IFRD2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IFRD2_HUMAN
• UniProt AC: Q12894
• Protein Name: Interferon-related developmental regulator 2
• Gene Name: IFRD2
• Organism: Homo sapiens (Human).
• Sequence Length: 506
• Protein Sequence: MAWNSPSRRPVWQGGAPREDGGARGVWLPSSGQVSAQRTGRRLVGLEPTPTGSLTPRPPRPVPGMPRARKGNTLRKGGQRRGGGARSSAQADSGSSDDEAASEARSTASECPSLLSTTAEDSLGGDVVDEQGQQEDLEEKLKEYVDCLTDKSAKTRQGALESLRLALASRLLPDFLLERRLTLADALEKCLKKGKGEEQALAAAVLGLLCVQLGPGPKGEELFHSLQPLLVSVLSDSTASPAARLHCASALGLGCYVAAADIQDLVSCLACLESVFSRFYGLGGSSTSPVVPASLHGLLSAALQAWALLLTICPSTQISHILDRQLPRLPQLLSSESVNLRIAAGETIALLFELARDLEEEFVYEDMEALCSVLRTLATDSNKYRAKADRRRQRSTFRAVLHSVEGGECEEEIVRFGFEVLYMDSWARHRIYAAFKEVLGSGMHHHLQNNELLRDIFGLGPVLLLDATALKACKVPRFEKHLYNAAAFKARTKARSRVRDKRADIL

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
53 (in isoform 2)	Phosphorylation	-	31.39	22210691
55 (in isoform 2)	Phosphorylation	-	20.96	22210691
75 (in isoform 2)	Phosphorylation	-	33.27	22210691
87	Phosphorylation	RRGGGARSSAQADSG CCCCCCCCCCCCCCC	29.50	25850435
88	Phosphorylation	RGGGARSSAQADSGS CCCCCCCCCCCCCCC	20.88	25850435
93	Phosphorylation	RSSAQADSGSSDDEA CCCCCCCCCCCCHHH	43.52	26055452
95	Phosphorylation	SAQADSGSSDDEAAS CCCCCCCCCCHHHHH	34.25	26055452
96	Phosphorylation	AQADSGSSDDEAASE CCCCCCCCCHHHHHH	53.24	21955146
102	Phosphorylation	SSDDEAASEARSTAS CCCHHHHHHHHHHHH	38.55	29262532
106 (in isoform 2)	Phosphorylation	-	35.06	22210691
112 (in isoform 2)	Phosphorylation	-	24.78	22210691
142	Ubiquitination	EDLEEKLKEYVDCLT CCHHHHHHHHHHHHH	59.05	29967540
151	Ubiquitination	YVDCLTDKSAKTRQG HHHHHHCCCCCHHHH	47.26	29967540
151	Acetylation	YVDCLTDKSAKTRQG HHHHHHCCCCCHHHH	47.26	12429897
152	O-linked_Glycosylation	VDCLTDKSAKTRQGA HHHHHCCCCCHHHHH	37.50	30379171
154	Acetylation	CLTDKSAKTRQGALE HHHCCCCCHHHHHHH	51.86	12429907
155	O-linked_Glycosylation	LTDKSAKTRQGALES HHCCCCCHHHHHHHH	28.13	30379171
162	Phosphorylation	TRQGALESLRLALAS HHHHHHHHHHHHHHH	21.46	19413330
182	Phosphorylation	FLLERRLTLADALEK HHHHHCCHHHHHHHH	20.35	23312004
240	Phosphorylation	VLSDSTASPAARLHC HHCCCCCCHHHHHHH	18.37	26329039
376	Phosphorylation	ALCSVLRTLATDSNK HHHHHHHHHCCCCHH	19.31	23312004
379	Phosphorylation	SVLRTLATDSNKYRA HHHHHHCCCCHHHHH	42.97	23312004
381	Phosphorylation	LRTLATDSNKYRAKA HHHHCCCCHHHHHHH	30.76	23312004
384	Phosphorylation	LATDSNKYRAKADRR HCCCCHHHHHHHHHH	21.76	23312004
471	Acetylation	LLDATALKACKVPRF HHHHHHHHHCCCCHH	49.64	25953088
480	Ubiquitination	CKVPRFEKHLYNAAA CCCCHHHHHHHHHHH	35.88	29967540
483	Phosphorylation	PRFEKHLYNAAAFKA CHHHHHHHHHHHHHH	11.50	25159151
489	Methylation	LYNAAAFKARTKARS HHHHHHHHHHHHHHH	32.03	115971353
489	Ubiquitination	LYNAAAFKARTKARS HHHHHHHHHHHHHHH	32.03	23000965
493	Ubiquitination	AAFKARTKARSRVRD HHHHHHHHHHHHHHH	35.93	23000965
591	Ubiquitination	-------------------------------------------------------------------------------------------- --------------------------------------------------------------------------------------------		-

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

Oops, there are no upstream regulatory protein records of IFRD2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IFRD2_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 IFRD2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
NOP58_HUMAN	NOP58	physical	26344197
UBE2O_HUMAN	UBE2O	physical	28514442
EIF3J_HUMAN	EIF3J	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.