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Q14258

- TRI25_HUMAN

UniProt

Q14258 - TRI25_HUMAN

Protein

E3 ubiquitin/ISG15 ligase TRIM25

Gene

TRIM25

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    Functions as a ubiquitin E3 ligase and as an ISG15 E3 ligase. Involved in innate immune defense against viruses by mediating ubiquitination of DDX58. Mediates 'Lys-63'-linked polyubiquitination of the DDX58 N-terminal CARD-like region which is crucial for triggering the cytosolic signal transduction that leads to the production of interferons in response to viral infection. Promotes ISGylation of 14-3-3 sigma (SFN), an adapter protein implicated in the regulation of a large spectrum signaling pathway. Mediates estrogen action in various target organs.3 Publications

    Catalytic activityi

    ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
    ATP + [ISG15] + [protein]-lysine = AMP + diphosphate + [protein]-N-ISGyllysine.

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri13 – 5442RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: UniProtKB-EC
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. sequence-specific DNA binding transcription factor activity Source: ProtInc
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. defense response to virus Source: UniProtKB-KW
    2. innate immune response Source: UniProt
    3. negative regulation of type I interferon production Source: Reactome
    4. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProt
    5. positive regulation of NF-kappaB transcription factor activity Source: UniProt
    6. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProt
    7. protein ubiquitination Source: UniProtKB-UniPathway
    8. regulation of viral entry into host cell Source: UniProt
    9. regulation of viral release from host cell Source: UniProt
    10. response to estrogen Source: Ensembl
    11. response to vitamin D Source: Ensembl
    12. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Antiviral defense, Host-virus interaction, Immunity, Innate immunity, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.
    REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_25026. TRAF3-dependent IRF activation pathway.
    REACT_25039. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin/ISG15 ligase TRIM25 (EC:6.3.2.19, EC:6.3.2.n3)
    Alternative name(s):
    Estrogen-responsive finger protein
    RING finger protein 147
    Tripartite motif-containing protein 25
    Ubiquitin/ISG15-conjugating enzyme TRIM25
    Zinc finger protein 147
    Gene namesi
    Name:TRIM25
    Synonyms:EFP, RNF147, ZNF147
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:12932. TRIM25.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Colocalized with DDX58 at cytoplasmic perinuclear bodies.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi21 – 211K → R: No effect on ISGylation. 1 Publication
    Mutagenesisi65 – 651K → R: No effect on ISGylation. 1 Publication
    Mutagenesisi112 – 1121K → R: No effect on ISGylation. 1 Publication
    Mutagenesisi117 – 1171K → R: No ISGylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA37519.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 630630E3 ubiquitin/ISG15 ligase TRIM25PRO_0000056233Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei100 – 1001Phosphoserine1 Publication
    Cross-linki117 – 117Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)
    Modified residuei273 – 2731N6-acetyllysine1 Publication
    Modified residuei567 – 5671N6-acetyllysine1 Publication

    Post-translational modificationi

    Auto-ISGylated.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ14258.
    PaxDbiQ14258.
    PeptideAtlasiQ14258.
    PRIDEiQ14258.

    PTM databases

    PhosphoSiteiQ14258.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Inductioni

    By interferons.2 Publications

    Gene expression databases

    ArrayExpressiQ14258.
    BgeeiQ14258.
    CleanExiHS_TRIM25.
    GenevestigatoriQ14258.

    Organism-specific databases

    HPAiHPA005909.

    Interactioni

    Subunit structurei

    Interacts (via SPRY domain) with DDX58 (via CARD domain). Interacts (via coiled coil) with influenza A virus NS1 protein; this interaction specifically inhibits TRIM25 multimerization and TRIM25-mediated DDX58 CARD ubiquitination, thereby suppressing DDX58 signal transduction.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NSP034963EBI-2341129,EBI-2547442From a different organism.

    Protein-protein interaction databases

    BioGridi113500. 54 interactions.
    IntActiQ14258. 17 interactions.
    STRINGi9606.ENSP00000323889.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14258.
    SMRiQ14258. Positions 7-53, 190-360, 436-628.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini439 – 630192B30.2/SPRYPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni180 – 450271Interaction with influenza A virus NS1Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili217 – 30791Sequence AnalysisAdd
    BLAST

    Domaini

    The RING-type zinc finger is important for ISG15 E3 ligase activity and autoISGylation. AutoISGylation negatively regulates ISG15 E3 ligase activity.
    The C-terminal B30.2/SPRY domain interacts with the first N-terminal CARD domain of DDX58.

    Sequence similaritiesi

    Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri13 – 5442RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG253760.
    HOVERGENiHBG101063.
    InParanoidiQ14258.
    KOiK10652.
    OMAiEANSTRK.
    OrthoDBiEOG7CG6ZK.
    PhylomeDBiQ14258.
    TreeFamiTF351086.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR001870. B30.2/SPRY.
    IPR003879. Butyrophylin.
    IPR008985. ConA-like_lec_gl_sf.
    IPR006574. PRY.
    IPR018355. SPla/RYanodine_receptor_subgr.
    IPR003877. SPRY_rcpt.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF13765. PRY. 1 hit.
    PF00622. SPRY. 1 hit.
    [Graphical view]
    PRINTSiPR01407. BUTYPHLNCDUF.
    SMARTiSM00589. PRY. 1 hit.
    SM00184. RING. 1 hit.
    SM00449. SPRY. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS50188. B302_SPRY. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q14258-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAELCPLAEE LSCSICLEPF KEPVTTPCGH NFCGSCLNET WAVQGSPYLC    50
    PQCRAVYQAR PQLHKNTVLC NVVEQFLQAD LAREPPADVW TPPARASAPS 100
    PNAQVACDHC LKEAAVKTCL VCMASFCQEH LQPHFDSPAF QDHPLQPPVR 150
    DLLRRKCSQH NRLREFFCPE HSECICHICL VEHKTCSPAS LSQASADLEA 200
    TLRHKLTVMY SQINGASRAL DDVRNRQQDV RMTANRKVEQ LQQEYTEMKA 250
    LLDASETTST RKIKEEEKRV NSKFDTIYQI LLKKKSEIQT LKEEIEQSLT 300
    KRDEFEFLEK ASKLRGISTK PVYIPEVELN HKLIKGIHQS TIDLKNELKQ 350
    CIGRLQEPTP SSGDPGEHDP ASTHKSTRPV KKVSKEEKKS KKPPPVPALP 400
    SKLPTFGAPE QLVDLKQAGL EAAAKATSSH PNSTSLKAKV LETFLAKSRP 450
    ELLEYYIKVI LDYNTAHNKV ALSECYTVAS VAEMPQNYRP HPQRFTYCSQ 500
    VLGLHCYKKG IHYWEVELQK NNFCGVGICY GSMNRQGPES RLGRNSASWC 550
    VEWFNTKISA WHNNVEKTLP STKATRVGVL LNCDHGFVIF FAVADKVHLM 600
    YKFRVDFTEA LYPAFWVFSA GATLSICSPK 630
    Length:630
    Mass (Da):70,973
    Last modified:November 30, 2010 - v2
    Checksum:iEB0AB353F0AD4C80
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti89 – 891V → G.
    Corresponds to variant rs7212260 [ dbSNP | Ensembl ].
    VAR_024614
    Natural varianti358 – 3581P → L.3 Publications
    Corresponds to variant rs205498 [ dbSNP | Ensembl ].
    VAR_024615

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D21205 mRNA. Translation: BAA04747.1.
    AC015912 Genomic DNA. No translation available.
    BC016924 mRNA. Translation: AAH16924.1.
    BC042541 mRNA. Translation: AAH42541.1.
    CCDSiCCDS11591.1.
    PIRiA49656.
    RefSeqiNP_005073.2. NM_005082.4.
    UniGeneiHs.528952.

    Genome annotation databases

    EnsembliENST00000316881; ENSP00000323889; ENSG00000121060.
    ENST00000537230; ENSP00000445961; ENSG00000121060.
    GeneIDi7706.
    KEGGihsa:7706.
    UCSCiuc002iut.3. human.

    Polymorphism databases

    DMDMi313104033.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    TRIM25 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D21205 mRNA. Translation: BAA04747.1 .
    AC015912 Genomic DNA. No translation available.
    BC016924 mRNA. Translation: AAH16924.1 .
    BC042541 mRNA. Translation: AAH42541.1 .
    CCDSi CCDS11591.1.
    PIRi A49656.
    RefSeqi NP_005073.2. NM_005082.4.
    UniGenei Hs.528952.

    3D structure databases

    ProteinModelPortali Q14258.
    SMRi Q14258. Positions 7-53, 190-360, 436-628.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113500. 54 interactions.
    IntActi Q14258. 17 interactions.
    STRINGi 9606.ENSP00000323889.

    PTM databases

    PhosphoSitei Q14258.

    Polymorphism databases

    DMDMi 313104033.

    Proteomic databases

    MaxQBi Q14258.
    PaxDbi Q14258.
    PeptideAtlasi Q14258.
    PRIDEi Q14258.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000316881 ; ENSP00000323889 ; ENSG00000121060 .
    ENST00000537230 ; ENSP00000445961 ; ENSG00000121060 .
    GeneIDi 7706.
    KEGGi hsa:7706.
    UCSCi uc002iut.3. human.

    Organism-specific databases

    CTDi 7706.
    GeneCardsi GC17M054965.
    HGNCi HGNC:12932. TRIM25.
    HPAi HPA005909.
    MIMi 600453. gene.
    neXtProti NX_Q14258.
    PharmGKBi PA37519.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG253760.
    HOVERGENi HBG101063.
    InParanoidi Q14258.
    KOi K10652.
    OMAi EANSTRK.
    OrthoDBi EOG7CG6ZK.
    PhylomeDBi Q14258.
    TreeFami TF351086.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_115831. ISG15 antiviral mechanism.
    REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_25026. TRAF3-dependent IRF activation pathway.
    REACT_25039. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.

    Miscellaneous databases

    ChiTaRSi TRIM25. human.
    GeneWikii TRIM25.
    GenomeRNAii 7706.
    NextBioi 29876.
    PROi Q14258.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14258.
    Bgeei Q14258.
    CleanExi HS_TRIM25.
    Genevestigatori Q14258.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR001870. B30.2/SPRY.
    IPR003879. Butyrophylin.
    IPR008985. ConA-like_lec_gl_sf.
    IPR006574. PRY.
    IPR018355. SPla/RYanodine_receptor_subgr.
    IPR003877. SPRY_rcpt.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF13765. PRY. 1 hit.
    PF00622. SPRY. 1 hit.
    [Graphical view ]
    PRINTSi PR01407. BUTYPHLNCDUF.
    SMARTi SM00589. PRY. 1 hit.
    SM00184. RING. 1 hit.
    SM00449. SPRY. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS50188. B302_SPRY. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic binding-site cloning reveals an estrogen-responsive gene that encodes a RING finger protein."
      Inoue S., Orimo A., Hosoi T., Kondo S., Toyoshima H., Kondo T., Ikegami A., Ouchi Y., Orimo H., Muramatsu M.
      Proc. Natl. Acad. Sci. U.S.A. 90:11117-11121(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-358.
      Tissue: Placenta.
    2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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 LEU-358.
      Tissue: Lymph.
    4. "Systemic distribution of estrogen-responsive finger protein (Efp) in human tissues."
      Shimada N., Suzuki T., Inoue S., Kato K., Imatani A., Sekine H., Ohara S., Shimosegawa T., Sasano H.
      Mol. Cell. Endocrinol. 218:147-153(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    5. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "A ubiquitin E3 ligase Efp is up-regulated by interferons and conjugated with ISG15."
      Nakasato N., Ikeda K., Urano T., Horie-Inoue K., Takeda S., Inoue S.
      Biochem. Biophys. Res. Commun. 351:540-546(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, FUNCTION.
    7. "The interferon-inducible ubiquitin-protein isopeptide ligase (E3) EFP also functions as an ISG15 E3 ligase."
      Zou W., Zhang D.-E.
      J. Biol. Chem. 281:3989-3994(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A ISG15 E3 LIGASE, INDUCTION.
    8. "Negative regulation of ISG15 E3 ligase EFP through its autoISGylation."
      Zou W., Wang J., Zhang D.-E.
      Biochem. Biophys. Res. Commun. 354:321-327(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISGYLATION AT LYS-117, MUTAGENESIS OF LYS-21; LYS-65; LYS-112 AND LYS-117, AUTOISGYLATION.
    9. "TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity."
      Gack M.U., Shin Y.C., Joo C.H., Urano T., Liang C., Sun L., Takeuchi O., Akira S., Chen Z., Inoue S., Jung J.U.
      Nature 446:916-920(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN UBIQUITIN LIGASE, SUBCELLULAR LOCATION, INTERACTION WITH DDX58.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I."
      Gack M.U., Albrecht R.A., Urano T., Inn K.-S., Huang I.-C., Carnero E., Farzan M., Inoue S., Jung J.U., Garcia-Sastre A.
      Cell Host Microbe 5:439-449(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INFLUENZA VIRUS PROTEIN NS1.
    12. "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-273 AND LYS-567, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-358, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTRI25_HUMAN
    AccessioniPrimary (citable) accession number: Q14258
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 149 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 17
      Human chromosome 17: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3