dbPTM

TWF2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TWF2_HUMAN
UniProt AC	Q6IBS0
Protein Name	Twinfilin-2
Gene Name	TWF2
Organism	Homo sapiens (Human).
Sequence Length	349
Subcellular Localization	Cytoplasm, cytoskeleton . Cytoplasm, perinuclear region . Cell projection, stereocilium. Perinuclear and G-actin-rich cortical actin structure sublocalization.
Protein Description	Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles. May play a role in regulating the mature length of the middle and short rows of stereocilia (By similarity)..
Protein Sequence	MAHQTGIHATEELKEFFAKARAGSVRLIKVVIEDEQLVLGASQEPVGRWDQDYDRAVLPLLDAQQPCYLLYRLDSQNAQGFEWLFLAWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDELFGTVKDDLSFAGYQKHLSSCAAPAPLTSAERELQQIRINEVKTEISVESKHQTLQGLAFPLQPEAQRALQQLKQKMVNYIQMKLDLERETIELVHTEPTDVAQLPSRVPRDAARYHFFLYKHTHEGDPLESVVFIYSMPGYKCSIKERMLYSSCKSRLLDSVEQDFHLEIAKKIEIGDGAELTAEFLYDEVHPKQHAFKQAFAKPKGPGGKRGHKRLIRGPGENGDDS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAHQTGIHA ------CCCCCCCCC	11.96	19413330
5	Phosphorylation	---MAHQTGIHATEE ---CCCCCCCCCCHH	28.39	27050516
14	Acetylation	IHATEELKEFFAKAR CCCCHHHHHHHHHHH	56.61	19608861
19	Acetylation	ELKEFFAKARAGSVR HHHHHHHHHHCCCEE	32.99	19608861
24	Phosphorylation	FAKARAGSVRLIKVV HHHHHCCCEEEEEEE	11.77	29514088
98	Acetylation	DNSPVRLKMLYAATR CCCHHHHHHHHHHHH	19.12	25953088
109	Acetylation	AATRATVKKEFGGGH HHHHHHHHHHHCCCC	42.08	12435391
110	Acetylation	ATRATVKKEFGGGHI HHHHHHHHHHCCCCC	54.67	19825739
110	Malonylation	ATRATVKKEFGGGHI HHHHHHHHHHCCCCC	54.67	26320211
118	Acetylation	EFGGGHIKDELFGTV HHCCCCCCCCHHEEC	39.20	26822725
136	Ubiquitination	LSFAGYQKHLSSCAA CCCCCHHHHHHHCCC	37.72	29967540
136	Acetylation	LSFAGYQKHLSSCAA CCCCCHHHHHHHCCC	37.72	26051181
139	O-linked_Glycosylation	AGYQKHLSSCAAPAP CCHHHHHHHCCCCCC	24.08	29351928
139	Phosphorylation	AGYQKHLSSCAAPAP CCHHHHHHHCCCCCC	24.08	23312004
140	Phosphorylation	GYQKHLSSCAAPAPL CHHHHHHHCCCCCCC	17.71	23312004
141	S-nitrosylation	YQKHLSSCAAPAPLT HHHHHHHCCCCCCCC	3.17	2212679
148	Phosphorylation	CAAPAPLTSAERELQ CCCCCCCCHHHHHHH	25.49	50558245
149	Phosphorylation	AAPAPLTSAERELQQ CCCCCCCHHHHHHHH	35.50	25159151
149	O-linked_Glycosylation	AAPAPLTSAERELQQ CCCCCCCHHHHHHHH	35.50	29351928
163	Sumoylation	QIRINEVKTEISVES HHHHCCCCCEEEECC	33.97	-
163	Sumoylation	QIRINEVKTEISVES HHHHCCCCCEEEECC	33.97	-
167	Phosphorylation	NEVKTEISVESKHQT CCCCCEEEECCCCCC	17.38	101544677
171	Ubiquitination	TEISVESKHQTLQGL CEEEECCCCCCHHHH	26.65	29967540
174	Phosphorylation	SVESKHQTLQGLAFP EECCCCCCHHHHHCC	22.29	28555341
194	Acetylation	QRALQQLKQKMVNYI HHHHHHHHHHHHHHH	43.46	25953088
194	Ubiquitination	QRALQQLKQKMVNYI HHHHHHHHHHHHHHH	43.46	29967540
196	Acetylation	ALQQLKQKMVNYIQM HHHHHHHHHHHHHHH	43.14	25953088
200	Phosphorylation	LKQKMVNYIQMKLDL HHHHHHHHHHHHHHH	4.90	25072903
276	Ubiquitination	RMLYSSCKSRLLDSV HHHHHHHHHHHHHHH	40.33	24816145
304	Phosphorylation	IGDGAELTAEFLYDE ECCCCEEEEHHHHCC	18.69	28060719
309	Phosphorylation	ELTAEFLYDEVHPKQ EEEEHHHHCCCCHHH	18.51	27273156
315	Ubiquitination	LYDEVHPKQHAFKQA HHCCCCHHHHHHHHH	39.58	29967540
320	Ubiquitination	HPKQHAFKQAFAKPK CHHHHHHHHHHCCCC	41.31	29967540
325	Ubiquitination	AFKQAFAKPKGPGGK HHHHHHCCCCCCCCC	40.59	27667366
325	Acetylation	AFKQAFAKPKGPGGK HHHHHHCCCCCCCCC	40.59	25953088
340	Methylation	RGHKRLIRGPGENGD CCCCCCCCCCCCCCC	50.25	-
349	Phosphorylation	PGENGDDS------- CCCCCCCC-------	47.03	26846344

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 TWF2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TWF2_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 TWF2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KRT85_HUMAN	KRT85	physical	17353931
K1H1_HUMAN	KRT31	physical	17353931
KRT82_HUMAN	KRT82	physical	17353931
CAZA1_HUMAN	CAPZA1	physical	17353931
CAPZB_HUMAN	CAPZB	physical	17353931
CAZA2_HUMAN	CAPZA2	physical	17353931
KRT36_HUMAN	KRT36	physical	17353931
RB6I2_HUMAN	ERC1	physical	17353931
SCG1_HUMAN	CHGB	physical	16169070
GDIR1_HUMAN	ARHGDIA	physical	21900206
UBAC1_HUMAN	UBAC1	physical	22939629
UBL7_HUMAN	UBL7	physical	22939629
VPS36_HUMAN	VPS36	physical	22939629
UHRF2_HUMAN	UHRF2	physical	22939629
UTP6_HUMAN	UTP6	physical	22939629
ASNS_HUMAN	ASNS	physical	22863883
CAN2_HUMAN	CAPN2	physical	22863883
MCTS1_HUMAN	MCTS1	physical	22863883
PDIA4_HUMAN	PDIA4	physical	22863883
PLPHP_HUMAN	PROSC	physical	22863883
PSMD9_HUMAN	PSMD9	physical	22863883
RISC_HUMAN	SCPEP1	physical	22863883
TBCB_HUMAN	TBCB	physical	22863883
TBB2A_HUMAN	TUBB2A	physical	22863883
UBXN1_HUMAN	UBXN1	physical	22863883
XPO1_HUMAN	XPO1	physical	22863883
1433E_HUMAN	YWHAE	physical	22863883
CAP2_HUMAN	CAP2	physical	28514442
ACTA_HUMAN	ACTA2	physical	28514442
CAP1_HUMAN	CAP1	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442
ACTB_HUMAN	ACTB	physical	28514442
ACTC_HUMAN	ACTC1	physical	28514442

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 TWF2_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]
"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-14 AND LYS-19, AND MASSSPECTROMETRY.	19608861 [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 TYR-309 AND SER-349, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND MASSSPECTROMETRY.	18669648 [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-309, AND MASSSPECTROMETRY.	15592455 [Abstract]