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Protein

Profilin-1

Gene

PFN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • actin binding Source: UniProtKB
  • actin monomer binding Source: UniProtKB
  • adenyl-nucleotide exchange factor activity Source: UniProtKB
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • proline-rich region binding Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton organization Source: InterPro
  • cellular response to growth factor stimulus Source: Ensembl
  • negative regulation of actin filament bundle assembly Source: UniProtKB
  • negative regulation of actin filament polymerization Source: UniProtKB
  • negative regulation of stress fiber assembly Source: UniProtKB
  • neural tube closure Source: Ensembl
  • positive regulation of actin filament bundle assembly Source: GO_Central
  • positive regulation of actin filament polymerization Source: UniProtKB
  • positive regulation of ATPase activity Source: UniProtKB
  • positive regulation of DNA metabolic process Source: Ensembl
  • positive regulation of epithelial cell migration Source: UniProtKB
  • positive regulation of ruffle assembly Source: UniProtKB
  • positive regulation of stress fiber assembly Source: Ensembl
  • positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • positive regulation of viral transcription Source: Ensembl
  • protein stabilization Source: UniProtKB
  • Wnt signaling pathway, planar cell polarity pathway Source: Reactome
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000108518-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-376176. Signaling by Robo receptor.
R-HSA-4086400. PCP/CE pathway.
R-HSA-5663220. RHO GTPases Activate Formins.
SIGNORiP07737.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:8881. PFN1.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • cell-cell adherens junction Source: BHF-UCL
  • cell cortex Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • neuron projection Source: Ensembl
  • nucleus Source: UniProtKB
  • synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Amyotrophic lateral sclerosis 18 (ALS18)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:614808
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06892571C → G in ALS18; the mutant protein is detected in the insoluble fraction of cells. 1 PublicationCorresponds to variant rs387907264dbSNPEnsembl.1
Natural variantiVAR_068926114M → T in ALS18; the mutant protein is detected in the insoluble fraction of cells. 1 PublicationCorresponds to variant rs387907265dbSNPEnsembl.1
Natural variantiVAR_068927117E → G in ALS18; unknown pathological significance; like the wild-type the mutant protein is detected in the soluble fraction of cells. 1 PublicationCorresponds to variant rs140547520dbSNPEnsembl.1
Natural variantiVAR_068928118G → V in ALS18; the mutant protein is detected in the insoluble fraction of cells. 1 PublicationCorresponds to variant rs387907266dbSNPEnsembl.1

Keywords - Diseasei

Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNETi5216.
MalaCardsiPFN1.
MIMi614808. phenotype.
OpenTargetsiENSG00000108518.
Orphaneti803. Amyotrophic lateral sclerosis.
PharmGKBiPA33219.

Protein family/group databases

Allergomei907. Hom s Profilin.

Polymorphism and mutation databases

BioMutaiPFN1.
DMDMi130979.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001995712 – 140Profilin-1Add BLAST139

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei28PhosphoserineBy similarity1
Cross-linki54Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei57PhosphoserineCombined sources1
Modified residuei85PhosphoserineCombined sources1
Modified residuei105N6-acetyllysineCombined sources1
Modified residuei108N6-acetyllysineCombined sources1
Modified residuei129PhosphotyrosineCombined sources1
Modified residuei138Phosphoserine; by ROCK11 Publication1

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.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP07737.
PaxDbiP07737.
PeptideAtlasiP07737.
PRIDEiP07737.
TopDownProteomicsiP07737.

2D gel databases

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

PTM databases

iPTMnetiP07737.
PhosphoSitePlusiP07737.
SwissPalmiP07737.

Miscellaneous databases

PMAP-CutDBP07737.

Expressioni

Tissue specificityi

Expressed in epididymis (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000108518.
CleanExiHS_PFN1.
ExpressionAtlasiP07737. baseline and differential.
GenevisibleiP07737. HS.

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.

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • actin monomer binding Source: UniProtKB
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • proline-rich region binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111237. 62 interactors.
DIPiDIP-30N.
IntActiP07737. 44 interactors.
MINTiMINT-1372667.
STRINGi9606.ENSP00000225655.

Structurei

Secondary structure

1140
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 12Combined sources8
Beta strandi13 – 15Combined sources3
Beta strandi17 – 28Combined sources12
Beta strandi30 – 34Combined sources5
Helixi40 – 42Combined sources3
Helixi45 – 52Combined sources8
Helixi58 – 60Combined sources3
Beta strandi64 – 66Combined sources3
Beta strandi69 – 77Combined sources9
Beta strandi78 – 80Combined sources3
Turni81 – 83Combined sources3
Beta strandi85 – 90Combined sources6
Beta strandi93 – 96Combined sources4
Beta strandi100 – 105Combined sources6
Beta strandi107 – 115Combined sources9
Helixi121 – 137Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4X1LX-ray2.16A1-140[»]
4X1MX-ray2.17A1-140[»]
4X25X-ray2.23A/B1-140[»]
ProteinModelPortaliP07737.
SMRiP07737.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07737.

Family & Domainsi

Sequence similaritiesi

Belongs to the profilin family.Curated

Phylogenomic databases

eggNOGiKOG1755. Eukaryota.
ENOG41126PD. LUCA.
GeneTreeiENSGT00390000010143.
HOGENOMiHOG000171592.
HOVERGENiHBG053683.
InParanoidiP07737.
KOiK05759.
OMAiHLRRAQY.
PhylomeDBiP07737.
TreeFamiTF331744.

Family and domain databases

CDDicd00148. PROF. 1 hit.
InterProiIPR005455. PFN.
IPR005454. Profilin1/2/3_vertebrate.
IPR027310. Profilin_CS.
[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

        10         20         30         40         50
MAGWNAYIDN LMADGTCQDA AIVGYKDSPS VWAAVPGKTF VNITPAEVGV
60 70 80 90 100
LVGKDRSSFY VNGLTLGGQK CSVIRDSLLQ DGEFSMDLRT KSTGGAPTFN
110 120 130 140
VTVTKTDKTL VLLMGKEGVH GGLINKKCYE MASHLRRSQY
Length:140
Mass (Da):15,054
Last modified:January 23, 2007 - v2
Checksum:iF725119E55A289EB
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06892571C → G in ALS18; the mutant protein is detected in the insoluble fraction of cells. 1 PublicationCorresponds to variant rs387907264dbSNPEnsembl.1
Natural variantiVAR_068926114M → T in ALS18; the mutant protein is detected in the insoluble fraction of cells. 1 PublicationCorresponds to variant rs387907265dbSNPEnsembl.1
Natural variantiVAR_068927117E → G in ALS18; unknown pathological significance; like the wild-type the mutant protein is detected in the soluble fraction of cells. 1 PublicationCorresponds to variant rs140547520dbSNPEnsembl.1
Natural variantiVAR_068928118G → V in ALS18; the mutant protein is detected in the insoluble fraction of cells. 1 PublicationCorresponds to variant rs387907266dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4X1LX-ray2.16A1-140[»]
4X1MX-ray2.17A1-140[»]
4X25X-ray2.23A/B1-140[»]
ProteinModelPortaliP07737.
SMRiP07737.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111237. 62 interactors.
DIPiDIP-30N.
IntActiP07737. 44 interactors.
MINTiMINT-1372667.
STRINGi9606.ENSP00000225655.

Protein family/group databases

Allergomei907. Hom s Profilin.

PTM databases

iPTMnetiP07737.
PhosphoSitePlusiP07737.
SwissPalmiP07737.

Polymorphism and mutation databases

BioMutaiPFN1.
DMDMi130979.

2D gel databases

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

Proteomic databases

EPDiP07737.
PaxDbiP07737.
PeptideAtlasiP07737.
PRIDEiP07737.
TopDownProteomicsiP07737.

Protocols and materials databases

DNASUi5216.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000225655; ENSP00000225655; ENSG00000108518.
GeneIDi5216.
KEGGihsa:5216.
UCSCiuc002gaa.5. human.

Organism-specific databases

CTDi5216.
DisGeNETi5216.
GeneCardsiPFN1.
GeneReviewsiPFN1.
HGNCiHGNC:8881. PFN1.
HPAiCAB037134.
CAB037140.
MalaCardsiPFN1.
MIMi176610. gene.
614808. phenotype.
neXtProtiNX_P07737.
OpenTargetsiENSG00000108518.
Orphaneti803. Amyotrophic lateral sclerosis.
PharmGKBiPA33219.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1755. Eukaryota.
ENOG41126PD. LUCA.
GeneTreeiENSGT00390000010143.
HOGENOMiHOG000171592.
HOVERGENiHBG053683.
InParanoidiP07737.
KOiK05759.
OMAiHLRRAQY.
PhylomeDBiP07737.
TreeFamiTF331744.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000108518-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-376176. Signaling by Robo receptor.
R-HSA-4086400. PCP/CE pathway.
R-HSA-5663220. RHO GTPases Activate Formins.
SIGNORiP07737.

Miscellaneous databases

ChiTaRSiPFN1. human.
EvolutionaryTraceiP07737.
GeneWikiiProfilin_1.
GenomeRNAii5216.
PMAP-CutDBP07737.
PROiP07737.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000108518.
CleanExiHS_PFN1.
ExpressionAtlasiP07737. baseline and differential.
GenevisibleiP07737. HS.

Family and domain databases

CDDicd00148. PROF. 1 hit.
InterProiIPR005455. PFN.
IPR005454. Profilin1/2/3_vertebrate.
IPR027310. Profilin_CS.
[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]
ProtoNetiSearch...

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: November 30, 2016
This is version 188 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.