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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 Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
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: Actin-binding; Cytoskeletal; Motility/polarity/chemotaxis
Chromosomal Location of Human Ortholog: 17p13.3
Cellular Component: cell cortex; cytoplasm; cytosol; focal adhesion; membrane; nucleus
Molecular Function: actin binding; actin monomer binding; adenyl-nucleotide exchange factor activity; phosphatidylinositol-4,5-bisphosphate binding; protein binding
Biological Process: negative regulation of actin filament bundle formation; negative regulation of actin filament polymerization; negative regulation of stress fiber formation; positive regulation of actin filament bundle formation; positive regulation of actin filament polymerization; positive regulation of ATPase activity; protein stabilization; Wnt receptor signaling pathway, planar cell polarity pathway
Disease: Amyotrophic Lateral Sclerosis 18
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
apoptosis, inhibited: S138‑p
carcinogenesis, induced: Y129‑p, S138‑p
cell cycle regulation: S138‑p
transcription, induced: Y129‑p
activity, inhibited: S138‑p
molecular association, regulation: Y60‑p, Y129‑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



 LTP 

LTP: 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.


 HTP 

HTP: 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 S28‑p AIVGyKDsPsVWAAV
0 2 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 T44‑p GktFVNItPAEVGVL
0 3 K54‑ac EVGVLVGkDRsSFyV
0 112 K54‑ub EVGVLVGkDRsSFyV
0 1 K54‑sc EVGVLVGkDRsSFyV
1 4 S57‑p VLVGkDRsSFyVNGL
1 1 S58 LVGkDRsSFyVNGLt
1 63 Y60‑p GkDRsSFyVNGLtLG
0 6 T65‑p SFyVNGLtLGGQkCs
0 90 K70‑ub GLtLGGQkCsVIRDs
0 1 K70‑sc GLtLGGQkCsVIRDs
0 3 S72‑p tLGGQkCsVIRDsLL
0 1 S77‑p kCsVIRDsLLQDGEF
0 3 S85‑p LLQDGEFsMDLRtks
1 2 T90‑p EFsMDLRtkstGGAP
0 2 K91‑ac FsMDLRtkstGGAPt
0 17 K91‑ub FsMDLRtkstGGAPt
1 4 S92‑p sMDLRtkstGGAPtF
1 5 T93‑p MDLRtkstGGAPtFN
0 4 T98‑p kstGGAPtFNVtVtk
0 1 T102‑p GAPtFNVtVtktDkt
0 2 T104‑p PtFNVtVtktDktLV
0 5 K105‑ac tFNVtVtktDktLVL
0 97 K105‑ub tFNVtVtktDktLVL
0 1 K105‑sc tFNVtVtktDktLVL
0 1 T106‑p FNVtVtktDktLVLL
0 4 K108‑ac VtVtktDktLVLLMG
0 5 K108‑ub VtVtktDktLVLLMG
1 2 T109‑p tVtktDktLVLLMGk
0 1 K116 tLVLLMGKEGVHGGL
0 1 K116‑sc tLVLLMGkEGVHGGL
0 14 K126‑ac VHGGLINkkCyEMAs
0 87 K126‑ub VHGGLINkkCyEMAs
0 1 K126‑sc VHGGLINkkCyEMAs
0 4 K127‑ub HGGLINkkCyEMAsH
2 663 Y129‑p GLINkkCyEMAsHLR
0 1 S133‑p kkCyEMAsHLRRsQy
7 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
T44 GkTFVsITPAEVGVL
K54 EVGVLVGKDRssFFV
K54‑ub EVGVLVGkDRssFFV
K54‑sc EVGVLVGkDRssFFV
S57‑p VLVGkDRssFFVNGL
S58‑p LVGkDRssFFVNGLt
F60 GkDRssFFVNGLtLG
T65‑p sFFVNGLtLGGQkCS
K70‑ub GLtLGGQkCSVIRDS
K70 GLtLGGQKCSVIRDS
S72 tLGGQkCSVIRDSLL
S77 kCSVIRDSLLQDGEF
T85 LLQDGEFTMDLRtKs
T90‑p EFTMDLRtKstGGAP
K91 FTMDLRtKstGGAPT
K91 FTMDLRtKstGGAPT
S92‑p TMDLRtKstGGAPTF
T93‑p 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
T44 GKTFVSITPAEVGVL
K54‑ac EVGVLVGkDRSSFFV
K54 EVGVLVGKDRSSFFV
K54 EVGVLVGKDRSSFFV
S57 VLVGkDRSSFFVNGL
S58 LVGkDRSSFFVNGLT
F60 GkDRSSFFVNGLTLG
T65 SFFVNGLTLGGQkCS
K70‑ub GLTLGGQkCSVIRDS
K70 GLTLGGQKCSVIRDS
S72 TLGGQkCSVIRDSLL
S77 kCSVIRDSLLQDGEF
T85 LLQDGEFTMDLRTKS
T90 EFTMDLRTKSTGGAP
K91 FTMDLRTKSTGGAPT
K91 FTMDLRTKSTGGAPT
S92 TMDLRTKSTGGAPTF
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
T44 GKTFVNITPAEVGIL
K54 EVGILVGKDRSSFFV
K54 EVGILVGKDRSSFFV
K54 EVGILVGKDRSSFFV
S57 ILVGKDRSSFFVNGL
S58 LVGKDRSSFFVNGLT
F60 GKDRSSFFVNGLTLG
T65 SFFVNGLTLGGQKCS
K70 GLTLGGQKCSVIRDS
K70 GLTLGGQKCSVIRDS
S72 TLGGQKCSVIRDSLL
S77 KCSVIRDSLLQDGEF
T85 LLQDGEFTMDLRTKS
T90 EFTMDLRTKSTGGAP
K91 FTMDLRTKSTGGAPT
K91 FTMDLRTKSTGGAPT
S92 TMDLRTKSTGGAPTF
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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