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P07737

- PROF1_HUMAN

UniProt

P07737 - PROF1_HUMAN

Protein

Profilin-1

Gene

PFN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR.1 Publication

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. adenyl-nucleotide exchange factor activity Source: UniProt
    3. phosphatidylinositol-4,5-bisphosphate binding Source: UniProt
    4. poly(A) RNA binding Source: UniProtKB
    5. proline-rich region binding Source: UniProtKB
    6. protein binding Source: IntAct

    GO - Biological processi

    1. actin cytoskeleton organization Source: InterPro
    2. blood coagulation Source: Reactome
    3. cell death Source: UniProtKB-KW
    4. cellular response to growth factor stimulus Source: Ensembl
    5. negative regulation of actin filament bundle assembly Source: UniProt
    6. negative regulation of actin filament polymerization Source: UniProt
    7. negative regulation of stress fiber assembly Source: UniProt
    8. neural tube closure Source: Ensembl
    9. platelet activation Source: Reactome
    10. platelet degranulation Source: Reactome
    11. positive regulation of actin filament polymerization Source: UniProt
    12. positive regulation of ATPase activity Source: UniProt
    13. positive regulation of DNA metabolic process Source: Ensembl
    14. positive regulation of epithelial cell migration Source: UniProt
    15. positive regulation of ruffle assembly Source: UniProt
    16. positive regulation of stress fiber assembly Source: Ensembl
    17. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    18. positive regulation of viral transcription Source: Ensembl

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_172581. PCP/CE pathway.
    REACT_19351. Signaling by Robo receptor.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Profilin-1
    Alternative name(s):
    Epididymis tissue protein Li 184a
    Profilin I
    Gene namesi
    Name:PFN1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:8881. PFN1.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. cytoskeleton Source: UniProtKB-SubCell
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. membrane Source: UniProtKB
    6. neuron projection Source: Ensembl
    7. nucleus Source: Ensembl
    8. synapse Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    Amyotrophic lateral sclerosis 18 (ALS18) [MIM:614808]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti71 – 711C → G in ALS18; the mutant protein is detected in the insoluble fraction of cells. 1 Publication
    VAR_068925
    Natural varianti114 – 1141M → T in ALS18; the mutant protein is detected in the insoluble fraction of cells. 1 Publication
    VAR_068926
    Natural varianti117 – 1171E → G in ALS18; unknown pathological significance; like the wild-type the mutant protein is detected in the soluble fraction of cells. 1 Publication
    Corresponds to variant rs140547520 [ dbSNP | Ensembl ].
    VAR_068927
    Natural varianti118 – 1181G → V in ALS18; the mutant protein is detected in the insoluble fraction of cells. 1 Publication
    VAR_068928

    Keywords - Diseasei

    Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

    Organism-specific databases

    MIMi614808. phenotype.
    Orphaneti803. Amyotrophic lateral sclerosis.
    PharmGKBiPA33219.

    Protein family/group databases

    Allergomei907. Hom s Profilin.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 140139Profilin-1PRO_0000199571Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Cross-linki54 – 54Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
    Modified residuei85 – 851Phosphoserine1 Publication
    Modified residuei105 – 1051N6-acetyllysine1 Publication
    Modified residuei108 – 1081N6-acetyllysine1 Publication
    Modified residuei129 – 1291Phosphotyrosine1 Publication
    Modified residuei138 – 1381Phosphoserine; by ROCK11 Publication

    Post-translational modificationi

    Phosphorylation at Ser-138 reduces its affinity for G-actin and blocks its interaction with HTT, reducing its ability to inhibit androgen receptor (AR) and HTT aggregation.3 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP07737.
    PaxDbiP07737.
    PeptideAtlasiP07737.
    PRIDEiP07737.

    2D gel databases

    DOSAC-COBS-2DPAGEP07737.
    OGPiP07737.
    REPRODUCTION-2DPAGEIPI00216691.
    UCD-2DPAGEP07737.

    PTM databases

    PhosphoSiteiP07737.

    Miscellaneous databases

    PMAP-CutDBP07737.

    Expressioni

    Tissue specificityi

    Expressed in epididymis (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP07737.
    BgeeiP07737.
    CleanExiHS_PFN1.
    GenevestigatoriP07737.

    Organism-specific databases

    HPAiCAB037134.
    CAB037140.

    Interactioni

    Subunit structurei

    Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio. Found in a complex with XPO6, Ran, ACTB and PFN1. Interacts with VASP. Interacts with HTT.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    WASF1Q925582EBI-713780,EBI-1548747
    WaslO088164EBI-713780,EBI-6142604From a different organism.

    Protein-protein interaction databases

    BioGridi111237. 52 interactions.
    DIPiDIP-30N.
    IntActiP07737. 37 interactions.
    MINTiMINT-1372667.
    STRINGi9606.ENSP00000225655.

    Structurei

    Secondary structure

    1
    140
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 128
    Beta strandi14 – 163
    Beta strandi17 – 2812
    Beta strandi30 – 345
    Helixi40 – 423
    Helixi45 – 528
    Helixi58 – 603
    Beta strandi64 – 663
    Beta strandi69 – 779
    Beta strandi78 – 803
    Turni81 – 833
    Beta strandi85 – 906
    Beta strandi93 – 964
    Beta strandi100 – 1056
    Beta strandi107 – 1159
    Helixi121 – 13717

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AWIX-ray2.20A/B3-140[»]
    1CF0X-ray2.20A/B3-140[»]
    1CJFX-ray2.30A/B2-140[»]
    1FIKX-ray2.30A2-140[»]
    1FILX-ray2.00A2-140[»]
    1PFLNMR-A2-140[»]
    2PAVX-ray1.80P2-140[»]
    2PBDX-ray1.50P2-140[»]
    3CHWX-ray2.30P2-140[»]
    ProteinModelPortaliP07737.
    SMRiP07737. Positions 2-140.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07737.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the profilin family.Curated

    Phylogenomic databases

    eggNOGiNOG269129.
    HOGENOMiHOG000171592.
    HOVERGENiHBG053683.
    InParanoidiP07737.
    KOiK05759.
    OMAiHLRRAQY.
    OrthoDBiEOG7JMGGT.
    PhylomeDBiP07737.
    TreeFamiTF331744.

    Family and domain databases

    InterProiIPR005454. Profilin_chordates.
    IPR027310. Profilin_CS.
    IPR005455. Profilin_eukaryotes/bac.
    [Graphical view]
    PfamiPF00235. Profilin. 1 hit.
    [Graphical view]
    PRINTSiPR01639. PROFILINMAML.
    SMARTiSM00392. PROF. 1 hit.
    [Graphical view]
    SUPFAMiSSF55770. SSF55770. 1 hit.
    PROSITEiPS00414. PROFILIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P07737-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGWNAYIDN LMADGTCQDA AIVGYKDSPS VWAAVPGKTF VNITPAEVGV    50
    LVGKDRSSFY VNGLTLGGQK CSVIRDSLLQ DGEFSMDLRT KSTGGAPTFN 100
    VTVTKTDKTL VLLMGKEGVH GGLINKKCYE MASHLRRSQY 140
    Length:140
    Mass (Da):15,054
    Last modified:January 23, 2007 - v2
    Checksum:iF725119E55A289EB
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti71 – 711C → G in ALS18; the mutant protein is detected in the insoluble fraction of cells. 1 Publication
    VAR_068925
    Natural varianti114 – 1141M → T in ALS18; the mutant protein is detected in the insoluble fraction of cells. 1 Publication
    VAR_068926
    Natural varianti117 – 1171E → G in ALS18; unknown pathological significance; like the wild-type the mutant protein is detected in the soluble fraction of cells. 1 Publication
    Corresponds to variant rs140547520 [ dbSNP | Ensembl ].
    VAR_068927
    Natural varianti118 – 1181G → V in ALS18; the mutant protein is detected in the insoluble fraction of cells. 1 Publication
    VAR_068928

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03191 mRNA. Translation: AAA36486.1.
    GU727630 mRNA. Translation: ADU87632.1.
    BT007001 mRNA. Translation: AAP35647.1.
    AK312168 mRNA. Translation: BAG35102.1.
    CR407670 mRNA. Translation: CAG28598.1.
    CH471108 Genomic DNA. Translation: EAW90381.1.
    CH471108 Genomic DNA. Translation: EAW90383.1.
    CH471108 Genomic DNA. Translation: EAW90384.1.
    BC002475 mRNA. Translation: AAH02475.1.
    BC006768 mRNA. Translation: AAH06768.1.
    BC013439 mRNA. Translation: AAH13439.1.
    BC015164 mRNA. Translation: AAH15164.1.
    BC057828 mRNA. Translation: AAH57828.1.
    CCDSiCCDS11061.1.
    PIRiA28622.
    RefSeqiNP_005013.1. NM_005022.3.
    UniGeneiHs.494691.

    Genome annotation databases

    EnsembliENST00000225655; ENSP00000225655; ENSG00000108518.
    GeneIDi5216.
    KEGGihsa:5216.
    UCSCiuc002gaa.4. human.

    Polymorphism databases

    DMDMi130979.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03191 mRNA. Translation: AAA36486.1 .
    GU727630 mRNA. Translation: ADU87632.1 .
    BT007001 mRNA. Translation: AAP35647.1 .
    AK312168 mRNA. Translation: BAG35102.1 .
    CR407670 mRNA. Translation: CAG28598.1 .
    CH471108 Genomic DNA. Translation: EAW90381.1 .
    CH471108 Genomic DNA. Translation: EAW90383.1 .
    CH471108 Genomic DNA. Translation: EAW90384.1 .
    BC002475 mRNA. Translation: AAH02475.1 .
    BC006768 mRNA. Translation: AAH06768.1 .
    BC013439 mRNA. Translation: AAH13439.1 .
    BC015164 mRNA. Translation: AAH15164.1 .
    BC057828 mRNA. Translation: AAH57828.1 .
    CCDSi CCDS11061.1.
    PIRi A28622.
    RefSeqi NP_005013.1. NM_005022.3.
    UniGenei Hs.494691.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AWI X-ray 2.20 A/B 3-140 [» ]
    1CF0 X-ray 2.20 A/B 3-140 [» ]
    1CJF X-ray 2.30 A/B 2-140 [» ]
    1FIK X-ray 2.30 A 2-140 [» ]
    1FIL X-ray 2.00 A 2-140 [» ]
    1PFL NMR - A 2-140 [» ]
    2PAV X-ray 1.80 P 2-140 [» ]
    2PBD X-ray 1.50 P 2-140 [» ]
    3CHW X-ray 2.30 P 2-140 [» ]
    ProteinModelPortali P07737.
    SMRi P07737. Positions 2-140.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111237. 52 interactions.
    DIPi DIP-30N.
    IntActi P07737. 37 interactions.
    MINTi MINT-1372667.
    STRINGi 9606.ENSP00000225655.

    Protein family/group databases

    Allergomei 907. Hom s Profilin.

    PTM databases

    PhosphoSitei P07737.

    Polymorphism databases

    DMDMi 130979.

    2D gel databases

    DOSAC-COBS-2DPAGE P07737.
    OGPi P07737.
    REPRODUCTION-2DPAGE IPI00216691.
    UCD-2DPAGE P07737.

    Proteomic databases

    MaxQBi P07737.
    PaxDbi P07737.
    PeptideAtlasi P07737.
    PRIDEi P07737.

    Protocols and materials databases

    DNASUi 5216.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000225655 ; ENSP00000225655 ; ENSG00000108518 .
    GeneIDi 5216.
    KEGGi hsa:5216.
    UCSCi uc002gaa.4. human.

    Organism-specific databases

    CTDi 5216.
    GeneCardsi GC17M004848.
    GeneReviewsi PFN1.
    HGNCi HGNC:8881. PFN1.
    HPAi CAB037134.
    CAB037140.
    MIMi 176610. gene.
    614808. phenotype.
    neXtProti NX_P07737.
    Orphaneti 803. Amyotrophic lateral sclerosis.
    PharmGKBi PA33219.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG269129.
    HOGENOMi HOG000171592.
    HOVERGENi HBG053683.
    InParanoidi P07737.
    KOi K05759.
    OMAi HLRRAQY.
    OrthoDBi EOG7JMGGT.
    PhylomeDBi P07737.
    TreeFami TF331744.

    Enzyme and pathway databases

    Reactomei REACT_172581. PCP/CE pathway.
    REACT_19351. Signaling by Robo receptor.

    Miscellaneous databases

    ChiTaRSi PFN1. human.
    EvolutionaryTracei P07737.
    GeneWikii Profilin_1.
    GenomeRNAii 5216.
    NextBioi 20172.
    PMAP-CutDB P07737.
    PROi P07737.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07737.
    Bgeei P07737.
    CleanExi HS_PFN1.
    Genevestigatori P07737.

    Family and domain databases

    InterProi IPR005454. Profilin_chordates.
    IPR027310. Profilin_CS.
    IPR005455. Profilin_eukaryotes/bac.
    [Graphical view ]
    Pfami PF00235. Profilin. 1 hit.
    [Graphical view ]
    PRINTSi PR01639. PROFILINMAML.
    SMARTi SM00392. PROF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55770. SSF55770. 1 hit.
    PROSITEi PS00414. PROFILIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human profilin. Molecular cloning, sequence comparison, and chromosomal analysis."
      Kwiatkowski D.J., Bruns G.A.P.
      J. Biol. Chem. 263:5910-5915(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Systematic mapping and functional analysis of a family of human epididymal secretory sperm-located proteins."
      Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C., Jin S., Liu J., Zhu P., Liu Y.
      Mol. Cell. Proteomics 9:2517-2528(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Epididymis.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "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].
      Tissue: Brain.
    5. "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 (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
      Tissue: Colon, Lung, Pancreas and Placenta.
    8. "The primary structure of human platelet profilin: reinvestigation of the calf spleen profilin sequence."
      Ampe C., Markey F., Lindberg U., Vandekerckhove J.
      FEBS Lett. 228:17-21(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-140, ACETYLATION AT ALA-2.
    9. "Distinct biochemical characteristics of the two human profilin isoforms."
      Gieselmann R., Kwiatkowski D.J., Janmey P.A., Witke W.
      Eur. J. Biochem. 229:621-628(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    10. "Exportin 6: a novel nuclear export receptor that is specific for profilin.actin complexes."
      Stueven T., Hartmann E., Goerlich D.
      EMBO J. 22:5928-5940(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH RAN; ACTB AND XPO6.
    11. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation."
      Shao J., Welch W.J., Diprospero N.A., Diamond M.I.
      Mol. Cell. Biol. 28:5196-5208(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HTT, PHOSPHORYLATION AT SER-138.
    13. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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-105 AND LYS-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern."
      Metzler W.J., Constantine K.L., Friedrichs M.S., Bell A.J., Ernst E.G., Lavoie T.B., Mueller L.
      Biochemistry 32:13818-13829(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    19. Fedorov A.A., Pollard T.D., Almo S.C.
      Submitted (APR-1996) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    20. "Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation."
      Mahoney N.M., Janmey P.A., Almo S.C.
      Nat. Struct. Biol. 4:953-960(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF COMPLEX WITH POLY-PRO.
    21. "Profilin binds proline-rich ligands in two distinct amide backbone orientations."
      Mahoney N.M., Rozwarski D.A., Fedorov E., Fedorov A.A., Almo S.C.
      Nat. Struct. Biol. 6:666-671(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH POLY-PRO.
    22. "Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP."
      Ferron F., Rebowski G., Lee S.H., Dominguez R.
      EMBO J. 26:4597-4606(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-140 IN COMPLEXES WITH VASP AND MONOMERIC ACTIN, INTERACTION WITH VASP.
    23. "Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding."
      Baek K., Liu X., Ferron F., Shu S., Korn E.D., Dominguez R.
      Proc. Natl. Acad. Sci. U.S.A. 105:11748-11753(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-140 IN COMPLEX WITH VASP AND ACTIN.
    24. Cited for: VARIANTS ALS18 GLY-71; THR-114; GLY-117 AND VAL-118, CHARACTERIZATION OF VARIANTS ALS18 GLY-71; THR-114; GLY-117 AND VAL-118.

    Entry informationi

    Entry nameiPROF1_HUMAN
    AccessioniPrimary (citable) accession number: P07737
    Secondary accession number(s): Q53Y44
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 164 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

    3D-structure, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3