LYRM2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LYRM2_HUMAN
• UniProt AC: Q9NU23
• Protein Name: LYR motif-containing protein 2
• Gene Name: LYRM2
• Organism: Homo sapiens (Human).
• Sequence Length: 88
• Protein Sequence: MAASRLPPATLTLKQFVRRQQVLLLYRRILQTIRQVPNDSDRKYLKDWAREEFRRNKSATEEDTIRMMITQGNMQLKELEKTLALAKS

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
14	Ubiquitination	PPATLTLKQFVRRQQ CCCEEHHHHHHHHHH	36.13	21890473
58	Phosphorylation	EEFRRNKSATEEDTI HHHHHCCCCCHHHHH	43.93	26471730
60	Phosphorylation	FRRNKSATEEDTIRM HHHCCCCCHHHHHHH	47.18	21815630
81	Ubiquitination	MQLKELEKTLALAKS HHHHHHHHHHHHHCC	62.56	21890473

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

Oops, there are no upstream regulatory protein records of LYRM2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LYRM2_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 LYRM2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FAM9B_HUMAN	FAM9B	physical	25416956
LYRM2_HUMAN	LYRM2	physical	27499296
ECH1_HUMAN	ECH1	physical	27499296
ACPM_HUMAN	NDUFAB1	physical	27499296
PDIP2_HUMAN	POLDIP2	physical	27499296
RM13_HUMAN	MRPL13	physical	27499296
C1QBP_HUMAN	C1QBP	physical	27499296
MPPB_HUMAN	PMPCB	physical	27499296
ACPM_HUMAN	NDUFAB1	physical	28514442
OXSM_HUMAN	OXSM	physical	28514442
ACADS_HUMAN	ACADS	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.