CE022_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CE022_HUMAN
• UniProt AC: Q49AR2
• Protein Name: UPF0489 protein C5orf22
• Gene Name: C5orf22
• Organism: Homo sapiens (Human).
• Sequence Length: 442
• Protein Sequence: MSDSAGGRAGLRRYPKLPVWVVEDHQEVLPFIYRAIGSKHLPASNVSFLHFDSHPDLLIPVNMPADTVFDKETLFGELSIENWIMPAVYAGHFSHVIWFHPTWAQQIREGRHHFLVGKDTSTTTIRVTSTDHYFLSDGLYVPEDQLENQKPLQLDVIMVKPYKLCNNQEENDAVSSAKKPKLALEDSENTASTNCDSSSEGLEKDTATQRSDQTCLEPSCSCSSENQECQTAASTGEILEILKKGKAFVLDIDLDFFSVKNPFKEMFTQEEYKILQELYQFKKPGTNLTEEDLVDIVDTRIHQLEDLEATFADLCDGDDEETVQRWASNPGMESLVPLVQSLKKRMEVPDYEMVHQAGLTCDYSELPHHISTEQEIECLIQSVHYLLKNLPNPTLVTIARSSLDDYCPSDQVDTIQEKVLNMLRALYGNLDLQVYAAESPPS

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
18 (in isoform 2)	Ubiquitination	-	24.85	21906983
73	Phosphorylation	DTVFDKETLFGELSI CCCCCCCHHCEEECC	32.88	-
118	Ubiquitination	RHHFLVGKDTSTTTI CCEEEEECCCCCCEE	50.80	21890473
118 (in isoform 1)	Ubiquitination	-	50.80	21890473
150	Sumoylation	EDQLENQKPLQLDVI HHHHCCCCCCEEEEE	60.31	-
163	Ubiquitination	VIMVKPYKLCNNQEE EEEEECCCCCCCCCC	55.90	-
175	Phosphorylation	QEENDAVSSAKKPKL CCCCCHHHHCCCCCE	26.71	22199227
176	Phosphorylation	EENDAVSSAKKPKLA CCCCHHHHCCCCCEE	37.19	21815630
187	Phosphorylation	PKLALEDSENTASTN CCEECCCCCCCCCCC	24.30	29978859
190	Phosphorylation	ALEDSENTASTNCDS ECCCCCCCCCCCCCC	20.24	30576142
192	Phosphorylation	EDSENTASTNCDSSS CCCCCCCCCCCCCCC	20.36	29507054
193	Phosphorylation	DSENTASTNCDSSSE CCCCCCCCCCCCCCC	37.08	28450419
197	Phosphorylation	TASTNCDSSSEGLEK CCCCCCCCCCCCCCC	37.65	25159151
198	Phosphorylation	ASTNCDSSSEGLEKD CCCCCCCCCCCCCCC	21.11	25159151
199	Phosphorylation	STNCDSSSEGLEKDT CCCCCCCCCCCCCCC	39.37	30576142
204	Ubiquitination	SSSEGLEKDTATQRS CCCCCCCCCCCCCCC	66.48	-
206	Phosphorylation	SEGLEKDTATQRSDQ CCCCCCCCCCCCCCC	42.55	26552605
208	Phosphorylation	GLEKDTATQRSDQTC CCCCCCCCCCCCCCC	26.97	30576142
282	Ubiquitination	LQELYQFKKPGTNLT HHHHHHCCCCCCCCC	42.40	-
283	Ubiquitination	QELYQFKKPGTNLTE HHHHHCCCCCCCCCH	50.39	-
283 (in isoform 1)	Ubiquitination	-	50.39	21890473
283	Ubiquitination	QELYQFKKPGTNLTE HHHHHCCCCCCCCCH	50.39	22053931
341	Phosphorylation	SLVPLVQSLKKRMEV HHHHHHHHHHHHCCC	34.38	28555341
344	Ubiquitination	PLVQSLKKRMEVPDY HHHHHHHHHCCCCCH	63.37	-
418	Ubiquitination	QVDTIQEKVLNMLRA HHHHHHHHHHHHHHH	35.33	-
439	Phosphorylation	LQVYAAESPPS---- EEEEEECCCCC----	37.07	24719451

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

Oops, there are no upstream regulatory protein records of CE022_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CE022_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 CE022_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ELOF1_HUMAN	ELOF1	physical	16189514

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

"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-197, AND MASSSPECTROMETRY.
PubMed: 19413330