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Protein

Leucine-rich repeat flightless-interacting protein 2

Gene

LRRFIP2

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

Functioni

May function as activator of the canonical Wnt signaling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding.2 Publications

GO - Molecular functioni

  • LRR domain binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

SignaLinkiQ9Y608.
SIGNORiQ9Y608.

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine-rich repeat flightless-interacting protein 2
Short name:
LRR FLII-interacting protein 2
Gene namesi
Name:LRRFIP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:6703. LRRFIP2.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi190 – 1901S → A: No change in LPS-induced NFKB activity. 1 Publication
Mutagenesisi200 – 2001S → A: No change in LPS-induced NFKB activity. 1 Publication
Mutagenesisi202 – 2021S → A: Reduction in LPS-induced NFKB activity. 1 Publication
Mutagenesisi202 – 2021S → E: No change in LPS-induced NFKB activity. Interacts with MYD88 in an LPS-inducible manner. 1 Publication

Organism-specific databases

Orphaneti144. Hereditary nonpolyposis colon cancer.
PharmGKBiPA30466.

Polymorphism and mutation databases

BioMutaiLRRFIP2.
DMDMi74721508.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 721721Leucine-rich repeat flightless-interacting protein 2PRO_0000245246Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181PhosphoserineCombined sources
Modified residuei190 – 1901Phosphoserine1 Publication
Modified residuei202 – 2021Phosphoserine1 Publication
Modified residuei309 – 3091PhosphoserineCombined sources
Modified residuei312 – 3121PhosphoserineCombined sources
Modified residuei320 – 3201PhosphoserineCombined sources
Modified residuei324 – 3241PhosphoserineCombined sources
Modified residuei328 – 3281PhosphoserineCombined sources
Modified residuei331 – 3311PhosphothreonineBy similarity
Modified residuei332 – 3321PhosphoserineBy similarity
Modified residuei333 – 3331PhosphoserineBy similarity
Isoform 2 (identifier: Q9Y608-2)
Modified residuei96 – 961PhosphoserineCombined sources
Modified residuei101 – 1011PhosphoserineCombined sources
Isoform 5 (identifier: Q9Y608-5)
Modified residuei168 – 1681PhosphoserineCombined sources
Modified residuei173 – 1731PhosphoserineCombined sources

Post-translational modificationi

Ser-190 and Ser-202 are phosphorylated in response to LPS stimulation. Ser-202 phosphorylation regulates the LPS-induced interaction with MYD88.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Y608.
MaxQBiQ9Y608.
PaxDbiQ9Y608.
PeptideAtlasiQ9Y608.
PRIDEiQ9Y608.

PTM databases

iPTMnetiQ9Y608.
PhosphoSiteiQ9Y608.

Expressioni

Tissue specificityi

Widely expressed, with highest levels in heart and skeletal muscle.1 Publication

Gene expression databases

BgeeiQ9Y608.
CleanExiHS_LRRFIP2.
ExpressionAtlasiQ9Y608. baseline and differential.
GenevisibleiQ9Y608. HS.

Organism-specific databases

HPAiHPA035956.
HPA042023.

Interactioni

Subunit structurei

Interacts (via N-terminus) with DVL3. Interacts with FLII. Weakly interacts with MYD88 in resting cells. Following LPS-stimulation, the interaction with MYD88 is rapidly enhanced; the complex gradually dissociates to basal levels after 6 hours of stimulation. Interaction with MYD88 is regulated by LPS-induced phosphorylation at Ser-202. In the presence of LPS, competes with FLII for MYD88-binding.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATPAF2Q8N5M13EBI-1023718,EBI-1166928
DVL3Q929972EBI-1023718,EBI-739789

GO - Molecular functioni

  • LRR domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114643. 43 interactions.
IntActiQ9Y608. 39 interactions.
MINTiMINT-2824015.
STRINGi9606.ENSP00000338727.

Structurei

3D structure databases

ProteinModelPortaliQ9Y608.
SMRiQ9Y608. Positions 375-457.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 370370DVL3-bindingAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili22 – 4928Sequence analysisAdd
BLAST
Coiled coili349 – 524176Sequence analysisAdd
BLAST
Coiled coili566 – 714149Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi118 – 342225Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the LRRFIP family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2010. Eukaryota.
ENOG4111H1S. LUCA.
GeneTreeiENSGT00530000063564.
HOGENOMiHOG000294125.
HOVERGENiHBG061558.
InParanoidiQ9Y608.
OMAiDRKWGQI.
OrthoDBiEOG7DNNTX.
PhylomeDBiQ9Y608.
TreeFamiTF314109.

Family and domain databases

InterProiIPR019139. LRRFIP1/2.
[Graphical view]
PANTHERiPTHR19212. PTHR19212. 3 hits.
PfamiPF09738. DUF2051. 3 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y608-1) [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
MGTPASGRKR TPVKDRFSAE DEALSNIARE AEARLAAKRA ARAEARDIRM
60 70 80 90 100
RELERQQKEY SLHSFDRKWG QIQKWLEDSE RARYSHRSSH HRPYLGVEDA
110 120 130 140 150
LSIRSVGSHR YDMFKDRSSR LSSLNHSYSH SHGMKKRSSD SHKDLLSGLY
160 170 180 190 200
FDQRNYSSLR HSKPTSAYYT RQSSSLYSDP LATYKSDRAS PTANSGLLRS
210 220 230 240 250
ASLASLYNGG LYNPYGPRTP SECSYYSSRI SSARSSPGFT NDDTASIVSS
260 270 280 290 300
DRASRGRRES VVSAADYFSR SNRRGSVVSE VDDISIPDLS SLDEKSDKQY
310 320 330 340 350
AENYTRPSSR NSASATTPLS GNSSRRGSGD TSSLIDPDTS LSELRDIYDL
360 370 380 390 400
KDQIQDVEGR YMQGLKELKE SLSEVEEKYK KAMVSNAQLD NEKNNLIYQV
410 420 430 440 450
DTLKDVIEEQ EEQMAEFYRE NEEKSKELER QKHMCSVLQH KMEELKEGLR
460 470 480 490 500
QRDELIEEKQ RMQQKIDTMT KEVFDLQETL LWKDKKIGAL EKQKEYIACL
510 520 530 540 550
RNERDMLREE LADLQETVKT GEKHGLVIIP DGTPNGDVSH EPVAGAITVV
560 570 580 590 600
SQEAAQVLES AGEGPLDVRL RKLAGEKEEL LSQIRKLKLQ LEEERQKCSR
610 620 630 640 650
NDGTVGDLAG LQNGSDLQFI EMQRDANRQI SEYKFKLSKA EQDITTLEQS
660 670 680 690 700
ISRLEGQVLR YKTAAENAEK VEDELKAEKR KLQRELRTAL DKIEEMEMTN
710 720
SHLAKRLEKM KANRTALLAQ Q
Length:721
Mass (Da):82,171
Last modified:November 1, 1999 - v1
Checksum:i94B18B274656CB0B
GO
Isoform 2 (identifier: Q9Y608-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     60-291: Missing.
     346-369: Missing.
     457-521: Missing.

Show »
Length:400
Mass (Da):45,414
Checksum:iAD687735EAFE04F6
GO
Isoform 3 (identifier: Q9Y608-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-621: Missing.

Show »
Length:100
Mass (Da):11,736
Checksum:iEFCDC5B6AC68785F
GO
Isoform 4 (identifier: Q9Y608-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     60-291: Missing.
     457-521: Missing.

Show »
Length:424
Mass (Da):48,294
Checksum:iA5BFF9F6869503DE
GO
Isoform 5 (identifier: Q9Y608-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     60-76: Missing.
     111-124: Missing.
     146-202: Missing.
     220-291: Missing.
     346-369: Missing.
     489-522: Missing.

Note: No experimental confirmation available.Combined sources
Show »
Length:503
Mass (Da):57,394
Checksum:i965FF6DABB76907F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti143 – 1431K → E.
Corresponds to variant rs34902788 [ dbSNP | Ensembl ].
VAR_050001

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 621621Missing in isoform 3. 1 PublicationVSP_019674Add
BLAST
Alternative sequencei60 – 291232Missing in isoform 2 and isoform 4. 2 PublicationsVSP_019675Add
BLAST
Alternative sequencei60 – 7617Missing in isoform 5. 1 PublicationVSP_056969Add
BLAST
Alternative sequencei111 – 12414Missing in isoform 5. 1 PublicationVSP_056970Add
BLAST
Alternative sequencei146 – 20257Missing in isoform 5. 1 PublicationVSP_056971Add
BLAST
Alternative sequencei220 – 29172Missing in isoform 5. 1 PublicationVSP_056972Add
BLAST
Alternative sequencei346 – 36924Missing in isoform 2 and isoform 5. 2 PublicationsVSP_019676Add
BLAST
Alternative sequencei457 – 52165Missing in isoform 2 and isoform 4. 2 PublicationsVSP_019677Add
BLAST
Alternative sequencei489 – 52234Missing in isoform 5. 1 PublicationVSP_056973Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF115509 mRNA. Translation: AAD41257.1.
AK000255 mRNA. Translation: BAA91035.1.
AK291514 mRNA. Translation: BAF84203.1.
AK302282 mRNA. Translation: BAG63625.1.
CR749705 mRNA. Translation: CAH18481.1.
AC006583 Genomic DNA. No translation available.
AC126118 Genomic DNA. No translation available.
BC053668 mRNA. Translation: AAH53668.1.
CCDSiCCDS2664.1. [Q9Y608-1]
CCDS2665.1. [Q9Y608-2]
CCDS46791.1. [Q9Y608-4]
CCDS63592.1. [Q9Y608-5]
PIRiT50611.
RefSeqiNP_001127841.1. NM_001134369.2. [Q9Y608-4]
NP_001269620.1. NM_001282691.1. [Q9Y608-5]
NP_006300.1. NM_006309.3. [Q9Y608-1]
NP_060194.1. NM_017724.2. [Q9Y608-2]
XP_005265595.1. XM_005265538.2. [Q9Y608-1]
XP_005265596.1. XM_005265539.2. [Q9Y608-1]
XP_005265597.1. XM_005265540.1. [Q9Y608-1]
XP_011532519.1. XM_011534217.1. [Q9Y608-1]
XP_011532520.1. XM_011534218.1. [Q9Y608-1]
XP_011532521.1. XM_011534219.1. [Q9Y608-1]
UniGeneiHs.740522.

Genome annotation databases

EnsembliENST00000336686; ENSP00000338727; ENSG00000093167. [Q9Y608-1]
ENST00000354379; ENSP00000346349; ENSG00000093167. [Q9Y608-2]
ENST00000396428; ENSP00000379705; ENSG00000093167. [Q9Y608-5]
ENST00000421276; ENSP00000416364; ENSG00000093167. [Q9Y608-4]
ENST00000440230; ENSP00000405480; ENSG00000093167. [Q9Y608-4]
GeneIDi9209.
KEGGihsa:9209.
UCSCiuc003cgs.4. human. [Q9Y608-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF115509 mRNA. Translation: AAD41257.1.
AK000255 mRNA. Translation: BAA91035.1.
AK291514 mRNA. Translation: BAF84203.1.
AK302282 mRNA. Translation: BAG63625.1.
CR749705 mRNA. Translation: CAH18481.1.
AC006583 Genomic DNA. No translation available.
AC126118 Genomic DNA. No translation available.
BC053668 mRNA. Translation: AAH53668.1.
CCDSiCCDS2664.1. [Q9Y608-1]
CCDS2665.1. [Q9Y608-2]
CCDS46791.1. [Q9Y608-4]
CCDS63592.1. [Q9Y608-5]
PIRiT50611.
RefSeqiNP_001127841.1. NM_001134369.2. [Q9Y608-4]
NP_001269620.1. NM_001282691.1. [Q9Y608-5]
NP_006300.1. NM_006309.3. [Q9Y608-1]
NP_060194.1. NM_017724.2. [Q9Y608-2]
XP_005265595.1. XM_005265538.2. [Q9Y608-1]
XP_005265596.1. XM_005265539.2. [Q9Y608-1]
XP_005265597.1. XM_005265540.1. [Q9Y608-1]
XP_011532519.1. XM_011534217.1. [Q9Y608-1]
XP_011532520.1. XM_011534218.1. [Q9Y608-1]
XP_011532521.1. XM_011534219.1. [Q9Y608-1]
UniGeneiHs.740522.

3D structure databases

ProteinModelPortaliQ9Y608.
SMRiQ9Y608. Positions 375-457.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114643. 43 interactions.
IntActiQ9Y608. 39 interactions.
MINTiMINT-2824015.
STRINGi9606.ENSP00000338727.

PTM databases

iPTMnetiQ9Y608.
PhosphoSiteiQ9Y608.

Polymorphism and mutation databases

BioMutaiLRRFIP2.
DMDMi74721508.

Proteomic databases

EPDiQ9Y608.
MaxQBiQ9Y608.
PaxDbiQ9Y608.
PeptideAtlasiQ9Y608.
PRIDEiQ9Y608.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336686; ENSP00000338727; ENSG00000093167. [Q9Y608-1]
ENST00000354379; ENSP00000346349; ENSG00000093167. [Q9Y608-2]
ENST00000396428; ENSP00000379705; ENSG00000093167. [Q9Y608-5]
ENST00000421276; ENSP00000416364; ENSG00000093167. [Q9Y608-4]
ENST00000440230; ENSP00000405480; ENSG00000093167. [Q9Y608-4]
GeneIDi9209.
KEGGihsa:9209.
UCSCiuc003cgs.4. human. [Q9Y608-1]

Organism-specific databases

CTDi9209.
GeneCardsiLRRFIP2.
HGNCiHGNC:6703. LRRFIP2.
HPAiHPA035956.
HPA042023.
MIMi614043. gene.
neXtProtiNX_Q9Y608.
Orphaneti144. Hereditary nonpolyposis colon cancer.
PharmGKBiPA30466.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2010. Eukaryota.
ENOG4111H1S. LUCA.
GeneTreeiENSGT00530000063564.
HOGENOMiHOG000294125.
HOVERGENiHBG061558.
InParanoidiQ9Y608.
OMAiDRKWGQI.
OrthoDBiEOG7DNNTX.
PhylomeDBiQ9Y608.
TreeFamiTF314109.

Enzyme and pathway databases

SignaLinkiQ9Y608.
SIGNORiQ9Y608.

Miscellaneous databases

ChiTaRSiLRRFIP2. human.
GenomeRNAii9209.
PROiQ9Y608.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y608.
CleanExiHS_LRRFIP2.
ExpressionAtlasiQ9Y608. baseline and differential.
GenevisibleiQ9Y608. HS.

Family and domain databases

InterProiIPR019139. LRRFIP1/2.
[Graphical view]
PANTHERiPTHR19212. PTHR19212. 3 hits.
PfamiPF09738. DUF2051. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 1), REGION, TISSUE SPECIFICITY, INTERACTION WITH FLII.
    Tissue: Skeletal muscle.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
    Tissue: Colon mucosa and Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Testis.
  4. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 2).
    Tissue: Skin.
  6. "Unambiguous characterization of site-specific phosphorylation of leucine-rich repeat Fli-I-interacting protein 2 (LRRFIP2) in Toll-like receptor 4 (TLR4)-mediated signaling."
    Gunawardena H.P., Huang Y., Kenjale R., Wang H., Xie L., Chen X.
    J. Biol. Chem. 286:10897-10910(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 186-218 AND 326-345, PHOSPHORYLATION AT SER-190 AND SER-202, MUTAGENESIS OF SER-190; SER-200 AND SER-202, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Identification of the Wnt signaling activator leucine-rich repeat in Flightless interaction protein 2 by a genome-wide functional analysis."
    Liu J., Bang A.G., Kintner C., Orth A.P., Chanda S.K., Ding S., Schultz P.G.
    Proc. Natl. Acad. Sci. U.S.A. 102:1927-1932(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DVL3.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
    Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
    Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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.
  15. "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-320; SER-324 AND SER-328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-320, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309; SER-320; SER-324 AND SER-328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312; SER-324 AND SER-328, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiLRRF2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y608
Secondary accession number(s): A8K649
, A8MXR0, B4DY63, Q68CV3, Q9NXH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: November 1, 1999
Last modified: July 6, 2016
This is version 120 of the entry and version 1 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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