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Q13045

- FLII_HUMAN

UniProt

Q13045 - FLII_HUMAN

Protein

Protein flightless-1 homolog

Gene

FLII

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (01 Jan 1998)
      Previous versions | rss
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    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.By similarity1 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

    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.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

    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 homologPRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 427427Interaction with LRRFIP1 and LRRFIP2Add
    BLAST
    Regioni495 – 827333Interaction with ACTL6AAdd
    BLAST

    Compositional bias

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

    Sequence similaritiesi

    Contains 5 gelsolin-like repeats.Curated
    Contains 15 LRR (leucine-rich) repeats.Curated

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 11M → V in BAG58522. (PubMed:14702039)Curated
    Sequence conflicti298 – 2981Y → N in BAG58522. (PubMed:14702039)Curated

    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. CuratedVSP_046887Add
    BLAST
    Alternative sequencei138 – 19154Missing in isoform 2. 1 PublicationVSP_044686Add
    BLAST
    Alternative sequencei416 – 4161Missing in isoform 2. 1 PublicationVSP_044687

    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

    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: October 1, 2014
    This is version 151 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