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profilin 1 (human)

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: Motility/polarity/chemotaxis; Actin binding protein; Cytoskeletal protein Cellular Component: cytoplasm; synapse; nucleus; actin cytoskeleton Molecular Function: protein binding; phosphatidylinositol-4,5-bisphosphate binding; Rho GTPase binding; actin binding; receptor binding Biological Process: positive regulation of DNA metabolic process; platelet activation; platelet degranulation; positive regulation of viral transcription; positive regulation of stress fiber formation; neural tube closure; positive regulation of transcription from RNA polymerase II promoter; actin cytoskeleton organization and biogenesis; blood coagulation 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:  Regulation of Actin Dynamics Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below profilin 1 1AWI - A/B=3-140 (human) 1CF0 - A/B=3-140 (human) 1CJF - A/B=1-140 (human) 1FIK - A=1-140 (human) 1FIL - A=1-140 (human) 1PFL - A=1-140 (human) 2PAV - P=2-140 (human) 2PBD - P=2-140 (human) 3CHW - P=2-140 (human) 1HLU - P=1-140 (cow) 1PNE - A=1-140 (cow) 2BTF - P=1-140 (cow) 3U4L - P=2-140 (cow) 3UB5 - P=2-140 (cow)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1AWI 1CF0 1CJF 1FIK 1FIL 1PFL 2PAV 2PBD 3CHW  |  Phospho3D  |  DISEASE  |  Source  |  InnateDB  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Sites Implicated In
inhibition: 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

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
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	1		T90-p	EFsMDLRtkStGGAP
0	2		K91-a	FsMDLRtkStGGAPT
0	16		K91-u	FsMDLRtkStGGAPT
0	1		T93-p	MDLRtkStGGAPTFN
0	1		T102-p	GAPTFNVtVtktDkT
0	1		T104-p	PTFNVtVtktDkTLV
0	3		K105-a	TFNVtVtktDkTLVL
0	96		K105-u	TFNVtVtktDkTLVL
0	1		T106-p	FNVtVtktDkTLVLL
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	653		Y129-p	GLINkkCyEMAsHLR
0	1		S133-p	kkCyEMAsHLRRsQy
5	0		S138-p	MAsHLRRsQy_____
0	1		Y140-p	sHLRRsQy_______

	mouse
Y7	_MAGWNAYIDSLMAD
Y25	QDAAIVGYKDSPSVW
K38	VWAAVPGKTFVsITP
K38	VWAAVPGKTFVsITP
S42-p	VPGKTFVsITPAEVG
K54-u	EVGVLVGkDRSSFFV
F60	GkDRSSFFVNGLtLG
T65-p	SFFVNGLtLGGQkCS
K70-u	GLtLGGQkCSVIRDS
S72	tLGGQkCSVIRDSLL
T85	LLQDGEFTMDLRTKS
T90	EFTMDLRTKSTGGAP
K91	FTMDLRTKSTGGAPT
K91	FTMDLRTKSTGGAPT
T93	MDLRTKSTGGAPTFN
T102	GAPTFNVTVTMTAKT
T104	PTFNVTVTMTAKTLV
M105	TFNVTVTMTAKTLVL
M105	TFNVTVTMTAKTLVL
T106	FNVTVTMTAKTLVLL
K108	VTVTMTAKTLVLLMG
K108	VTVTMTAKTLVLLMG
K116-u	TLVLLMGkEGVHGGL
K126	VHGGLINKkCyEMAS
K126-u	VHGGLINkkCyEMAS
K127-u	HGGLINkkCyEMASH
Y129-p	GLINkkCyEMASHLR
S133	kkCyEMASHLRRsQY
S138-p	MASHLRRsQY_____
Y140	SHLRRsQY_______

	rat
Y7	_MAGWNAYIDSLMAD
Y25	QDAAIVGYKDSPSVW
K38	VWAAVPGKTFVSITP
K38	VWAAVPGKTFVSITP
S42	VPGKTFVSITPAEVG
K54	EVGVLVGKDRSSFFV
F60	GKDRSSFFVNGLTLG
T65	SFFVNGLTLGGQkCS
K70-u	GLTLGGQkCSVIRDS
S72	TLGGQkCSVIRDSLL
T85	LLQDGEFTMDLRTKS
T90	EFTMDLRTKSTGGAP
K91	FTMDLRTKSTGGAPT
K91	FTMDLRTKSTGGAPT
T93	MDLRTKSTGGAPTFN
T102	GAPTFNVTVTMTAKT
T104	PTFNVTVTMTAKTLV
M105	TFNVTVTMTAKTLVL
M105	TFNVTVTMTAKTLVL
T106	FNVTVTMTAKTLVLL
K108	VTVTMTAKTLVLLMG
K108	VTVTMTAKTLVLLMG
K116	TLVLLMGKEGVHGGL
K126	VHGGLINKKCyEMAS
K126-u	VHGGLINkKCyEMAS
K127	HGGLINkKCyEMASH
Y129-p	GLINkKCyEMASHLR
S133	kKCyEMASHLRRSQY
S138	MASHLRRSQY_____
Y140	SHLRRSQY_______

	cow
Y7	_MAGWNAYIDNLMAD
Y25	QDAAIVGYKDSPSVW
K38	VWAAVPGKTFVNITP
K38	VWAAVPGKTFVNITP
N42	VPGKTFVNITPAEVG
K54	EVGILVGKDRSSFFV
F60	GKDRSSFFVNGLTLG
T65	SFFVNGLTLGGQKCS
K70	GLTLGGQKCSVIRDS
S72	TLGGQKCSVIRDSLL
T85	LLQDGEFTMDLRTKS
T90	EFTMDLRTKSTGGAP
K91	FTMDLRTKSTGGAPT
K91	FTMDLRTKSTGGAPT
T93	MDLRTKSTGGAPTFN
T102	GAPTFNITVTMTAKT
T104	PTFNITVTMTAKTLV
M105	TFNITVTMTAKTLVL
M105	TFNITVTMTAKTLVL
T106	FNITVTMTAKTLVLL
K108	ITVTMTAKTLVLLMG
K108	ITVTMTAKTLVLLMG
K116	TLVLLMGKEGVHGGM
K126	VHGGMINKKCyEMAS
K126	VHGGMINKKCyEMAS
K127	HGGMINKKCyEMASH
Y129-p	GMINKKCyEMASHLR
S133	KKCyEMASHLRRsQY
S138-p	MASHLRRsQY_____
Y140	SHLRRsQY_______

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