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Q7L576

- CYFP1_HUMAN

UniProt

Q7L576 - CYFP1_HUMAN

Protein

Cytoplasmic FMR1-interacting protein 1

Gene

CYFIP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit is an adapter between EIF4E and FMR1. Promotes the translation repression activity of FMR1 in brain probably by mediating its association with EIF4E and mRNA By similarity. Regulates formation of membrane ruffles and lamellipodia. Plays a role in axon outgrowth. Binds to F-actin but not to RNA. Part of the WAVE complex that regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1. Regulator of epithelial morphogenesis. May act as an invasion suppressor in cancers.By similarity4 Publications

    GO - Molecular functioni

    1. actin filament binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein complex binding Source: UniProt
    4. Rac GTPase binding Source: UniProtKB

    GO - Biological processi

    1. axon extension Source: UniProtKB
    2. cognition Source: UniProt
    3. lamellipodium assembly Source: UniProtKB
    4. positive regulation of Arp2/3 complex-mediated actin nucleation Source: UniProt
    5. Rac protein signal transduction Source: UniProt
    6. regulation of cell shape Source: UniProtKB-KW
    7. ruffle organization Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Cell shape, Differentiation, Neurogenesis

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytoplasmic FMR1-interacting protein 1
    Alternative name(s):
    Specifically Rac1-associated protein 1
    Short name:
    Sra-1
    p140sra-1
    Gene namesi
    Name:CYFIP1Imported
    Synonyms:KIAA0068Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:13759. CYFIP1.

    Subcellular locationi

    Cytoplasmperinuclear region By similarity. Cell projectionlamellipodium By similarity. Cell projectionruffle By similarity. Cell junctionsynapsesynaptosome By similarity
    Note: Highly expressed in the perinuclear region. Enriched in synaptosomes, membrane ruffles and at the tips of lamellipodia By similarity.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. extracellular vesicular exosome Source: UniProt
    3. lamellipodium Source: UniProtKB
    4. mRNA cap binding complex Source: UniProtKB
    5. neuron projection Source: UniProtKB
    6. perinuclear region of cytoplasm Source: UniProtKB
    7. ruffle Source: UniProtKB
    8. SCAR complex Source: UniProt
    9. synapse Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm, Synapse, Synaptosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi179 – 1791C → R: Reduced interaction with RAC1. 1 Publication
    Mutagenesisi190 – 1901R → D: Reduced interaction with RAC1. 1 Publication
    Mutagenesisi434 – 4341E → K: Reduced interaction with RAC1; when associated with A-626. 1 Publication
    Mutagenesisi626 – 6261F → A: Reduced interaction with RAC1; when associated with K-434. 1 Publication
    Mutagenesisi632 – 6321M → D: Reduced interaction with RAC1. 1 Publication
    Mutagenesisi697 – 6971L → D: Constitutive induction of the formation of actin filaments; when associated with D-704. 1 Publication
    Mutagenesisi704 – 7041Y → D: Constitutive induction of the formation of actin filaments; when associated with D-697. 1 Publication
    Mutagenesisi841 – 8411L → A: Constitutive induction of the formation of actin filaments; when associated with 844-A-A-845. 1 Publication
    Mutagenesisi844 – 8452FW → AA: Constitutive induction of the formation of actin filaments; when associated with A-841.

    Organism-specific databases

    Orphaneti72. Angelman syndrome.
    PharmGKBiPA38367.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12531253Cytoplasmic FMR1-interacting protein 1PRO_0000279706Add
    BLAST

    Proteomic databases

    MaxQBiQ7L576.
    PaxDbiQ7L576.
    PRIDEiQ7L576.

    PTM databases

    PhosphoSiteiQ7L576.

    Expressioni

    Gene expression databases

    ArrayExpressiQ7L576.
    BgeeiQ7L576.
    CleanExiHS_CYFIP1.
    GenevestigatoriQ7L576.

    Interactioni

    Subunit structurei

    Component of the WAVE1 complex composed of ABI2, CYFIP1 or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterdimer containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by WAVE1, ABI2 and BRK1. Component of the CYFIP1-EIF4E-FMR1 complex which is composed of CYFIP, EIF4E and FMR1. Interacts with FMR1 but does not bind to related proteins FXR1 or FXR2. Interaction with EIF4E stimulates FMR1 binding. Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1, NCKAP1/NAP1 and WASF2/WAVE2. Interacts with the active GTP-bound form of RAC1. Interacts through its C-terminus with the C-terminus of DPYSL2/CRMP2 which is necessary for DPYSL2-induced axon outgrowth. Interacts with NYAP1, NYAP2 and MYO16.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Eif4eP630732EBI-1048143,EBI-2000006From a different organism.
    FMR1Q067874EBI-1048143,EBI-366305
    NCKAP1Q9Y2A73EBI-1048143,EBI-389845

    Protein-protein interaction databases

    BioGridi116800. 26 interactions.
    DIPiDIP-38873N.
    IntActiQ7L576. 28 interactions.
    MINTiMINT-1731056.
    STRINGi9606.ENSP00000324549.

    Structurei

    Secondary structure

    1
    1253
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 1711
    Helixi59 – 8426
    Helixi90 – 923
    Helixi104 – 14340
    Helixi148 – 1503
    Helixi155 – 17723
    Helixi179 – 19315
    Turni194 – 1963
    Helixi201 – 21515
    Helixi219 – 22911
    Helixi234 – 25017
    Helixi257 – 27418
    Beta strandi275 – 2784
    Helixi281 – 2866
    Helixi292 – 30110
    Beta strandi304 – 3085
    Beta strandi311 – 3144
    Helixi316 – 3205
    Turni323 – 3253
    Helixi326 – 3316
    Helixi346 – 36520
    Helixi384 – 41734
    Turni422 – 4243
    Helixi434 – 4385
    Helixi440 – 4423
    Helixi445 – 46723
    Helixi469 – 48921
    Turni490 – 4923
    Helixi493 – 5019
    Helixi505 – 51814
    Beta strandi522 – 5254
    Helixi531 – 5344
    Helixi556 – 57015
    Turni580 – 5834
    Helixi586 – 59813
    Helixi599 – 6013
    Helixi602 – 6065
    Helixi608 – 6158
    Helixi619 – 6213
    Helixi625 – 6306
    Turni631 – 6333
    Helixi640 – 6423
    Helixi644 – 65512
    Helixi658 – 6603
    Turni661 – 6633
    Helixi664 – 6685
    Helixi670 – 68011
    Helixi685 – 72137
    Helixi725 – 7339
    Helixi747 – 7504
    Beta strandi755 – 7573
    Beta strandi760 – 7623
    Helixi764 – 78825
    Helixi792 – 7943
    Helixi795 – 81319
    Helixi821 – 8288
    Beta strandi832 – 8365
    Helixi838 – 84912
    Helixi851 – 8544
    Beta strandi855 – 8584
    Turni859 – 8624
    Beta strandi863 – 8664
    Helixi869 – 8713
    Helixi885 – 8873
    Helixi892 – 90110
    Helixi902 – 9065
    Helixi911 – 94232
    Helixi944 – 95512
    Helixi965 – 9673
    Helixi969 – 97911
    Helixi981 – 9844
    Turni987 – 9926
    Helixi993 – 102533
    Helixi1026 – 10294
    Helixi1043 – 105311
    Helixi1055 – 10573
    Helixi1059 – 10668
    Helixi1069 – 108315
    Helixi1086 – 10883
    Beta strandi1090 – 10923
    Helixi1093 – 11019
    Turni1107 – 11104
    Beta strandi1121 – 11233
    Helixi1127 – 113913
    Helixi1149 – 11535
    Helixi1156 – 116712
    Helixi1171 – 11777
    Helixi1179 – 119012
    Helixi1201 – 122525

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3P8CX-ray2.29A1-1253[»]
    4N78X-ray2.43A1-1253[»]
    ProteinModelPortaliQ7L576.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7L576.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the CYFIP family.Sequence Analysis

    Phylogenomic databases

    eggNOGiNOG306641.
    HOGENOMiHOG000272573.
    HOVERGENiHBG053209.
    InParanoidiQ7L576.
    KOiK05749.
    OMAiSSNIYKL.
    OrthoDBiEOG7ZSHS2.
    PhylomeDBiQ7L576.
    TreeFamiTF312925.

    Family and domain databases

    InterProiIPR008081. Cytoplasmic_FMR1-int.
    IPR016536. Cytoplasmic_FMR1-int_sub.
    [Graphical view]
    PANTHERiPTHR12195. PTHR12195. 1 hit.
    PfamiPF05994. FragX_IP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF008153. FMR1_interacting. 1 hit.
    PRINTSiPR01698. CYTOFMRPINTP.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7L576-1) [UniParc]FASTAAdd to Basket

    Also known as: 3

    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

    MAAQVTLEDA LSNVDLLEEL PLPDQQPCIE PPPSSLLYQP NFNTNFEDRN     50
    AFVTGIARYI EQATVHSSMN EMLEEGQEYA VMLYTWRSCS RAIPQVKCNE 100
    QPNRVEIYEK TVEVLEPEVT KLMNFMYFQR NAIERFCGEV RRLCHAERRK 150
    DFVSEAYLIT LGKFINMFAV LDELKNMKCS VKNDHSAYKR AAQFLRKMAD 200
    PQSIQESQNL SMFLANHNKI TQSLQQQLEV ISGYEELLAD IVNLCVDYYE 250
    NRMYLTPSEK HMLLKVMGFG LYLMDGSVSN IYKLDAKKRI NLSKIDKYFK 300
    QLQVVPLFGD MQIELARYIK TSAHYEENKS RWTCTSSGSS PQYNICEQMI 350
    QIREDHMRFI SELARYSNSE VVTGSGRQEA QKTDAEYRKL FDLALQGLQL 400
    LSQWSAHVME VYSWKLVHPT DKYSNKDCPD SAEEYERATR YNYTSEEKFA 450
    LVEVIAMIKG LQVLMGRMES VFNHAIRHTV YAALQDFSQV TLREPLRQAI 500
    KKKKNVIQSV LQAIRKTVCD WETGHEPFND PALRGEKDPK SGFDIKVPRR 550
    AVGPSSTQLY MVRTMLESLI ADKSGSKKTL RSSLEGPTIL DIEKFHRESF 600
    FYTHLINFSE TLQQCCDLSQ LWFREFFLEL TMGRRIQFPI EMSMPWILTD 650
    HILETKEASM MEYVLYSLDL YNDSAHYALT RFNKQFLYDE IEAEVNLCFD 700
    QFVYKLADQI FAYYKVMAGS LLLDKRLRSE CKNQGATIHL PPSNRYETLL 750
    KQRHVQLLGR SIDLNRLITQ RVSAAMYKSL ELAIGRFESE DLTSIVELDG 800
    LLEINRMTHK LLSRYLTLDG FDAMFREANH NVSAPYGRIT LHVFWELNYD 850
    FLPNYCYNGS TNRFVRTVLP FSQEFQRDKQ PNAQPQYLHG SKALNLAYSS 900
    IYGSYRNFVG PPHFQVICRL LGYQGIAVVM EELLKVVKSL LQGTILQYVK 950
    TLMEVMPKIC RLPRHEYGSP GILEFFHHQL KDIVEYAELK TVCFQNLREV 1000
    GNAILFCLLI EQSLSLEEVC DLLHAAPFQN ILPRVHVKEG ERLDAKMKRL 1050
    ESKYAPLHLV PLIERLGTPQ QIAIAREGDL LTKERLCCGL SMFEVILTRI 1100
    RSFLDDPIWR GPLPSNGVMH VDECVEFHRL WSAMQFVYCI PVGTHEFTVE 1150
    QCFGDGLHWA GCMIIVLLGQ QRRFAVLDFC YHLLKVQKHD GKDEIIKNVP 1200
    LKKMVERIRK FQILNDEIIT ILDKYLKSGD GEGTPVEHVR CFQPPIHQSL 1250
    ASS 1253
    Length:1,253
    Mass (Da):145,182
    Last modified:July 5, 2004 - v1
    Checksum:iD8F45E13207BEF16
    GO
    Isoform 2 (identifier: Q7L576-2) [UniParc]FASTAAdd to Basket

    Also known as: 4

    The sequence of this isoform differs from the canonical sequence as follows:
         1-431: Missing.
         432-557: AEEYERATRY...PRRAVGPSST → MAESLGSAEL...SPPQMFPWII

    Show »
    Length:822
    Mass (Da):94,467
    Checksum:i035E45763DC5F6C4
    GO
    Isoform 3 (identifier: Q7L576-3) [UniParc]FASTAAdd to Basket

    Also known as: 5

    The sequence of this isoform differs from the canonical sequence as follows:
         1-806: Missing.

    Show »
    Length:447
    Mass (Da):51,534
    Checksum:i1D9F2A088E5891A2
    GO

    Sequence cautioni

    The sequence BAA07552.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti583 – 5831S → N in AAW51478. 1 PublicationCurated
    Sequence conflicti583 – 5831S → N in BAC86825. (PubMed:14702039)Curated
    Sequence conflicti898 – 8981Y → H in AAW51478. 1 PublicationCurated
    Sequence conflicti898 – 8981Y → H in BAC86825. (PubMed:14702039)Curated
    Sequence conflicti930 – 9301M → R in AAW51478. 1 PublicationCurated
    Sequence conflicti930 – 9301M → R in BAC86825. (PubMed:14702039)Curated
    Sequence conflicti1176 – 11761V → A in AAW51479. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti532 – 5321A → P.
    Corresponds to variant rs34683919 [ dbSNP | Ensembl ].
    VAR_053849
    Natural varianti820 – 8201G → D.
    Corresponds to variant rs17137190 [ dbSNP | Ensembl ].
    VAR_053850
    Natural varianti820 – 8201G → S.2 Publications
    Corresponds to variant rs7170637 [ dbSNP | Ensembl ].
    VAR_053851

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 806806Missing in isoform 3. 1 PublicationVSP_052345Add
    BLAST
    Alternative sequencei1 – 431431Missing in isoform 2. 2 PublicationsVSP_052346Add
    BLAST
    Alternative sequencei432 – 557126AEEYE…GPSST → MAESLGSAELLRQLKSLGME RLLHAVNTFLRQSCTYLPLL TFGGKTSFVSLDVYGTEANC SATSCSFPKAAATWPRRQAP GPLGELVRGPPDQGVAEQSF SHGLFEFGITNVPCIFSPPQ MFPWII in isoform 2. 2 PublicationsVSP_052347Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY763577 mRNA. Translation: AAW51476.1.
    AY763578 mRNA. Translation: AAW51477.1.
    AY763579 mRNA. Translation: AAW51478.1.
    AY763580 mRNA. Translation: AAW51479.1.
    D38549 mRNA. Translation: BAA07552.1. Different initiation.
    AK127094 mRNA. Translation: BAC86825.1.
    AK291604 mRNA. Translation: BAF84293.1.
    CH471258 Genomic DNA. Translation: EAW65555.1.
    BC001306 mRNA. Translation: AAH01306.2.
    BC005097 mRNA. Translation: AAH05097.1.
    CCDSiCCDS10009.1. [Q7L576-1]
    CCDS45189.1. [Q7L576-2]
    RefSeqiNP_001028200.1. NM_001033028.1. [Q7L576-2]
    NP_001274739.1. NM_001287810.1. [Q7L576-1]
    NP_055423.1. NM_014608.3. [Q7L576-1]
    XP_005272600.1. XM_005272543.1. [Q7L576-1]
    UniGeneiHs.26704.

    Genome annotation databases

    GeneIDi23191.
    KEGGihsa:23191.
    UCSCiuc001yus.3. human. [Q7L576-1]
    uc001yuu.3. human. [Q7L576-2]
    uc001yuv.3. human. [Q7L576-3]

    Polymorphism databases

    DMDMi74738589.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY763577 mRNA. Translation: AAW51476.1 .
    AY763578 mRNA. Translation: AAW51477.1 .
    AY763579 mRNA. Translation: AAW51478.1 .
    AY763580 mRNA. Translation: AAW51479.1 .
    D38549 mRNA. Translation: BAA07552.1 . Different initiation.
    AK127094 mRNA. Translation: BAC86825.1 .
    AK291604 mRNA. Translation: BAF84293.1 .
    CH471258 Genomic DNA. Translation: EAW65555.1 .
    BC001306 mRNA. Translation: AAH01306.2 .
    BC005097 mRNA. Translation: AAH05097.1 .
    CCDSi CCDS10009.1. [Q7L576-1 ]
    CCDS45189.1. [Q7L576-2 ]
    RefSeqi NP_001028200.1. NM_001033028.1. [Q7L576-2 ]
    NP_001274739.1. NM_001287810.1. [Q7L576-1 ]
    NP_055423.1. NM_014608.3. [Q7L576-1 ]
    XP_005272600.1. XM_005272543.1. [Q7L576-1 ]
    UniGenei Hs.26704.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3P8C X-ray 2.29 A 1-1253 [» ]
    4N78 X-ray 2.43 A 1-1253 [» ]
    ProteinModelPortali Q7L576.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116800. 26 interactions.
    DIPi DIP-38873N.
    IntActi Q7L576. 28 interactions.
    MINTi MINT-1731056.
    STRINGi 9606.ENSP00000324549.

    PTM databases

    PhosphoSitei Q7L576.

    Polymorphism databases

    DMDMi 74738589.

    Proteomic databases

    MaxQBi Q7L576.
    PaxDbi Q7L576.
    PRIDEi Q7L576.

    Protocols and materials databases

    DNASUi 23191.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 23191.
    KEGGi hsa:23191.
    UCSCi uc001yus.3. human. [Q7L576-1 ]
    uc001yuu.3. human. [Q7L576-2 ]
    uc001yuv.3. human. [Q7L576-3 ]

    Organism-specific databases

    CTDi 23191.
    GeneCardsi GC15P023873.
    HGNCi HGNC:13759. CYFIP1.
    MIMi 606322. gene.
    neXtProti NX_Q7L576.
    Orphaneti 72. Angelman syndrome.
    PharmGKBi PA38367.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG306641.
    HOGENOMi HOG000272573.
    HOVERGENi HBG053209.
    InParanoidi Q7L576.
    KOi K05749.
    OMAi SSNIYKL.
    OrthoDBi EOG7ZSHS2.
    PhylomeDBi Q7L576.
    TreeFami TF312925.

    Miscellaneous databases

    ChiTaRSi CYFIP1. human.
    EvolutionaryTracei Q7L576.
    GeneWikii CYFIP1.
    GenomeRNAii 23191.
    NextBioi 44673.
    PROi Q7L576.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7L576.
    Bgeei Q7L576.
    CleanExi HS_CYFIP1.
    Genevestigatori Q7L576.

    Family and domain databases

    InterProi IPR008081. Cytoplasmic_FMR1-int.
    IPR016536. Cytoplasmic_FMR1-int_sub.
    [Graphical view ]
    PANTHERi PTHR12195. PTHR12195. 1 hit.
    Pfami PF05994. FragX_IP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF008153. FMR1_interacting. 1 hit.
    PRINTSi PR01698. CYTOFMRPINTP.
    ProtoNeti Search...

    Publicationsi

    1. Jiang Y.-H., Beaudet A.L.
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), VARIANT SER-820.
    2. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
      Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
      DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow1 Publication.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT SER-820.
      Tissue: BrainImported and Placenta.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: BrainImported and PlacentaImported.
    6. Bienvenut W.V., Claeys D., Boldt K., von Kriegsheim A.F., Kolch W.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 50-58; 111-130; 151-163; 366-377; 441-448; 505-515; 564-573; 754-760; 815-826; 867-877; 1054-1076; 1211-1224 AND 1228-1240, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma and Hepatoma.
    7. "p140Sra-1 (specifically Rac1-associated protein) is a novel specific target for Rac1 small GTPase."
      Kobayashi K., Kuroda S., Fukata M., Nakamura T., Nagase T., Nomura N., Matsuura Y., Yoshida-Kubomura N., Iwamatsu A., Kaibuchi K.
      J. Biol. Chem. 273:291-295(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "CRMP-2 is involved in kinesin-1-dependent transport of the Sra-1/WAVE1 complex and axon formation."
      Kawano Y., Yoshimura T., Tsuboi D., Kawabata S., Kaneko-Kawano T., Shirataki H., Takenawa T., Kaibuchi K.
      Mol. Cell. Biol. 25:9920-9935(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DPYSL2.
    9. Cited for: FUNCTION.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF WAVE1 COMPLEX, FUNCTION, INTERACTION WITH RAC1, MUTAGENESIS OF CYS-179; ARG-190; GLU-434; PHE-626; MET-632; LEU-697; TYR-704; LEU-841 AND 844-PHE-TRP-845, SUBUNIT.

    Entry informationi

    Entry nameiCYFP1_HUMAN
    AccessioniPrimary (citable) accession number: Q7L576
    Secondary accession number(s): A8K6D9
    , Q14467, Q5IED0, Q6ZSX1, Q9BSD9, Q9BVC7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Breakpoint hotspot for the Prader-Willi/Angelman syndromes and may be implicated in autism. Commonly altered in tumors.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3