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P14625

- ENPL_HUMAN

UniProt

P14625 - ENPL_HUMAN

Protein

Endoplasmin

Gene

HSP90B1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors By similarity. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity.By similarity1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei107 – 1071ATPBy similarity
    Binding sitei149 – 1491ATPBy similarity
    Binding sitei162 – 1621ATPBy similarity
    Binding sitei168 – 1681ATPBy similarity
    Binding sitei199 – 1991ATP; via amide nitrogenBy similarity
    Binding sitei448 – 4481ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium ion binding Source: UniProtKB
    3. low-density lipoprotein particle receptor binding Source: MGI
    4. protein binding Source: UniProtKB
    5. protein phosphatase binding Source: MGI
    6. RNA binding Source: UniProtKB
    7. virion binding Source: UniProtKB

    GO - Biological processi

    1. actin rod assembly Source: MGI
    2. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    3. cellular protein metabolic process Source: Reactome
    4. cellular response to ATP Source: MGI
    5. endoplasmic reticulum unfolded protein response Source: Reactome
    6. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
    7. innate immune response Source: Reactome
    8. negative regulation of apoptotic process Source: UniProtKB
    9. protein folding Source: InterPro
    10. protein transport Source: UniProtKB
    11. regulation of phosphoprotein phosphatase activity Source: MGI
    12. response to hypoxia Source: UniProtKB
    13. sequestering of calcium ion Source: UniProtKB
    14. toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    ATP-binding, Calcium, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_118632. Trafficking and processing of endosomal TLR.
    REACT_163699. Scavenging by Class A Receptors.
    REACT_18423. ATF6-alpha activates chaperone genes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoplasmin
    Alternative name(s):
    94 kDa glucose-regulated protein
    Short name:
    GRP-94
    Heat shock protein 90 kDa beta member 1
    Tumor rejection antigen 1
    gp96 homolog
    Gene namesi
    Name:HSP90B1
    Synonyms:GRP94, TRA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:12028. HSP90B1.

    Subcellular locationi

    Endoplasmic reticulum lumen. Melanosome
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. endocytic vesicle lumen Source: Reactome
    3. endoplasmic reticulum Source: UniProtKB
    4. endoplasmic reticulum lumen Source: UniProtKB
    5. endoplasmic reticulum membrane Source: UniProtKB
    6. extracellular region Source: Reactome
    7. extracellular vesicular exosome Source: UniProt
    8. melanosome Source: UniProtKB-SubCell
    9. membrane Source: UniProtKB
    10. midbody Source: UniProtKB
    11. nucleus Source: UniProt
    12. perinuclear region of cytoplasm Source: UniProtKB
    13. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36705.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 21211 PublicationAdd
    BLAST
    Chaini22 – 803782EndoplasminPRO_0000013598Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi62 – 621N-linked (GlcNAc...)1 Publication
    Glycosylationi107 – 1071N-linked (GlcNAc...)2 Publications
    Disulfide bondi138 – 138InterchainBy similarity
    Glycosylationi217 – 2171N-linked (GlcNAc...)2 Publications
    Modified residuei306 – 3061Phosphoserine2 Publications
    Modified residuei404 – 4041N6-succinyllysineBy similarity
    Glycosylationi445 – 4451N-linked (GlcNAc...)2 Publications
    Modified residuei479 – 4791N6-acetyllysineBy similarity
    Glycosylationi481 – 4811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi502 – 5021N-linked (GlcNAc...)Sequence Analysis
    Modified residuei633 – 6331N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP14625.
    PaxDbiP14625.
    PeptideAtlasiP14625.
    PRIDEiP14625.

    2D gel databases

    DOSAC-COBS-2DPAGEP14625.
    OGPiP14625.
    REPRODUCTION-2DPAGEIPI00027230.

    PTM databases

    PhosphoSiteiP14625.

    Miscellaneous databases

    PMAP-CutDBP14625.

    Expressioni

    Gene expression databases

    ArrayExpressiP14625.
    BgeeiP14625.
    CleanExiHS_HSP90B1.
    GenevestigatoriP14625.

    Organism-specific databases

    HPAiCAB005224.
    HPA003901.
    HPA008424.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 By similarity. Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Interacts with AIMP1; regulates its retention in the endoplasmic reticulum. Interacts with OS9. Interacts with CNPY3. This interaction is disrupted in the presence of ATP By similarity. Interacts with TLR4 and TLR9, but not with TLR3. Interacts with MZB1 in a calcium-dependent manner By similarity. Interacts with METTL23.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi113036. 79 interactions.
    DIPiDIP-36060N.
    IntActiP14625. 42 interactions.
    MINTiMINT-210408.
    STRINGi9606.ENSP00000299767.

    Structurei

    Secondary structure

    1
    803
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi80 – 9213
    Helixi99 – 11820
    Turni119 – 1213
    Turni123 – 1286
    Beta strandi134 – 1396
    Turni140 – 1434
    Beta strandi144 – 1496
    Helixi156 – 1605
    Helixi175 – 18410
    Helixi189 – 1946
    Helixi198 – 2047
    Beta strandi206 – 2149
    Beta strandi221 – 2255
    Beta strandi230 – 2345
    Beta strandi241 – 25111
    Helixi256 – 2594
    Helixi261 – 27111
    Beta strandi279 – 2846
    Beta strandi331 – 3355

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4NH9X-ray2.77A69-337[»]
    ProteinModelPortaliP14625.
    SMRiP14625. Positions 72-755.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi800 – 8034Prevents secretion from ER

    Sequence similaritiesi

    Belongs to the heat shock protein 90 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0326.
    HOGENOMiHOG000031988.
    HOVERGENiHBG007374.
    InParanoidiP14625.
    KOiK09487.
    OMAiQSSHHPS.
    OrthoDBiEOG780RM0.
    PhylomeDBiP14625.
    TreeFamiTF105969.

    Family and domain databases

    Gene3Di3.30.565.10. 2 hits.
    HAMAPiMF_00505. HSP90.
    InterProiIPR003594. HATPase_ATP-bd.
    IPR019805. Heat_shock_protein_90_CS.
    IPR001404. Hsp90_fam.
    IPR020575. Hsp90_N.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view]
    PANTHERiPTHR11528. PTHR11528. 1 hit.
    PfamiPF00183. HSP90. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002583. Hsp90. 1 hit.
    PRINTSiPR00775. HEATSHOCK90.
    SMARTiSM00387. HATPase_c. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 2 hits.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    PS00298. HSP90. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P14625-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRALWVLGLC CVLLTFGSVR ADDEVDVDGT VEEDLGKSRE GSRTDDEVVQ    50
    REEEAIQLDG LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF 100
    LRELISNASD ALDKIRLISL TDENALSGNE ELTVKIKCDK EKNLLHVTDT 150
    GVGMTREELV KNLGTIAKSG TSEFLNKMTE AQEDGQSTSE LIGQFGVGFY 200
    SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT LGRGTTITLV 250
    LKEEASDYLE LDTIKNLVKK YSQFINFPIY VWSSKTETVE EPMEEEEAAK 300
    EEKEESDDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV 350
    EEDEYKAFYK SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE 400
    YGSKKSDYIK LYVRRVFITD DFHDMMPKYL NFVKGVVDSD DLPLNVSRET 450
    LQQHKLLKVI RKKLVRKTLD MIKKIADDKY NDTFWKEFGT NIKLGVIEDH 500
    SNRTRLAKLL RFQSSHHPTD ITSLDQYVER MKEKQDKIYF MAGSSRKEAE 550
    SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE 600
    SEKTKESREA VEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS 650
    QYGWSGNMER IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIRDMLRR 700
    IKEDEDDKTV LDLAVVLFET ATLRSGYLLP DTKAYGDRIE RMLRLSLNID 750
    PDAKVEEEPE EEPEETAEDT TEDTEQDEDE EMDVGTDEEE ETAKESTAEK 800
    DEL 803
    Length:803
    Mass (Da):92,469
    Last modified:April 1, 1990 - v1
    Checksum:i9BF6705A7A2ED0D0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti188 – 1881T → S in AAK74072. 1 PublicationCurated
    Sequence conflicti419 – 4191T → P in AAK74072. 1 PublicationCurated
    Sequence conflicti803 – 8031L → F in AAK74072. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15187 mRNA. Translation: CAA33261.1.
    M33716 Genomic DNA. Translation: AAA68201.1.
    BC066656 mRNA. Translation: AAH66656.1.
    M26596 Genomic DNA. Translation: AAA58621.1.
    AY040226 mRNA. Translation: AAK74072.1.
    CCDSiCCDS9094.1.
    PIRiA35954.
    RefSeqiNP_003290.1. NM_003299.2.
    UniGeneiHs.192374.

    Genome annotation databases

    EnsembliENST00000299767; ENSP00000299767; ENSG00000166598.
    GeneIDi7184.
    KEGGihsa:7184.
    UCSCiuc001tkb.2. human.

    Polymorphism databases

    DMDMi119360.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15187 mRNA. Translation: CAA33261.1 .
    M33716 Genomic DNA. Translation: AAA68201.1 .
    BC066656 mRNA. Translation: AAH66656.1 .
    M26596 Genomic DNA. Translation: AAA58621.1 .
    AY040226 mRNA. Translation: AAK74072.1 .
    CCDSi CCDS9094.1.
    PIRi A35954.
    RefSeqi NP_003290.1. NM_003299.2.
    UniGenei Hs.192374.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4NH9 X-ray 2.77 A 69-337 [» ]
    ProteinModelPortali P14625.
    SMRi P14625. Positions 72-755.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113036. 79 interactions.
    DIPi DIP-36060N.
    IntActi P14625. 42 interactions.
    MINTi MINT-210408.
    STRINGi 9606.ENSP00000299767.

    Chemistry

    BindingDBi P14625.
    ChEMBLi CHEMBL1075323.
    DrugBanki DB00615. Rifabutin.

    PTM databases

    PhosphoSitei P14625.

    Polymorphism databases

    DMDMi 119360.

    2D gel databases

    DOSAC-COBS-2DPAGE P14625.
    OGPi P14625.
    REPRODUCTION-2DPAGE IPI00027230.

    Proteomic databases

    MaxQBi P14625.
    PaxDbi P14625.
    PeptideAtlasi P14625.
    PRIDEi P14625.

    Protocols and materials databases

    DNASUi 7184.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000299767 ; ENSP00000299767 ; ENSG00000166598 .
    GeneIDi 7184.
    KEGGi hsa:7184.
    UCSCi uc001tkb.2. human.

    Organism-specific databases

    CTDi 7184.
    GeneCardsi GC12P104324.
    H-InvDB HIX0056796.
    HGNCi HGNC:12028. HSP90B1.
    HPAi CAB005224.
    HPA003901.
    HPA008424.
    MIMi 191175. gene.
    neXtProti NX_P14625.
    PharmGKBi PA36705.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0326.
    HOGENOMi HOG000031988.
    HOVERGENi HBG007374.
    InParanoidi P14625.
    KOi K09487.
    OMAi QSSHHPS.
    OrthoDBi EOG780RM0.
    PhylomeDBi P14625.
    TreeFami TF105969.

    Enzyme and pathway databases

    Reactomei REACT_118632. Trafficking and processing of endosomal TLR.
    REACT_163699. Scavenging by Class A Receptors.
    REACT_18423. ATF6-alpha activates chaperone genes.

    Miscellaneous databases

    ChiTaRSi HSP90B1. human.
    GeneWikii HSP90B1.
    GenomeRNAii 7184.
    NextBioi 28164.
    PMAP-CutDB P14625.
    PROi P14625.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14625.
    Bgeei P14625.
    CleanExi HS_HSP90B1.
    Genevestigatori P14625.

    Family and domain databases

    Gene3Di 3.30.565.10. 2 hits.
    HAMAPi MF_00505. HSP90.
    InterProi IPR003594. HATPase_ATP-bd.
    IPR019805. Heat_shock_protein_90_CS.
    IPR001404. Hsp90_fam.
    IPR020575. Hsp90_N.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view ]
    PANTHERi PTHR11528. PTHR11528. 1 hit.
    Pfami PF00183. HSP90. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002583. Hsp90. 1 hit.
    PRINTSi PR00775. HEATSHOCK90.
    SMARTi SM00387. HATPase_c. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 2 hits.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS00298. HSP90. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human homologue of murine tumor rejection antigen gp96: 5'-regulatory and coding regions and relationship to stress-induced proteins."
      Maki R.G., Old L.J., Srivastava P.K.
      Proc. Natl. Acad. Sci. U.S.A. 87:5658-5662(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
      Tissue: Blood.
    2. "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].
      Tissue: Skin.
    3. "Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors."
      Chang S.C., Erwin A.E., Lee A.S.
      Mol. Cell. Biol. 9:2153-2162(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
      Tissue: Liver.
    4. "The association of heat shock protein gp96 with HBV-derived peptides in vitro."
      Meng S., Tien P.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-803.
      Tissue: Liver.
    5. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 22-39.
      Tissue: Platelet.
    6. "A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
      Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
      Mol. Biol. Cell 13:4456-4469(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPONENT OF A CHAPERONE COMPLEX.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    8. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
      Zhang H., Li X.-J., Martin D.B., Aebersold R.
      Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-217 AND ASN-445.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone."
      Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B., Bona R., Han D., Li Z.
      Nat. Commun. 1:79-79(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CNPY3; TLR4 AND TLR9.
    11. Erratum
      Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B., Bona R., Han D., Li Z.
      Nat. Commun. 3:653-653(2012)
    12. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    13. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
      Lewandrowski U., Moebius J., Walter U., Sickmann A.
      Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-107.
      Tissue: Platelet.
    14. "OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD."
      Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R.
      Nat. Cell Biol. 10:272-282(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH OS9.
    15. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-62; ASN-107; ASN-217 AND ASN-445.
      Tissue: Liver.
    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-306, 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-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity."
      Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.
      PLoS Genet. 9:E1003210-E1003210(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH METTL23.

    Entry informationi

    Entry nameiENPL_HUMAN
    AccessioniPrimary (citable) accession number: P14625
    Secondary accession number(s): Q96A97
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 175 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

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

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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

    Dasty 3