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Q13045

- FLII_HUMAN

UniProt

Q13045 - FLII_HUMAN

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Protein
Protein flightless-1 homolog
Gene
FLII, FLIL
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May play a role as coactivator in transcriptional activation by hormone-activated nuclear receptors (NR) and acts in cooperation with NCOA2 and CARM1. Involved in estrogen hormone signaling. Involved in early embryonic development By similarity. May play a role in regulation of cytoskeletal rearrangements involved in cytokinesis and cell migration, by inhibiting Rac1-dependent paxillin phosphorylation.1 Publication

GO - Molecular functioni

  1. actin binding Source: ProtInc
  2. protein binding Source: UniProtKB

GO - Biological processi

  1. multicellular organismal development Source: UniProtKB-KW
  2. muscle contraction Source: ProtInc
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein flightless-1 homolog
Gene namesi
Name:FLII
Synonyms:FLIL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:3750. FLII.

Subcellular locationi

Nucleus By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cell junctionfocal adhesion By similarity
Note: Colocalizes to actin-rich structures in blastocysts and, together with HRAS, RHOA and CDC42, in migrating fibroblasts. Localizes to centrosomes By similarity.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. focal adhesion Source: UniProtKB-SubCell
  3. microtubule organizing center Source: HPA
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi586 – 5861E → K: No change in ESR1 binding but reduced binding to ACTL6A and reduced coactivator function. 1 Publication
Mutagenesisi603 – 6031G → S: No change in binding to ACTL6A or in coactivator function. 1 Publication

Organism-specific databases

Orphaneti819. Smith-Magenis syndrome.
PharmGKBiPA28171.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12691269Protein flightless-1 homolog
PRO_0000218750Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei21 – 211N6-acetyllysine1 Publication
Modified residuei406 – 4061Phosphoserine2 Publications
Modified residuei436 – 4361Phosphoserine; by SGK33 Publications
Modified residuei818 – 8181Phosphothreonine; by SGK31 Publication
Modified residuei856 – 8561Phosphoserine7 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13045.
PaxDbiQ13045.
PeptideAtlasiQ13045.
PRIDEiQ13045.

PTM databases

PhosphoSiteiQ13045.

Expressioni

Tissue specificityi

Strongest expression in skeletal muscle with high expression also in the heart and lung.1 Publication

Gene expression databases

ArrayExpressiQ13045.
BgeeiQ13045.
CleanExiHS_FLII.
GenevestigatoriQ13045.

Organism-specific databases

HPAiCAB016132.
HPA007084.
HPA008903.

Interactioni

Subunit structurei

Interacts with actin, ACTL6A, NCOA2, CARM1 and MYD88. Interacts with LRRFIP1 and LRRFIP2. Upon LPS stimulation, LRRFIP2 competes for MYD88-binding. LRRFIP1 constitutively blocks the interaction with MyD88, even in the absence of LPS. Interacts with the nuclear receptors ESR1 and THRB. Interacts with SGK3.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRFIP1Q32MZ42EBI-351549,EBI-1369100

Protein-protein interaction databases

BioGridi108603. 30 interactions.
IntActiQ13045. 7 interactions.
MINTiMINT-1399971.
STRINGi9606.ENSP00000324573.

Structurei

3D structure databases

ProteinModelPortaliQ13045.
SMRiQ13045. Positions 2-415, 485-1264.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati7 – 3226LRR 1
Add
BLAST
Repeati33 – 5523LRR 2
Add
BLAST
Repeati56 – 7823LRR 3
Add
BLAST
Repeati80 – 10324LRR 4
Add
BLAST
Repeati104 – 12623LRR 5
Add
BLAST
Repeati127 – 14923LRR 6
Add
BLAST
Repeati150 – 17324LRR 7
Add
BLAST
Repeati175 – 19622LRR 8
Add
BLAST
Repeati197 – 22226LRR 9
Add
BLAST
Repeati223 – 24523LRR 10
Add
BLAST
Repeati247 – 26822LRR 11
Add
BLAST
Repeati269 – 29123LRR 12
Add
BLAST
Repeati293 – 31624LRR 13
Add
BLAST
Repeati318 – 33922LRR 14
Add
BLAST
Repeati340 – 36324LRR 15
Add
BLAST
Repeati501 – 55959Gelsolin-like 1
Add
BLAST
Repeati640 – 67031Gelsolin-like 2
Add
BLAST
Repeati755 – 79844Gelsolin-like 3
Add
BLAST
Repeati1068 – 111548Gelsolin-like 4
Add
BLAST
Repeati1176 – 121843Gelsolin-like 5
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 427427Interaction with LRRFIP1 and LRRFIP2
Add
BLAST
Regioni495 – 827333Interaction with ACTL6A
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi411 – 4155Poly-Ala
Compositional biasi892 – 97887Glu-rich
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiCOG4886.
HOGENOMiHOG000016110.
HOVERGENiHBG051627.
InParanoidiQ13045.
OMAiMEEWNED.
PhylomeDBiQ13045.
TreeFamiTF313468.

Family and domain databases

Gene3Di3.40.20.10. 7 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PfamiPF00626. Gelsolin. 4 hits.
PF00560. LRR_1. 1 hit.
PF12799. LRR_4. 1 hit.
PF13504. LRR_7. 2 hits.
PF13855. LRR_8. 2 hits.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 6 hits.
SM00369. LRR_TYP. 1 hit.
[Graphical view]
PROSITEiPS51450. LRR. 11 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13045-1) [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

MEATGVLPFV RGVDLSGNDF KGGYFPENVK AMTSLRWLKL NRTGLCYLPE     50
ELAALQKLEH LSVSHNNLTT LHGELSSLPS LRAIVARANS LKNSGVPDDI 100
FKLDDLSVLD LSHNQLTECP RELENAKNML VLNLSHNSID TIPNQLFINL 150
TDLLYLDLSE NRLESLPPQM RRLVHLQTLV LNGNPLLHAQ LRQLPAMTAL 200
QTLHLRSTQR TQSNLPTSLE GLSNLADVDL SCNDLTRVPE CLYTLPSLRR 250
LNLSSNQITE LSLCIDQWVH VETLNLSRNQ LTSLPSAICK LSKLKKLYLN 300
SNKLDFDGLP SGIGKLTNLE EFMAANNNLE LVPESLCRCP KLRKLVLNKN 350
HLVTLPEAIH FLTEIEVLDV RENPNLVMPP KPADRAAEWY NIDFSLQNQL 400
RLAGASPATV AAAAAAGSGP KDPMARKMRL RRRKDSAQDD QAKQVLKGMS 450
DVAQEKNKKQ EESADARAPS GKVRRWDQGL EKPRLDYSEF FTEDVGQLPG 500
LTIWQIENFV PVLVEEAFHG KFYEADCYIV LKTFLDDSGS LNWEIYYWIG 550
GEATLDKKAC SAIHAVNLRN YLGAECRTVR EEMGDESEEF LQVFDNDISY 600
IEGGTASGFY TVEDTHYVTR MYRVYGKKNI KLEPVPLKGT SLDPRFVFLL 650
DRGLDIYVWR GAQATLSSTT KARLFAEKIN KNERKGKAEI TLLVQGQELP 700
EFWEALGGEP SEIKKHVPED FWPPQPKLYK VGLGLGYLEL PQINYKLSVE 750
HKQRPKVELM PRMRLLQSLL DTRCVYILDC WSDVFIWLGR KSPRLVRAAA 800
LKLGQELCGM LHRPRHATVS RSLEGTEAQV FKAKFKNWDD VLTVDYTRNA 850
EAVLQSPGLS GKVKRDAEKK DQMKADLTAL FLPRQPPMSL AEAEQLMEEW 900
NEDLDGMEGF VLEGKKFARL PEEEFGHFYT QDCYVFLCRY WVPVEYEEEE 950
KKEDKEEKAE GKEGEEATAE AEEKQPEEDF QCIVYFWQGR EASNMGWLTF 1000
TFSLQKKFES LFPGKLEVVR MTQQQENPKF LSHFKRKFII HRGKRKAVQG 1050
AQQPSLYQIR TNGSALCTRC IQINTDSSLL NSEFCFILKV PFESEDNQGI 1100
VYAWVGRASD PDEAKLAEDI LNTMFDTSYS KQVINEGEEP ENFFWVGIGA 1150
QKPYDDDAEY MKHTRLFRCS NEKGYFAVTE KCSDFCQDDL ADDDIMLLDN 1200
GQEVYMWVGT QTSQVEIKLS LKACQVYIQH MRSKEHERPR RLRLVRKGNE 1250
QHAFTRCFHA WSAFCKALA 1269
Length:1,269
Mass (Da):144,751
Last modified:January 1, 1998 - v2
Checksum:i29AC7C07738B7B47
GO
Isoform 2 (identifier: Q13045-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     138-191: Missing.
     416-416: Missing.

Note: No experimental confirmation available.

Show »
Length:1,214
Mass (Da):138,493
Checksum:iC0ACCF1BB28C366C
GO
Isoform 3 (identifier: Q13045-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MEATGVLPFVRGVDLSGNDFK → MDLRGLRPVP

Show »
Length:1,258
Mass (Da):143,652
Checksum:i8D087C091CFAD08B
GO

Sequence cautioni

The sequence BAG58522.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1243 – 12431R → H.
Corresponds to variant rs8821 [ dbSNP | Ensembl ].
VAR_029258

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2121MEATG…GNDFK → MDLRGLRPVP in isoform 3.
VSP_046887Add
BLAST
Alternative sequencei138 – 19154Missing in isoform 2.
VSP_044686Add
BLAST
Alternative sequencei416 – 4161Missing in isoform 2.
VSP_044687

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → V in BAG58522. 1 Publication
Sequence conflicti298 – 2981Y → N in BAG58522. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U80184 Genomic DNA. Translation: AAC02796.1.
AK295655 mRNA. Translation: BAG58522.1. Different initiation.
AC127537 Genomic DNA. No translation available.
BC025300 mRNA. Translation: AAH25300.1.
U01184 mRNA. Translation: AAC03568.1.
CCDSiCCDS11192.1. [Q13045-1]
CCDS58521.1. [Q13045-3]
CCDS58522.1. [Q13045-2]
PIRiA49674.
RefSeqiNP_001243193.1. NM_001256264.1. [Q13045-3]
NP_001243194.1. NM_001256265.1. [Q13045-2]
NP_002009.1. NM_002018.3. [Q13045-1]
UniGeneiHs.513984.

Genome annotation databases

EnsembliENST00000327031; ENSP00000324573; ENSG00000177731. [Q13045-1]
ENST00000545457; ENSP00000438536; ENSG00000177731. [Q13045-2]
ENST00000579294; ENSP00000463534; ENSG00000177731. [Q13045-3]
GeneIDi2314.
KEGGihsa:2314.
UCSCiuc002gsq.2. human. [Q13045-1]

Polymorphism databases

DMDMi18202493.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U80184 Genomic DNA. Translation: AAC02796.1 .
AK295655 mRNA. Translation: BAG58522.1 . Different initiation.
AC127537 Genomic DNA. No translation available.
BC025300 mRNA. Translation: AAH25300.1 .
U01184 mRNA. Translation: AAC03568.1 .
CCDSi CCDS11192.1. [Q13045-1 ]
CCDS58521.1. [Q13045-3 ]
CCDS58522.1. [Q13045-2 ]
PIRi A49674.
RefSeqi NP_001243193.1. NM_001256264.1. [Q13045-3 ]
NP_001243194.1. NM_001256265.1. [Q13045-2 ]
NP_002009.1. NM_002018.3. [Q13045-1 ]
UniGenei Hs.513984.

3D structure databases

ProteinModelPortali Q13045.
SMRi Q13045. Positions 2-415, 485-1264.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108603. 30 interactions.
IntActi Q13045. 7 interactions.
MINTi MINT-1399971.
STRINGi 9606.ENSP00000324573.

PTM databases

PhosphoSitei Q13045.

Polymorphism databases

DMDMi 18202493.

Proteomic databases

MaxQBi Q13045.
PaxDbi Q13045.
PeptideAtlasi Q13045.
PRIDEi Q13045.

Protocols and materials databases

DNASUi 2314.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000327031 ; ENSP00000324573 ; ENSG00000177731 . [Q13045-1 ]
ENST00000545457 ; ENSP00000438536 ; ENSG00000177731 . [Q13045-2 ]
ENST00000579294 ; ENSP00000463534 ; ENSG00000177731 . [Q13045-3 ]
GeneIDi 2314.
KEGGi hsa:2314.
UCSCi uc002gsq.2. human. [Q13045-1 ]

Organism-specific databases

CTDi 2314.
GeneCardsi GC17M018148.
HGNCi HGNC:3750. FLII.
HPAi CAB016132.
HPA007084.
HPA008903.
MIMi 600362. gene.
neXtProti NX_Q13045.
Orphaneti 819. Smith-Magenis syndrome.
PharmGKBi PA28171.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4886.
HOGENOMi HOG000016110.
HOVERGENi HBG051627.
InParanoidi Q13045.
OMAi MEEWNED.
PhylomeDBi Q13045.
TreeFami TF313468.

Miscellaneous databases

ChiTaRSi FLII. human.
GeneWikii FLII.
GenomeRNAii 2314.
NextBioi 35508702.
PROi Q13045.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13045.
Bgeei Q13045.
CleanExi HS_FLII.
Genevestigatori Q13045.

Family and domain databases

Gene3Di 3.40.20.10. 7 hits.
InterProi IPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR007122. Villin/Gelsolin.
[Graphical view ]
PANTHERi PTHR11977. PTHR11977. 1 hit.
Pfami PF00626. Gelsolin. 4 hits.
PF00560. LRR_1. 1 hit.
PF12799. LRR_4. 1 hit.
PF13504. LRR_7. 2 hits.
PF13855. LRR_8. 2 hits.
[Graphical view ]
PRINTSi PR00597. GELSOLIN.
SMARTi SM00262. GEL. 6 hits.
SM00369. LRR_TYP. 1 hit.
[Graphical view ]
PROSITEi PS51450. LRR. 11 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic structure, evolution, and expression of human FLII, a gelsolin and leucine-rich-repeat family member: overlap with LLGL."
    Campbell H.D., Fountain S., Young I.G., Claudianos C., Hoheisel J.D., Chen K.-S., Lupski J.R.
    Genomics 42:46-54(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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] (ISOFORM 2).
    Tissue: Hippocampus.
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [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] (ISOFORM 1).
    Tissue: Kidney.
  5. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-11, ACETYLATION AT MET-1.
    Tissue: Platelet.
  6. "The Drosophila melanogaster flightless-I gene involved in gastrulation and muscle degeneration encodes gelsolin-like and leucine-rich repeat domains and is conserved in Caenorhabditis elegans and humans."
    Campbell H.D., Schimansky T., Claudianos C., Ozsarac N., Kasprzak A.B., Cotsell J.N., Young I.G., de Couet H.G., Miklos G.L.G.
    Proc. Natl. Acad. Sci. U.S.A. 90:11386-11390(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-1269 (ISOFORM 1).
    Tissue: Hippocampus.
  7. "Identification of the binding partners for flightless I, a novel protein bridging the leucine-rich repeat and the gelsolin superfamilies."
    Liu Y.-T., Yin H.L.
    J. Biol. Chem. 273:7920-7927(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACTIN AND LRRFIP1, TISSUE SPECIFICITY.
  8. "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: INTERACTION WITH LRRFIP1.
  9. "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: INTERACTION WITH LRRFIP1 AND LRRFIP2.
    Tissue: Skeletal muscle.
  10. "Developmentally essential protein flightless I is a nuclear receptor coactivator with actin binding activity."
    Lee Y.-H., Campbell H.D., Stallcup M.R.
    Mol. Cell. Biol. 24:2103-2117(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CARM1; ESR1; THRB; NCOA2 AND ACTL6A, MUTAGENESIS OF GLU-586 AND GLY-603.
  11. "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-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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-406 AND SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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].
  16. "Identification of Flightless-I as a substrate of the cytokine-independent survival kinase CISK."
    Xu J., Liao L., Qin J., Xu J., Liu D., Songyang Z.
    J. Biol. Chem. 284:14377-14385(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-436 AND THR-818, INTERACTION WITH SGK3.
  17. "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: INTERACTION WITH LRRFIP1; LRRFIP2 AND MYD88.
  18. "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-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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-406; SER-436 AND SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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-436 AND SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFLII_HUMAN
AccessioniPrimary (citable) accession number: Q13045
Secondary accession number(s): B4DIL0, F5H407, J3QLG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 150 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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

External Data

Dasty 3

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