dbPTM

F222B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	F222B_HUMAN
UniProt AC	Q8WU58
Protein Name	Protein FAM222B
Gene Name	FAM222B
Organism	Homo sapiens (Human).
Sequence Length	562
Subcellular Localization
Protein Description
Protein Sequence	MLACLPGPGDLSFQLLSHTQMNTGLQKWDTTQKMRTAHYPTPAELDAYAKKVANNPLTIKIFPNSVKVPQRKHVRRTVNGLDTSAQRYSPYPTQAATKAGLLAIVKVPAKSILKDFDGTRARLLPEAIMNPPVAPYATVAPSTLAHPQAQALARQQALQHAQTLAHAPPQTLQHPQGIPPPQALSHPQSLQQPQGLGHPQPMAQTQGLVHPQALAHQGLQHPHNPLLHGGRKMPDSDAPPNVTVSTSTIPLSMAATLQHSQPPDLSSIVHQINQFCQTRAGISTTSVCEGQIANPSPISRSLLINASTRVSTHSVPTPMPSCVVNPMEHTHAATAALPAAGPVNLPTGISRVPTGYPSDLKPVTWNQHQLAHLQQMCSEASGTPAPGLTGKHAAGRELAGPGFVGKAPAYPQELCLAQSFHLKPPLEKPTPSPPVNGMAAPLAYPNGHYFQPLWNNILPTPNSDSSGSQDLAMPFHGGQPTGAPLDCAAAPGAHYRAGTGGGPVASQNSLMQTVDYLSGDFQQACFREQSLAMLSKAHRAPGNRAPDPTESRSLHIQHPGYR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Phosphorylation	LPGPGDLSFQLLSHT CCCCCCHHHHHHHCC	18.71	24043423
17	Phosphorylation	DLSFQLLSHTQMNTG CHHHHHHHCCCCCCC	32.83	24043423
19	Phosphorylation	SFQLLSHTQMNTGLQ HHHHHHCCCCCCCCC	26.57	24043423
23	Phosphorylation	LSHTQMNTGLQKWDT HHCCCCCCCCCCCCC	33.65	24043423
50	Acetylation	AELDAYAKKVANNPL HHHHHHHHHHHCCCE	34.79	19820279
89	Phosphorylation	DTSAQRYSPYPTQAA CCCCHHCCCCCCHHH	21.83	-
111	Phosphorylation	IVKVPAKSILKDFDG EEEECHHHHHHCCCC	34.95	24719451
283	Phosphorylation	CQTRAGISTTSVCEG HHHCCCCCCCCCCCC	25.39	27251275
284	Phosphorylation	QTRAGISTTSVCEGQ HHCCCCCCCCCCCCC	22.59	27251275
285	Phosphorylation	TRAGISTTSVCEGQI HCCCCCCCCCCCCCC	16.63	27251275
286	Phosphorylation	RAGISTTSVCEGQIA CCCCCCCCCCCCCCC	25.51	27251275
296	Phosphorylation	EGQIANPSPISRSLL CCCCCCCCCCCHHHE	34.37	29255136
298	Phosphorylation	QIANPSPISRSLLIN CCCCCCCCCHHHEEC	6.66	-
299	O-linked_Glycosylation	IANPSPISRSLLINA CCCCCCCCHHHEECC	21.14	28657654
299	Phosphorylation	IANPSPISRSLLINA CCCCCCCCHHHEECC	21.14	29255136
301	Phosphorylation	NPSPISRSLLINAST CCCCCCHHHEECCCC	22.27	28555341
361	Ubiquitination	TGYPSDLKPVTWNQH CCCCCCCCCCCCCHH	42.29	-
361	Acetylation	TGYPSDLKPVTWNQH CCCCCCCCCCCCCHH	42.29	26051181
363	Ubiquitination	YPSDLKPVTWNQHQL CCCCCCCCCCCHHHH	10.41	-
406	Acetylation	AGPGFVGKAPAYPQE CCCCCCCCCCCCHHH	45.99	30587295
553	Phosphorylation	PDPTESRSLHIQHPG CCCCCCCCCCCCCCC	33.31	28555341

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 F222B_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of F222B_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 F222B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of F222B_HUMAN !!

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 F222B_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND MASSSPECTROMETRY.	19369195 [Abstract]