dbPTM

PROF2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PROF2_HUMAN
UniProt AC	P35080
Protein Name	Profilin-2
Gene Name	PFN2
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..
Protein Sequence	MAGWQSYVDNLMCDGCCQEAAIVGYCDAKYVWAATAGGVFQSITPIEIDMIVGKDREGFFTNGLTLGAKKCSVIRDSLYVDGDCTMDIRTKSQGGEPTYNVAVGRAGRVLVFVMGKEGVHGGGLNKKAYSMAKYLRDSGF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGWQSYVD ------CCCHHHHHH	28.12	22223895
6	Phosphorylation	--MAGWQSYVDNLMC --CCCHHHHHHHCCC	22.18	18491316
7	Phosphorylation	-MAGWQSYVDNLMCD -CCCHHHHHHHCCCC	9.20	18491316
61	Phosphorylation	KDREGFFTNGLTLGA CCCCCCCCCCEEECC	26.56	23403867
65	Phosphorylation	GFFTNGLTLGAKKCS CCCCCCEEECCEECC	25.25	23403867
69 (in isoform 2)	Ubiquitination	-	53.14	-
69	Ubiquitination	NGLTLGAKKCSVIRD CCEEECCEECCEECC	53.14	32015554
69	Acetylation	NGLTLGAKKCSVIRD CCEEECCEECCEECC	53.14	25953088
70	Ubiquitination	GLTLGAKKCSVIRDS CEEECCEECCEECCE	31.07	23503661
72	Phosphorylation	TLGAKKCSVIRDSLY EECCEECCEECCEEE	29.47	21406692
77	Phosphorylation	KCSVIRDSLYVDGDC ECCEECCEEEECCCC	16.26	21406692
79	Phosphorylation	SVIRDSLYVDGDCTM CEECCEEEECCCCEE	10.63	21406692
84	Glutathionylation	SLYVDGDCTMDIRTK EEEECCCCEEEEEEC	4.09	22555962
85	Phosphorylation	LYVDGDCTMDIRTKS EEECCCCEEEEEECC	23.71	21406692
86	Sulfoxidation	YVDGDCTMDIRTKSQ EECCCCEEEEEECCC	5.18	30846556
91	Ubiquitination	CTMDIRTKSQGGEPT CEEEEEECCCCCCCE	30.82	32142685
91 (in isoform 1)	Ubiquitination	-	30.82	21906983
91 (in isoform 2)	Ubiquitination	-	30.82	21890473
92	Phosphorylation	TMDIRTKSQGGEPTY EEEEEECCCCCCCEE	33.18	26356563
98	Phosphorylation	KSQGGEPTYNVAVGR CCCCCCCEEEEEEEC	24.35	28152594
99	Nitration	SQGGEPTYNVAVGRA CCCCCCEEEEEEECC	20.53	-
99	Phosphorylation	SQGGEPTYNVAVGRA CCCCCCEEEEEEECC	20.53	21082442
105	Methylation	TYNVAVGRAGRVLVF EEEEEEECCCCEEEE	27.54	115488903
114	Sulfoxidation	GRVLVFVMGKEGVHG CCEEEEEECCCCCCC	4.27	30846556
123 (in isoform 2)	Phosphorylation	-	30.57	25849741
126	Ubiquitination	VHGGGLNKKAYSMAK CCCCCCCHHHHHHHH	43.77	23000965
127	Ubiquitination	HGGGLNKKAYSMAKY CCCCCCHHHHHHHHH	52.03	23000965
127 (in isoform 2)	Ubiquitination	-	52.03	21890473
129	Phosphorylation	GGLNKKAYSMAKYLR CCCCHHHHHHHHHHH	14.09	26437602
129 (in isoform 2)	Phosphorylation	-	14.09	28152594
133	Acetylation	KKAYSMAKYLRDSGF HHHHHHHHHHHHCCC	35.85	23236377
134 (in isoform 2)	Phosphorylation	-	9.46	24927040

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
Oops, there are no upstream regulatory protein records of PROF2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PROF2_HUMAN !!

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 PROF2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FHOD1_HUMAN	FHOD1	physical	12677009
ROCK1_HUMAN	ROCK1	physical	14517206
MO4L1_MOUSE	Morf4l1	physical	12391155
SIN3A_HUMAN	SIN3A	physical	12391155
VASP_HUMAN	VASP	physical	7737110
EVL_HUMAN	EVL	physical	10945997
FMNL1_HUMAN	FMNL1	physical	10958683
HD_HUMAN	HTT	physical	15383276
NAT6_HUMAN	NAT6	physical	28514442
INF2_HUMAN	INF2	physical	28514442
PALLD_HUMAN	PALLD	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442
ACTA_HUMAN	ACTA2	physical	28514442
ACTB_HUMAN	ACTB	physical	28514442
DIAP1_HUMAN	DIAPH1	physical	28514442
BLVRB_HUMAN	BLVRB	physical	28514442
ENAH_HUMAN	ENAH	physical	28514442
VASP_HUMAN	VASP	physical	28514442
GELS_HUMAN	GSN	physical	27173435
EIF3K_HUMAN	EIF3K	physical	27173435
ARPC4_HUMAN	ARPC4	physical	27173435
SESD1_HUMAN	SESTD1	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PROF2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-99, AND MASSSPECTROMETRY.	18083107 [Abstract]