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Protein Page:
profilin 1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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: Cytoskeletal protein; Motility/polarity/chemotaxis; Actin binding protein
Cellular Component: neuron projection; cytoskeleton; membrane; synapse; nucleus; cytosol
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; neural tube closure; positive regulation of stress fiber formation; 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.


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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 2 S28-p AIVGyKDsPsVWAAV
0 1 S30-p VGyKDsPsVWAAVPG
0 4 K38-ac VWAAVPGktFVNITP
0 3 K38-ub VWAAVPGktFVNITP
0 1 K38-sc VWAAVPGktFVNITP
0 1 T39-p WAAVPGktFVNITPA
0 2 N42 VPGktFVNITPAEVG
0 1 K54-ac EVGVLVGkDRsSFyV
0 112 K54-ub EVGVLVGkDRsSFyV
0 1 K54-sc EVGVLVGkDRsSFyV
0 1 S57-p VLVGkDRsSFyVNGL
1 61 Y60-p GkDRsSFyVNGLtLG
0 5 T65-p SFyVNGLtLGGQkCs
0 89 K70-ub GLtLGGQkCsVIRDs
0 1 K70-sc GLtLGGQkCsVIRDs
0 1 S72-p tLGGQkCsVIRDsLL
0 1 S77-p kCsVIRDsLLQDGEF
0 2 S85-p LLQDGEFsMDLRtkS
0 1 T90-p EFsMDLRtkStGGAP
0 2 K91-ac FsMDLRtkStGGAPt
0 16 K91-ub FsMDLRtkStGGAPt
0 2 T93-p MDLRtkStGGAPtFN
0 3 T98-p kStGGAPtFNVtVtk
0 1 T102-p GAPtFNVtVtktDkt
0 1 T104-p PtFNVtVtktDktLV
0 4 K105-ac tFNVtVtktDktLVL
0 96 K105-ub tFNVtVtktDktLVL
0 1 K105-sc tFNVtVtktDktLVL
0 1 T106-p FNVtVtktDktLVLL
0 3 K108-ac VtVtktDktLVLLMG
0 4 K108-ub VtVtktDktLVLLMG
0 2 T109-p tVtktDktLVLLMGk
0 1 K116 tLVLLMGKEGVHGGL
0 1 K116-sc tLVLLMGkEGVHGGL
0 13 K126-ac VHGGLINkkCyEMAs
0 85 K126-ub VHGGLINkkCyEMAs
0 1 K126-sc VHGGLINkkCyEMAs
0 4 K127-ub HGGLINkkCyEMAsH
2 661 Y129-p GLINkkCyEMAsHLR
0 1 S133-p kkCyEMAsHLRRsQy
6 0 S138-p MAsHLRRsQy_____
0 1 Y140-p sHLRRsQy_______
  mouse

 
Y7 _MAGWNAYIDSLMAD
Y25 QDAAIVGYKDsPSVW
S28-p AIVGYKDsPSVWAAV
S30 VGYKDsPSVWAAVPG
K38 VWAAVPGKTFVsITP
K38 VWAAVPGKTFVsITP
K38-sc VWAAVPGkTFVsITP
T39 WAAVPGkTFVsITPA
S42-p VPGkTFVsITPAEVG
K54 EVGVLVGKDRSSFFV
K54-ub EVGVLVGkDRSSFFV
K54-sc EVGVLVGkDRSSFFV
S57 VLVGkDRSSFFVNGL
F60 GkDRSSFFVNGLtLG
T65-p SFFVNGLtLGGQkCS
K70-ub GLtLGGQkCSVIRDS
K70 GLtLGGQKCSVIRDS
S72 tLGGQkCSVIRDSLL
S77 kCSVIRDSLLQDGEF
T85 LLQDGEFTMDLRTKS
T90 EFTMDLRTKSTGGAP
K91 FTMDLRTKSTGGAPT
K91 FTMDLRTKSTGGAPT
T93 MDLRTKSTGGAPTFN
T98 KSTGGAPTFNVTVTM
T102 GAPTFNVTVTMTAKT
T104 PTFNVTVTMTAKTLV
M105 TFNVTVTMTAKTLVL
M105 TFNVTVTMTAKTLVL
M105 TFNVTVTMTAKTLVL
T106 FNVTVTMTAKTLVLL
K108 VTVTMTAKTLVLLMG
K108 VTVTMTAKTLVLLMG
T109 TVTMTAKTLVLLMGk
K116-ub TLVLLMGkEGVHGGL
K116 TLVLLMGKEGVHGGL
K126 VHGGLINKkCyEMAS
K126-ub VHGGLINkkCyEMAS
K126 VHGGLINKkCyEMAS
K127-ub HGGLINkkCyEMASH
Y129-p GLINkkCyEMASHLR
S133 kkCyEMASHLRRsQY
S138-p MASHLRRsQY_____
Y140 SHLRRsQY_______
  rat

 
Y7 _MAGWNAYIDSLMAD
Y25 QDAAIVGYKDsPsVW
S28-p AIVGYKDsPsVWAAV
S30-p VGYKDsPsVWAAVPG
K38 VWAAVPGKTFVSITP
K38 VWAAVPGKTFVSITP
K38 VWAAVPGKTFVSITP
T39 WAAVPGKTFVSITPA
S42 VPGKTFVSITPAEVG
K54-ac EVGVLVGkDRSSFFV
K54 EVGVLVGKDRSSFFV
K54 EVGVLVGKDRSSFFV
S57 VLVGkDRSSFFVNGL
F60 GkDRSSFFVNGLTLG
T65 SFFVNGLTLGGQkCS
K70-ub GLTLGGQkCSVIRDS
K70 GLTLGGQKCSVIRDS
S72 TLGGQkCSVIRDSLL
S77 kCSVIRDSLLQDGEF
T85 LLQDGEFTMDLRTKS
T90 EFTMDLRTKSTGGAP
K91 FTMDLRTKSTGGAPT
K91 FTMDLRTKSTGGAPT
T93 MDLRTKSTGGAPTFN
T98 KSTGGAPTFNVTVTM
T102 GAPTFNVTVTMTAKT
T104 PTFNVTVTMTAKTLV
M105 TFNVTVTMTAKTLVL
M105 TFNVTVTMTAKTLVL
M105 TFNVTVTMTAKTLVL
T106 FNVTVTMTAKTLVLL
K108 VTVTMTAKTLVLLMG
K108 VTVTMTAKTLVLLMG
T109 TVTMTAKTLVLLMGK
K116 TLVLLMGKEGVHGGL
K116 TLVLLMGKEGVHGGL
K126 VHGGLINKKCyEMAS
K126-ub VHGGLINkKCyEMAS
K126 VHGGLINKKCyEMAS
K127 HGGLINkKCyEMASH
Y129-p GLINkKCyEMASHLR
S133 kKCyEMASHLRRSQY
S138 MASHLRRSQY_____
Y140 SHLRRSQY_______
  cow

 
Y7 _MAGWNAYIDNLMAD
Y25 QDAAIVGYKDSPSVW
S28 AIVGYKDSPSVWAAV
S30 VGYKDSPSVWAAVPG
K38 VWAAVPGKTFVNITP
K38 VWAAVPGKTFVNITP
K38 VWAAVPGKTFVNITP
T39 WAAVPGKTFVNITPA
N42 VPGKTFVNITPAEVG
K54 EVGILVGKDRSSFFV
K54 EVGILVGKDRSSFFV
K54 EVGILVGKDRSSFFV
S57 ILVGKDRSSFFVNGL
F60 GKDRSSFFVNGLTLG
T65 SFFVNGLTLGGQKCS
K70 GLTLGGQKCSVIRDS
K70 GLTLGGQKCSVIRDS
S72 TLGGQKCSVIRDSLL
S77 KCSVIRDSLLQDGEF
T85 LLQDGEFTMDLRTKS
T90 EFTMDLRTKSTGGAP
K91 FTMDLRTKSTGGAPT
K91 FTMDLRTKSTGGAPT
T93 MDLRTKSTGGAPTFN
T98 KSTGGAPTFNITVTM
T102 GAPTFNITVTMTAKT
T104 PTFNITVTMTAKTLV
M105 TFNITVTMTAKTLVL
M105 TFNITVTMTAKTLVL
M105 TFNITVTMTAKTLVL
T106 FNITVTMTAKTLVLL
K108 ITVTMTAKTLVLLMG
K108 ITVTMTAKTLVLLMG
T109 TVTMTAKTLVLLMGK
K116 TLVLLMGKEGVHGGM
K116 TLVLLMGKEGVHGGM
K126 VHGGMINKKCyEMAS
K126 VHGGMINKKCyEMAS
K126 VHGGMINKKCyEMAS
K127 HGGMINKKCyEMASH
Y129-p GMINKKCyEMASHLR
S133 KKCyEMASHLRRsQY
S138-p MASHLRRsQY_____
Y140 SHLRRsQY_______
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