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Q92613

- JADE3_HUMAN

UniProt

Q92613 - JADE3_HUMAN

Protein

Protein Jade-3

Gene

JADE3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri200 – 25051PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. zinc ion binding Source: InterPro

    GO - Biological processi

    1. histone H3 acetylation Source: UniProtKB
    2. histone H4-K12 acetylation Source: UniProtKB
    3. histone H4-K5 acetylation Source: UniProtKB
    4. histone H4-K8 acetylation Source: UniProtKB

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein Jade-3
    Alternative name(s):
    Jade family PHD finger protein 3
    PHD finger protein 16
    Gene namesi
    Name:JADE3
    Synonyms:KIAA0215, PHF16
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:22982. JADE3.

    Subcellular locationi

    GO - Cellular componenti

    1. histone acetyltransferase complex Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134993233.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 823823Protein Jade-3PRO_0000059309Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei30 – 301N6-acetyllysine1 Publication
    Modified residuei32 – 321N6-acetyllysine1 Publication
    Modified residuei38 – 381N6-acetyllysine1 Publication
    Modified residuei85 – 851Phosphoserine2 Publications
    Modified residuei566 – 5661Phosphoserine4 Publications
    Modified residuei601 – 6011N6-acetyllysineBy similarity
    Modified residuei638 – 6381N6-acetyllysine1 Publication
    Modified residuei735 – 7351N6-acetyllysineBy similarity
    Modified residuei774 – 7741Phosphoserine1 Publication
    Modified residuei776 – 7761Phosphoserine1 Publication
    Modified residuei780 – 7801Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ92613.
    PaxDbiQ92613.
    PRIDEiQ92613.

    PTM databases

    PhosphoSiteiQ92613.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed, with highest levels in placenta and uterus.1 Publication

    Inductioni

    By estradiol in estrogen-responsive breast cancer cells.1 Publication

    Gene expression databases

    ArrayExpressiQ92613.
    BgeeiQ92613.
    CleanExiHS_PHF16.
    GenevestigatoriQ92613.

    Organism-specific databases

    HPAiHPA006007.

    Interactioni

    Subunit structurei

    Component of the HBO1 complex composed at least of ING4 or ING5, KAT7/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3.1 Publication

    Protein-protein interaction databases

    BioGridi115113. 6 interactions.
    STRINGi9606.ENSP00000218343.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92613.
    SMRiQ92613. Positions 198-248, 252-366.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the JADE family.Curated
    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri200 – 25051PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5141.
    HOGENOMiHOG000220882.
    HOVERGENiHBG053585.
    InParanoidiQ92613.
    OMAiASVCRYD.
    OrthoDBiEOG738044.
    PhylomeDBiQ92613.
    TreeFamiTF316118.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR019542. Enhancer_polycomb-like_N.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF10513. EPL1. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view]
    SMARTiSM00249. PHD. 2 hits.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 1 hit.
    PROSITEiPS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q92613-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRHRPVSSS DSSDESPSTS FTSGSMYRIK SKIPNEHKKP AEVFRKDLIS    50
    AMKLPDSHHI NPDSYYLFAD TWKEEWEKGV QVPASPDTVP QPSLRIIAEK 100
    VKDVLFIRPR KYIHCSSPDT TEPGYINIME LAASVCRYDL DDMDIFWLQE 150
    LNEDLAEMGC GPVDENLMEK TVEVLERHCH ENMNHAIETE EGLGIEYDED 200
    VICDVCRSPD SEEGNDMVFC DKCNVCVHQA CYGILKVPEG SWLCRSCVLG 250
    IYPQCVLCPK KGGALKTTKT GTKWAHVSCA LWIPEVSIAC PERMEPITKI 300
    SHIPPSRWAL VCNLCKLKTG ACIQCSIKSC ITAFHVTCAF EHGLEMKTIL 350
    DEGDEVKFKS YCLKHSQNRQ KLGEAEYPHH RAKEQSQAKS EKTSLRAQKL 400
    RELEEEFYSL VRVEDVAAEL GMPTLAVDFI YNYWKLKRKS NFNKPLFPPK 450
    EDEENGLVQP KEESIHTRMR MFMHLRQDLE RVRNLCYMIS RREKLKLSHN 500
    KIQEQIFGLQ VQLLNQEIDA GLPLTNALEN SLFYPPPRIT LKLKMPKSTP 550
    EDHRNSSTET DQQPHSPDSS SSVHSIRNMQ VPQESLEMRT KSYPRYPLES 600
    KNNRLLASLS HSRSEAKESS PAWRTPSSEC YHGQSLGKPL VLQAALHGQS 650
    SIGNGKSQPN SKFAKSNGLE GSWSGNVTQK DSSSEMFCDQ EPVFSPHLVS 700
    QGSFRKSTVE HFSRSFKETT NRWVKNTEDL QCYVKPTKNM SPKEQFWGRQ 750
    VLRRSAGRAP YQENDGYCPD LELSDSEAES DGNKEKVRVR KDSSDRENPP 800
    HDSRRDCHGK SKTHPLSHSS MQR 823
    Length:823
    Mass (Da):93,808
    Last modified:February 1, 1997 - v1
    Checksum:i4E47E2A124D0CE38
    GO

    Sequence cautioni

    The sequence BAA13205.2 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF127774 mRNA. Translation: AAD51905.1.
    D86969 mRNA. Translation: BAA13205.2. Different initiation.
    Z83822 Genomic DNA. No translation available.
    BC114487 mRNA. Translation: AAI14488.1.
    BC113880 mRNA. Translation: AAI13881.1.
    BN000289 mRNA. Translation: CAE30502.1.
    CCDSiCCDS14271.1.
    RefSeqiNP_001070913.1. NM_001077445.2.
    NP_055550.1. NM_014735.4.
    UniGeneiHs.371977.

    Genome annotation databases

    EnsembliENST00000218343; ENSP00000218343; ENSG00000102221.
    ENST00000397189; ENSP00000380373; ENSG00000102221.
    GeneIDi9767.
    KEGGihsa:9767.
    UCSCiuc004dgx.3. human.

    Polymorphism databases

    DMDMi34098663.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF127774 mRNA. Translation: AAD51905.1 .
    D86969 mRNA. Translation: BAA13205.2 . Different initiation.
    Z83822 Genomic DNA. No translation available.
    BC114487 mRNA. Translation: AAI14488.1 .
    BC113880 mRNA. Translation: AAI13881.1 .
    BN000289 mRNA. Translation: CAE30502.1 .
    CCDSi CCDS14271.1.
    RefSeqi NP_001070913.1. NM_001077445.2.
    NP_055550.1. NM_014735.4.
    UniGenei Hs.371977.

    3D structure databases

    ProteinModelPortali Q92613.
    SMRi Q92613. Positions 198-248, 252-366.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115113. 6 interactions.
    STRINGi 9606.ENSP00000218343.

    PTM databases

    PhosphoSitei Q92613.

    Polymorphism databases

    DMDMi 34098663.

    Proteomic databases

    MaxQBi Q92613.
    PaxDbi Q92613.
    PRIDEi Q92613.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000218343 ; ENSP00000218343 ; ENSG00000102221 .
    ENST00000397189 ; ENSP00000380373 ; ENSG00000102221 .
    GeneIDi 9767.
    KEGGi hsa:9767.
    UCSCi uc004dgx.3. human.

    Organism-specific databases

    CTDi 9767.
    GeneCardsi GC0XP046771.
    HGNCi HGNC:22982. JADE3.
    HPAi HPA006007.
    MIMi 300618. gene.
    neXtProti NX_Q92613.
    PharmGKBi PA134993233.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5141.
    HOGENOMi HOG000220882.
    HOVERGENi HBG053585.
    InParanoidi Q92613.
    OMAi ASVCRYD.
    OrthoDBi EOG738044.
    PhylomeDBi Q92613.
    TreeFami TF316118.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.

    Miscellaneous databases

    GeneWikii PHF16.
    GenomeRNAii 9767.
    NextBioi 36762.
    PROi Q92613.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92613.
    Bgeei Q92613.
    CleanExi HS_PHF16.
    Genevestigatori Q92613.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR019542. Enhancer_polycomb-like_N.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF10513. EPL1. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view ]
    SMARTi SM00249. PHD. 2 hits.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 1 hit.
    PROSITEi PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of human estrogen-inducible transcripts that potentially mediate the apoptotic response in breast cancer."
      Szelei J., Soto A.M., Geck P., Desronvil M., Prechtl N.V., Weill B.C., Sonnenschein C.
      J. Steroid Biochem. Mol. Biol. 72:89-102(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION BY ESTRADIOL.
    2. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
      Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
      DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Bone marrow.
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
    5. "Identification of Jade1, a gene encoding a PHD zinc finger protein, in a gene trap mutagenesis screen for genes involved in anteroposterior axis development."
      Tzouanacou E., Tweedie S., Wilson V.
      Mol. Cell. Biol. 23:8553-8562(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    6. "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-566, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
      Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
      Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE HBO1 COMPLEX.
    8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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-85 AND SER-566, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774; SER-776 AND SER-780, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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].
    12. "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-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-32; LYS-38 AND LYS-638, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-566, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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-566, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiJADE3_HUMAN
    AccessioniPrimary (citable) accession number: Q92613
    Secondary accession number(s): Q6IE79
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 15, 2003
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 113 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 X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3