SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P07737

- PROF1_HUMAN

UniProt

P07737 - PROF1_HUMAN

(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)

Protein
Profilin-1
Gene
PFN1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 ATPase activity Source: UniProt
  12. positive regulation of DNA metabolic process Source: Ensembl
  13. positive regulation of actin filament polymerization Source: UniProt
  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
Complete GO annotation...

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. neuron projection Source: Ensembl
  6. nucleus Source: Ensembl
  7. synapse Source: Ensembl
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 – 11Removed1 Publication
Chaini2 – 140139Profilin-1
PRO_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.

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.3 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

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.

Miscellaneous databases

EvolutionaryTraceiP07737.

Family & Domainsi

Sequence similaritiesi

Belongs to the profilin family.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 163 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

Similar proteinsi