dbPTM

PROF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PROF1_HUMAN
UniProt AC	P07737
Protein Name	Profilin-1
Gene Name	PFN1
Organism	Homo sapiens (Human).
Sequence Length	140
Subcellular Localization	Cytoplasm, cytoskeleton.
Protein Description	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..
Protein Sequence	MAGWNAYIDNLMADGTCQDAAIVGYKDSPSVWAAVPGKTFVNITPAEVGVLVGKDRSSFYVNGLTLGGQKCSVIRDSLLQDGEFSMDLRTKSTGGAPTFNVTVTKTDKTLVLLMGKEGVHGGLINKKCYEMASHLRRSQY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGWNAYID ------CCCHHHHHH	31.54	19413330
7	Phosphorylation	-MAGWNAYIDNLMAD -CCCHHHHHHHHCCC	12.95	28464451
16	Phosphorylation	DNLMADGTCQDAAIV HHHCCCCCCCCEEEE	13.93	23090842
25	Phosphorylation	QDAAIVGYKDSPSVW CCEEEEEECCCCCEE	10.75	23090842
26	Ubiquitination	DAAIVGYKDSPSVWA CEEEEEECCCCCEEE	45.89	29967540
28	Phosphorylation	AIVGYKDSPSVWAAV EEEEECCCCCEEEEC	18.21	30266825
30	Phosphorylation	VGYKDSPSVWAAVPG EEECCCCCEEEECCC	33.95	30266825
38	Acetylation	VWAAVPGKTFVNITP EEEECCCCEEEECCH	32.49	129315
38	Ubiquitination	VWAAVPGKTFVNITP EEEECCCCEEEECCH	32.49	22817900
38	Succinylation	VWAAVPGKTFVNITP EEEECCCCEEEECCH	32.49	23954790
39	Phosphorylation	WAAVPGKTFVNITPA EEECCCCEEEECCHH	38.44	21712546
44	Phosphorylation	GKTFVNITPAEVGVL CCEEEECCHHHEEEE	15.96	23898821
54	Ubiquitination	EVGVLVGKDRSSFYV HEEEEEECCCCCEEE	42.35	27667366
54	Methylation	EVGVLVGKDRSSFYV HEEEEEECCCCCEEE	42.35	66724225
54	Malonylation	EVGVLVGKDRSSFYV HEEEEEECCCCCEEE	42.35	26320211
54	Neddylation	EVGVLVGKDRSSFYV HEEEEEECCCCCEEE	42.35	32015554
54	Sumoylation	EVGVLVGKDRSSFYV HEEEEEECCCCCEEE	42.35	28112733
54	Acetylation	EVGVLVGKDRSSFYV HEEEEEECCCCCEEE	42.35	23954790
54	Ubiquitination	EVGVLVGKDRSSFYV HEEEEEECCCCCEEE	42.35	21890473
54	2-Hydroxyisobutyrylation	EVGVLVGKDRSSFYV HEEEEEECCCCCEEE	42.35	-
56	Methylation	GVLVGKDRSSFYVNG EEEEECCCCCEEECC	37.37	115488893
57	Phosphorylation	VLVGKDRSSFYVNGL EEEECCCCCEEECCE	34.63	25159151
58	Phosphorylation	LVGKDRSSFYVNGLT EEECCCCCEEECCEE	22.84	25159151
60	Phosphorylation	GKDRSSFYVNGLTLG ECCCCCEEECCEEEC	8.58	21712546
60	Nitration	GKDRSSFYVNGLTLG ECCCCCEEECCEEEC	8.58	-
65	Phosphorylation	SFYVNGLTLGGQKCS CEEECCEEECCEEEE	25.42	28152594
70	Malonylation	GLTLGGQKCSVIRDS CEEECCEEEEEEEHH	31.58	26320211
70	Neddylation	GLTLGGQKCSVIRDS CEEECCEEEEEEEHH	31.58	32015554
70	Acetylation	GLTLGGQKCSVIRDS CEEECCEEEEEEEHH	31.58	25953088
70	Ubiquitination	GLTLGGQKCSVIRDS CEEECCEEEEEEEHH	31.58	23000965
70	Ubiquitination	GLTLGGQKCSVIRDS CEEECCEEEEEEEHH	31.58	21890473
72	Phosphorylation	TLGGQKCSVIRDSLL EECCEEEEEEEHHHC	27.84	28152594
77	Phosphorylation	KCSVIRDSLLQDGEF EEEEEEHHHCCCCEE	22.56	27422710
85	Phosphorylation	LLQDGEFSMDLRTKS HCCCCEEEEEEECCC	13.69	22817900
86	Sulfoxidation	LQDGEFSMDLRTKST CCCCEEEEEEECCCC	7.36	21406390
90	Phosphorylation	EFSMDLRTKSTGGAP EEEEEEECCCCCCCC	36.32	30108239
91	Ubiquitination	FSMDLRTKSTGGAPT EEEEEECCCCCCCCE	39.32	23000965
91	Ubiquitination	FSMDLRTKSTGGAPT EEEEEECCCCCCCCE	39.32	21890473
91	2-Hydroxyisobutyrylation	FSMDLRTKSTGGAPT EEEEEECCCCCCCCE	39.32	-
91	Malonylation	FSMDLRTKSTGGAPT EEEEEECCCCCCCCE	39.32	26320211
91	Neddylation	FSMDLRTKSTGGAPT EEEEEECCCCCCCCE	39.32	32015554
91	Acetylation	FSMDLRTKSTGGAPT EEEEEECCCCCCCCE	39.32	26051181
92	Phosphorylation	SMDLRTKSTGGAPTF EEEEECCCCCCCCEE	31.50	25159151
93	Phosphorylation	MDLRTKSTGGAPTFN EEEECCCCCCCCEEE	40.99	25159151
98	Phosphorylation	KSTGGAPTFNVTVTK CCCCCCCEEEEEEEE	27.58	23403867
102	Phosphorylation	GAPTFNVTVTKTDKT CCCEEEEEEEECCCE	24.46	23403867
104	Phosphorylation	PTFNVTVTKTDKTLV CEEEEEEEECCCEEE	20.89	23403867
105	Malonylation	TFNVTVTKTDKTLVL EEEEEEEECCCEEEE	50.84	26320211
105	Ubiquitination	TFNVTVTKTDKTLVL EEEEEEEECCCEEEE	50.84	27667366
105	Neddylation	TFNVTVTKTDKTLVL EEEEEEEECCCEEEE	50.84	32015554
105	Ubiquitination	TFNVTVTKTDKTLVL EEEEEEEECCCEEEE	50.84	21890473
105	Acetylation	TFNVTVTKTDKTLVL EEEEEEEECCCEEEE	50.84	19608861
106	Phosphorylation	FNVTVTKTDKTLVLL EEEEEEECCCEEEEE	33.10	20068231
108	Ubiquitination	VTVTKTDKTLVLLMG EEEEECCCEEEEEEC	49.33	23000965
108	2-Hydroxyisobutyrylation	VTVTKTDKTLVLLMG EEEEECCCEEEEEEC	49.33	-
108	Acetylation	VTVTKTDKTLVLLMG EEEEECCCEEEEEEC	49.33	19608861
108	Malonylation	VTVTKTDKTLVLLMG EEEEECCCEEEEEEC	49.33	26320211
108	Ubiquitination	VTVTKTDKTLVLLMG EEEEECCCEEEEEEC	49.33	21890473
109	Phosphorylation	TVTKTDKTLVLLMGK EEEECCCEEEEEECC	25.55	20068231
114	Sulfoxidation	DKTLVLLMGKEGVHG CCEEEEEECCCCCCC	6.70	21406390
116	Ubiquitination	TLVLLMGKEGVHGGL EEEEEECCCCCCCCC	37.01	33845483
116	Succinylation	TLVLLMGKEGVHGGL EEEEEECCCCCCCCC	37.01	23954790
116	2-Hydroxyisobutyrylation	TLVLLMGKEGVHGGL EEEEEECCCCCCCCC	37.01	-
116	Neddylation	TLVLLMGKEGVHGGL EEEEEECCCCCCCCC	37.01	32015554
116	Acetylation	TLVLLMGKEGVHGGL EEEEEECCCCCCCCC	37.01	25953088
126	2-Hydroxyisobutyrylation	VHGGLINKKCYEMAS CCCCCCCHHHHHHHH	36.91	-
126	Ubiquitination	VHGGLINKKCYEMAS CCCCCCCHHHHHHHH	36.91	27667366
126	Ubiquitination	VHGGLINKKCYEMAS CCCCCCCHHHHHHHH	36.91	21890473
126	Acetylation	VHGGLINKKCYEMAS CCCCCCCHHHHHHHH	36.91	23749302
126	Succinylation	VHGGLINKKCYEMAS CCCCCCCHHHHHHHH	36.91	23954790
126	Neddylation	VHGGLINKKCYEMAS CCCCCCCHHHHHHHH	36.91	32015554
127	Acetylation	HGGLINKKCYEMASH CCCCCCHHHHHHHHH	37.25	26051181
127	Ubiquitination	HGGLINKKCYEMASH CCCCCCHHHHHHHHH	37.25	22817900
127	2-Hydroxyisobutyrylation	HGGLINKKCYEMASH CCCCCCHHHHHHHHH	37.25	-
128	Glutathionylation	GGLINKKCYEMASHL CCCCCHHHHHHHHHH	3.57	22555962
128	S-palmitoylation	GGLINKKCYEMASHL CCCCCHHHHHHHHHH	3.57	29575903
128	S-nitrosylation	GGLINKKCYEMASHL CCCCCHHHHHHHHHH	3.57	25040305
129	Phosphorylation	GLINKKCYEMASHLR CCCCHHHHHHHHHHH	20.02	27273156
129	Nitration	GLINKKCYEMASHLR CCCCHHHHHHHHHHH	20.02	-
131	Sulfoxidation	INKKCYEMASHLRRS CCHHHHHHHHHHHHH	1.55	30846556
133	Phosphorylation	KKCYEMASHLRRSQY HHHHHHHHHHHHHCC	23.03	26356563
138	Phosphorylation	MASHLRRSQY----- HHHHHHHHCC-----	27.65	28112733
140	Phosphorylation	SHLRRSQY------- HHHHHHCC-------	23.05	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
129	Y	Phosphorylation	Kinase	SRC	P12931	PSP
129	Y	Phosphorylation	Kinase	KDR	P35968	GPS
138	S	Phosphorylation	Kinase	ROCK1	Q13464	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
138	S	Phosphorylation		18573880
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.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PROF1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ACTB_HUMAN	ACTB	physical	10411937
ERG28_HUMAN	C14orf1	physical	16169070
DLG5_HUMAN	DLG5	physical	16169070
TLE1_HUMAN	TLE1	physical	16169070
DPYL1_HUMAN	CRMP1	physical	16169070
LRIF1_HUMAN	LRIF1	physical	16169070
U119A_HUMAN	UNC119	physical	16169070
WASF1_HUMAN	WASF1	physical	9843499
RHOQ_HUMAN	RHOQ	physical	10445846
VIPR1_HUMAN	VIPR1	physical	10867004
WASL_HUMAN	WASL	physical	10867004
FMNL1_HUMAN	FMNL1	physical	10958683
ENAH_HUMAN	ENAH	physical	9473484
GEPH_HUMAN	GPHN	physical	9473484
THIM_HUMAN	ACAA2	physical	22939629
SET_HUMAN	SET	physical	22939629
SRPRB_HUMAN	SRPRB	physical	22939629
RM53_HUMAN	MRPL53	physical	22939629
RAD51_HUMAN	RAD51	physical	19338310
ESR1_HUMAN	ESR1	physical	23576398
CHIP_HUMAN	STUB1	physical	24661873
COF1_HUMAN	CFL1	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614808	Amyotrophic lateral sclerosis 18 (ALS18)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PROF1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"The primary structure of human platelet profilin: reinvestigation ofthe calf spleen profilin sequence."; Ampe C., Markey F., Lindberg U., Vandekerckhove J.; FEBS Lett. 228:17-21(1988). Cited for: PROTEIN SEQUENCE OF 2-140, AND ACETYLATION AT ALA-2.	3342873 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105 AND LYS-108, AND MASSSPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105, AND MASS SPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Phosphorylation of profilin by ROCK1 regulates polyglutamineaggregation."; Shao J., Welch W.J., Diprospero N.A., Diamond M.I.; Mol. Cell. Biol. 28:5196-5208(2008). Cited for: FUNCTION, INTERACTION WITH HTT, AND PHOSPHORYLATION AT SER-138.	18573880 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129, AND MASSSPECTROMETRY.	15592455 [Abstract]
Ubiquitylation
Reference	PubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-54, AND MASSSPECTROMETRY.	18781797 [Abstract]

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