NHLC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NHLC1_HUMAN
• UniProt AC: Q6VVB1
• Protein Name: E3 ubiquitin-protein ligase NHLRC1
• Gene Name: NHLRC1
• Organism: Homo sapiens (Human).
• Sequence Length: 395
• Subcellular Localization: Endoplasmic reticulum. Nucleus. Localizes at the endoplasmic reticulum and, to a lesser extent, in the nucleus.
• Protein Description: E3 ubiquitin-protein ligase. Together with the phosphatase EPM2A/laforin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. In complex with EPM2A/laforin and HSP70, suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Ubiquitinates the glycogen-targeting protein phosphatase subunits PPP1R3C/PTG and PPP1R3D in a laforin-dependent manner and targets them for proteasome-dependent degradation, thus decreasing glycogen accumulation. Polyubiquitinates EPM2A/laforin and ubiquitinates AGL and targets them for proteasome-dependent degradation. Also promotes proteasome-independent protein degradation through the macroautophagy pathway..
• Protein Sequence: MAAEASESGPALHELMREAEISLLECKVCFEKFGHRQQRRPRNLSCGHVVCLACVAALAHPRTLALECPFCRRACRGCDTSDCLPVLHLIELLGSALRQSPAAHRAAPSAPGALTCHHTFGGWGTLVNPTGLALCPKTGRVVVVHDGRRRVKIFDSGGGCAHQFGEKGDAAQDIRYPVDVTITNDCHVVVTDAGDRSIKVFDFFGQIKLVIGGQFSLPWGVETTPQNGIVVTDAEAGSLHLLDVDFAEGVLRRTERLQAHLCNPRGVAVSWLTGAIAVLEHPLALGTGVCSTRVKVFSSSMQLVGQVDTFGLSLYFPSKITASAVTFDHQGNVIVADTSGPAILCLGKPEEFPVPKPMVTHGLSHPVALTFTKENSLLVLDTASHSIKVYKVDWG

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
176	Phosphorylation	DAAQDIRYPVDVTIT CCCCCCCCCCEEEEE	14.14	22210691
181	Phosphorylation	IRYPVDVTITNDCHV CCCCCEEEEECCCEE	20.02	22210691
183	Phosphorylation	YPVDVTITNDCHVVV CCCEEEEECCCEEEE	18.68	22210691
197	Phosphorylation	VTDAGDRSIKVFDFF EECCCCCEEEEEECC	31.34	28555341
309	Phosphorylation	QLVGQVDTFGLSLYF CEEEEEECCCEEEEC	22.27	22210691
313	Phosphorylation	QVDTFGLSLYFPSKI EEECCCEEEECCCCC	22.77	22210691
376	Phosphorylation	LTFTKENSLLVLDTA EEEECCCEEEEEECC	24.95	-

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

Oops, there are no upstream regulatory protein records of NHLC1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NHLC1_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 NHLC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GDE_HUMAN	AGL	physical	17908927
EPM2A_HUMAN	EPM2A	physical	16115820
EPM2A_HUMAN	EPM2A	physical	15930137
PPR3C_HUMAN	PPP1R3C	physical	18070875
DVL2_HUMAN	DVL2	physical	22223637
NNAT_HUMAN	NNAT	physical	21742036
HSP74_HUMAN	HSPA4	physical	19892702
EPM2A_HUMAN	EPM2A	physical	18617530
EPM2A_HUMAN	EPM2A	physical	22578008
PRDM8_HUMAN	PRDM8	physical	22961547
UB2D3_HUMAN	UBE2D3	physical	22223637
UBE2H_HUMAN	UBE2H	physical	15930137
UB2D1_HUMAN	UBE2D1	physical	15930137
UB2D3_HUMAN	UBE2D3	physical	15930137
UB2E1_HUMAN	UBE2E1	physical	15930137
GYS1_HUMAN	GYS1	physical	22578008
NHLC1_HUMAN	NHLRC1	physical	26648032
EPM2A_HUMAN	EPM2A	physical	26648032

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.