PYM1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PYM1_HUMAN
• UniProt AC: Q9BRP8
• Protein Name: Partner of Y14 and mago {ECO:0000250|UniProtKB:P82804}
• Gene Name: PYM1 {ECO:0000312|HGNC:HGNC:30258}
• Organism: Homo sapiens (Human).
• Sequence Length: 204
• Subcellular Localization: Cytoplasm . Nucleus, nucleolus . Nucleus, nucleoplasm . Shuttles between the nucleus and the cytoplasm (PubMed:14968132). Nuclear export is mediated by XPO1/CRM1 (PubMed:14968132).
• Protein Description: Key regulator of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon-exon junction on mRNAs and serves as a positional landmark for the intron exon structure of genes and directs post-transcriptional processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or translation. Acts as an EJC disassembly factor, allowing translation-dependent EJC removal and recycling by disrupting mature EJC from spliced mRNAs. Its association with the 40S ribosomal subunit probably prevents a translation-independent disassembly of the EJC from spliced mRNAs, by restricting its activity to mRNAs that have been translated. Interferes with NMD and enhances translation of spliced mRNAs, probably by antagonizing EJC functions. May bind RNA; the relevance of RNA-binding remains unclear in vivo, RNA-binding was detected by PubMed:14968132, while PubMed:19410547 did not detect RNA-binding activity independently of the EJC..
• Protein Sequence: MEAAGSPAATETGKYIASTQRPDGTWRKQRRVKEGYVPQEEVPVYENKYVKFFKSKPELPPGLSPEATAPVTPSRPEGGEPGLSKTAKRNLKRKEKRRQQQEKGEAEALSRTLDKVSLEETAQLPSAPQGSRAAPTAASDQPDSAATTEKAKKIKNLKKKLRQVEELQQRIQAGEVSQPSKEQLEKLARRRALEEELEDLELGL

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
1	Acetylation	-------MEAAGSPA -------CCCCCCCC		20068231
1	Sulfoxidation	-------MEAAGSPA -------CCCCCCCC		28465586
6	Phosphorylation	--MEAAGSPAATETG --CCCCCCCCCCCCC		29255136
10	Phosphorylation	AAGSPAATETGKYIA CCCCCCCCCCCCCEE		29255136
12	Phosphorylation	GSPAATETGKYIAST CCCCCCCCCCCEECC		21406692
15	Phosphorylation	AATETGKYIASTQRP CCCCCCCCEECCCCC		21406692
18	O-linked_Glycosylation	ETGKYIASTQRPDGT CCCCCEECCCCCCCC		OGP
18	Phosphorylation	ETGKYIASTQRPDGT CCCCCEECCCCCCCC		21406692
19	O-linked_Glycosylation	TGKYIASTQRPDGTW CCCCEECCCCCCCCC		OGP
19	Phosphorylation	TGKYIASTQRPDGTW CCCCEECCCCCCCCC		21406692
25	Phosphorylation	STQRPDGTWRKQRRV CCCCCCCCCCCCCCC		21406692
33	Acetylation	WRKQRRVKEGYVPQE CCCCCCCCCCCCCHH		26051181
36	Phosphorylation	QRRVKEGYVPQEEVP CCCCCCCCCCHHHCC		-
45	Phosphorylation	PQEEVPVYENKYVKF CHHHCCCCCCCCEEE		25159151
47	Ubiquitination	EEVPVYENKYVKFFK HHCCCCCCCCEEEEC		29967540
48	Acetylation	EVPVYENKYVKFFKS HCCCCCCCCEEEECC		26051181
48	Ubiquitination	EVPVYENKYVKFFKS HCCCCCCCCEEEECC		29967540
49	Phosphorylation	VPVYENKYVKFFKSK CCCCCCCCEEEECCC		28796482
51	Ubiquitination	VYENKYVKFFKSKPE CCCCCCEEEECCCCC		-
55	Phosphorylation	KYVKFFKSKPELPPG CCEEEECCCCCCCCC		22199227
64	Phosphorylation	PELPPGLSPEATAPV CCCCCCCCCCCCCCC		25159151
68	Phosphorylation	PGLSPEATAPVTPSR CCCCCCCCCCCCCCC		27134283
72	Phosphorylation	PEATAPVTPSRPEGG CCCCCCCCCCCCCCC		25159151
74	Phosphorylation	ATAPVTPSRPEGGEP CCCCCCCCCCCCCCC		22199227
84	Phosphorylation	EGGEPGLSKTAKRNL CCCCCCCCHHHHHHH		29978859
102	Ubiquitination	EKRRQQQEKGEAEAL HHHHHHHHHHHHHHH		24816145
103	Ubiquitination	KRRQQQEKGEAEALS HHHHHHHHHHHHHHH		24816145
103	Acetylation	KRRQQQEKGEAEALS HHHHHHHHHHHHHHH		30591735
110	Phosphorylation	KGEAEALSRTLDKVS HHHHHHHHHHHCCCC		30576142
112	Phosphorylation	EAEALSRTLDKVSLE HHHHHHHHHCCCCHH		30266825
117	Phosphorylation	SRTLDKVSLEETAQL HHHHCCCCHHHHCCC		23401153
121	Phosphorylation	DKVSLEETAQLPSAP CCCCHHHHCCCCCCC		30266825
126	Phosphorylation	EETAQLPSAPQGSRA HHHCCCCCCCCCCCC		27251275
131	Phosphorylation	LPSAPQGSRAAPTAA CCCCCCCCCCCCCCC		28555341
136	O-linked_Glycosylation	QGSRAAPTAASDQPD CCCCCCCCCCCCCCC		OGP
139	Phosphorylation	RAAPTAASDQPDSAA CCCCCCCCCCCCCHH		21815630
144	Phosphorylation	AASDQPDSAATTEKA CCCCCCCCHHHHHHH		21815630
147	O-linked_Glycosylation	DQPDSAATTEKAKKI CCCCCHHHHHHHHHH		OGP
147	Phosphorylation	DQPDSAATTEKAKKI CCCCCHHHHHHHHHH		25072903
148	Phosphorylation	QPDSAATTEKAKKIK CCCCHHHHHHHHHHH		25072903
177	Phosphorylation	RIQAGEVSQPSKEQL HHHCCCCCCCCHHHH		25159151
180	Ubiquitination	AGEVSQPSKEQLEKL CCCCCCCCHHHHHHH		24816145
181	Ubiquitination	GEVSQPSKEQLEKLA CCCCCCCHHHHHHHH		24816145
181	Acetylation	GEVSQPSKEQLEKLA CCCCCCCHHHHHHHH		26051181
186	Malonylation	PSKEQLEKLARRRAL CCHHHHHHHHHHHHH		26320211
186	Acetylation	PSKEQLEKLARRRAL CCHHHHHHHHHHHHH		26051181

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

Oops, there are no upstream regulatory protein records of PYM1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PYM1_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 PYM1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
UBIM_HUMAN	FAU	physical	22863883
PNO1_HUMAN	PNO1	physical	22863883
RS14_HUMAN	RPS14	physical	22863883
RS15A_HUMAN	RPS15A	physical	22863883
RS16_HUMAN	RPS16	physical	22863883
RS25_HUMAN	RPS25	physical	22863883
RS3A_HUMAN	RPS3A	physical	22863883
RS3_HUMAN	RPS3	physical	22863883
RS6_HUMAN	RPS6	physical	22863883
RS8_HUMAN	RPS8	physical	22863883
RS9_HUMAN	RPS9	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
ZN503_HUMAN	ZNF503	physical	22863883
RT4I1_HUMAN	RTN4IP1	physical	25416956
NELFE_HUMAN	NELFE	physical	26344197
RT4I1_HUMAN	RTN4IP1	physical	21516116
MD2BP_HUMAN	MAD2L1BP	physical	28514442
RBM8A_HUMAN	RBM8A	physical	28514442
CASC3_HUMAN	CASC3	physical	28514442
DCAF5_HUMAN	DCAF5	physical	28514442
MD2L1_HUMAN	MAD2L1	physical	28514442
RS16_HUMAN	RPS16	physical	28514442

Drug and Disease Associations

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