Q32MZ4 (LRRF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	LRRFIP1
Synonyms:	GCF2, TRIP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	808 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.5 Ref.6 Ref.7 Ref.11
Subunit structure	Interacts with FLII. Interacts with MYD88. Competes with FLII for MyD88-binding, even in the absence of LPS. Ref.2 Ref.11
Subcellular location	Nucleus. Cytoplasm Ref.2 Ref.6.
Tissue specificity	Ubiquitously expressed. Ref.1 Ref.2
Developmental stage	Widely expressed in fetal tissues. Ref.2
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 process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	DNA-binding
Molecular function	Repressor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of transcription, DNA-dependent Non-traceable author statement Ref.1. Source: UniProtKB regulation of transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Traceable author statement Ref.2. Source: ProtInc cytoskeleton Traceable author statement Ref.2. Source: ProtInc nucleus Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW double-stranded RNA binding Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FLII	Q13045	2	EBI-1369100,EBI-351549

Alternative products

This entry describes 3 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.13

Chain

2 – 808

807

Leucine-rich repeat flightless-interacting protein 1

PRO_0000248392

Regions

Region

485 – 584

100

DNA-binding

Coiled coil

128 – 250

123

Potential

Compositional bias

567 – 593

27

Lys-rich

Amino acid modifications

Modified residue

2

1

N-acetylthreonine Ref.13

Modified residue

16

1

Phosphoserine Ref.9 Ref.13

Modified residue

115

1

Phosphoserine Ref.12

Modified residue

120

1

Phosphoserine Ref.10 Ref.12 Ref.13

Modified residue

123

1

Phosphothreonine By similarity

Modified residue

555

1

Phosphoserine Ref.13 Ref.15

Modified residue

581

1

Phosphoserine Ref.10 Ref.13

Modified residue

618

1

Phosphoserine Ref.10 Ref.12

Modified residue

676

1

Phosphothreonine Ref.10

Modified residue

714

1

Phosphoserine Ref.10 Ref.13

Modified residue

733

1

Phosphoserine Ref.10

Modified residue

766

1

Phosphoserine Ref.13

Natural variations

Alternative sequence

52 – 83

32

Missing in isoform 3.

VSP_020264

Alternative sequence

137 – 160

24

Missing in isoform 2 and isoform 3.

VSP_020265

Natural variant

68

1

S → C in a breast cancer sample; somatic mutation. Ref.16

VAR_036037

Natural variant

275

1

Q → R.
Corresponds to variant rs3213869 [ dbSNP | Ensembl ].

VAR_027291

Natural variant

418

1

N → S.
Corresponds to variant rs2001301 [ dbSNP | Ensembl ].

VAR_027292

Natural variant

609

1

E → K.
Corresponds to variant rs3739041 [ dbSNP | Ensembl ].

VAR_027293

Natural variant

633

1

K → E.
Corresponds to variant rs3739041 [ dbSNP | Ensembl ].

VAR_056111

Natural variant

645

1

P → L.
Corresponds to variant rs3739040 [ dbSNP | Ensembl ].

VAR_027294

Natural variant

779

1

R → G.
Corresponds to variant rs3739039 [ dbSNP | Ensembl ].

VAR_027295

Natural variant

783

1

H → D.
Corresponds to variant rs3739038 [ dbSNP | Ensembl ].

VAR_027296

Experimental info

Sequence conflict

17

1

P → L in AAC32037. Ref.1

Sequence conflict

26

1

R → W in AAC32037. Ref.1

Sequence conflict

125

1

I → F in CAA11076. Ref.2

Sequence conflict

327

1

T → A in AAC32037. Ref.1

Sequence conflict

562

1

L → F in AAI08915. Ref.4

Sequence conflict

665

1

T → P in AAC32037. Ref.1

Sequence conflict

684

1

V → A in AAC32037. Ref.1

Secondary structure

1

.

.

.

.

808

Helix Strand Turn

Details...

Helix

171 – 242

72

Turn

243 – 245

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 5, 2006. Version 2. Checksum: 4E6140DF2471A7C9	FASTA	808	89,253
	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
	Isoform 2 [UniParc]. Checksum: DDB6D45C670DBE97	FASTA	784	86,404
	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 ASIREIKDSL AEVEEKYKKA MVSNAQLDNE KTNFMYQVDT LKDMLLELEE 190 200 210 220 230 240 QLAESRRQYE EKNKEFEREK HAHSILQFQF AEVKEALKQR EEMLEKHGII LNSEIATNGE 250 260 270 280 290 300 TSDTLNNVGY QGPTKMTKEE LNALKSTGDG TLGRASEVEV KNEIVANVGK REILHNTEKE 310 320 330 340 350 360 QHTEDTVKDC VDIEVFPAGE NTEDQKSSED TAPFLGTLAG ATYEEQVQSQ ILESSSLPEN 370 380 390 400 410 420 TVQVESNEVM GAPDDRTRTP LEPSNCWSDL DGGNHTENVG EAAVTQVEEQ AGTVASCPLG 430 440 450 460 470 480 HSDDTVYHDD KCMVEVPQEL ETSTGHSLEK EFTNQEAAEP KEVPAHSTEV GRDHNEEEGE 490 500 510 520 530 540 ETGLRDEKPI KTEVPGSPAG TEGNCQEATG PSTVDTQNEP LDMKEPDEEK SDQQGEALDS 550 560 570 580 590 600 SQKKTKNKKK KNKKKKSPVP VETLKDVKKE LTYQNTDLSE IKEEEQVKST DRKSAVEAQN 610 620 630 640 650 660 EVTENPKQKI AAESSENVDC PENPKIKLDG KLDQEGDDVQ TAAEEVLADG DTLDFEDDTV 670 680 690 700 710 720 QSSGPRAGGE ELDEGVAKDN AKIDGATQSS PAEPKSEDAD RCTLPEHESP SQDISDACEA 730 740 750 760 770 780 ESTERCEMSE HPSQTVRKAL DSNSLENDDL SAPGREPGHF NPESREDTRG GNEKGKSKED CTMS
	Isoform 3 [UniParc]. Checksum: F99016BC7CE54A60	FASTA	752	82,689
	10 20 30 40 50 60 MTSPAAAQSR EIDCLSPEAQ KLAEARLAAK RAARAEAREI RMKELERQQK EVEERPEKDF 70 80 90 100 110 120 TEKGSRNMPG LSAATLASLG GTSSRRGSGD TSISIDTEAS IREIKDSLAE VEEKYKKAMV 130 140 150 160 170 180 SNAQLDNEKT NFMYQVDTLK DMLLELEEQL AESRRQYEEK NKEFEREKHA HSILQFQFAE 190 200 210 220 230 240 VKEALKQREE MLEKHGIILN SEIATNGETS DTLNNVGYQG PTKMTKEELN ALKSTGDGTL 250 260 270 280 290 300 GRASEVEVKN EIVANVGKRE ILHNTEKEQH TEDTVKDCVD IEVFPAGENT EDQKSSEDTA 310 320 330 340 350 360 PFLGTLAGAT YEEQVQSQIL ESSSLPENTV QVESNEVMGA PDDRTRTPLE PSNCWSDLDG 370 380 390 400 410 420 GNHTENVGEA AVTQVEEQAG TVASCPLGHS DDTVYHDDKC MVEVPQELET STGHSLEKEF 430 440 450 460 470 480 TNQEAAEPKE VPAHSTEVGR DHNEEEGEET GLRDEKPIKT EVPGSPAGTE GNCQEATGPS 490 500 510 520 530 540 TVDTQNEPLD MKEPDEEKSD QQGEALDSSQ KKTKNKKKKN KKKKSPVPVE TLKDVKKELT 550 560 570 580 590 600 YQNTDLSEIK EEEQVKSTDR KSAVEAQNEV TENPKQKIAA ESSENVDCPE NPKIKLDGKL 610 620 630 640 650 660 DQEGDDVQTA AEEVLADGDT LDFEDDTVQS SGPRAGGEEL DEGVAKDNAK IDGATQSSPA 670 680 690 700 710 720 EPKSEDADRC TLPEHESPSQ DISDACEAES TERCEMSEHP SQTVRKALDS NSLENDDLSA 730 740 750 PGREPGHFNP ESREDTRGGN EKGKSKEDCT MS

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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.
[12]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[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: 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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. Tissue: Cervix carcinoma.
[14]	"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].
[15]	"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, MASS SPECTROMETRY.
[16]	"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. , 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.
BC001385 mRNA. Translation: AAH01385.1. Sequence problems.
BC108913 mRNA. Translation: AAI08914.1.
BC108914 mRNA. Translation: AAI08915.1.

IPI

IPI00006207.
IPI00382733.
IPI00785113.

RefSeq

NP_001131024.1. NM_001137552.1.
NP_001131025.1. NM_001137553.1.
NP_004726.2. NM_004735.3.

UniGene

Hs.471779.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4H22	X-ray	2.89	A/B/C/D	162-249	[»]

ProteinModelPortal

Q32MZ4.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q32MZ4. 1 interaction.

STRING

9606.ENSP00000375857.

PTM databases

PhosphoSite

Q32MZ4.

Polymorphism databases

DMDM

114149995.

Proteomic databases

PaxDb

Q32MZ4.

PRIDE

Q32MZ4.

Protocols and materials databases

DNASU

9208.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000244815; ENSP00000244815; ENSG00000124831.
ENST00000289175; ENSP00000289175; ENSG00000124831.
ENST00000392000; ENSP00000375857; ENSG00000124831.

GeneID

9208.

KEGG

hsa:9208.

UCSC

uc002vxd.3. human.
uc002vxe.3. human.
uc002vxf.3. human.

Organism-specific databases

CTD

9208.

GeneCards

GC02P238617.

H-InvDB

HIX0030126.

HGNC

HGNC:6702. LRRFIP1.

HPA

HPA006979.

MIM

603256. gene.

neXtProt

NX_Q32MZ4.

PharmGKB

PA30465.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG296572.

HOGENOM

HOG000113391.

HOVERGEN

HBG081935.

InParanoid

Q32MZ4.

OMA

NTEKEQH.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.

Gene expression databases

ArrayExpress

Q32MZ4.

Bgee

Q32MZ4.

CleanEx

HS_LRRFIP1.

Genevestigator

Q32MZ4.

Family and domain databases

InterPro

IPR019139. Leu-rich_rep_flightless-int_pr.
[Graphical view]

PANTHER

PTHR19212. PTHR19212. 1 hit.

Pfam

PF09738. DUF2051. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

LRRFIP1. human.

GenomeRNAi

9208.

NextBio

34517.

SOURCE

Search...

Entry information

Entry name

LRRF1_HUMAN

Accession

Primary (citable) accession number: Q32MZ4
Secondary accession number(s): O75766 , O75799, Q32MZ5, Q53T49, Q6PKG2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	September 5, 2006
Last modified:	April 3, 2013
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.