Skip Header

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

UniProtKB - P07737 (PROF1_HUMAN)

(max 400 entries)x

Your basket is currently empty. i

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: -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 Source: BHF-UCL
  • phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  • proline-rich region binding Source: UniProtKB
  • Rho GTPase binding Source: Ensembl
  • RNA binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • actin cytoskeleton organization Source: InterPro
  • 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 epithelial cell migration Source: UniProtKB
  • positive regulation of ruffle assembly Source: UniProtKB
  • protein stabilization Source: UniProtKB
  • regulation of transcription by RNA polymerase II Source: Ensembl
  • Wnt signaling pathway, planar cell polarity pathway Source: Reactome
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionActin-binding

Enzyme and pathway databases

ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-376176 Signaling by ROBO receptors
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000108518.7
HGNCiHGNC:8881 PFN1
MIMi176610 gene
neXtProtiNX_P07737

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 dbSNP:rs387907264EnsemblClinVar.1
Natural variantiVAR_068926114M → T in ALS18; the mutant protein is detected in the insoluble fraction of cells. 1 PublicationCorresponds to variant dbSNP:rs387907265EnsemblClinVar.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 dbSNP:rs140547520EnsemblClinVar.1
Natural variantiVAR_068928118G → V in ALS18; the mutant protein is detected in the insoluble fraction of cells. 1 PublicationCorresponds to variant dbSNP:rs387907266EnsemblClinVar.1

Keywords - Diseasei

Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNETi5216
GeneReviewsiPFN1
MalaCardsiPFN1
MIMi614808 phenotype
OpenTargetsiENSG00000108518
Orphaneti803 Amyotrophic lateral sclerosis
PharmGKBiPA33219

Protein family/group databases

Allergomei907 Hom s Profilin

Chemistry databases

DrugBankiDB07908 7-HYDROXY-4-METHYL-3-(2-HYDROXY-ETHYL)COUMARIN

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 SUMO2); alternateCombined sources
Cross-linki54Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
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
ProteomicsDBi52024
TopDownProteomicsiP07737

2D gel databases

DOSAC-COBS-2DPAGEiP07737
OGPiP07737
REPRODUCTION-2DPAGEiIPI00216691
UCD-2DPAGEiP07737

PTM databases

iPTMnetiP07737
PhosphoSitePlusiP07737
SwissPalmiP07737

Miscellaneous databases

PMAP-CutDBiP07737

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

Show more details

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • actin monomer binding Source: UniProtKB
  • cadherin binding Source: BHF-UCL
  • proline-rich region binding Source: UniProtKB
  • Rho GTPase binding Source: Ensembl
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi111237, 76 interactors
CORUMiP07737
DIPiDIP-30N
IntActiP07737, 50 interactors
MINTiP07737
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

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
InterProiView protein in InterPro
IPR005455 PFN
IPR036140 PFN_sf
IPR005454 Profilin1/2/3_vertebrate
IPR027310 Profilin_CS
PfamiView protein in Pfam
PF00235 Profilin, 1 hit
PRINTSiPR01639 PROFILINMAML
SMARTiView protein in SMART
SM00392 PROF, 1 hit
SUPFAMiSSF55770 SSF55770, 1 hit
PROSITEiView protein in PROSITE
PS00414 PROFILIN, 1 hit

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 dbSNP:rs387907264EnsemblClinVar.1
Natural variantiVAR_068926114M → T in ALS18; the mutant protein is detected in the insoluble fraction of cells. 1 PublicationCorresponds to variant dbSNP:rs387907265EnsemblClinVar.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 dbSNP:rs140547520EnsemblClinVar.1
Natural variantiVAR_068928118G → V in ALS18; the mutant protein is detected in the insoluble fraction of cells. 1 PublicationCorresponds to variant dbSNP:rs387907266EnsemblClinVar.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

Similar proteinsi

Entry informationi

Entry nameiPROF1_HUMAN
AccessioniPrimary (citable) accession number: P07737
Secondary accession number(s): Q53Y44
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 204 of the entry and version 2 of the sequence. See 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health