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Q32MZ4

- LRRF1_HUMAN

UniProt

Q32MZ4 - LRRF1_HUMAN

Protein

Leucine-rich repeat flightless-interacting protein 1

Gene

LRRFIP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (05 Sep 2006)
      Previous versions | rss
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    Functioni

    Transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. May control smooth muscle cells proliferation following artery injury through PDGFA repression. May also bind double-stranded RNA. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding.5 Publications

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. double-stranded RNA binding Source: ProtInc
    3. protein binding Source: IntAct
    4. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. innate immune response Source: Reactome
    2. negative regulation of transcription, DNA-templated Source: UniProtKB
    3. positive regulation of type I interferon production Source: Reactome
    4. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_121141. Signaling by FGFR1 fusion mutants.
    REACT_163743. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Leucine-rich repeat flightless-interacting protein 1
    Short name:
    LRR FLII-interacting protein 1
    Alternative name(s):
    GC-binding factor 2
    TAR RNA-interacting protein
    Gene namesi
    Name:LRRFIP1
    Synonyms:GCF2, TRIP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:6702. LRRFIP1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoskeleton Source: ProtInc
    3. cytosol Source: Reactome
    4. nucleus Source: UniProtKB
    5. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30465.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 808807Leucine-rich repeat flightless-interacting protein 1PRO_0000248392Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine2 Publications
    Modified residuei16 – 161Phosphoserine2 Publications
    Modified residuei115 – 1151Phosphoserine1 Publication
    Modified residuei120 – 1201Phosphoserine3 Publications
    Modified residuei555 – 5551Phosphoserine2 Publications
    Modified residuei581 – 5811Phosphoserine2 Publications
    Modified residuei618 – 6181Phosphoserine2 Publications
    Modified residuei676 – 6761Phosphothreonine1 Publication
    Modified residuei714 – 7141Phosphoserine2 Publications
    Modified residuei733 – 7331Phosphoserine1 Publication
    Modified residuei766 – 7661Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ32MZ4.
    PaxDbiQ32MZ4.
    PRIDEiQ32MZ4.

    PTM databases

    PhosphoSiteiQ32MZ4.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.2 Publications

    Developmental stagei

    Widely expressed in fetal tissues.1 Publication

    Gene expression databases

    ArrayExpressiQ32MZ4.
    BgeeiQ32MZ4.
    CleanExiHS_LRRFIP1.
    GenevestigatoriQ32MZ4.

    Organism-specific databases

    HPAiHPA006979.

    Interactioni

    Subunit structurei

    Homodimer. May also form higher oligomers. Interacts with FLII. Interacts with MYD88. Competes with FLII for MyD88-binding, even in the absence of LPS.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FLIIQ130452EBI-1369100,EBI-351549

    Protein-protein interaction databases

    BioGridi114642. 22 interactions.
    IntActiQ32MZ4. 1 interaction.
    STRINGi9606.ENSP00000375857.

    Structurei

    Secondary structure

    1
    808
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi171 – 24272
    Turni243 – 2453

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4H22X-ray2.89A/B/C/D162-249[»]
    ProteinModelPortaliQ32MZ4.
    SMRiQ32MZ4. Positions 167-249.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni485 – 584100DNA-bindingAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili128 – 2501231 PublicationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi567 – 59327Lys-richAdd
    BLAST

    Domaini

    The DNA-binding domain is intrinsically unstructured.1 Publication
    The coiled coil mediates dimerization.1 Publication

    Sequence similaritiesi

    Belongs to the LRRFIP family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG296572.
    HOGENOMiHOG000113391.
    HOVERGENiHBG081935.
    InParanoidiQ32MZ4.
    OMAiISSRIMG.
    OrthoDBiEOG7DNNTX.
    PhylomeDBiQ32MZ4.
    TreeFamiTF314109.

    Family and domain databases

    InterProiIPR019139. Leu-rich_rep_flightless-int_pr.
    [Graphical view]
    PANTHERiPTHR19212. PTHR19212. 1 hit.
    PfamiPF09738. DUF2051. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q32MZ4-1) [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

    MTSPAAAQSR EIDCLSPEAQ KLAEARLAAK RAARAEAREI RMKELERQQK    50
    EEDSERYSRR SRRNTSASDE DERMSVGSRG SLRVEERPEK DFTEKGSRNM 100
    PGLSAATLAS LGGTSSRRGS GDTSISIDTE ASIREIKELN ELKDQIQDVE 150
    GKYMQGLKEM KDSLAEVEEK YKKAMVSNAQ LDNEKTNFMY QVDTLKDMLL 200
    ELEEQLAESR RQYEEKNKEF EREKHAHSIL QFQFAEVKEA LKQREEMLEK 250
    HGIILNSEIA TNGETSDTLN NVGYQGPTKM TKEELNALKS TGDGTLGRAS 300
    EVEVKNEIVA NVGKREILHN TEKEQHTEDT VKDCVDIEVF PAGENTEDQK 350
    SSEDTAPFLG TLAGATYEEQ VQSQILESSS LPENTVQVES NEVMGAPDDR 400
    TRTPLEPSNC WSDLDGGNHT ENVGEAAVTQ VEEQAGTVAS CPLGHSDDTV 450
    YHDDKCMVEV PQELETSTGH SLEKEFTNQE AAEPKEVPAH STEVGRDHNE 500
    EEGEETGLRD EKPIKTEVPG SPAGTEGNCQ EATGPSTVDT QNEPLDMKEP 550
    DEEKSDQQGE ALDSSQKKTK NKKKKNKKKK SPVPVETLKD VKKELTYQNT 600
    DLSEIKEEEQ VKSTDRKSAV EAQNEVTENP KQKIAAESSE NVDCPENPKI 650
    KLDGKLDQEG DDVQTAAEEV LADGDTLDFE DDTVQSSGPR AGGEELDEGV 700
    AKDNAKIDGA TQSSPAEPKS EDADRCTLPE HESPSQDISD ACEAESTERC 750
    EMSEHPSQTV RKALDSNSLE NDDLSAPGRE PGHFNPESRE DTRGGNEKGK 800
    SKEDCTMS 808
    Length:808
    Mass (Da):89,253
    Last modified:September 5, 2006 - v2
    Checksum:i4E6140DF2471A7C9
    GO
    Isoform 2 (identifier: Q32MZ4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         137-160: Missing.

    Show »
    Length:784
    Mass (Da):86,404
    Checksum:iDDB6D45C670DBE97
    GO
    Isoform 3 (identifier: Q32MZ4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         52-83: Missing.
         137-160: Missing.

    Show »
    Length:752
    Mass (Da):82,689
    Checksum:iF99016BC7CE54A60
    GO
    Isoform 4 (identifier: Q32MZ4-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-22: MTSPAAAQSREIDCLSPEAQKL → MDMGTQGSGRKRLPNRERLTAEDDALNQIARE
         51-51: E → EIYQVQKKYYGLDTKWGDIEQWM
         83-83: R → RSQPDLEYGG...RASSARASPV
         249-249: E → EEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELK
         297-450: GRASEVEVKN...CPLGHSDDTV → DIRLKKLVDE...ANRSALLSQQ
         451-808: Missing.

    Show »
    Length:640
    Mass (Da):73,060
    Checksum:iE7B967AF138F79C3
    GO

    Sequence cautioni

    The sequence AAH01385.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAY14672.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 171P → L in AAC32037. (PubMed:9705290)Curated
    Sequence conflicti26 – 261R → W in AAC32037. (PubMed:9705290)Curated
    Sequence conflicti125 – 1251I → F in CAA11076. (PubMed:9671805)Curated
    Sequence conflicti327 – 3271T → A in AAC32037. (PubMed:9705290)Curated
    Sequence conflicti562 – 5621L → F in AAI08915. (PubMed:15489334)Curated
    Sequence conflicti665 – 6651T → P in AAC32037. (PubMed:9705290)Curated
    Sequence conflicti684 – 6841V → A in AAC32037. (PubMed:9705290)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti68 – 681S → C in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036037
    Natural varianti275 – 2751Q → R.
    Corresponds to variant rs3213869 [ dbSNP | Ensembl ].
    VAR_027291
    Natural varianti418 – 4181N → S.
    Corresponds to variant rs2001301 [ dbSNP | Ensembl ].
    VAR_027292
    Natural varianti609 – 6091E → K.
    Corresponds to variant rs3739041 [ dbSNP | Ensembl ].
    VAR_027293
    Natural varianti633 – 6331K → E.
    Corresponds to variant rs3739041 [ dbSNP | Ensembl ].
    VAR_056111
    Natural varianti645 – 6451P → L.
    Corresponds to variant rs3739040 [ dbSNP | Ensembl ].
    VAR_027294
    Natural varianti779 – 7791R → G.
    Corresponds to variant rs3739039 [ dbSNP | Ensembl ].
    VAR_027295
    Natural varianti783 – 7831H → D.
    Corresponds to variant rs3739038 [ dbSNP | Ensembl ].
    VAR_027296

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2222MTSPA…EAQKL → MDMGTQGSGRKRLPNRERLT AEDDALNQIARE in isoform 4. 1 PublicationVSP_046809Add
    BLAST
    Alternative sequencei51 – 511E → EIYQVQKKYYGLDTKWGDIE QWM in isoform 4. 1 PublicationVSP_046810
    Alternative sequencei52 – 8332Missing in isoform 3. 2 PublicationsVSP_020264Add
    BLAST
    Alternative sequencei83 – 831R → RSQPDLEYGGPYAWTNGYDG ELYGSQSLNRRSGRPSCLYS AARPSGSYRASVLDEGSFGG TRRGSTSGSRAPSEYSGHLN SSSRASSRASSARASPV in isoform 4. 1 PublicationVSP_046811
    Alternative sequencei137 – 16024Missing in isoform 2 and isoform 3. 3 PublicationsVSP_020265Add
    BLAST
    Alternative sequencei249 – 2491E → EEIRQLQQKQASSIREISDL QETIEWKDKKIGALERQKEF FDSVRSERDDLREEVVMLKE ELK in isoform 4. 1 PublicationVSP_046812
    Alternative sequencei297 – 450154GRASE…SDDTV → DIRLKKLVDERECLLEQIKK LKGQLEERQKIGKLDNLRSE DDVLENGTDMHVMDLQRDAN RQISDLKFKLAKSEQEITAL EQNVIRLESQVSRYKSAAEN AEKIEDELKAEKRKLQRELR SALDKTEELEVSNGHLVKRL EKMKANRSALLSQQ in isoform 4. 1 PublicationVSP_046813Add
    BLAST
    Alternative sequencei451 – 808358Missing in isoform 4. 1 PublicationVSP_046814Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U69609 mRNA. Translation: AAC32037.1.
    AJ223075 mRNA. Translation: CAA11076.1.
    AC012076 Genomic DNA. Translation: AAY14672.1. Sequence problems.
    AC096574 Genomic DNA. No translation available.
    BC001385 mRNA. Translation: AAH01385.1. Sequence problems.
    BC108913 mRNA. Translation: AAI08914.1.
    BC108914 mRNA. Translation: AAI08915.1.
    AF115510 mRNA. Translation: AAD41258.1.
    CCDSiCCDS2521.1. [Q32MZ4-2]
    CCDS46551.1. [Q32MZ4-4]
    CCDS46552.1. [Q32MZ4-1]
    CCDS46553.1. [Q32MZ4-3]
    RefSeqiNP_001131022.1. NM_001137550.1. [Q32MZ4-4]
    NP_001131024.1. NM_001137552.1. [Q32MZ4-1]
    NP_001131025.1. NM_001137553.1. [Q32MZ4-3]
    NP_004726.2. NM_004735.3. [Q32MZ4-2]
    UniGeneiHs.471779.

    Genome annotation databases

    EnsembliENST00000244815; ENSP00000244815; ENSG00000124831. [Q32MZ4-2]
    ENST00000289175; ENSP00000289175; ENSG00000124831. [Q32MZ4-3]
    ENST00000308482; ENSP00000310109; ENSG00000124831. [Q32MZ4-4]
    ENST00000392000; ENSP00000375857; ENSG00000124831. [Q32MZ4-1]
    GeneIDi9208.
    KEGGihsa:9208.
    UCSCiuc002vxd.3. human. [Q32MZ4-2]
    uc002vxe.3. human. [Q32MZ4-1]
    uc002vxf.3. human. [Q32MZ4-3]

    Polymorphism databases

    DMDMi114149995.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U69609 mRNA. Translation: AAC32037.1 .
    AJ223075 mRNA. Translation: CAA11076.1 .
    AC012076 Genomic DNA. Translation: AAY14672.1 . Sequence problems.
    AC096574 Genomic DNA. No translation available.
    BC001385 mRNA. Translation: AAH01385.1 . Sequence problems.
    BC108913 mRNA. Translation: AAI08914.1 .
    BC108914 mRNA. Translation: AAI08915.1 .
    AF115510 mRNA. Translation: AAD41258.1 .
    CCDSi CCDS2521.1. [Q32MZ4-2 ]
    CCDS46551.1. [Q32MZ4-4 ]
    CCDS46552.1. [Q32MZ4-1 ]
    CCDS46553.1. [Q32MZ4-3 ]
    RefSeqi NP_001131022.1. NM_001137550.1. [Q32MZ4-4 ]
    NP_001131024.1. NM_001137552.1. [Q32MZ4-1 ]
    NP_001131025.1. NM_001137553.1. [Q32MZ4-3 ]
    NP_004726.2. NM_004735.3. [Q32MZ4-2 ]
    UniGenei Hs.471779.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4H22 X-ray 2.89 A/B/C/D 162-249 [» ]
    ProteinModelPortali Q32MZ4.
    SMRi Q32MZ4. Positions 167-249.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114642. 22 interactions.
    IntActi Q32MZ4. 1 interaction.
    STRINGi 9606.ENSP00000375857.

    PTM databases

    PhosphoSitei Q32MZ4.

    Polymorphism databases

    DMDMi 114149995.

    Proteomic databases

    MaxQBi Q32MZ4.
    PaxDbi Q32MZ4.
    PRIDEi Q32MZ4.

    Protocols and materials databases

    DNASUi 9208.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000244815 ; ENSP00000244815 ; ENSG00000124831 . [Q32MZ4-2 ]
    ENST00000289175 ; ENSP00000289175 ; ENSG00000124831 . [Q32MZ4-3 ]
    ENST00000308482 ; ENSP00000310109 ; ENSG00000124831 . [Q32MZ4-4 ]
    ENST00000392000 ; ENSP00000375857 ; ENSG00000124831 . [Q32MZ4-1 ]
    GeneIDi 9208.
    KEGGi hsa:9208.
    UCSCi uc002vxd.3. human. [Q32MZ4-2 ]
    uc002vxe.3. human. [Q32MZ4-1 ]
    uc002vxf.3. human. [Q32MZ4-3 ]

    Organism-specific databases

    CTDi 9208.
    GeneCardsi GC02P238617.
    H-InvDB HIX0030126.
    HGNCi HGNC:6702. LRRFIP1.
    HPAi HPA006979.
    MIMi 603256. gene.
    neXtProti NX_Q32MZ4.
    PharmGKBi PA30465.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG296572.
    HOGENOMi HOG000113391.
    HOVERGENi HBG081935.
    InParanoidi Q32MZ4.
    OMAi ISSRIMG.
    OrthoDBi EOG7DNNTX.
    PhylomeDBi Q32MZ4.
    TreeFami TF314109.

    Enzyme and pathway databases

    Reactomei REACT_121141. Signaling by FGFR1 fusion mutants.
    REACT_163743. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.

    Miscellaneous databases

    ChiTaRSi LRRFIP1. human.
    GeneWikii LRRFIP1.
    GenomeRNAii 9208.
    NextBioi 34517.
    PROi Q32MZ4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q32MZ4.
    Bgeei Q32MZ4.
    CleanExi HS_LRRFIP1.
    Genevestigatori Q32MZ4.

    Family and domain databases

    InterProi IPR019139. Leu-rich_rep_flightless-int_pr.
    [Graphical view ]
    PANTHERi PTHR19212. PTHR19212. 1 hit.
    Pfami PF09738. DUF2051. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of a transcription regulator with homology to GC-binding factor."
      Reed A.L., Yamazaki H., Kaufman J.D., Rubinstein Y., Murphy B.A., Johnson A.C.
      J. Biol. Chem. 273:21594-21602(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Ovarian carcinoma.
    2. "TRIP: a novel double stranded RNA binding protein which interacts with the leucine rich repeat of flightless I."
      Wilson S.A., Brown E.C., Kingsman A.J., Kingsman S.M.
      Nucleic Acids Res. 26:3460-3467(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH FLII, DEVELOPMENTAL STAGE.
      Tissue: Cervix carcinoma.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(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] (ISOFORMS 1 AND 3).
      Tissue: Melanoma.
    5. "Novel proteins interacting with the leucine-rich repeat domain of human flightless-I identified by the yeast two-hybrid system."
      Fong K.S.K., de Couet H.G.
      Genomics 58:146-157(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-626 (ISOFORM 4).
      Tissue: Heart.
    6. "GC factor 2 represses platelet-derived growth factor A-chain gene transcription and is itself induced by arterial injury."
      Khachigian L.M., Santiago F.S., Rafty L.A., Chan O.L.-W., Delbridge G.J., Bobik A., Collins T., Johnson A.C.
      Circ. Res. 84:1258-1267(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    7. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. Cited for: FUNCTION.
    9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-581; SER-618; THR-676; SER-714 AND SER-733, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    13. "Modulation of TLR signaling by multiple MyD88-interacting partners including leucine-rich repeat Fli-I-interacting proteins."
      Dai P., Jeong S.Y., Yu Y., Leng T., Wu W., Xie L., Chen X.
      J. Immunol. 182:3450-3460(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FLII AND MYD88.
    14. "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-115; SER-120 AND SER-618, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-120; SER-555; SER-581; SER-714 AND SER-766, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Crystal structure of the dimeric coiled-coil domain of the cytosolic nucleic acid sensor LRRFIP1."
      Nguyen J.B., Modis Y.
      J. Struct. Biol. 181:82-88(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 162-249, DOMAIN, COILED COIL, DNA-BINDING, SUBUNIT.
    19. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-68.

    Entry informationi

    Entry nameiLRRF1_HUMAN
    AccessioniPrimary (citable) accession number: Q32MZ4
    Secondary accession number(s): E9PGZ2
    , O75766, O75799, Q32MZ5, Q53T49, Q6PKG2, Q9Y607
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2006
    Last sequence update: September 5, 2006
    Last modified: October 1, 2014
    This is version 89 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 2
      Human chromosome 2: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3