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O95466

- FMNL_HUMAN

UniProt

O95466 - FMNL_HUMAN

Protein

Formin-like protein 1

Gene

FMNL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    May play a role in the control of cell motility and survival of macrophages By similarity. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape.By similarity1 Publication

    GO - Molecular functioni

    1. actin filament binding Source: UniProtKB
    2. GTPase activating protein binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. Rac GTPase binding Source: UniProtKB

    GO - Biological processi

    1. actin filament severing Source: UniProtKB
    2. cortical actin cytoskeleton organization Source: UniProtKB
    3. regulation of cell shape Source: UniProtKB
    4. substrate-dependent cell migration Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Formin-like protein 1
    Alternative name(s):
    CLL-associated antigen KW-13
    Leukocyte formin
    Gene namesi
    Name:FMNL1
    Synonyms:C17orf1, C17orf1B, FMNL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:1212. FMNL1.

    Subcellular locationi

    Cytoplasm By similarity. Cell membrane 1 Publication; Lipid-anchor 1 Publication. Cytoplasmic vesiclephagosome By similarity
    Note: Recruited to actin-rich phagosomes during phagocytosis. Translocates to the plasma membrane upon activation by RAC1 By similarity.By similarity
    Isoform 3 : Cytoplasmcell cortex. Cell projectionbleb
    Note: Colocalized with F-actin in bleb protrusions.

    GO - Cellular componenti

    1. bleb Source: UniProtKB-SubCell
    2. cell cortex Source: UniProtKB-SubCell
    3. cytosol Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. membrane Source: UniProtKB
    6. phagocytic vesicle Source: UniProtKB
    7. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28186.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 11001099Formin-like protein 1PRO_0000194890Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication
    Modified residuei7 – 71Phosphoserine1 Publication
    Modified residuei184 – 1841Phosphoserine3 Publications
    Modified residuei624 – 6241Phosphoserine4 Publications

    Post-translational modificationi

    Myristoylation mediates membrane localization and blebbing.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein

    Proteomic databases

    MaxQBiO95466.
    PaxDbiO95466.
    PRIDEiO95466.

    PTM databases

    PhosphoSiteiO95466.

    Expressioni

    Tissue specificityi

    Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

    Gene expression databases

    ArrayExpressiO95466.
    BgeeiO95466.
    CleanExiHS_FMNL1.
    GenevestigatoriO95466.

    Organism-specific databases

    HPAiHPA008129.
    HPA028288.

    Interactioni

    Subunit structurei

    Interacts with RAC1, PFN1 and PFN2 By similarity. Interacts (activated by RAC1) with SRGAP2 (via SH3 domain); regulates the actin filament severing activity of FMNL1.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SRGAP2O750443EBI-720020,EBI-1051034

    Protein-protein interaction databases

    BioGridi107208. 63 interactions.
    IntActiO95466. 5 interactions.
    MINTiMINT-1188250.
    STRINGi9606.ENSP00000329219.

    Structurei

    3D structure databases

    ProteinModelPortaliO95466.
    SMRiO95466. Positions 219-421, 633-1074.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 468442GBD/FH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini632 – 1023392FH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1059 – 109032DADPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi459 – 616158Pro-richAdd
    BLAST

    Domaini

    The DAD domain regulates activation via by an autoinhibitory interaction with the N-terminus. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments By similarity.By similarity

    Sequence similaritiesi

    Belongs to the formin homology family.Curated
    Contains 1 DAD (diaphanous autoregulatory) domain.PROSITE-ProRule annotation
    Contains 1 FH2 (formin homology 2) domain.PROSITE-ProRule annotation
    Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG149898.
    HOVERGENiHBG053118.
    OMAiFSESTPM.
    OrthoDBiEOG7F7W8J.
    PhylomeDBiO95466.
    TreeFamiTF325155.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR014767. Diaphanous_autoregulatory.
    IPR015425. FH2_Formin.
    IPR010472. FH3_dom.
    IPR027657. FMNL1.
    IPR010473. GTPase-bd.
    IPR014768. GTPase-bd/formin_homology_3.
    [Graphical view]
    PANTHERiPTHR23213:SF188. PTHR23213:SF188. 1 hit.
    PfamiPF06367. Drf_FH3. 1 hit.
    PF06371. Drf_GBD. 2 hits.
    PF02181. FH2. 1 hit.
    [Graphical view]
    SMARTiSM00498. FH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 2 hits.
    PROSITEiPS51231. DAD. 1 hit.
    PS51444. FH2. 1 hit.
    PS51232. GBD_FH3. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95466-1) [UniParc]FASTAAdd to Basket

    Also known as: FMNL1alpha

    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

    MGNAAGSAEQ PAGPAAPPPK QPAPPKQPMP AAGELEERFN RALNCMNLPP     50
    DKVQLLSQYD NEKKWELICD QERFQVKNPP AAYIQKLKSY VDTGGVSRKV 100
    AADWMSNLGF KRRVQESTQV LRELETSLRT NHIGWVQEFL NEENRGLDVL 150
    LEYLAFAQCS VTYDMESTDN GASNSEKNKP LEQSVEDLSK GPPSSVPKSR 200
    HLTIKLTPAH SRKALRNSRI VSQKDDVHVC IMCLRAIMNY QSGFSLVMNH 250
    PACVNEIALS LNNKNPRTKA LVLELLAAVC LVRGGHDIIL AAFDNFKEVC 300
    GEQHRFEKLM EYFRNEDSNI DFMVACMQFI NIVVHSVENM NFRVFLQYEF 350
    THLGLDLYLE RLRLTESDKL QVQIQAYLDN IFDVGALLED TETKNAVLEH 400
    MEELQEQVAL LTERLRDAEN ESMAKIAELE KQLSQARKEL ETLRERFSES 450
    TAMGPSRRPP EPEKAPPAAP TRPSALELKV EELEEKGLIR ILRGPGDAVS 500
    IEILPVAVAT PSGGDAPTPG VPTGSPSPDL APAAEPAPGA APPPPPPLPG 550
    LPSPQEAPPS APPQAPPLPG SPEPPPAPPL PGDLPPPPPP PPPPPGTDGP 600
    VPPPPPPPPP PPGGPPDALG RRDSELGPGV KAKKPIQTKF RMPLLNWVAL 650
    KPSQITGTVF TELNDEKVLQ ELDMSDFEEQ FKTKSQGPSL DLSALKSKAA 700
    QKAPSKATLI EANRAKNLAI TLRKGNLGAE RICQAIEAYD LQALGLDFLE 750
    LLMRFLPTEY ERSLITRFER EQRPMEELSE EDRFMLCFSR IPRLPERMTT 800
    LTFLGNFPDT AQLLMPQLNA IIAASMSIKS SDKLRQILEI VLAFGNYMNS 850
    SKRGAAYGFR LQSLDALLEM KSTDRKQTLL HYLVKVIAEK YPQLTGFHSD 900
    LHFLDKAGSV SLDSVLADVR SLQRGLELTQ REFVRQDDCM VLKEFLRANS 950
    PTMDKLLADS KTAQEAFESV VEYFGENPKT TSPGLFFSLF SRFIKAYKKA 1000
    EQEVEQWKKE AAAQEAGADT PGKGEPPAPK SPPKARRPQM DLISELKRRQ 1050
    QKEPLIYESD RDGAIEDIIT VIKTVPFTAR TGKRTSRLLC EASLGEEMPL 1100
    Length:1,100
    Mass (Da):121,854
    Last modified:June 16, 2009 - v3
    Checksum:i91F9CE2B3B526FFC
    GO
    Isoform 2 (identifier: O95466-2) [UniParc]FASTAAdd to Basket

    Also known as: FMNL1beta

    The sequence of this isoform differs from the canonical sequence as follows:
         1071-1100: VIKTVPFTARTGKRTSRLLCEASLGEEMPL → DLRNQPYIRADTGRRSARRRPPGPPLQVTSDLSL

    Show »
    Length:1,104
    Mass (Da):122,409
    Checksum:i74CFC7C3D5ABCC23
    GO
    Isoform 3 (identifier: O95466-3) [UniParc]FASTAAdd to Basket

    Also known as: FMNL1gamma

    The sequence of this isoform differs from the canonical sequence as follows:
         1070-1070: T → TGKGLARPWSYPQSVLLCFLLTQCAILWGTGCHTASCYLFCFSFLFPFSTPLHLPHPHS

    Note: Due to intron retention. Constitutively activated form, probably due to alterations in the DAD domain.

    Show »
    Length:1,158
    Mass (Da):128,335
    Checksum:i43D0BA60ABEA6AD5
    GO

    Sequence cautioni

    The sequence AAH21906.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA07870.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti455 – 4551P → A in AAP32476. 1 PublicationCurated
    Sequence conflicti455 – 4551P → A in AAL99920. 1 PublicationCurated
    Sequence conflicti455 – 4551P → A in AAH73988. (PubMed:15489334)Curated
    Sequence conflicti602 – 6021Missing in AAH21906. (PubMed:15489334)Curated
    Sequence conflicti629 – 6291G → R in CAA07870. (PubMed:9799091)Curated
    Isoform 2 (identifier: O95466-2)
    Sequence conflicti1101 – 11022DL → EV in AAH21906. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1070 – 10701T → TGKGLARPWSYPQSVLLCFL LTQCAILWGTGCHTASCYLF CFSFLFPFSTPLHLPHPHS in isoform 3. 1 PublicationVSP_043845
    Alternative sequencei1071 – 110030VIKTV…EEMPL → DLRNQPYIRADTGRRSARRR PPGPPLQVTSDLSL in isoform 2. 3 PublicationsVSP_013977Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY278319 mRNA. Translation: AAP32476.1.
    AC008105 mRNA. No translation available.
    AF432213 mRNA. Translation: AAL99920.1.
    BC001710 mRNA. Translation: AAH01710.2.
    BC009000 mRNA. Translation: AAH09000.2.
    BC021906 mRNA. Translation: AAH21906.1. Different initiation.
    BC073988 mRNA. Translation: AAH73988.1.
    AJ008112 mRNA. Translation: CAA07870.1. Different initiation.
    CR456759 mRNA. Translation: CAG33040.1.
    FJ534522 mRNA. Translation: ACR19333.1.
    CCDSiCCDS11497.1. [O95466-1]
    RefSeqiNP_005883.2. NM_005892.3.
    XP_006722126.1. XM_006722063.1. [O95466-3]
    XP_006722131.1. XM_006722068.1. [O95466-1]
    XP_006722133.1. XM_006722070.1. [O95466-2]
    UniGeneiHs.100217.

    Genome annotation databases

    EnsembliENST00000328118; ENSP00000327442; ENSG00000184922. [O95466-2]
    ENST00000331495; ENSP00000329219; ENSG00000184922. [O95466-1]
    GeneIDi752.
    KEGGihsa:752.
    UCSCiuc002iin.3. human. [O95466-1]
    uc002iiq.3. human. [O95466-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY278319 mRNA. Translation: AAP32476.1 .
    AC008105 mRNA. No translation available.
    AF432213 mRNA. Translation: AAL99920.1 .
    BC001710 mRNA. Translation: AAH01710.2 .
    BC009000 mRNA. Translation: AAH09000.2 .
    BC021906 mRNA. Translation: AAH21906.1 . Different initiation.
    BC073988 mRNA. Translation: AAH73988.1 .
    AJ008112 mRNA. Translation: CAA07870.1 . Different initiation.
    CR456759 mRNA. Translation: CAG33040.1 .
    FJ534522 mRNA. Translation: ACR19333.1 .
    CCDSi CCDS11497.1. [O95466-1 ]
    RefSeqi NP_005883.2. NM_005892.3.
    XP_006722126.1. XM_006722063.1. [O95466-3 ]
    XP_006722131.1. XM_006722068.1. [O95466-1 ]
    XP_006722133.1. XM_006722070.1. [O95466-2 ]
    UniGenei Hs.100217.

    3D structure databases

    ProteinModelPortali O95466.
    SMRi O95466. Positions 219-421, 633-1074.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107208. 63 interactions.
    IntActi O95466. 5 interactions.
    MINTi MINT-1188250.
    STRINGi 9606.ENSP00000329219.

    PTM databases

    PhosphoSitei O95466.

    Proteomic databases

    MaxQBi O95466.
    PaxDbi O95466.
    PRIDEi O95466.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000328118 ; ENSP00000327442 ; ENSG00000184922 . [O95466-2 ]
    ENST00000331495 ; ENSP00000329219 ; ENSG00000184922 . [O95466-1 ]
    GeneIDi 752.
    KEGGi hsa:752.
    UCSCi uc002iin.3. human. [O95466-1 ]
    uc002iiq.3. human. [O95466-2 ]

    Organism-specific databases

    CTDi 752.
    GeneCardsi GC17P043299.
    HGNCi HGNC:1212. FMNL1.
    HPAi HPA008129.
    HPA028288.
    MIMi 604656. gene.
    neXtProti NX_O95466.
    PharmGKBi PA28186.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG149898.
    HOVERGENi HBG053118.
    OMAi FSESTPM.
    OrthoDBi EOG7F7W8J.
    PhylomeDBi O95466.
    TreeFami TF325155.

    Miscellaneous databases

    GeneWikii FMNL1.
    GenomeRNAii 752.
    NextBioi 3034.
    PROi O95466.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95466.
    Bgeei O95466.
    CleanExi HS_FMNL1.
    Genevestigatori O95466.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR014767. Diaphanous_autoregulatory.
    IPR015425. FH2_Formin.
    IPR010472. FH3_dom.
    IPR027657. FMNL1.
    IPR010473. GTPase-bd.
    IPR014768. GTPase-bd/formin_homology_3.
    [Graphical view ]
    PANTHERi PTHR23213:SF188. PTHR23213:SF188. 1 hit.
    Pfami PF06367. Drf_FH3. 1 hit.
    PF06371. Drf_GBD. 2 hits.
    PF02181. FH2. 1 hit.
    [Graphical view ]
    SMARTi SM00498. FH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 2 hits.
    PROSITEi PS51231. DAD. 1 hit.
    PS51444. FH2. 1 hit.
    PS51232. GBD_FH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human leukocyte formin: a new protein preferentially expressed in lymphocytes."
      Favaro P.M.B., Medina S.S., Basseres D.S., Costa F.F., Saad S.T.O.
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    2. "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].
    3. "Identification of novel tumor antigens in CLL by SEREX: assessment of their potential as targets for immunotherapeutic approaches."
      Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M., Barrett P., Gribben J.G.
      Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 110-1100 (ISOFORM 1).
    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] OF 419-1100 (ISOFORMS 1 AND 2).
      Tissue: Brain and Lymph.
    5. "The NIK protein kinase and C17orf1 genes: chromosomal mapping, gene structures and mutational screening in frontotemporal dementia and parkinsonism linked to chromosome 17."
      Aronsson F.C., Magnusson P., Andersson B., Karsten S.L., Shibasaki Y., Lendon C.L., Goate A.M., Brookes A.J.
      Hum. Genet. 103:340-345(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 629-1100 (ISOFORM 2).
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 642-1100 (ISOFORM 2).
    7. "Formin-like 1 (FMNL1) is regulated by N-terminal myristoylation and induces polarized membrane blebbing."
      Han Y., Eppinger E., Schuster I.G., Weigand L.U., Liang X., Kremmer E., Peschel C., Krackhardt A.M.
      J. Biol. Chem. 284:33409-33417(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 668-1100 (ISOFORM 3), MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
    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-624, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-624, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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-7; SER-184 AND SER-624, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "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-184 AND SER-624, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
      Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
      BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: INTERACTION WITH SRGAP2.

    Entry informationi

    Entry nameiFMNL_HUMAN
    AccessioniPrimary (citable) accession number: O95466
    Secondary accession number(s): D2DGW2
    , Q6DKG5, Q6IBP3, Q86UH1, Q8N671, Q8TDH1, Q96H10
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2002
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 127 of the entry and version 3 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, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3