NOL3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NOL3_HUMAN
• UniProt AC: O60936
• Protein Name: Nucleolar protein 3 {ECO:0000312|HGNC:HGNC:7869}
• Gene Name: NOL3 {ECO:0000312|HGNC:HGNC:7869}
• Organism: Homo sapiens (Human).
• Sequence Length: 208
• Subcellular Localization: Isoform 1: Nucleus, nucleolus . The SR-rich C-terminus mediates nuclear localization.; Isoform 3: Cytoplasm .; Isoform 2: Cytoplasm . Mitochondrion . Sarcoplasmic reticulum . Membrane ; Lipid-anchor . Phosphorylation at Thr-149 results in transl
• Protein Description: Isoform 1: May be involved in RNA splicing.; Isoform 2: Functions as an apoptosis repressor that blocks multiple modes of cell death. Inhibits extrinsic apoptotic pathways through two different ways. Firstly by interacting with FAS and FADD upon FAS activation blocking death-inducing signaling complex (DISC) assembly (By similarity). Secondly by interacting with CASP8 in a mitochondria localization- and phosphorylation-dependent manner, limiting the amount of soluble CASP8 available for DISC-mediated activation (By similarity). Inhibits intrinsic apoptotic pathway in response to a wide range of stresses, through its interaction with BAX resulting in BAX inactivation, preventing mitochondrial dysfunction and release of pro-apoptotic factors. [PubMed: 15004034 Inhibits calcium-mediated cell death by functioning as a cytosolic calcium buffer, dissociating its interaction with CASP8 and maintaining calcium homeostasis]
• Protein Sequence: MGNAQERPSETIDRERKRLVETLQADSGLLLDALLARGVLTGPEYEALDALPDAERRVRRLLLLVQGKGEAACQELLRCAQRTAGAPDPAWDWQHVGPGYRDRSYDPPCPGHWTPEAPGSGTTCPGLPRASDPDEAGGPEGSEAVQSGTPEEPEPELEAEASKEAEPEPEPEPELEPEAEAEPEPELEPEPDPEPEPDFEERDESEDS

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
2	Myristoylation	------MGNAQERPS ------CCCCCCCCC	37.87	25255805
17	Ubiquitination	ETIDRERKRLVETLQ HHHHHHHHHHHHHHH	45.38	PubMed
22	Phosphorylation	ERKRLVETLQADSGL HHHHHHHHHHHCCHH	19.38	20068231
27	Phosphorylation	VETLQADSGLLLDAL HHHHHHCCHHHHHHH	34.06	20068231
68	Ubiquitination	LLLLVQGKGEAACQE HHHHHCCCHHHHHHH	36.16	PubMed
83	Phosphorylation	LLRCAQRTAGAPDPA HHHHHHHHCCCCCCC	19.84	-
83 (in isoform 1)	Phosphorylation	-	19.84	24719451
104	Phosphorylation	GPGYRDRSYDPPCPG CCCCCCCCCCCCCCC	1.70	20068231
105	Phosphorylation	PGYRDRSYDPPCPGH CCCCCCCCCCCCCCC	13.46	20068231
109 (in isoform 1)	Phosphorylation	-	21.09	24719451
114	Phosphorylation	PPCPGHWTPEAPGSG CCCCCCCCCCCCCCC	20.68	25159151
120	Phosphorylation	WTPEAPGSGTTCPGL CCCCCCCCCCCCCCC	47.59	20068231
122	Phosphorylation	PEAPGSGTTCPGLPR CCCCCCCCCCCCCCC	41.71	20068231
123	Phosphorylation	EAPGSGTTCPGLPRA CCCCCCCCCCCCCCC	40.16	20068231
131	Phosphorylation	CPGLPRASDPDEAGG CCCCCCCCCCCCCCC	37.90	28985074
142	Phosphorylation	EAGGPEGSEAVQSGT CCCCCCCCHHHHCCC	8.33	26699800
147	Phosphorylation	EGSEAVQSGTPEEPE CCCHHHHCCCCCCCC	57.72	30278072
149 (in isoform 1)	Phosphorylation	-	35.15	23403867
149	Phosphorylation	SEAVQSGTPEEPEPE CHHHHCCCCCCCCHH	35.15	28355574
151 (in isoform 1)	Phosphorylation	-	27.68	23403867
162	Phosphorylation	PELEAEASKEAEPEP HHHHHHHHHCCCCCC	6.29	27251275
163	Ubiquitination	ELEAEASKEAEPEPE HHHHHHHHCCCCCCC	43.87	PubMed
176 (in isoform 3)	Phosphorylation	-	7.64	27251275
205	Phosphorylation	DFEERDESEDS---- CHHHCCCCCCC----	45.88	28348404
208	Phosphorylation	ERDESEDS------- HCCCCCCC-------	37.79	28348404
209 (in isoform 3)	Phosphorylation	-	45.09	27251275
267 (in isoform 3)	Phosphorylation	-		27251275

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
149	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
149	T	Phosphorylation	Kinase	CK2	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:17142834

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
149	T	Phosphorylation	Dephosphorylated at Thr-149 by calcineurin; doesn't inhibit the association between FADD and CASP8 and the consequent apoptosis.	-
149	T	Phosphorylation	Phosphorylation at Thr-149 is required for its antiapoptotic effect by blocking death-inducing signaling complex death-inducing signaling complex (DISC) activity through the control of interaction with CASP8.	-
149	T	Phosphorylation	Phosphorylation at Thr-149 results in translocation to mitochondria and this translocation enables the binding to CASP8.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of NOL3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NOL3_HUMAN	NOL3	physical	16189514
SHPS1_HUMAN	SIRPA	physical	16189514
NIF3L_HUMAN	NIF3L1	physical	16189514
EKI2_HUMAN	ETNK2	physical	16189514
SRSF9_HUMAN	SRSF9	physical	10196175
EHD4_HUMAN	EHD4	physical	22863883
NOL3_HUMAN	NOL3	physical	25416956
DAXX_HUMAN	DAXX	physical	27488634

Drug and Disease Associations

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