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Q99543

- DNJC2_HUMAN

UniProt

Q99543 - DNJC2_HUMAN

Protein

DnaJ homolog subfamily C member 2

Gene

DNAJC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 4 (18 May 2010)
      Previous versions | rss
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    Functioni

    Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation. Specifically binds DNA sequence 5'-GTCAAGC-3'.3 Publications

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. DNA binding Source: InterPro
    3. histone binding Source: UniProtKB
    4. Hsp70 protein binding Source: UniProtKB
    5. poly(A) RNA binding Source: UniProtKB
    6. ubiquitin binding Source: UniProtKB

    GO - Biological processi

    1. 'de novo' cotranslational protein folding Source: UniProtKB
    2. chromatin modification Source: UniProtKB-KW
    3. DNA replication Source: Ensembl
    4. negative regulation of cell growth Source: Ensembl
    5. negative regulation of DNA biosynthetic process Source: Ensembl
    6. positive regulation of transcription, DNA-templated Source: UniProtKB
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Chaperone, Chromatin regulator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DnaJ homolog subfamily C member 2
    Alternative name(s):
    M-phase phosphoprotein 11
    Zuotin-related factor 1
    Cleaved into the following chain:
    Gene namesi
    Name:DNAJC2
    Synonyms:MPHOSPH11, MPP11, ZRF1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:13192. DNAJC2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProtKB
    3. nuclear membrane Source: HPA
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi512 – 5132HQ → AA: Loss of function. 1 Publication

    Organism-specific databases

    PharmGKBiPA162383835.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 621621DnaJ homolog subfamily C member 2PRO_0000425752Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate1 Publication
    Chaini2 – 621620DnaJ homolog subfamily C member 2, N-terminally processedPRO_0000071123Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei47 – 471Phosphoserine5 Publications
    Modified residuei49 – 491Phosphoserine5 Publications
    Modified residuei60 – 601Phosphoserine2 Publications
    Modified residuei63 – 631Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated in M (mitotic) phase.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ99543.
    PaxDbiQ99543.
    PRIDEiQ99543.

    PTM databases

    PhosphoSiteiQ99543.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Inductioni

    Expression is repressed by CEBPA. Strongly overexpressed in leukemic cells.3 Publications

    Gene expression databases

    ArrayExpressiQ99543.
    BgeeiQ99543.
    CleanExiHS_DNAJC2.
    GenevestigatoriQ99543.

    Organism-specific databases

    HPAiHPA020454.
    HPA049603.

    Interactioni

    Subunit structurei

    Interacts (via ZRF1-UBD region) with ID1 By similarity. Component of ribosome-associated complex (RAC), a heterodimer composed of Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type chaperone DNAJC2.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi117946. 3 interactions.
    DIPiDIP-60462N.
    STRINGi9606.ENSP00000368565.

    Structurei

    Secondary structure

    1
    621
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi556 – 56813
    Helixi576 – 5838
    Helixi589 – 61830

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2M2ENMR-A551-621[»]
    ProteinModelPortaliQ99543.
    SMRiQ99543. Positions 87-163, 551-620.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini88 – 16174JPROSITE-ProRule annotationAdd
    BLAST
    Domaini449 – 51163SANT 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini549 – 60456SANT 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni23 – 319Epitope (recognized by CD8(+) cytotoxic T-lymphocytes)
    Regioni160 – 25091ZRF1-UBDAdd
    BLAST

    Domaini

    The ZRF1-UBD region specifically recognizes and binds H2AK119ub. The ZRF1-UBD region is also involved in protein-protein interactions with other proteins, suggesting that it may be masked by some regulator, thereby preventing its association with H2AK119ub.1 Publication

    Sequence similaritiesi

    Contains 1 J domain.PROSITE-ProRule annotation
    Contains 2 SANT domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5269.
    HOGENOMiHOG000006900.
    HOVERGENiHBG008782.
    InParanoidiQ99543.
    KOiK09522.
    OMAiLTSCTKE.
    OrthoDBiEOG73V6KR.
    PhylomeDBiQ99543.
    TreeFamiTF105834.

    Family and domain databases

    Gene3Di1.10.10.60. 1 hit.
    1.10.287.110. 1 hit.
    InterProiIPR001623. DnaJ_domain.
    IPR018253. DnaJ_domain_CS.
    IPR009057. Homeodomain-like.
    IPR001005. SANT/Myb.
    IPR017884. SANT_dom.
    [Graphical view]
    PfamiPF00226. DnaJ. 1 hit.
    PF00249. Myb_DNA-binding. 2 hits.
    [Graphical view]
    SMARTiSM00271. DnaJ. 1 hit.
    SM00717. SANT. 2 hits.
    [Graphical view]
    SUPFAMiSSF46565. SSF46565. 1 hit.
    SSF46689. SSF46689. 2 hits.
    PROSITEiPS00636. DNAJ_1. 1 hit.
    PS50076. DNAJ_2. 1 hit.
    PS51293. SANT. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99543-1) [UniParc]FASTAAdd to Basket

    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

    MLLLPSAADG RGTAITHALT SASTLCQVEP VGRWFEAFVK RRNRNASASF    50
    QELEDKKELS EESEDEELQL EEFPMLKTLD PKDWKNQDHY AVLGLGHVRY 100
    KATQRQIKAA HKAMVLKHHP DKRKAAGEPI KEGDNDYFTC ITKAYEMLSD 150
    PVKRRAFNSV DPTFDNSVPS KSEAKDNFFE VFTPVFERNS RWSNKKNVPK 200
    LGDMNSSFED VDIFYSFWYN FDSWREFSYL DEEEKEKAEC RDERRWIEKQ 250
    NRATRAQRKK EEMNRIRTLV DNAYSCDPRI KKFKEEEKAK KEAEKKAKAE 300
    AKRKEQEAKE KQRQAELEAA RLAKEKEEEE VRQQALLAKK EKDIQKKAIK 350
    KERQKLRNSC KTWNHFSDNE AERVKMMEEV EKLCDRLELA SLQCLNETLT 400
    SCTKEVGKAA LEKQIEEINE QIRKEKEEAE ARMRQASKNT EKSTGGGGNG 450
    SKNWSEDDLQ LLIKAVNLFP AGTNSRWEVI ANYMNIHSSS GVKRTAKDVI 500
    GKAKSLQKLD PHQKDDINKK AFDKFKKEHG VVPQADNATP SERFEGPYTD 550
    FTPWTTEEQK LLEQALKTYP VNTPERWEKI AEAVPGRTKK DCMKRYKELV 600
    EMVKAKKAAQ EQVLNASRAK K 621
    Length:621
    Mass (Da):71,996
    Last modified:May 18, 2010 - v4
    Checksum:iE4DAEE7A73D0F64C
    GO
    Isoform 2 (identifier: Q99543-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         362-414: Missing.

    Show »
    Length:568
    Mass (Da):65,913
    Checksum:i390BA8AC8C0DFCAD
    GO

    Sequence cautioni

    The sequence AAI39752.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAA66913.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti252 – 2521R → G in CAA66913. (PubMed:8885239)Curated
    Sequence conflicti472 – 4721G → R in CAA66913. (PubMed:8885239)Curated
    Sequence conflicti578 – 5781E → K in AAI39752. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei362 – 41453Missing in isoform 2. 1 PublicationVSP_023562Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98260 mRNA. Translation: CAA66913.1. Different initiation.
    AC004668 Genomic DNA. No translation available.
    BC000859 mRNA. Translation: AAH00859.1.
    BC139751 mRNA. Translation: AAI39752.1. Different initiation.
    CCDSiCCDS43628.1. [Q99543-1]
    CCDS47679.1. [Q99543-2]
    RefSeqiNP_001123359.1. NM_001129887.1. [Q99543-2]
    NP_055192.1. NM_014377.1. [Q99543-1]
    UniGeneiHs.558476.

    Genome annotation databases

    EnsembliENST00000249270; ENSP00000249270; ENSG00000105821. [Q99543-2]
    ENST00000379263; ENSP00000368565; ENSG00000105821. [Q99543-1]
    GeneIDi27000.
    KEGGihsa:27000.
    UCSCiuc003vbo.3. human. [Q99543-1]
    uc010lix.3. human. [Q99543-2]

    Polymorphism databases

    DMDMi296439472.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98260 mRNA. Translation: CAA66913.1 . Different initiation.
    AC004668 Genomic DNA. No translation available.
    BC000859 mRNA. Translation: AAH00859.1 .
    BC139751 mRNA. Translation: AAI39752.1 . Different initiation.
    CCDSi CCDS43628.1. [Q99543-1 ]
    CCDS47679.1. [Q99543-2 ]
    RefSeqi NP_001123359.1. NM_001129887.1. [Q99543-2 ]
    NP_055192.1. NM_014377.1. [Q99543-1 ]
    UniGenei Hs.558476.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2M2E NMR - A 551-621 [» ]
    ProteinModelPortali Q99543.
    SMRi Q99543. Positions 87-163, 551-620.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117946. 3 interactions.
    DIPi DIP-60462N.
    STRINGi 9606.ENSP00000368565.

    PTM databases

    PhosphoSitei Q99543.

    Polymorphism databases

    DMDMi 296439472.

    Proteomic databases

    MaxQBi Q99543.
    PaxDbi Q99543.
    PRIDEi Q99543.

    Protocols and materials databases

    DNASUi 27000.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000249270 ; ENSP00000249270 ; ENSG00000105821 . [Q99543-2 ]
    ENST00000379263 ; ENSP00000368565 ; ENSG00000105821 . [Q99543-1 ]
    GeneIDi 27000.
    KEGGi hsa:27000.
    UCSCi uc003vbo.3. human. [Q99543-1 ]
    uc010lix.3. human. [Q99543-2 ]

    Organism-specific databases

    CTDi 27000.
    GeneCardsi GC07M102952.
    HGNCi HGNC:13192. DNAJC2.
    HPAi HPA020454.
    HPA049603.
    MIMi 605502. gene.
    neXtProti NX_Q99543.
    PharmGKBi PA162383835.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5269.
    HOGENOMi HOG000006900.
    HOVERGENi HBG008782.
    InParanoidi Q99543.
    KOi K09522.
    OMAi LTSCTKE.
    OrthoDBi EOG73V6KR.
    PhylomeDBi Q99543.
    TreeFami TF105834.

    Miscellaneous databases

    GeneWikii ZRF1.
    GenomeRNAii 27000.
    NextBioi 49486.
    PROi Q99543.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99543.
    Bgeei Q99543.
    CleanExi HS_DNAJC2.
    Genevestigatori Q99543.

    Family and domain databases

    Gene3Di 1.10.10.60. 1 hit.
    1.10.287.110. 1 hit.
    InterProi IPR001623. DnaJ_domain.
    IPR018253. DnaJ_domain_CS.
    IPR009057. Homeodomain-like.
    IPR001005. SANT/Myb.
    IPR017884. SANT_dom.
    [Graphical view ]
    Pfami PF00226. DnaJ. 1 hit.
    PF00249. Myb_DNA-binding. 2 hits.
    [Graphical view ]
    SMARTi SM00271. DnaJ. 1 hit.
    SM00717. SANT. 2 hits.
    [Graphical view ]
    SUPFAMi SSF46565. SSF46565. 1 hit.
    SSF46689. SSF46689. 2 hits.
    PROSITEi PS00636. DNAJ_1. 1 hit.
    PS50076. DNAJ_2. 1 hit.
    PS51293. SANT. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of novel M phase phosphoproteins by expression cloning."
      Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L., Westendorf J.M.
      Mol. Biol. Cell 7:1455-1469(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PHOSPHORYLATION.
      Tissue: Blood.
    2. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Bienvenut W.V., Glen H., Frame M.C.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-11, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Osteosarcoma.
    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] OF 7-621 (ISOFORM 1).
      Tissue: Cervix.
    5. "A putative oncogenic role for MPP11 in head and neck squamous cell cancer."
      Resto V.A., Caballero O.L., Buta M.R., Westra W.H., Wu L., Westendorf J.M., Jen J., Hieter P., Sidransky D.
      Cancer Res. 60:5529-5535(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    6. "Characterization of several leukemia-associated antigens inducing humoral immune responses in acute and chronic myeloid leukemia."
      Greiner J., Ringhoffer M., Taniguchi M., Hauser T., Schmitt A., Dohner H., Schmitt M.
      Int. J. Cancer 106:224-231(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION IN LEUKEMIA.
    7. "mRNA expression of leukemia-associated antigens in patients with acute myeloid leukemia for the development of specific immunotherapies."
      Greiner J., Ringhoffer M., Taniguchi M., Li L., Schmitt A., Shiku H., Dohner H., Schmitt M.
      Int. J. Cancer 108:704-711(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION IN LEUKEMIA.
    8. "The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex."
      Otto H., Conz C., Maier P., Wolfle T., Suzuki C.K., Jeno P., Rucknagel P., Stahl J., Rospert S.
      Proc. Natl. Acad. Sci. U.S.A. 102:10064-10069(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE RAC COMPLEX, INTERACTION WITH HSPA14.
    9. "Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous."
      Hundley H.A., Walter W., Bairstow S., Craig E.A.
      Science 308:1032-1034(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF 512-HIS-GLN-513.
    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-47; SER-49; SER-60 AND SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "C/EBPalphap30 plays transcriptional regulatory roles distinct from C/EBPalphap42."
      Wang C., Chen X., Wang Y., Gong J., Hu G.
      Cell Res. 17:374-383(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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-47 AND SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Identification of a novel peptide derived from the M-phase phosphoprotein 11 (MPP11) leukemic antigen recognized by human CD8+ cytotoxic T lymphocytes."
      Al Qudaihi G., Lehe C., Dickinson A., Eltayeb K., Rasheed W., Chaudhri N., Aljurf M., Dermime S.
      Hematol. Oncol. Stem Cell Ther. 3:24-33(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: EPITOPE REGION.
    15. Cited for: FUNCTION AS CHROMATIN REGULATOR, SUBCELLULAR LOCATION, UBIQUITIN-BINDING, DOMAIN ZRF1-UBD.
    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-47 AND SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-47 AND SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDNJC2_HUMAN
    AccessioniPrimary (citable) accession number: Q99543
    Secondary accession number(s): A4VCI0, Q9BVX1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 132 of the entry and version 4 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

    Miscellaneous

    Constitutes a myeloid leukemia-associated antigen and might be a target for leukemia T-cell therapy.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

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