FCSD1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FCSD1_HUMAN
• UniProt AC: Q86WN1
• Protein Name: F-BAR and double SH3 domains protein 1
• Gene Name: FCHSD1
• Organism: Homo sapiens (Human).
• Sequence Length: 690
• Protein Sequence: MQPPPRKVKPAQEVKLRFLEQLSILQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGPFLKREGHRSGEMDSRGRTVFGAWRCLLDATVAGGQTRLQASDRYRDLAGGTGRSAKEQVLRKGTENLQRAQAEVLQSVRELSRSRKLYGQRERVWALAQEKAADVQARLNRSDHGIFHSRTSLQKLSTKLSAQSAQYSQQLQAARNEYLLNLVATNAHLDHYYQEELPALLKALVSELSEHLRDPLTSLSHTELEAAEVILEHAHRGEQTTSQVSWEQDLKLFLQEPGVFSPTPPQQFQPAGTDQVCVLEWGAEGVAGKSGLEKEVQRLTSRAARDYKIQNHGHRVLQRLEQRRQQASEREAPSIEQRLQEVRESIRRAQVSQVKGAARLALLQGAGLDVERWLKPAMTQAQDEVEQERRLSEARLSQRDLSPTAEDAELSDFEECEETGELFEEPAPQALATRALPCPAHVVFRYQAGREDELTITEGEWLEVIEEGDADEWVKARNQHGEVGFVPERYLNFPDLSLPESSQDSDNPCGAEPTAFLAQALYSYTGQSAEELSFPEGALIRLLPRAQDGVDDGFWRGEFGGRVGVFPSLLVEELLGPPGPPELSDPEQMLPSPSPPSFSPPAPTSVLDGPPAPVLPGDKALDFPGFLDMMAPRLRPMRPPPPPPAKAPDPGHPDPLT

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
72	Phosphorylation	LKREGHRSGEMDSRG HHCCCCCCCCCCCCC	33.17	-
77	Phosphorylation	HRSGEMDSRGRTVFG CCCCCCCCCCCCHHH	35.01	-
104	Phosphorylation	GQTRLQASDRYRDLA CCCEEEEHHHHHHCC	15.06	22210691
127	Phosphorylation	EQVLRKGTENLQRAQ HHHHHHCHHHHHHHH	25.41	25884760
140	Phosphorylation	AQAEVLQSVRELSRS HHHHHHHHHHHHHHH	20.98	25884760
175	Phosphorylation	VQARLNRSDHGIFHS HHHHHHCCCCCCCCC	32.65	28555341
188	Ubiquitination	HSRTSLQKLSTKLSA CCHHHHHHHHHHHHH	50.10	29967540
192	Ubiquitination	SLQKLSTKLSAQSAQ HHHHHHHHHHHHHHH	36.75	29967540
194	Phosphorylation	QKLSTKLSAQSAQYS HHHHHHHHHHHHHHH	26.31	24043423
197	Phosphorylation	STKLSAQSAQYSQQL HHHHHHHHHHHHHHH	19.63	24043423
200	Phosphorylation	LSAQSAQYSQQLQAA HHHHHHHHHHHHHHH	14.25	24043423
201	Phosphorylation	SAQSAQYSQQLQAAR HHHHHHHHHHHHHHH	10.20	24043423
239	Phosphorylation	ALLKALVSELSEHLR HHHHHHHHHHHHHHC	33.40	19362540
278	Phosphorylation	EQTTSQVSWEQDLKL CCCCCCCCHHHHHHH	19.77	-
425	Phosphorylation	VEQERRLSEARLSQR HHHHHHHHHHHHHHC	27.65	26091039
430	Phosphorylation	RLSEARLSQRDLSPT HHHHHHHHHCCCCCC	20.02	23911959
435	Phosphorylation	RLSQRDLSPTAEDAE HHHHCCCCCCHHHHC	25.21	26029660
437	Phosphorylation	SQRDLSPTAEDAELS HHCCCCCCHHHHCCC	39.02	28102081
444	Phosphorylation	TAEDAELSDFEECEE CHHHHCCCCHHHHHH	31.58	26657352
452	Phosphorylation	DFEECEETGELFEEP CHHHHHHHCCCCCCC	17.42	26657352
466	Phosphorylation	PAPQALATRALPCPA CCCHHHHHCCCCCCE	19.82	28102081

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

Oops, there are no upstream regulatory protein records of FCSD1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FCSD1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of FCSD1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
XRCC6_HUMAN	XRCC6	physical	19041431
ASAP1_HUMAN	ASAP1	physical	19041431
DYN2_HUMAN	DNM2	physical	19041431
ITSN2_HUMAN	ITSN2	physical	19041431
SBK1_HUMAN	SBK1	physical	19041431
FCSD1_HUMAN	FCHSD1	physical	26702831

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-127 AND SER-140, ANDMASS SPECTROMETRY.
PubMed: 18187866