQIV GTPVNSEDSD TRQTSHLQAR 250
    SLSEINKPNF YNNDFDDDFS HRSSENILTV HEQANVESLK ETKQNCKDLD 300
    EDANGITDEG KEINEKSSQL KNLSELQDTS LQQLVSQRHS TPQNKNAVSV 350
    HSNLNSEAVM KSLTQTFATV EVGRWNNNKK SPIKASDLTK FGDCGGSDDE 400
    EESTVISVSE DMNSEGNVDF ECDTKLYTSA PNTSQGKDNS VLLVLSSDES 450
    QQSENSENEE DTLCFVENSG QRESLSGDTG SLSCDNALFV IDTTPGMSAD 500
    KNFYLEEEDK ASEVAIEEEK EEEEDEKSEE DSSDHDENED EFSDEEDFLN 550
    STKAKLLKLT SSSIDPGLSI KQLGGLYINF NADKLQSNKR TLTQIKEKKK 600
    NELLQKAVIT PDFEKNHCVP PYSESKYQLQ KKRRKERQKT AGDGWFGMKA 650
    PEMTNELKND LKALKMRASM DPKRFYKKND RDGFPKYFQI GTIVDNPADF 700
    YHSRIPKKQR KRTIVEELLA DSEFRRYNRR KYSEIMAEKA ANAAGKKFRK 750
    KKKFRN 756
    Length:756
    Mass (Da):84,469
    Last modified:February 5, 2008 - v2
    Checksum:i5C58EFABA2B42E4B
    GO

    Sequence cautioni

    The sequence AAH47688.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAA50601.1 differs from that shown. Reason: Frameshift at positions 717 and 726.
    The sequence CAI21812.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti47 – 471A → D in AAQ95169. (PubMed:15047147)Curated
    Sequence conflicti47 – 471A → D in AAA50601. 1 PublicationCurated
    Sequence conflicti67 – 671R → S in AAQ95169. (PubMed:15047147)Curated
    Sequence conflicti67 – 671R → S in AAA50601. 1 PublicationCurated
    Sequence conflicti648 – 6481M → I in BAD96442. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti309 – 3091E → D.4 Publications
    Corresponds to variant rs3747965 [ dbSNP | Ensembl ].
    VAR_038748
    Natural varianti341 – 3411T → A.
    Corresponds to variant rs3179879 [ dbSNP | Ensembl ].
    VAR_038749
    Natural varianti430 – 4301A → V.
    Corresponds to variant rs35650636 [ dbSNP | Ensembl ].
    VAR_038750
    Natural varianti477 – 4771G → E.
    Corresponds to variant rs41292661 [ dbSNP | Ensembl ].
    VAR_061710
    Natural varianti676 – 6761Y → F.
    Corresponds to variant rs12748154 [ dbSNP | Ensembl ].
    VAR_038751

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB046574 mRNA. Translation: BAD08331.1.
    AY394925 mRNA. Translation: AAQ95169.1.
    U15552 mRNA. Translation: AAA50601.1. Frameshift.
    AY336729 mRNA. Translation: AAR02407.1.
    AK292379 mRNA. Translation: BAF85068.1.
    AK222722 mRNA. Translation: BAD96442.1.
    AL049796 Genomic DNA. Translation: CAI21812.1. Sequence problems.
    CH471097 Genomic DNA. Translation: EAW73064.1.
    BC047688 mRNA. Translation: AAH47688.1. Sequence problems.
    BC130622 mRNA. Translation: AAI30623.1.
    CCDSiCCDS44174.1.
    PIRiG01522.
    RefSeqiNP_055412.2. NM_014597.4.
    UniGeneiHs.601998.
    Hs.85769.

    Genome annotation databases

    EnsembliENST00000436063; ENSP00000411010; ENSG00000067334.
    GeneIDi30836.
    KEGGihsa:30836.
    UCSCiuc001dqf.3. human.

    Polymorphism databases

    DMDMi166987398.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB046574 mRNA. Translation: BAD08331.1 .
    AY394925 mRNA. Translation: AAQ95169.1 .
    U15552 mRNA. Translation: AAA50601.1 . Frameshift.
    AY336729 mRNA. Translation: AAR02407.1 .
    AK292379 mRNA. Translation: BAF85068.1 .
    AK222722 mRNA. Translation: BAD96442.1 .
    AL049796 Genomic DNA. Translation: CAI21812.1 . Sequence problems.
    CH471097 Genomic DNA. Translation: EAW73064.1 .
    BC047688 mRNA. Translation: AAH47688.1 . Sequence problems.
    BC130622 mRNA. Translation: AAI30623.1 .
    CCDSi CCDS44174.1.
    PIRi G01522.
    RefSeqi NP_055412.2. NM_014597.4.
    UniGenei Hs.601998.
    Hs.85769.

    3D structure databases

    ProteinModelPortali Q5QJE6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119052. 17 interactions.
    IntActi Q5QJE6. 3 interactions.
    MINTi MINT-3026940.
    STRINGi 9606.ENSP00000352137.

    PTM databases

    PhosphoSitei Q5QJE6.

    Polymorphism databases

    DMDMi 166987398.

    Proteomic databases

    MaxQBi Q5QJE6.
    PaxDbi Q5QJE6.
    PRIDEi Q5QJE6.

    Protocols and materials databases

    DNASUi 30836.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000436063 ; ENSP00000411010 ; ENSG00000067334 .
    GeneIDi 30836.
    KEGGi hsa:30836.
    UCSCi uc001dqf.3. human.

    Organism-specific databases

    CTDi 30836.
    GeneCardsi GC01M094331.
    H-InvDB HIX0023574.
    HGNCi HGNC:24013. DNTTIP2.
    HPAi HPA044502.
    MIMi 611199. gene.
    neXtProti NX_Q5QJE6.
    PharmGKBi PA142671963.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG273245.
    HOVERGENi HBG106308.
    InParanoidi Q5QJE6.
    OMAi EAESHVS.
    OrthoDBi EOG76T9SJ.
    PhylomeDBi Q5QJE6.
    TreeFami TF105964.

    Miscellaneous databases

    ChiTaRSi DNTTIP2. human.
    GeneWikii DNTTIP2.
    GenomeRNAii 30836.
    NextBioi 52954.
    PROi Q5QJE6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5QJE6.
    Bgeei Q5QJE6.
    CleanExi HS_DNTTIP2.
    Genevestigatori Q5QJE6.

    Family and domain databases

    InterProi IPR014810. Fcf2.
    [Graphical view ]
    Pfami PF08698. Fcf2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Terminal deoxynucleotidyltransferase forms a ternary complex with a novel chromatin remodeling protein with 82 kDa and core histone."
      Fujita K., Shimazaki N., Ohta Y., Kubota T., Ibe S., Toji S., Tamai K., Fujisaki S., Hayano T., Koiwai O.
      Genes Cells 8:559-571(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-309, FUNCTION, IDENTIFICATION IN A COMPLEX WITH DNTT; PCNA AND CORE HISTONE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Thymus.
    2. "ERBP, a novel estrogen receptor binding protein enhancing the activity of estrogen receptor."
      Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W., Rao S.M., Zhu Y.-J.
      Biochem. Biophys. Res. Commun. 317:54-59(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESR1; ESR2; PPARG AND RXRA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    3. "cDNA encoding an acidic 82 kDa protein."
      Carlsson P.
      Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    4. "LPTS-RP2, one LPTS-interacting protein."
      Song H., Zhao M., Li T.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-309.
      Tissue: Liver.
    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].
      Tissue: Testis.
    6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon.
    7. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-309.
    9. "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], VARIANT ASP-309.
      Tissue: Brain and Skin.
    10. "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-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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 THR-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-117; THR-129; SER-141; SER-145; SER-148; SER-184; SER-194; THR-232; SER-324 AND SER-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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].
    15. "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-141 AND SER-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "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-21; SER-117; SER-141; THR-232; SER-251; SER-330; SER-434; SER-512 AND THR-610, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "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-117; SER-141; THR-232; SER-434 AND SER-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTDIF2_HUMAN
    AccessioniPrimary (citable) accession number: Q5QJE6
    Secondary accession number(s): Q12987
    , Q53H59, Q5TFJ4, Q6TLI0, Q76MJ8, Q86WX9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 79 of the entry and version 2 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 1
      Human chromosome 1: 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

    External Data

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