REN3A_HUMAN - dbPTM
REN3A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID REN3A_HUMAN
UniProt AC Q9H1J1
Protein Name Regulator of nonsense transcripts 3A
Gene Name UPF3A
Organism Homo sapiens (Human).
Sequence Length 476
Subcellular Localization Nucleus. Cytoplasm. Shuttling between the nucleus and the cytoplasm.
Protein Description Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC) and serving as link between the EJC core and NMD machinery. Recruits UPF2 at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. However, UPF3A is shown to be only marginally active in NMD as compared to UPF3B. Binds spliced mRNA upstream of exon-exon junctions. In vitro, weakly stimulates translation..
Protein Sequence MRSEKEGAGGLRAAVAARGPSGREKLSALEVQFHRDSQQQEAETPPTSSSGCGGGAGKPREEKRTALSKVVIRRLPPGLTKEQLEEQLRPLPAHDYFEFFAADLSLYPHLYSRAYINFRNPDDILLFRDRFDGYIFLDSKGLEYPAVVEFAPFQKIAKKKLRKKDAKTGSIEDDPEYKKFLETYCVEEEKTSANPETLLGEMEAKTRELIARRTTPLLEYIKNRKLEKQRIREEKREERRRRELEKKRLREEEKRRRREEERCKKKETDKQKKIAEKEVRIKLLKKPEKGEEPTTEKPKERGEEIDTGGGKQESCAPGAVVKARPMEGSLEEPQETSHSGSDKEHRDVERSQEQESEAQRYHVDDGRRHRAHHEPERLSRRSEDEQRWGKGPGQDRGKKGSQDSGAPGEAMERLGRAQRCDDSPAPRKERLANKDRPALQLYDPGARFRARECGGNRRICKAEGSGTGPEKREEAE
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 Orthologous
Protein Cluster
44PhosphorylationSQQQEAETPPTSSSG
CHHHCCCCCCCCCCC		41.4328165663
47PhosphorylationQEAETPPTSSSGCGG
HCCCCCCCCCCCCCC		42.30-
68PhosphorylationEEKRTALSKVVIRRL
HHHHHHHHHHHHHHC		22.4222817900
112PhosphorylationSLYPHLYSRAYINFR
HHHHHHHHCCCCCCC		19.4524719451
144PhosphorylationLDSKGLEYPAVVEFA
ECCCCCCCCEEEECC		11.09-
168PhosphorylationLRKKDAKTGSIEDDP
HHHCCCCCCCCCCCH		37.5724719451
170PhosphorylationKKDAKTGSIEDDPEY
HCCCCCCCCCCCHHH		28.2123312004
179UbiquitinationEDDPEYKKFLETYCV
CCCHHHHHHHHHHCC		55.04-
183PhosphorylationEYKKFLETYCVEEEK
HHHHHHHHHCCHHHC		25.1129978859
184PhosphorylationYKKFLETYCVEEEKT
HHHHHHHHCCHHHCC		5.7825159151
205UbiquitinationLLGEMEAKTRELIAR
HHHHHHHHHHHHHHH		34.50-
214PhosphorylationRELIARRTTPLLEYI
HHHHHHHHHHHHHHH		27.4922210691
215PhosphorylationELIARRTTPLLEYIK
HHHHHHHHHHHHHHH		15.3224719451
220PhosphorylationRTTPLLEYIKNRKLE
HHHHHHHHHHCCHHH		19.7122210691
311AcetylationEIDTGGGKQESCAPG
CCCCCCCCCCCCCCC		54.9226051181
314PhosphorylationTGGGKQESCAPGAVV
CCCCCCCCCCCCCEE		17.0624708550
329PhosphorylationKARPMEGSLEEPQET
EEEECCCCCCCCCCC		21.2121406692
336PhosphorylationSLEEPQETSHSGSDK
CCCCCCCCCCCCCCH		26.8830266825
337PhosphorylationLEEPQETSHSGSDKE
CCCCCCCCCCCCCHH		18.2030266825
339PhosphorylationEPQETSHSGSDKEHR
CCCCCCCCCCCHHHH		39.5030266825
341PhosphorylationQETSHSGSDKEHRDV
CCCCCCCCCHHHHHH		48.8230266825
351PhosphorylationEHRDVERSQEQESEA
HHHHHHHHHHHHHHH		25.2726714015
356PhosphorylationERSQEQESEAQRYHV
HHHHHHHHHHHHCCC		37.6226714015
379PhosphorylationHHEPERLSRRSEDEQ
CCCHHHHHCCCHHHH		31.6924719451
382PhosphorylationPERLSRRSEDEQRWG
HHHHHCCCHHHHHHC		48.5728102081
401PhosphorylationQDRGKKGSQDSGAPG
CCCCCCCCCCCCCCH		39.4328857561
404PhosphorylationGKKGSQDSGAPGEAM
CCCCCCCCCCCHHHH		29.2628102081
442PhosphorylationDRPALQLYDPGARFR
CCCCHHHCCCCHHHE		13.7127642862
465PhosphorylationRICKAEGSGTGPEKR
EEEECCCCCCCHHHH		25.37-
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

Oops, there are no upstream regulatory protein records of REN3A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of REN3A_HUMAN !!
Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of REN3A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GSK3B_HUMANGSK3Bphysical
15231747
IFM2_HUMANIFITM2physical
15231747
RENT2_HUMANUPF2physical
14527413
REN3B_HUMANUPF3Bphysical
14527413
DCP2_HUMANDCP2physical
14527413
XRN1_HUMANXRN1physical
14527413
EXOSX_HUMANEXOSC10physical
14527413
EXOS2_HUMANEXOSC2physical
14527413
EXOS4_HUMANEXOSC4physical
14527413
PARN_HUMANPARNphysical
14527413
SMG1_HUMANSMG1physical
11544179
RENT1_HUMANUPF1physical
11544179
HBB_HUMANHBBphysical
11163187
A4_HUMANAPPphysical
21832049
HBB_HUMANHBBphysical
21145460
HD_HUMANHTTphysical
23275563
HBB_HUMANHBBphysical
28514442
CAH1_HUMANCA1physical
28514442
HBD_HUMANHBDphysical
28514442
CASC3_HUMANCASC3physical
28514442
AGGF1_HUMANAGGF1physical
28514442
APOA1_HUMANAPOA1physical
28514442
A1AT_HUMANSERPINA1physical
28514442
RNPS1_HUMANRNPS1physical
28514442
LONM_HUMANLONP1physical
28514442
ALBU_HUMANALBphysical
28514442
CK5P3_HUMANCDK5RAP3physical
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.
Regulatory Network of REN3A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASSSPECTROMETRY.

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