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Q96PY5

- FMNL2_HUMAN

UniProt

Q96PY5 - FMNL2_HUMAN

Protein

Formin-like protein 2

Gene

FMNL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 3 (26 May 2009)
      Previous versions | rss
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    Functioni

    Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics.1 Publication

    GO - Biological processi

    1. cortical actin cytoskeleton organization Source: UniProtKB
    2. cytoskeleton organization Source: UniProtKB
    3. regulation of cell morphogenesis Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Formin-like protein 2
    Alternative name(s):
    Formin homology 2 domain-containing protein 2
    Gene namesi
    Name:FMNL2
    Synonyms:FHOD2, KIAA1902
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:18267. FMNL2.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28144.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 10861085Formin-like protein 2PRO_0000289093Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate

    Proteomic databases

    MaxQBiQ96PY5.
    PaxDbiQ96PY5.
    PRIDEiQ96PY5.

    PTM databases

    PhosphoSiteiQ96PY5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ96PY5.
    BgeeiQ96PY5.
    CleanExiHS_FMNL2.
    GenevestigatoriQ96PY5.

    Organism-specific databases

    HPAiHPA005464.

    Interactioni

    Protein-protein interaction databases

    BioGridi125355. 6 interactions.
    IntActiQ96PY5. 2 interactions.
    MINTiMINT-1199986.
    STRINGi9606.ENSP00000288670.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96PY5.
    SMRiQ96PY5. Positions 222-368, 617-1021.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 469447GBD/FH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini616 – 1007392FH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1040 – 107940DADPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi525 – 60379Pro-richAdd
    BLAST

    Domaini

    The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. 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

    eggNOGiNOG270361.
    HOGENOMiHOG000231209.
    HOVERGENiHBG053118.
    InParanoidiQ96PY5.
    OMAiTENEAMA.
    OrthoDBiEOG7F7W8J.
    PhylomeDBiQ96PY5.
    TreeFamiTF325155.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR014767. Diaphanous_autoregulatory.
    IPR015425. FH2_Formin.
    IPR010472. FH3_dom.
    IPR027656. FMNL2.
    IPR010473. GTPase-bd.
    IPR014768. GTPase-bd/formin_homology_3.
    IPR017987. Wilms_tumour.
    [Graphical view]
    PANTHERiPTHR23213:SF180. PTHR23213:SF180. 1 hit.
    PfamiPF06367. Drf_FH3. 1 hit.
    PF06371. Drf_GBD. 2 hits.
    PF02181. FH2. 1 hit.
    [Graphical view]
    PRINTSiPR00049. WILMSTUMOUR.
    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 (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96PY5-1) [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

    MGNAGSMDSQ QTDFRAHNVP LKLPMPEPGE LEERFAIVLN AMNLPPDKAR     50
    LLRQYDNEKK WELICDQERF QVKNPPHTYI QKLKGYLDPA VTRKKFRRRV 100
    QESTQVLREL EISLRTNHIG WVREFLNEEN KGLDVLVEYL SFAQYAVTFD 150
    FESVESTVES SVDKSKPWSR SIEDLHRGSN LPSPVGNSVS RSGRHSALRY 200
    NTLPSRRTLK NSRLVSKKDD VHVCIMCLRA IMNYQYGFNM VMSHPHAVNE 250
    IALSLNNKNP RTKALVLELL AAVCLVRGGH EIILSAFDNF KEVCGEKQRF 300
    EKLMEHFRNE DNNIDFMVAS MQFINIVVHS VEDMNFRVHL QYEFTKLGLD 350
    EYLDKLKHTE SDKLQVQIQA YLDNVFDVGA LLEDAETKNA ALERVEELEE 400
    NISHLSEKLQ DTENEAMSKI VELEKQLMQR NKELDVVREI YKDANTQVHT 450
    LRKMVKEKEE AIQRQSTLEK KIHELEKQGT IKIQKKGDGD IAILPVVASG 500
    TLSMGSEVVA GNSVGPTMGA ASSGPLPPPP PPLPPSSDTP ETVQNGPVTP 550
    PMPPPPPPPP PPPPPPPPPP PPPLPGPAAE TVPAPPLAPP LPSAPPLPGT 600
    SSPTVVFNSG LAAVKIKKPI KTKFRMPVFN WVALKPNQIN GTVFNEIDDE 650
    RILEDLNVDE FEEIFKTKAQ GPAIDLSSSK QKIPQKGSNK VTLLEANRAK 700
    NLAITLRKAG KTADEICKAI HVFDLKTLPV DFVECLMRFL PTENEVKVLR 750
    LYERERKPLE NLSDEDRFMM QFSKIERLMQ KMTIMAFIGN FAESIQMLTP 800
    QLHAIIAASV SIKSSQKLKK ILEIILALGN YMNSSKRGAV YGFKLQSLDL 850
    LLDTKSTDRK QTLLHYISNV VKEKYHQVSL FYNELHYVEK AAAVSLENVL 900
    LDVKELQRGM DLTKREYTMH DHNTLLKEFI LNNEGKLKKL QDDAKIAQDA 950
    FDDVVKYFGE NPKTTPPSVF FPVFVRFVKA YKQAEEENEL RKKQEQALME 1000
    KLLEQEALME QQDPKSPSHK SKRQQQELIA ELRRRQVKDN RHVYEGKDGA 1050
    IEDIITVLKT VPFTARTAKR GSRFFCEPVL TEEYHY 1086

    Note: No experimental confirmation available.

    Length:1,086
    Mass (Da):123,321
    Last modified:May 26, 2009 - v3
    Checksum:i951ED0A26232F640
    GO
    Isoform 2 (identifier: Q96PY5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1057-1086: VLKTVPFTARTAKRGSRFFCEPVLTEEYHY → DLRNQPYRRADAVRRSVRRRFDDQNLRSVNGAEITM

    Show »
    Length:1,092
    Mass (Da):124,107
    Checksum:iA20AA3D76733A717
    GO

    Sequence cautioni

    The sequence AAI13879.1 differs from that shown. Reason: Aberrant splicing.
    The sequence AAI14439.1 differs from that shown. Reason: Aberrant splicing.
    The sequence BAB67795.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAX88959.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti570 – 5701P → PP in BAB67795. (PubMed:11572484)Curated
    Sequence conflicti570 – 5701P → PP in AAI67159. (PubMed:15489334)Curated
    Sequence conflicti570 – 5701P → PP in CAD39058. (PubMed:17974005)Curated
    Sequence conflicti579 – 5791A → S in BAB67795. (PubMed:11572484)Curated
    Sequence conflicti579 – 5791A → S in AAI67159. (PubMed:15489334)Curated
    Sequence conflicti964 – 9641T → R in CAD39058. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti352 – 3521Y → C.
    Corresponds to variant rs34119671 [ dbSNP | Ensembl ].
    VAR_032570
    Natural varianti504 – 5041M → T.
    Corresponds to variant rs11897929 [ dbSNP | Ensembl ].
    VAR_032571

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1057 – 108630VLKTV…EEYHY → DLRNQPYRRADAVRRSVRRR FDDQNLRSVNGAEITM in isoform 2. 3 PublicationsVSP_025887Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB067489 mRNA. Translation: BAB67795.1. Different initiation.
    AC012066 Genomic DNA. No translation available.
    AC012443 Genomic DNA. Translation: AAX88959.1. Sequence problems.
    AC093794 Genomic DNA. No translation available.
    BC113878 mRNA. Translation: AAI13879.1. Sequence problems.
    BC114438 mRNA. Translation: AAI14439.1. Sequence problems.
    BC167159 mRNA. Translation: AAI67159.1.
    AL834396 mRNA. Translation: CAD39058.1.
    CCDSiCCDS46429.1. [Q96PY5-3]
    RefSeqiNP_443137.2. NM_052905.3. [Q96PY5-3]
    XP_006712291.1. XM_006712228.1. [Q96PY5-1]
    UniGeneiHs.654630.

    Genome annotation databases

    EnsembliENST00000288670; ENSP00000288670; ENSG00000157827. [Q96PY5-3]
    GeneIDi114793.
    KEGGihsa:114793.
    UCSCiuc002tye.3. human. [Q96PY5-3]

    Polymorphism databases

    DMDMi238054383.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB067489 mRNA. Translation: BAB67795.1 . Different initiation.
    AC012066 Genomic DNA. No translation available.
    AC012443 Genomic DNA. Translation: AAX88959.1 . Sequence problems.
    AC093794 Genomic DNA. No translation available.
    BC113878 mRNA. Translation: AAI13879.1 . Sequence problems.
    BC114438 mRNA. Translation: AAI14439.1 . Sequence problems.
    BC167159 mRNA. Translation: AAI67159.1 .
    AL834396 mRNA. Translation: CAD39058.1 .
    CCDSi CCDS46429.1. [Q96PY5-3 ]
    RefSeqi NP_443137.2. NM_052905.3. [Q96PY5-3 ]
    XP_006712291.1. XM_006712228.1. [Q96PY5-1 ]
    UniGenei Hs.654630.

    3D structure databases

    ProteinModelPortali Q96PY5.
    SMRi Q96PY5. Positions 222-368, 617-1021.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125355. 6 interactions.
    IntActi Q96PY5. 2 interactions.
    MINTi MINT-1199986.
    STRINGi 9606.ENSP00000288670.

    PTM databases

    PhosphoSitei Q96PY5.

    Polymorphism databases

    DMDMi 238054383.

    Proteomic databases

    MaxQBi Q96PY5.
    PaxDbi Q96PY5.
    PRIDEi Q96PY5.

    Protocols and materials databases

    DNASUi 114793.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000288670 ; ENSP00000288670 ; ENSG00000157827 . [Q96PY5-3 ]
    GeneIDi 114793.
    KEGGi hsa:114793.
    UCSCi uc002tye.3. human. [Q96PY5-3 ]

    Organism-specific databases

    CTDi 114793.
    GeneCardsi GC02P153191.
    HGNCi HGNC:18267. FMNL2.
    HPAi HPA005464.
    neXtProti NX_Q96PY5.
    PharmGKBi PA28144.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG270361.
    HOGENOMi HOG000231209.
    HOVERGENi HBG053118.
    InParanoidi Q96PY5.
    OMAi TENEAMA.
    OrthoDBi EOG7F7W8J.
    PhylomeDBi Q96PY5.
    TreeFami TF325155.

    Miscellaneous databases

    ChiTaRSi FMNL2. human.
    GeneWikii FMNL2.
    GenomeRNAii 114793.
    NextBioi 79219.
    PROi Q96PY5.

    Gene expression databases

    ArrayExpressi Q96PY5.
    Bgeei Q96PY5.
    CleanExi HS_FMNL2.
    Genevestigatori Q96PY5.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR014767. Diaphanous_autoregulatory.
    IPR015425. FH2_Formin.
    IPR010472. FH3_dom.
    IPR027656. FMNL2.
    IPR010473. GTPase-bd.
    IPR014768. GTPase-bd/formin_homology_3.
    IPR017987. Wilms_tumour.
    [Graphical view ]
    PANTHERi PTHR23213:SF180. PTHR23213:SF180. 1 hit.
    Pfami PF06367. Drf_FH3. 1 hit.
    PF06371. Drf_GBD. 2 hits.
    PF02181. FH2. 1 hit.
    [Graphical view ]
    PRINTSi PR00049. WILMSTUMOUR.
    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. "Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins."
      Nagase T., Kikuno R., Ohara O.
      DNA Res. 8:179-187(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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).
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-1086 (ISOFORM 2).
      Tissue: Amygdala.
    5. "Identification and characterization of human FMNL1, FMNL2 and FMNL3 genes in silico."
      Katoh M., Katoh M.
      Int. J. Oncol. 22:1161-1168(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION (ISOFORMS 1 AND 2).
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system."
      Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T.
      Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION AT GLY-2.
    8. "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.
    9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiFMNL2_HUMAN
    AccessioniPrimary (citable) accession number: Q96PY5
    Secondary accession number(s): B2RZH5
    , Q14CC9, Q4ZG52, Q8N3E0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: May 26, 2009
    Last modified: October 1, 2014
    This is version 97 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 2
      Human chromosome 2: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3