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Protein

E3 ubiquitin/ISG15 ligase TRIM25

Gene

TRIM25

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.

Pathway:iprotein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

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

GO - Molecular functioni

  • acid-amino acid ligase activity Source: UniProtKB-EC
  • poly(A) RNA binding Source: UniProtKB
  • sequence-specific DNA binding transcription factor activity Source: ProtInc
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cytokine-mediated signaling pathway Source: Reactome
  • defense response to virus Source: UniProtKB-KW
  • DNA repair Source: Reactome
  • innate immune response Source: UniProtKB
  • interferon-gamma-mediated signaling pathway Source: Reactome
  • negative regulation of type I interferon production Source: Reactome
  • negative regulation of viral entry into host cell Source: Ensembl
  • negative regulation of viral release from host cell Source: Ensembl
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • protein monoubiquitination Source: ParkinsonsUK-UCL
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: ParkinsonsUK-UCL
  • regulation of viral entry into host cell Source: UniProtKB
  • regulation of viral release from host cell Source: UniProtKB
  • translesion synthesis Source: Reactome
  • viral process Source: UniProtKB-KW
Complete GO annotation...

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

BRENDAi2.3.2.B10. 2681.
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_25078. Interferon gamma signaling.
REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
REACT_355250. Termination of translesion DNA synthesis.
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 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:12932. TRIM25.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiTRIM25.
DMDMi313104033.

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 residuei278 – 2781Phosphotyrosine1 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

BgeeiQ14258.
CleanExiHS_TRIM25.
ExpressionAtlasiQ14258. baseline and differential.
GenevisibleiQ14258. HS.

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
F1BA495EBI-2341129,EBI-9687469From a different organism.
DDX58O957864EBI-2341129,EBI-995350
NSP034963EBI-2341129,EBI-2547442From a different organism.

Protein-protein interaction databases

BioGridi113500. 57 interactions.
IntActiQ14258. 29 interactions.
STRINGi9606.ENSP00000323889.

Structurei

Secondary structure

1
630
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi195 – 301107Combined sources
Helixi304 – 31411Combined sources
Helixi331 – 35424Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CFGX-ray2.80A/B1-630[»]
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.
GeneTreeiENSGT00760000118995.
HOVERGENiHBG101063.
InParanoidiQ14258.
KOiK10652.
OMAiEYTEMKA.
OrthoDBiEOG7CG6ZK.
PhylomeDBiQ14258.
TreeFamiTF351086.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
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

        10         20         30         40         50
MAELCPLAEE LSCSICLEPF KEPVTTPCGH NFCGSCLNET WAVQGSPYLC
60 70 80 90 100
PQCRAVYQAR PQLHKNTVLC NVVEQFLQAD LAREPPADVW TPPARASAPS
110 120 130 140 150
PNAQVACDHC LKEAAVKTCL VCMASFCQEH LQPHFDSPAF QDHPLQPPVR
160 170 180 190 200
DLLRRKCSQH NRLREFFCPE HSECICHICL VEHKTCSPAS LSQASADLEA
210 220 230 240 250
TLRHKLTVMY SQINGASRAL DDVRNRQQDV RMTANRKVEQ LQQEYTEMKA
260 270 280 290 300
LLDASETTST RKIKEEEKRV NSKFDTIYQI LLKKKSEIQT LKEEIEQSLT
310 320 330 340 350
KRDEFEFLEK ASKLRGISTK PVYIPEVELN HKLIKGIHQS TIDLKNELKQ
360 370 380 390 400
CIGRLQEPTP SSGDPGEHDP ASTHKSTRPV KKVSKEEKKS KKPPPVPALP
410 420 430 440 450
SKLPTFGAPE QLVDLKQAGL EAAAKATSSH PNSTSLKAKV LETFLAKSRP
460 470 480 490 500
ELLEYYIKVI LDYNTAHNKV ALSECYTVAS VAEMPQNYRP HPQRFTYCSQ
510 520 530 540 550
VLGLHCYKKG IHYWEVELQK NNFCGVGICY GSMNRQGPES RLGRNSASWC
560 570 580 590 600
VEWFNTKISA WHNNVEKTLP STKATRVGVL LNCDHGFVIF FAVADKVHLM
610 620 630
YKFRVDFTEA LYPAFWVFSA GATLSICSPK
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

TRIM25 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CFGX-ray2.80A/B1-630[»]
ProteinModelPortaliQ14258.
SMRiQ14258. Positions 7-53, 190-360, 436-628.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113500. 57 interactions.
IntActiQ14258. 29 interactions.
STRINGi9606.ENSP00000323889.

PTM databases

PhosphoSiteiQ14258.

Polymorphism and mutation databases

BioMutaiTRIM25.
DMDMi313104033.

Proteomic databases

MaxQBiQ14258.
PaxDbiQ14258.
PeptideAtlasiQ14258.
PRIDEiQ14258.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7706.
GeneCardsiGC17M054965.
HGNCiHGNC:12932. TRIM25.
HPAiHPA005909.
MIMi600453. gene.
neXtProtiNX_Q14258.
PharmGKBiPA37519.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG253760.
GeneTreeiENSGT00760000118995.
HOVERGENiHBG101063.
InParanoidiQ14258.
KOiK10652.
OMAiEYTEMKA.
OrthoDBiEOG7CG6ZK.
PhylomeDBiQ14258.
TreeFamiTF351086.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B10. 2681.
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_25078. Interferon gamma signaling.
REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
REACT_355250. Termination of translesion DNA synthesis.

Miscellaneous databases

ChiTaRSiTRIM25. human.
GeneWikiiTRIM25.
GenomeRNAii7706.
NextBioi29876.
PROiQ14258.
SOURCEiSearch...

Gene expression databases

BgeeiQ14258.
CleanExiHS_TRIM25.
ExpressionAtlasiQ14258. baseline and differential.
GenevisibleiQ14258. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-278, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. 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: July 22, 2015
This is version 159 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.