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Protein Page:
Profilin-1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
Profilin-1 a ubiquitous actin monomer-binding protein belonging to the profilin family. At high concentrations, profilin 1 prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Deletion of this gene is associated with Miller-Dieker syndrome. Note: This description may include information from UniProtKB.
Protein type: Actin binding protein; Motility/polarity/chemotaxis; Cytoskeletal protein
Cellular Component: neuron projection; cytoskeleton; synapse; cytosol; nucleus
Molecular Function: protein binding; phosphatidylinositol-4,5-bisphosphate binding; Rho GTPase binding; adenyl-nucleotide exchange factor activity; actin binding; receptor binding
Biological Process: cell death; positive regulation of DNA metabolic process; platelet activation; negative regulation of actin filament bundle formation; negative regulation of stress fiber formation; negative regulation of actin filament polymerization; positive regulation of viral transcription; platelet degranulation; positive regulation of actin filament polymerization; positive regulation of ATPase activity; positive regulation of stress fiber formation; neural tube closure; positive regulation of transcription from RNA polymerase II promoter; blood coagulation; actin cytoskeleton organization and biogenesis
Reference #:  P07737 (UniProtKB)
Alt. Names/Synonyms: PFN1; PROF1; profilin 1; Profilin I; Profilin-1
Gene Symbols: PFN1
Molecular weight: 15,054 Da
Basal Isoelectric point: 8.44  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Profilin-1

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Source  |  InnateDB  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Sites Implicated In
activity, inhibited: S138‑p
molecular association, regulation: Y60‑p, S138‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 Y7-p _MAGWNAyIDNLMAD
0 5 Y25-p QDAAIVGyKDSPSVW
0 4 K38-a VWAAVPGkTFVNITP
0 3 K38-u VWAAVPGkTFVNITP
0 2 N42 VPGkTFVNITPAEVG
0 112 K54-u EVGVLVGkDRsSFyV
0 1 S57-p VLVGkDRsSFyVNGL
1 54 Y60-p GkDRsSFyVNGLtLG
0 5 T65-p SFyVNGLtLGGQkCs
0 89 K70-u GLtLGGQkCsVIRDS
0 1 S72-p tLGGQkCsVIRDSLL
0 1 S85-p LLQDGEFsMDLRTkS
0 2 K91-a FsMDLRTkStGGAPT
0 16 K91-u FsMDLRTkStGGAPT
0 1 T93-p MDLRTkStGGAPTFN
0 3 K105-a TFNVTVTkTDkTLVL
0 96 K105-u TFNVTVTkTDkTLVL
0 2 K108-a VTVTkTDkTLVLLMG
0 4 K108-u VTVTkTDkTLVLLMG
0 1 K116 TLVLLMGKEGVHGGL
0 13 K126-a VHGGLINkkCyEMAS
0 85 K126-u VHGGLINkkCyEMAS
0 4 K127-u HGGLINkkCyEMASH
1 655 Y129-p GLINkkCyEMASHLR
5 0 S138-p MASHLRRsQY_____
  mouse

 
Y7 _MAGWNAYIDSLMAD
Y25 QDAAIVGYKDSPSVW
K38 VWAAVPGKTFVsITP
K38 VWAAVPGKTFVsITP
S42-p VPGKTFVsITPAEVG
K54-u EVGVLVGkDRSSFFV
S57 VLVGkDRSSFFVNGL
F60 GkDRSSFFVNGLtLG
T65-p SFFVNGLtLGGQkCS
K70-u GLtLGGQkCSVIRDS
S72 tLGGQkCSVIRDSLL
T85 LLQDGEFTMDLRTKS
K91 FTMDLRTKSTGGAPT
K91 FTMDLRTKSTGGAPT
T93 MDLRTKSTGGAPTFN
M105 TFNVTVTMTAKTLVL
M105 TFNVTVTMTAKTLVL
K108 VTVTMTAKTLVLLMG
K108 VTVTMTAKTLVLLMG
K116-u TLVLLMGkEGVHGGL
K126 VHGGLINKkCyEMAS
K126-u VHGGLINkkCyEMAS
K127-u HGGLINkkCyEMASH
Y129-p GLINkkCyEMASHLR
S138-p MASHLRRsQY_____
  rat

 
Y7 _MAGWNAYIDSLMAD
Y25 QDAAIVGYKDSPSVW
K38 VWAAVPGKTFVSITP
K38 VWAAVPGKTFVSITP
S42 VPGKTFVSITPAEVG
K54 EVGVLVGKDRSSFFV
S57 VLVGKDRSSFFVNGL
F60 GKDRSSFFVNGLTLG
T65 SFFVNGLTLGGQkCS
K70-u GLTLGGQkCSVIRDS
S72 TLGGQkCSVIRDSLL
T85 LLQDGEFTMDLRTKS
K91 FTMDLRTKSTGGAPT
K91 FTMDLRTKSTGGAPT
T93 MDLRTKSTGGAPTFN
M105 TFNVTVTMTAKTLVL
M105 TFNVTVTMTAKTLVL
K108 VTVTMTAKTLVLLMG
K108 VTVTMTAKTLVLLMG
K116 TLVLLMGKEGVHGGL
K126 VHGGLINKKCyEMAS
K126-u VHGGLINkKCyEMAS
K127 HGGLINkKCyEMASH
Y129-p GLINkKCyEMASHLR
S138 MASHLRRSQY_____
  cow

 
Y7 _MAGWNAYIDNLMAD
Y25 QDAAIVGYKDSPSVW
K38 VWAAVPGKTFVNITP
K38 VWAAVPGKTFVNITP
N42 VPGKTFVNITPAEVG
K54 EVGILVGKDRSSFFV
S57 ILVGKDRSSFFVNGL
F60 GKDRSSFFVNGLTLG
T65 SFFVNGLTLGGQKCS
K70 GLTLGGQKCSVIRDS
S72 TLGGQKCSVIRDSLL
T85 LLQDGEFTMDLRTKS
K91 FTMDLRTKSTGGAPT
K91 FTMDLRTKSTGGAPT
T93 MDLRTKSTGGAPTFN
M105 TFNITVTMTAKTLVL
M105 TFNITVTMTAKTLVL
K108 ITVTMTAKTLVLLMG
K108 ITVTMTAKTLVLLMG
K116 TLVLLMGKEGVHGGM
K126 VHGGMINKKCyEMAS
K126 VHGGMINKKCyEMAS
K127 HGGMINKKCyEMASH
Y129-p GMINKKCyEMASHLR
S138-p MASHLRRsQY_____
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