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Q32MZ4 (LRRF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:LRRFIP1
Synonyms:GCF2, TRIP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length808 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6 Ref.7 Ref.8 Ref.13

Subunit structure

Homodimer. May also form higher oligomers. Interacts with FLII. Interacts with MYD88. Competes with FLII for MyD88-binding, even in the absence of LPS. Ref.2 Ref.13 Ref.18

Subcellular location

Nucleus. Cytoplasm Ref.2 Ref.7.

Tissue specificity

Ubiquitously expressed. Ref.1 Ref.2

Developmental stage

Widely expressed in fetal tissues. Ref.2

Domain

The DNA-binding domain is intrinsically unstructured. Ref.18

The coiled coil mediates dimerization. Ref.18

Sequence similarities

Belongs to the LRRFIP family.

Sequence caution

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.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandDNA-binding
   Molecular functionRepressor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processinnate immune response

Traceable author statement. Source: Reactome

negative regulation of transcription, DNA-templated

Non-traceable author statement Ref.1. Source: UniProtKB

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytoskeleton

Traceable author statement Ref.2. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

nucleus

Non-traceable author statement Ref.1. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Inferred from direct assay Ref.18. Source: UniProtKB

double-stranded RNA binding

Traceable author statement Ref.2. Source: ProtInc

protein binding

Inferred from physical interaction Ref.5Ref.2. Source: IntAct

protein homodimerization activity

Inferred from direct assay Ref.18. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FLIIQ130452EBI-1369100,EBI-351549

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q32MZ4-1)

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.
Isoform 2 (identifier: Q32MZ4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     137-160: Missing.
Isoform 3 (identifier: Q32MZ4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     52-83: Missing.
     137-160: Missing.
Isoform 4 (identifier: Q32MZ4-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 808807Leucine-rich repeat flightless-interacting protein 1
PRO_0000248392

Regions

Region485 – 584100DNA-binding
Coiled coil128 – 250123 Ref.18
Compositional bias567 – 59327Lys-rich

Amino acid modifications

Modified residue21N-acetylthreonine Ref.12 Ref.15
Modified residue161Phosphoserine Ref.10 Ref.15
Modified residue1151Phosphoserine Ref.14
Modified residue1201Phosphoserine Ref.11 Ref.14 Ref.15
Modified residue5551Phosphoserine Ref.15 Ref.17
Modified residue5811Phosphoserine Ref.11 Ref.15
Modified residue6181Phosphoserine Ref.11 Ref.14
Modified residue6761Phosphothreonine Ref.11
Modified residue7141Phosphoserine Ref.11 Ref.15
Modified residue7331Phosphoserine Ref.11
Modified residue7661Phosphoserine Ref.15

Natural variations

Alternative sequence1 – 2222MTSPA…EAQKL → MDMGTQGSGRKRLPNRERLT AEDDALNQIARE in isoform 4.
VSP_046809
Alternative sequence511E → EIYQVQKKYYGLDTKWGDIE QWM in isoform 4.
VSP_046810
Alternative sequence52 – 8332Missing in isoform 3.
VSP_020264
Alternative sequence831R → RSQPDLEYGGPYAWTNGYDG ELYGSQSLNRRSGRPSCLYS AARPSGSYRASVLDEGSFGG TRRGSTSGSRAPSEYSGHLN SSSRASSRASSARASPV in isoform 4.
VSP_046811
Alternative sequence137 – 16024Missing in isoform 2 and isoform 3.
VSP_020265
Alternative sequence2491E → EEIRQLQQKQASSIREISDL QETIEWKDKKIGALERQKEF FDSVRSERDDLREEVVMLKE ELK in isoform 4.
VSP_046812
Alternative sequence297 – 450154GRASE…SDDTV → DIRLKKLVDERECLLEQIKK LKGQLEERQKIGKLDNLRSE DDVLENGTDMHVMDLQRDAN RQISDLKFKLAKSEQEITAL EQNVIRLESQVSRYKSAAEN AEKIEDELKAEKRKLQRELR SALDKTEELEVSNGHLVKRL EKMKANRSALLSQQ in isoform 4.
VSP_046813
Alternative sequence451 – 808358Missing in isoform 4.
VSP_046814
Natural variant681S → C in a breast cancer sample; somatic mutation. Ref.19
VAR_036037
Natural variant2751Q → R.
Corresponds to variant rs3213869 [ dbSNP | Ensembl ].
VAR_027291
Natural variant4181N → S.
Corresponds to variant rs2001301 [ dbSNP | Ensembl ].
VAR_027292
Natural variant6091E → K.
Corresponds to variant rs3739041 [ dbSNP | Ensembl ].
VAR_027293
Natural variant6331K → E.
Corresponds to variant rs3739041 [ dbSNP | Ensembl ].
VAR_056111
Natural variant6451P → L.
Corresponds to variant rs3739040 [ dbSNP | Ensembl ].
VAR_027294
Natural variant7791R → G.
Corresponds to variant rs3739039 [ dbSNP | Ensembl ].
VAR_027295
Natural variant7831H → D.
Corresponds to variant rs3739038 [ dbSNP | Ensembl ].
VAR_027296

Experimental info

Sequence conflict171P → L in AAC32037. Ref.1
Sequence conflict261R → W in AAC32037. Ref.1
Sequence conflict1251I → F in CAA11076. Ref.2
Sequence conflict3271T → A in AAC32037. Ref.1
Sequence conflict5621L → F in AAI08915. Ref.4
Sequence conflict6651T → P in AAC32037. Ref.1
Sequence conflict6841V → A in AAC32037. Ref.1

Secondary structure

.... 808
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 5, 2006. Version 2.
Checksum: 4E6140DF2471A7C9

FASTA80889,253
        10         20         30         40         50         60 
MTSPAAAQSR EIDCLSPEAQ KLAEARLAAK RAARAEAREI RMKELERQQK EEDSERYSRR 

        70         80         90        100        110        120 
SRRNTSASDE DERMSVGSRG SLRVEERPEK DFTEKGSRNM PGLSAATLAS LGGTSSRRGS 

       130        140        150        160        170        180 
GDTSISIDTE ASIREIKELN ELKDQIQDVE GKYMQGLKEM KDSLAEVEEK YKKAMVSNAQ 

       190        200        210        220        230        240 
LDNEKTNFMY QVDTLKDMLL ELEEQLAESR RQYEEKNKEF EREKHAHSIL QFQFAEVKEA 

       250        260        270        280        290        300 
LKQREEMLEK HGIILNSEIA TNGETSDTLN NVGYQGPTKM TKEELNALKS TGDGTLGRAS 

       310        320        330        340        350        360 
EVEVKNEIVA NVGKREILHN TEKEQHTEDT VKDCVDIEVF PAGENTEDQK SSEDTAPFLG 

       370        380        390        400        410        420 
TLAGATYEEQ VQSQILESSS LPENTVQVES NEVMGAPDDR TRTPLEPSNC WSDLDGGNHT 

       430        440        450        460        470        480 
ENVGEAAVTQ VEEQAGTVAS CPLGHSDDTV YHDDKCMVEV PQELETSTGH SLEKEFTNQE 

       490        500        510        520        530        540 
AAEPKEVPAH STEVGRDHNE EEGEETGLRD EKPIKTEVPG SPAGTEGNCQ EATGPSTVDT 

       550        560        570        580        590        600 
QNEPLDMKEP DEEKSDQQGE ALDSSQKKTK NKKKKNKKKK SPVPVETLKD VKKELTYQNT 

       610        620        630        640        650        660 
DLSEIKEEEQ VKSTDRKSAV EAQNEVTENP KQKIAAESSE NVDCPENPKI KLDGKLDQEG 

       670        680        690        700        710        720 
DDVQTAAEEV LADGDTLDFE DDTVQSSGPR AGGEELDEGV AKDNAKIDGA TQSSPAEPKS 

       730        740        750        760        770        780 
EDADRCTLPE HESPSQDISD ACEAESTERC EMSEHPSQTV RKALDSNSLE NDDLSAPGRE 

       790        800 
PGHFNPESRE DTRGGNEKGK SKEDCTMS 

« Hide

Isoform 2 [UniParc].

Checksum: DDB6D45C670DBE97
Show »

FASTA78486,404
Isoform 3 [UniParc].

Checksum: F99016BC7CE54A60
Show »

FASTA75282,689
Isoform 4 [UniParc].

Checksum: E7B967AF138F79C3
Show »

FASTA64073,060

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"GCF2: expression and molecular analysis of repression."
Rikiyama T., Curtis J., Oikawa M., Zimonjic D.B., Popescu N., Murphy B.A., Wilson M.A., Johnson A.C.
Biochim. Biophys. Acta 1629:15-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"GCF2/LRRFIP1 represses tumor necrosis factor alpha expression."
Suriano A.R., Sanford A.N., Kim N., Oh M., Kennedy S., Henderson M.J., Dietzmann K., Sullivan K.E.
Mol. Cell. Biol. 25:9073-9081(2005) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-68.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2521.1. [Q32MZ4-2]
CCDS46551.1. [Q32MZ4-4]
CCDS46552.1. [Q32MZ4-1]
CCDS46553.1. [Q32MZ4-3]
RefSeqNP_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]
UniGeneHs.471779.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4H22X-ray2.89A/B/C/D162-249[»]
ProteinModelPortalQ32MZ4.
SMRQ32MZ4. Positions 167-249.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114642. 20 interactions.
IntActQ32MZ4. 1 interaction.
STRING9606.ENSP00000375857.

PTM databases

PhosphoSiteQ32MZ4.

Polymorphism databases

DMDM114149995.

Proteomic databases

MaxQBQ32MZ4.
PaxDbQ32MZ4.
PRIDEQ32MZ4.

Protocols and materials databases

DNASU9208.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000244815; ENSP00000244815; ENSG00000124831. [Q32MZ4-2]
ENST00000289175; ENSP00000289175; ENSG00000124831. [Q32MZ4-3]
ENST00000308482; ENSP00000310109; ENSG00000124831. [Q32MZ4-4]
ENST00000392000; ENSP00000375857; ENSG00000124831. [Q32MZ4-1]
GeneID9208.
KEGGhsa:9208.
UCSCuc002vxd.3. human. [Q32MZ4-2]
uc002vxe.3. human. [Q32MZ4-1]
uc002vxf.3. human. [Q32MZ4-3]

Organism-specific databases

CTD9208.
GeneCardsGC02P238617.
H-InvDBHIX0030126.
HGNCHGNC:6702. LRRFIP1.
HPAHPA006979.
MIM603256. gene.
neXtProtNX_Q32MZ4.
PharmGKBPA30465.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG296572.
HOGENOMHOG000113391.
HOVERGENHBG081935.
InParanoidQ32MZ4.
OMAISSRIMG.
OrthoDBEOG7DNNTX.
PhylomeDBQ32MZ4.
TreeFamTF314109.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ32MZ4.
BgeeQ32MZ4.
CleanExHS_LRRFIP1.
GenevestigatorQ32MZ4.

Family and domain databases

InterProIPR019139. Leu-rich_rep_flightless-int_pr.
[Graphical view]
PANTHERPTHR19212. PTHR19212. 1 hit.
PfamPF09738. DUF2051. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLRRFIP1. human.
GeneWikiLRRFIP1.
GenomeRNAi9208.
NextBio34517.
PROQ32MZ4.
SOURCESearch...

Entry information

Entry nameLRRF1_HUMAN
AccessionPrimary (citable) accession number: Q32MZ4
Secondary accession number(s): E9PGZ2 expand/collapse secondary AC list , O75766, O75799, Q32MZ5, Q53T49, Q6PKG2, Q9Y607
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: July 9, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM