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Q32MZ4

- LRRF1_HUMAN

UniProt

Q32MZ4 - LRRF1_HUMAN

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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

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 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ32MZ4.
CleanExiHS_LRRFIP1.
ExpressionAtlasiQ32MZ4. baseline and differential.
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. 23 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.
GeneTreeiENSGT00530000063564.
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

        10         20         30         40         50
MTSPAAAQSR EIDCLSPEAQ KLAEARLAAK RAARAEAREI RMKELERQQK
60 70 80 90 100
EEDSERYSRR SRRNTSASDE DERMSVGSRG SLRVEERPEK DFTEKGSRNM
110 120 130 140 150
PGLSAATLAS LGGTSSRRGS GDTSISIDTE ASIREIKELN ELKDQIQDVE
160 170 180 190 200
GKYMQGLKEM KDSLAEVEEK YKKAMVSNAQ LDNEKTNFMY QVDTLKDMLL
210 220 230 240 250
ELEEQLAESR RQYEEKNKEF EREKHAHSIL QFQFAEVKEA LKQREEMLEK
260 270 280 290 300
HGIILNSEIA TNGETSDTLN NVGYQGPTKM TKEELNALKS TGDGTLGRAS
310 320 330 340 350
EVEVKNEIVA NVGKREILHN TEKEQHTEDT VKDCVDIEVF PAGENTEDQK
360 370 380 390 400
SSEDTAPFLG TLAGATYEEQ VQSQILESSS LPENTVQVES NEVMGAPDDR
410 420 430 440 450
TRTPLEPSNC WSDLDGGNHT ENVGEAAVTQ VEEQAGTVAS CPLGHSDDTV
460 470 480 490 500
YHDDKCMVEV PQELETSTGH SLEKEFTNQE AAEPKEVPAH STEVGRDHNE
510 520 530 540 550
EEGEETGLRD EKPIKTEVPG SPAGTEGNCQ EATGPSTVDT QNEPLDMKEP
560 570 580 590 600
DEEKSDQQGE ALDSSQKKTK NKKKKNKKKK SPVPVETLKD VKKELTYQNT
610 620 630 640 650
DLSEIKEEEQ VKSTDRKSAV EAQNEVTENP KQKIAAESSE NVDCPENPKI
660 670 680 690 700
KLDGKLDQEG DDVQTAAEEV LADGDTLDFE DDTVQSSGPR AGGEELDEGV
710 720 730 740 750
AKDNAKIDGA TQSSPAEPKS EDADRCTLPE HESPSQDISD ACEAESTERC
760 770 780 790 800
EMSEHPSQTV RKALDSNSLE NDDLSAPGRE PGHFNPESRE DTRGGNEKGK

SKEDCTMS
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. 23 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 GC02P238536.
H-InvDB HIX0030126.
HGNCi HGNC:6702. LRRFIP1.
HPAi HPA006979.
MIMi 603256. gene.
neXtProti NX_Q32MZ4.
PharmGKBi PA30465.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG296572.
GeneTreei ENSGT00530000063564.
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

Bgeei Q32MZ4.
CleanExi HS_LRRFIP1.
ExpressionAtlasi Q32MZ4. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 90 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