dbPTM

FHOD1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FHOD1_HUMAN
UniProt AC	Q9Y613
Protein Name	FH1/FH2 domain-containing protein 1
Gene Name	FHOD1
Organism	Homo sapiens (Human).
Sequence Length	1164
Subcellular Localization	Cytoplasm. Cytoplasm, cytoskeleton. Cell projection, bleb. Predominantly cytoplasmic.
Protein Description	Required for the assembly of F-actin structures, such as stress fibers. Depends on the Rho-ROCK cascade for its activity. Contributes to the coordination of microtubules with actin fibers and plays a role in cell elongation. Acts synergistically with ROCK1 to promote SRC-dependent non-apoptotic plasma membrane blebbing..
Protein Sequence	MAGGEDRGDGEPVSVVTVRVQYLEDTDPFACANFPEPRRAPTCSLDGALPLGAQIPAVHRLLGAPLKLEDCALQVSPSGYYLDTELSLEEQREMLEGFYEEISKGRKPTLILRTQLSVRVNAILEKLYSSSGPELRRSLFSLKQIFQEDKDLVPEFVHSEGLSCLIRVGAAADHNYQSYILRALGQLMLFVDGMLGVVAHSDTIQWLYTLCASLSRLVVKTALKLLLVFVEYSENNAPLFIRAVNSVASTTGAPPWANLVSILEEKNGADPELLVYTVTLINKTLAALPDQDSFYDVTDALEQQGMEALVQRHLGTAGTDVDLRTQLVLYENALKLEDGDIEEAPGAGGRRERRKPSSEEGKRSRRSLEGGGCPARAPEPGPTGPASPVGPTSSTGPALLTGPASSPVGPPSGLQASVNLFPTISVAPSADTSSERSIYKARFLENVAAAETEKQVALAQGRAETLAGAMPNEAGGHPDARQLWDSPETAPAARTPQSPAPCVLLRAQRSLAPEPKEPLIPASPKAEPIWELPTRAPRLSIGDLDFSDLGEDEDQDMLNVESVEAGKDIPAPSPPLPLLSGVPPPPPLPPPPPIKGPFPPPPPLPLAAPLPHSVPDSSALPTKRKTVKLFWRELKLAGGHGVSASRFGPCATLWASLDPVSVDTARLEHLFESRAKEVLPSKKAGEGRRTMTTVLDPKRSNAINIGLTTLPPVHVIKAALLNFDEFAVSKDGIEKLLTMMPTEEERQKIEEAQLANPDIPLGPAENFLMTLASIGGLAARLQLWAFKLDYDSMEREIAEPLFDLKVGMEQLVQNATFRCILATLLAVGNFLNGSQSSGFELSYLEKVSEVKDTVRRQSLLHHLCSLVLQTRPESSDLYSEIPALTRCAKVDFEQLTENLGQLERRSRAAEESLRSLAKHELAPALRARLTHFLDQCARRVAMLRIVHRRVCNRFHAFLLYLGYTPQAAREVRIMQFCHTLREFALEYRTCRERVLQQQQKQATYRERNKTRGRMITETEKFSGVAGEAPSNPSVPVAVSSGPGRGDADSHASMKSLLTSRPEDTTHNRRSRGMVQSSSPIMPTVGPSTASPEEPPGSSLPSDTSDEIMDLLVQSVTKSSPRALAARERKRSRGNRKSLRRTLKSGLGDDLVQALGLSKGPGLEV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
31	Glutathionylation	EDTDPFACANFPEPR CCCCCCCCCCCCCCC	3.04	22555962
99	Phosphorylation	REMLEGFYEEISKGR HHHHHHHHHHHHCCC	24.41	-
107	Malonylation	EEISKGRKPTLILRT HHHHCCCCCEEEEEE	51.53	26320211
126	Ubiquitination	RVNAILEKLYSSSGP HHHHHHHHHHHCCCH	49.64	-
141	Phosphorylation	ELRRSLFSLKQIFQE HHHHHHHHHHHHHHH	39.69	24719451
176	Phosphorylation	GAAADHNYQSYILRA CCCCCCCHHHHHHHH	8.73	-
213	Phosphorylation	WLYTLCASLSRLVVK HHHHHHHHHHHHHHH	26.36	27174698
215	Phosphorylation	YTLCASLSRLVVKTA HHHHHHHHHHHHHHH	22.52	27174698
250	Phosphorylation	AVNSVASTTGAPPWA HHHHHHHCCCCCCCH	21.36	30576142
251	Phosphorylation	VNSVASTTGAPPWAN HHHHHHCCCCCCCHH	28.93	30576142
261	Phosphorylation	PPWANLVSILEEKNG CCCHHHHHHHHHHCC	25.31	30576142
335	Ubiquitination	VLYENALKLEDGDIE HHHCCCEECCCCCCC	47.63	-
357	Phosphorylation	RRERRKPSSEEGKRS CCCCCCCCCHHHHHH	54.11	30576142
358	Phosphorylation	RERRKPSSEEGKRSR CCCCCCCCHHHHHHH	48.47	26699800
364	Phosphorylation	SSEEGKRSRRSLEGG CCHHHHHHHHHHCCC	35.22	23403867
367	Phosphorylation	EGKRSRRSLEGGGCP HHHHHHHHHCCCCCC	29.66	29255136
387	Phosphorylation	PGPTGPASPVGPTSS CCCCCCCCCCCCCCC	24.21	28348404
401	Phosphorylation	STGPALLTGPASSPV CCCCCCCCCCCCCCC	41.80	28348404
405	Phosphorylation	ALLTGPASSPVGPPS CCCCCCCCCCCCCCC	38.00	27251275
406	Phosphorylation	LLTGPASSPVGPPSG CCCCCCCCCCCCCCC	26.22	27251275
439	Phosphorylation	TSSERSIYKARFLEN CCCCHHHHHHHHHHH	10.39	-
465	Phosphorylation	LAQGRAETLAGAMPN HHHCCHHHHHHCCCC	22.41	22964224
470	Sulfoxidation	AETLAGAMPNEAGGH HHHHHHCCCCCCCCC	3.42	21406390
486	Phosphorylation	DARQLWDSPETAPAA CHHHHCCCCCCCCCC	17.04	30266825
489	Phosphorylation	QLWDSPETAPAARTP HHCCCCCCCCCCCCC	41.13	30266825
495	Phosphorylation	ETAPAARTPQSPAPC CCCCCCCCCCCCCCH	22.43	30266825
498	Phosphorylation	PAARTPQSPAPCVLL CCCCCCCCCCCHHHH	25.00	25159151
510	Phosphorylation	VLLRAQRSLAPEPKE HHHHCHHHCCCCCCC	19.46	23403867
523	Phosphorylation	KEPLIPASPKAEPIW CCCCCCCCCCCCCCC	22.91	29255136
525	Ubiquitination	PLIPASPKAEPIWEL CCCCCCCCCCCCCCC	63.99	-
534	O-linked_Glycosylation	EPIWELPTRAPRLSI CCCCCCCCCCCCCEE	52.68	OGP
534	Phosphorylation	EPIWELPTRAPRLSI CCCCCCCCCCCCCEE	52.68	23403867
540	Phosphorylation	PTRAPRLSIGDLDFS CCCCCCCEECCCCHH	26.29	27732954
547	Phosphorylation	SIGDLDFSDLGEDED EECCCCHHHCCCCCC	31.43	28270605
573	Phosphorylation	GKDIPAPSPPLPLLS CCCCCCCCCCCCCCC	41.05	29255136
580	Phosphorylation	SPPLPLLSGVPPPPP CCCCCCCCCCCCCCC	45.48	29255136
635	Methylation	KLFWRELKLAGGHGV HHHHHHHHHHCCCCC	31.38	-
676	Ubiquitination	HLFESRAKEVLPSKK HHHHHHHHHHCCCCC	47.44	-
681	Phosphorylation	RAKEVLPSKKAGEGR HHHHHCCCCCCCCCC	42.50	24719451
690	Phosphorylation	KAGEGRRTMTTVLDP CCCCCCCCEEEECCC	19.94	25159151
692	Phosphorylation	GEGRRTMTTVLDPKR CCCCCCEEEECCCCC	17.09	22199227
693	Phosphorylation	EGRRTMTTVLDPKRS CCCCCEEEECCCCCC	14.30	28060719
700	Phosphorylation	TVLDPKRSNAINIGL EECCCCCCCCEEECC	36.42	22817900
708	Phosphorylation	NAINIGLTTLPPVHV CCEEECCCCCCHHHH	22.52	22817900
730	Ubiquitination	FDEFAVSKDGIEKLL CHHHCCCHHHHHHHH	54.07	-
738	Phosphorylation	DGIEKLLTMMPTEEE HHHHHHHHCCCCHHH	23.12	30206219
742	Phosphorylation	KLLTMMPTEEERQKI HHHHCCCCHHHHHHH	37.83	30206219
816	Phosphorylation	EQLVQNATFRCILAT HHHHHHHHHHHHHHH	21.11	-
823	Phosphorylation	TFRCILATLLAVGNF HHHHHHHHHHHHHHH	20.89	18452278
851	Ubiquitination	LEKVSEVKDTVRRQS HHHHHHHHHHHHHHH	43.56	-
874	Phosphorylation	VLQTRPESSDLYSEI HHHHCCCCCCHHHHC	31.66	-
878	Phosphorylation	RPESSDLYSEIPALT CCCCCCHHHHCHHHH	14.84	-
889	Ubiquitination	PALTRCAKVDFEQLT HHHHHHHCCCHHHHH	46.06	-
912	Phosphorylation	RSRAAEESLRSLAKH HHHHHHHHHHHHHHH	22.16	22985185
915	Phosphorylation	AAEESLRSLAKHELA HHHHHHHHHHHHCHH	37.66	22985185
918	Ubiquitination	ESLRSLAKHELAPAL HHHHHHHHHCHHHHH	42.79	-
960	Phosphorylation	RFHAFLLYLGYTPQA HHHHHHHHCCCCHHH	10.54	-
963	Phosphorylation	AFLLYLGYTPQAARE HHHHHCCCCHHHHHH	16.80	-
1000	Ubiquitination	RVLQQQQKQATYRER HHHHHHHHHHHHHHH	37.25	-
1010	Phosphorylation	TYRERNKTRGRMITE HHHHHHHHHCCCCCC	41.74	29514088
1016	Phosphorylation	KTRGRMITETEKFSG HHHCCCCCCCCCCCC	27.75	29514088
1018	Phosphorylation	RGRMITETEKFSGVA HCCCCCCCCCCCCCC	35.51	29514088
1039	Phosphorylation	PSVPVAVSSGPGRGD CCCCEEEECCCCCCC	21.60	22210691
1040	Phosphorylation	SVPVAVSSGPGRGDA CCCEEEECCCCCCCC	42.27	22210691
1044	Methylation	AVSSGPGRGDADSHA EEECCCCCCCCCCHH	42.84	-
1052	Phosphorylation	GDADSHASMKSLLTS CCCCCHHHHHHHHHC	22.71	27535140
1055	Phosphorylation	DSHASMKSLLTSRPE CCHHHHHHHHHCCCC	21.70	28555341
1058	Phosphorylation	ASMKSLLTSRPEDTT HHHHHHHHCCCCCCC	28.16	24719451
1076	Phosphorylation	RSRGMVQSSSPIMPT CCCCCCCCCCCCCCC	22.75	30624053
1077	Phosphorylation	SRGMVQSSSPIMPTV CCCCCCCCCCCCCCC	24.04	30624053
1078	Phosphorylation	RGMVQSSSPIMPTVG CCCCCCCCCCCCCCC	24.56	30624053
1083	Phosphorylation	SSSPIMPTVGPSTAS CCCCCCCCCCCCCCC	22.25	30624053
1087	Phosphorylation	IMPTVGPSTASPEEP CCCCCCCCCCCCCCC	30.58	30624053
1088	Phosphorylation	MPTVGPSTASPEEPP CCCCCCCCCCCCCCC	34.00	30624053
1090	Phosphorylation	TVGPSTASPEEPPGS CCCCCCCCCCCCCCC	32.69	30624053
1097	Phosphorylation	SPEEPPGSSLPSDTS CCCCCCCCCCCCCCH	34.18	30624053
1098	Phosphorylation	PEEPPGSSLPSDTSD CCCCCCCCCCCCCHH	50.65	30624053
1101	Phosphorylation	PPGSSLPSDTSDEIM CCCCCCCCCCHHHHH	59.83	30624053
1103	Phosphorylation	GSSLPSDTSDEIMDL CCCCCCCCHHHHHHH	42.27	30624053
1104	Phosphorylation	SSLPSDTSDEIMDLL CCCCCCCHHHHHHHH	37.93	30624053
1114	Phosphorylation	IMDLLVQSVTKSSPR HHHHHHHHHHCCCHH	25.03	26074081
1116	Phosphorylation	DLLVQSVTKSSPRAL HHHHHHHHCCCHHHH	30.38	26074081
1118	Phosphorylation	LVQSVTKSSPRALAA HHHHHHCCCHHHHHH	35.89	26074081
1119	Phosphorylation	VQSVTKSSPRALAAR HHHHHCCCHHHHHHH	21.69	26074081
1131	Phosphorylation	AARERKRSRGNRKSL HHHHHHHHHCCHHHH	47.80	18239683
1137	Phosphorylation	RSRGNRKSLRRTLKS HHHCCHHHHHHHHHH	24.70	18239683
1141	Phosphorylation	NRKSLRRTLKSGLGD CHHHHHHHHHHCCCH	31.91	28450419
1144	Phosphorylation	SLRRTLKSGLGDDLV HHHHHHHHCCCHHHH	42.22	28450419

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
99	Y	Phosphorylation	Kinase	SRC	P12931	PSP
498	S	Phosphorylation	Kinase	ERK2	P28482	PSP
498	S	Phosphorylation	Kinase	ERK1	P27361	PSP
1131	S	Phosphorylation	Kinase	PRKG1	Q13976	GPS
1131	S	Phosphorylation	Kinase	ROCK1	Q13464	PSP
1137	S	Phosphorylation	Kinase	ROCK1	Q13464	PSP
1141	T	Phosphorylation	Kinase	ROCK1	Q13464	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FHOD1_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 FHOD1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ACTG_HUMAN	ACTG1	physical	14576350
FHOD1_HUMAN	FHOD1	physical	14576350
FHOD1_HUMAN	FHOD1	physical	11590143
GALE_HUMAN	GALE	physical	26344197
SYTC_HUMAN	TARS	physical	26344197

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 FHOD1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498 AND SER-523, ANDMASS SPECTROMETRY.	19413330 [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-367; THR-495; SER-498;SER-523 AND THR-690, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-486; THR-495;SER-498; SER-523 AND SER-573, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-495; SER-498 ANDSER-523, AND MASS SPECTROMETRY.	18088087 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, AND MASSSPECTROMETRY.	15302935 [Abstract]