Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9Y4F1

- FARP1_HUMAN

UniProt

Q9Y4F1 - FARP1_HUMAN

Protein

FERM, RhoGEF and pleckstrin domain-containing protein 1

Gene

FARP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Functions as guanine nucleotide exchange factor for RAC1. May play a role in semaphorin signaling. Plays a role in the assembly and disassembly of dendritic filopodia, the formation of dendritic spines, regulation of dendrite length and ultimately the formation of synapses By similarity.By similarity

    GO - Molecular functioni

    1. Rac guanyl-nucleotide exchange factor activity Source: UniProtKB
    2. Rho guanyl-nucleotide exchange factor activity Source: ProtInc

    GO - Biological processi

    1. dendrite morphogenesis Source: UniProtKB
    2. negative regulation of phosphatase activity Source: UniProtKB
    3. positive regulation of Rac GTPase activity Source: GOC
    4. positive regulation of Rho GTPase activity Source: GOC
    5. synapse assembly Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein, Guanine-nucleotide releasing factor

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    FERM, RhoGEF and pleckstrin domain-containing protein 1
    Alternative name(s):
    Chondrocyte-derived ezrin-like protein
    Pleckstrin homology domain-containing family C member 2
    Short name:
    PH domain-containing family C member 2
    Gene namesi
    Name:FARP1
    Synonyms:CDEP, PLEKHC2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:3591. FARP1.

    Subcellular locationi

    Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junctionsynapse. Cell junctionsynapsesynaptosome By similarity. Cytoplasmcytosol By similarity. Cell projectionfilopodium By similarity. Cell projectiondendrite By similarity. Cell projectiondendritic spine By similarity
    Note: Recruited to the cell membrane via interaction with CADM1.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasm Source: HPA
    3. cytoskeleton Source: ProtInc
    4. cytosol Source: UniProtKB
    5. dendrite Source: UniProtKB
    6. dendritic spine Source: UniProtKB-SubCell
    7. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
    8. filopodium Source: UniProtKB-SubCell
    9. synapse Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Synapse, Synaptosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28004.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10451045FERM, RhoGEF and pleckstrin domain-containing protein 1PRO_0000232753Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei24 – 241Phosphothreonine2 Publications
    Modified residuei340 – 3401Phosphoserine1 Publication
    Modified residuei373 – 3731PhosphoserineBy similarity
    Modified residuei427 – 4271Phosphoserine3 Publications
    Modified residuei510 – 5101Phosphoserine1 Publication
    Modified residuei514 – 5141Phosphoserine1 Publication
    Modified residuei872 – 8721Phosphoserine1 Publication
    Modified residuei889 – 8891Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y4F1.
    PaxDbiQ9Y4F1.
    PRIDEiQ9Y4F1.

    PTM databases

    PhosphoSiteiQ9Y4F1.

    Expressioni

    Tissue specificityi

    Detected in cAMP-treated chondrocytes, but not in untreated chondrocytes. Detected in fetal brain, heart and spleen, and in adult testis, kidney and lung.1 Publication

    Inductioni

    Up-regulated in response to cAMP in cultured embryonic chondrocytes.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y4F1.
    BgeeiQ9Y4F1.
    CleanExiHS_FARP1.
    GenevestigatoriQ9Y4F1.

    Organism-specific databases

    HPAiHPA000760.

    Interactioni

    Subunit structurei

    Interacts with CADM1. Interacts with RAC1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi115462. 3 interactions.
    IntActiQ9Y4F1. 1 interaction.
    STRINGi9606.ENSP00000322926.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4H6YX-ray4.09A/B539-1035[»]
    ProteinModelPortaliQ9Y4F1.
    SMRiQ9Y4F1. Positions 43-317, 539-1029.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 320281FERMPROSITE-ProRule annotationAdd
    BLAST
    Domaini540 – 730191DHPROSITE-ProRule annotationAdd
    BLAST
    Domaini759 – 85698PH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini932 – 102998PH 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi449 – 4535Poly-Glu

    Domaini

    Intramolecular interaction between the DH domain and the PH domains can stabilize the protein in an autoinhibited conformation.1 Publication

    Sequence similaritiesi

    Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
    Contains 1 FERM domain.PROSITE-ProRule annotation
    Contains 2 PH domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG282099.
    HOGENOMiHOG000007957.
    HOVERGENiHBG081521.
    KOiK17477.
    OMAiEDRILTH.
    OrthoDBiEOG7B5WVD.
    PhylomeDBiQ9Y4F1.
    TreeFamiTF351276.

    Family and domain databases

    Gene3Di1.20.80.10. 1 hit.
    1.20.900.10. 1 hit.
    2.30.29.30. 3 hits.
    InterProiIPR019749. Band_41_domain.
    IPR019750. Band_41_fam.
    IPR000219. DH-domain.
    IPR000798. Ez/rad/moesin_like.
    IPR014847. FERM-adjacent.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR019747. FERM_CS.
    IPR000299. FERM_domain.
    IPR018979. FERM_N.
    IPR018980. FERM_PH-like_C.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF08736. FA. 1 hit.
    PF09380. FERM_C. 1 hit.
    PF00373. FERM_M. 1 hit.
    PF09379. FERM_N. 1 hit.
    PF00169. PH. 2 hits.
    PF00621. RhoGEF. 1 hit.
    [Graphical view]
    PRINTSiPR00935. BAND41.
    PR00661. ERMFAMILY.
    SMARTiSM00295. B41. 1 hit.
    SM00233. PH. 2 hits.
    SM00325. RhoGEF. 1 hit.
    [Graphical view]
    SUPFAMiSSF47031. SSF47031. 1 hit.
    SSF48065. SSF48065. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS50010. DH_2. 1 hit.
    PS00660. FERM_1. 1 hit.
    PS50057. FERM_3. 1 hit.
    PS50003. PH_DOMAIN. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y4F1-1) [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

    MGEIEQRPTP GSRLGAPENS GISTLERGQK PPPTPSGKLV SIKIQMLDDT     50
    QEAFEVPQRA PGKVLLDAVC NHLNLVEGDY FGLEFPDHKK ITVWLDLLKP 100
    IVKQIRRPKH VVVKFVVKFF PPDHTQLQEE LTRYLFALQV KQDLAQGRLT 150
    CNDTSAALLI SHIVQSEIGD FDEALDREHL AKNKYIPQQD ALEDKIVEFH 200
    HNHIGQTPAE SDFQLLEIAR RLEMYGIRLH PAKDREGTKI NLAVANTGIL 250
    VFQGFTKINA FNWAKVRKLS FKRKRFLIKL RPDANSAYQD TLEFLMASRD 300
    FCKSFWKICV EHHAFFRLFE EPKPKPKPVL FSRGSSFRFS GRTQKQVLDY 350
    VKEGGHKKVQ FERKHSKIHS IRSLASQPTE LNSEVLEQSQ QSTSLTFGEG 400
    AESPGGQSCR RGKEPKVSAG EPGSHPSPAP RRSPAGNKQA DGAASAPTEE 450
    EEEVVKDRTQ QSKPQPPQPS TGSLTGSPHL SELSVNSQGG VAPANVTLSP 500
    NLSPDTKQAS PLISPLLNDQ ACPRTDDEDE GRRKRFPTDK AYFIAKEVST 550
    TERTYLKDLE VITSWFQSTV SKEDAMPEAL KSLIFPNFEP LHKFHTNFLK 600
    EIEQRLALWE GRSNAQIRDY QRIGDVMLKN IQGMKHLAAH LWKHSEALEA 650
    LENGIKSSRR LENFCRDFEL QKVCYLPLNT FLLRPLHRLM HYKQVLERLC 700
    KHHPPSHADF RDCRAALAEI TEMVAQLHGT MIKMENFQKL HELKKDLIGI 750
    DNLVVPGREF IRLGSLSKLS GKGLQQRMFF LFNDVLLYTS RGLTASNQFK 800
    VHGQLPLYGM TIEESEDEWG VPHCLTLRGQ RQSIIVAASS RSEMEKWVED 850
    IQMAIDLAEK SSSPAPEFLA SSPPDNKSPD EATAADQESE DDLSASRTSL 900
    ERQAPHRGNT MVHVCWHRNT SVSMVDFSIA VENQLSGNLL RKFKNSNGWQ 950
    KLWVVFTNFC LFFYKSHQDN HPLASLPLLG YSLTIPSESE NIQKDYVFKL 1000
    HFKSHVYYFR AESEYTFERW MEVIRSATSS ASRPHVLSHK ESLVY 1045
    Length:1,045
    Mass (Da):118,633
    Last modified:November 1, 1999 - v1
    Checksum:i0E8B2D61C0F58417
    GO
    Isoform 2 (identifier: Q9Y4F1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         758-758: R → RPGSFSLMRTPHLGQARRIPCAPERRPLLLVK

    Note: No experimental confirmation available.

    Show »
    Length:1,076
    Mass (Da):122,113
    Checksum:i25A71B2C8C60A280
    GO
    Isoform 3 (identifier: Q9Y4F1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         58-129: QRAPGKVLLD...FPPDHTQLQE → MVSSSSFLKA...TVTEELLNLF
         130-1045: Missing.

    Show »
    Length:129
    Mass (Da):14,138
    Checksum:iED33383FA354AB1E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti644 – 6441H → Y in AAH71592. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81P → L.
    Corresponds to variant rs9300466 [ dbSNP | Ensembl ].
    VAR_048362
    Natural varianti714 – 7141R → L in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035851

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei58 – 12972QRAPG…TQLQE → MVSSSSFLKATGSSWTGWVL RCSMKPKHHSHLIEKFGEDR ILTHLTGSISYTNWAGSRSL AVTVTEELLNLF in isoform 3. 1 PublicationVSP_040989Add
    BLAST
    Alternative sequencei130 – 1045916Missing in isoform 3. 1 PublicationVSP_040990Add
    BLAST
    Alternative sequencei758 – 7581R → RPGSFSLMRTPHLGQARRIP CAPERRPLLLVK in isoform 2. 1 PublicationVSP_017976

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB008430 mRNA. Translation: BAA24267.1.
    AL136300, AL445223 Genomic DNA. Translation: CAI10952.1.
    AL136300, AL137249, AL161896 Genomic DNA. Translation: CAI10953.1.
    AL161896, AL136300, AL137249 Genomic DNA. Translation: CAI12946.1.
    AL445223, AL136300 Genomic DNA. Translation: CAI15981.1.
    AL137249, AL136300, AL161896 Genomic DNA. Translation: CAI39458.1.
    BC041595 mRNA. Translation: AAH41595.1.
    BC065020 mRNA. No translation available.
    BC071592 mRNA. Translation: AAH71592.1.
    CCDSiCCDS32000.1. [Q9Y4F1-3]
    CCDS66572.1. [Q9Y4F1-2]
    CCDS9487.1. [Q9Y4F1-1]
    PIRiJC5795.
    RefSeqiNP_001001715.2. NM_001001715.3. [Q9Y4F1-3]
    NP_001273768.1. NM_001286839.1.
    NP_005757.1. NM_005766.3. [Q9Y4F1-1]
    XP_006719976.1. XM_006719913.1. [Q9Y4F1-1]
    UniGeneiHs.403917.
    Hs.709933.
    Hs.729583.

    Genome annotation databases

    EnsembliENST00000319562; ENSP00000322926; ENSG00000152767. [Q9Y4F1-1]
    ENST00000376581; ENSP00000365765; ENSG00000152767. [Q9Y4F1-3]
    GeneIDi10160.
    KEGGihsa:10160.
    UCSCiuc001vni.3. human. [Q9Y4F1-3]
    uc001vnj.3. human. [Q9Y4F1-1]

    Polymorphism databases

    DMDMi74762059.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB008430 mRNA. Translation: BAA24267.1 .
    AL136300 , AL445223 Genomic DNA. Translation: CAI10952.1 .
    AL136300 , AL137249 , AL161896 Genomic DNA. Translation: CAI10953.1 .
    AL161896 , AL136300 , AL137249 Genomic DNA. Translation: CAI12946.1 .
    AL445223 , AL136300 Genomic DNA. Translation: CAI15981.1 .
    AL137249 , AL136300 , AL161896 Genomic DNA. Translation: CAI39458.1 .
    BC041595 mRNA. Translation: AAH41595.1 .
    BC065020 mRNA. No translation available.
    BC071592 mRNA. Translation: AAH71592.1 .
    CCDSi CCDS32000.1. [Q9Y4F1-3 ]
    CCDS66572.1. [Q9Y4F1-2 ]
    CCDS9487.1. [Q9Y4F1-1 ]
    PIRi JC5795.
    RefSeqi NP_001001715.2. NM_001001715.3. [Q9Y4F1-3 ]
    NP_001273768.1. NM_001286839.1.
    NP_005757.1. NM_005766.3. [Q9Y4F1-1 ]
    XP_006719976.1. XM_006719913.1. [Q9Y4F1-1 ]
    UniGenei Hs.403917.
    Hs.709933.
    Hs.729583.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4H6Y X-ray 4.09 A/B 539-1035 [» ]
    ProteinModelPortali Q9Y4F1.
    SMRi Q9Y4F1. Positions 43-317, 539-1029.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115462. 3 interactions.
    IntActi Q9Y4F1. 1 interaction.
    STRINGi 9606.ENSP00000322926.

    PTM databases

    PhosphoSitei Q9Y4F1.

    Polymorphism databases

    DMDMi 74762059.

    Proteomic databases

    MaxQBi Q9Y4F1.
    PaxDbi Q9Y4F1.
    PRIDEi Q9Y4F1.

    Protocols and materials databases

    DNASUi 10160.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000319562 ; ENSP00000322926 ; ENSG00000152767 . [Q9Y4F1-1 ]
    ENST00000376581 ; ENSP00000365765 ; ENSG00000152767 . [Q9Y4F1-3 ]
    GeneIDi 10160.
    KEGGi hsa:10160.
    UCSCi uc001vni.3. human. [Q9Y4F1-3 ]
    uc001vnj.3. human. [Q9Y4F1-1 ]

    Organism-specific databases

    CTDi 10160.
    GeneCardsi GC13P098795.
    HGNCi HGNC:3591. FARP1.
    HPAi HPA000760.
    MIMi 602654. gene.
    neXtProti NX_Q9Y4F1.
    PharmGKBi PA28004.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG282099.
    HOGENOMi HOG000007957.
    HOVERGENi HBG081521.
    KOi K17477.
    OMAi EDRILTH.
    OrthoDBi EOG7B5WVD.
    PhylomeDBi Q9Y4F1.
    TreeFami TF351276.

    Miscellaneous databases

    ChiTaRSi FARP1. human.
    GeneWikii FARP1.
    GenomeRNAii 10160.
    NextBioi 38464.
    PROi Q9Y4F1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y4F1.
    Bgeei Q9Y4F1.
    CleanExi HS_FARP1.
    Genevestigatori Q9Y4F1.

    Family and domain databases

    Gene3Di 1.20.80.10. 1 hit.
    1.20.900.10. 1 hit.
    2.30.29.30. 3 hits.
    InterProi IPR019749. Band_41_domain.
    IPR019750. Band_41_fam.
    IPR000219. DH-domain.
    IPR000798. Ez/rad/moesin_like.
    IPR014847. FERM-adjacent.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR019747. FERM_CS.
    IPR000299. FERM_domain.
    IPR018979. FERM_N.
    IPR018980. FERM_PH-like_C.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF08736. FA. 1 hit.
    PF09380. FERM_C. 1 hit.
    PF00373. FERM_M. 1 hit.
    PF09379. FERM_N. 1 hit.
    PF00169. PH. 2 hits.
    PF00621. RhoGEF. 1 hit.
    [Graphical view ]
    PRINTSi PR00935. BAND41.
    PR00661. ERMFAMILY.
    SMARTi SM00295. B41. 1 hit.
    SM00233. PH. 2 hits.
    SM00325. RhoGEF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47031. SSF47031. 1 hit.
    SSF48065. SSF48065. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS50010. DH_2. 1 hit.
    PS00660. FERM_1. 1 hit.
    PS50057. FERM_3. 1 hit.
    PS50003. PH_DOMAIN. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of CDEP, a novel human protein containing the ezrin-like domain of the band 4.1 superfamily and the Dbl homology domain of rho guanine nucleotide exchange factors."
      Koyano Y., Kawamoto T., Shen M., Yan W., Noshiro M., Fujii K., Kato Y.
      Biochem. Biophys. Res. Commun. 241:369-375(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, TISSUE SPECIFICITY.
      Tissue: Cartilage.
    2. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [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] (ISOFORMS 1; 2 AND 3).
      Tissue: Brain, Placenta and Skin.
    4. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-889, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. "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].
    10. "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 THR-24; SER-427; SER-510 AND SER-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-872 AND SER-889, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Structural basis for autoinhibition of the guanine nucleotide exchange factor FARP2."
      He X., Kuo Y.C., Rosche T.J., Zhang X.
      Structure 21:355-364(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.09 ANGSTROMS) OF 539-1035, DOMAIN.
    14. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-714.

    Entry informationi

    Entry nameiFARP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y4F1
    Secondary accession number(s): Q5JVI9, Q6IQ29
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 18, 2006
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 118 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: 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