REN3B_HUMAN - dbPTM
REN3B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID REN3B_HUMAN
UniProt AC Q9BZI7
Protein Name Regulator of nonsense transcripts 3B
Gene Name UPF3B
Organism Homo sapiens (Human).
Sequence Length 483
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. In cooperation with UPF2 stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA upstream of exon-exon junctions. In vitro, stimulates translation; the function is independent of association with UPF2 and components of the EJC core..
Protein Sequence MKEEKEHRPKEKRVTLLTPAGATGSGGGTSGDSSKGEDKQDRNKEKKEALSKVVIRRLPPTLTKEQLQEHLQPMPEHDYFEFFSNDTSLYPHMYARAYINFKNQEDIILFRDRFDGYVFLDNKGQEYPAIVEFAPFQKAAKKKTKKRDTKVGTIDDDPEYRKFLESYATDNEKMTSTPETLLEEIEAKNRELIAKKTTPLLSFLKNKQRMREEKREERRRREIERKRQREEERRKWKEEEKRKRKDIEKLKKIDRIPERDKLKDEPKIKVHRFLLQAVNQKNLLKKPEKGDEKELDKREKAKKLDKENLSDERASGQSCTLPKRSDSELKDEKPKRPEDESGRDYREREREYERDQERILRERERLKRQEEERRRQKERYEKEKTFKRKEEEMKKEKDTLRDKGKKAESTESIGSSEKTEKKEEVVKRDRIRNKDRPAMQLYQPGARSRNRLCPPDDSTKSGDSAAERKQESGISHRKEGGEE
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
15PhosphorylationRPKEKRVTLLTPAGA
CCCCCCEEEEECCCC		21.7823312004
18PhosphorylationEKRVTLLTPAGATGS
CCCEEEEECCCCCCC		17.7621815630
23PhosphorylationLLTPAGATGSGGGTS
EEECCCCCCCCCCCC		30.8430576142
25PhosphorylationTPAGATGSGGGTSGD
ECCCCCCCCCCCCCC		29.8821815630
29PhosphorylationATGSGGGTSGDSSKG
CCCCCCCCCCCCCCC		32.5830576142
30PhosphorylationTGSGGGTSGDSSKGE
CCCCCCCCCCCCCCC		43.8321815630
33PhosphorylationGGGTSGDSSKGEDKQ
CCCCCCCCCCCCCCC		37.1630576142
34PhosphorylationGGTSGDSSKGEDKQD
CCCCCCCCCCCCCCH		49.7930576142
35AcetylationGTSGDSSKGEDKQDR
CCCCCCCCCCCCCHH		70.9826051181
39UbiquitinationDSSKGEDKQDRNKEK
CCCCCCCCCHHHHHH		50.2024816145
79PhosphorylationQPMPEHDYFEFFSND
CCCCCCCCHHHCCCC		13.6022817900
98PhosphorylationPHMYARAYINFKNQE
CHHEEEEEECCCCHH		7.2822817900
117PhosphorylationFRDRFDGYVFLDNKG
EEECCCCEEEECCCC		7.0022817900
138UbiquitinationVEFAPFQKAAKKKTK
EEEHHHHHHHHHCCC		51.1732015554
160PhosphorylationTIDDDPEYRKFLESY
CCCCCHHHHHHHHHH		25.2125159151
162UbiquitinationDDDPEYRKFLESYAT
CCCHHHHHHHHHHCC		54.0929967540
166PhosphorylationEYRKFLESYATDNEK
HHHHHHHHHCCCCCC		23.3922167270
167PhosphorylationYRKFLESYATDNEKM
HHHHHHHHCCCCCCC		12.2525159151
169PhosphorylationKFLESYATDNEKMTS
HHHHHHCCCCCCCCC		30.9919664994
173UbiquitinationSYATDNEKMTSTPET
HHCCCCCCCCCCHHH		54.45-
175PhosphorylationATDNEKMTSTPETLL
CCCCCCCCCCHHHHH		40.2822199227
176PhosphorylationTDNEKMTSTPETLLE
CCCCCCCCCHHHHHH		38.1722199227
177PhosphorylationDNEKMTSTPETLLEE
CCCCCCCCHHHHHHH		18.9126055452
180PhosphorylationKMTSTPETLLEEIEA
CCCCCHHHHHHHHHH		37.5322199227
188UbiquitinationLLEEIEAKNRELIAK
HHHHHHHHCHHHHHH		43.6932015554
196UbiquitinationNRELIAKKTTPLLSF
CHHHHHHHHHHHHHH		48.9233845483
197PhosphorylationRELIAKKTTPLLSFL
HHHHHHHHHHHHHHH		32.7022199227
198PhosphorylationELIAKKTTPLLSFLK
HHHHHHHHHHHHHHH		22.3325159151
202PhosphorylationKKTTPLLSFLKNKQR
HHHHHHHHHHHHHHH		35.8924719451
205UbiquitinationTPLLSFLKNKQRMRE
HHHHHHHHHHHHHHH		61.1532015554
245UbiquitinationEEEKRKRKDIEKLKK
HHHHHHHHHHHHHHH		67.1224816145
252UbiquitinationKDIEKLKKIDRIPER
HHHHHHHHHCCCCCH		61.3424816145
293UbiquitinationKPEKGDEKELDKREK
CCCCCCHHHHHHHHH		69.2124816145
306UbiquitinationEKAKKLDKENLSDER
HHHHHCCCCCCCCHH		59.9624816145
310PhosphorylationKLDKENLSDERASGQ
HCCCCCCCCHHHCCC		49.3529255136
310UbiquitinationKLDKENLSDERASGQ
HCCCCCCCCHHHCCC		49.3524816145
315PhosphorylationNLSDERASGQSCTLP
CCCCHHHCCCCCCCC		43.5223403867
318PhosphorylationDERASGQSCTLPKRS
CHHHCCCCCCCCCCC		16.7623403867
320UbiquitinationRASGQSCTLPKRSDS
HHCCCCCCCCCCCCH		51.8724816145
320PhosphorylationRASGQSCTLPKRSDS
HHCCCCCCCCCCCCH		51.8723403867
323AcetylationGQSCTLPKRSDSELK
CCCCCCCCCCCHHHC		68.5926051181
323UbiquitinationGQSCTLPKRSDSELK
CCCCCCCCCCCHHHC		68.5924816145
325PhosphorylationSCTLPKRSDSELKDE
CCCCCCCCCHHHCCC		52.1729496963
327PhosphorylationTLPKRSDSELKDEKP
CCCCCCCHHHCCCCC		46.1826657352
333UbiquitinationDSELKDEKPKRPEDE
CHHHCCCCCCCCCCC		67.0124816145
352PhosphorylationYREREREYERDQERI
HHHHHHHHHHHHHHH		23.61-
371UbiquitinationERLKRQEEERRRQKE
HHHHHHHHHHHHHHH		48.7624816145
381UbiquitinationRRQKERYEKEKTFKR
HHHHHHHHHHHHHHH		62.0424816145
382UbiquitinationRQKERYEKEKTFKRK
HHHHHHHHHHHHHHH		56.4224816145
384UbiquitinationKERYEKEKTFKRKEE
HHHHHHHHHHHHHHH		71.0324816145
394UbiquitinationKRKEEEMKKEKDTLR
HHHHHHHHHHHHHHH		62.1524816145
395UbiquitinationRKEEEMKKEKDTLRD
HHHHHHHHHHHHHHH		69.5524816145
399PhosphorylationEMKKEKDTLRDKGKK
HHHHHHHHHHHHCHH		34.46-
406AcetylationTLRDKGKKAESTESI
HHHHHCHHCCCCCCC		67.0820167786
409PhosphorylationDKGKKAESTESIGSS
HHCHHCCCCCCCCCC		42.1925849741
410PhosphorylationKGKKAESTESIGSSE
HCHHCCCCCCCCCCC		25.8430576142
412PhosphorylationKKAESTESIGSSEKT
HHCCCCCCCCCCCCC		32.1325159151
415PhosphorylationESTESIGSSEKTEKK
CCCCCCCCCCCCHHH		33.3825159151
416PhosphorylationSTESIGSSEKTEKKE
CCCCCCCCCCCHHHH		37.5921815630
419PhosphorylationSIGSSEKTEKKEEVV
CCCCCCCCHHHHHHH		49.3223312004
421AcetylationGSSEKTEKKEEVVKR
CCCCCCHHHHHHHHH		71.3820167786
421UbiquitinationGSSEKTEKKEEVVKR
CCCCCCHHHHHHHHH		71.3824816145
434UbiquitinationKRDRIRNKDRPAMQL
HHHHHCCCCCCCHHH		45.3124816145
442PhosphorylationDRPAMQLYQPGARSR
CCCCHHHCCCCCCCC		8.8621945579
447MethylationQLYQPGARSRNRLCP
HHCCCCCCCCCCCCC		41.9024129315
447UbiquitinationQLYQPGARSRNRLCP
HHCCCCCCCCCCCCC		41.9024816145
448PhosphorylationLYQPGARSRNRLCPP
HCCCCCCCCCCCCCC		33.1130576142
458PhosphorylationRLCPPDDSTKSGDSA
CCCCCCCCCCCCCCH		45.15-
460UbiquitinationCPPDDSTKSGDSAAE
CCCCCCCCCCCCHHH		57.2924816145
461PhosphorylationPPDDSTKSGDSAAER
CCCCCCCCCCCHHHH		48.1730624053
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 REN3B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of REN3B_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 REN3B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TTC19_HUMANTTC19physical
15231747
RENT2_HUMANUPF2physical
15231747
MCRS1_HUMANMCRS1physical
15231747
RENT2_HUMANUPF2physical
12417715
RENT1_HUMANUPF1physical
11163187
RENT2_HUMANUPF2physical
11163187
HBB_HUMANHBBphysical
11163187
IF4A3_HUMANEIF4A3physical
19884259
RNPS1_HUMANRNPS1physical
22939629
RU2A_HUMANSNRPA1physical
22939629
PYM1_HUMANWIBGphysical
22939629
WBP11_HUMANWBP11physical
22939629
SNUT1_HUMANSART1physical
22939629
TOP2A_HUMANTOP2Aphysical
22939629
IF4A3_HUMANEIF4A3physical
22961380
CASC3_HUMANCASC3physical
22961380
MGN_HUMANMAGOHphysical
22961380
RBM8A_HUMANRBM8Aphysical
22961380
MEPCE_HUMANMEPCEphysical
26344197
RENT1_HUMANUPF1physical
26496610
CASC3_HUMANCASC3physical
26496610
RENT2_HUMANUPF2physical
26496610
S61A1_HUMANSEC61A1physical
26496610
NKAP_HUMANNKAPphysical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300676Mental retardation, X-linked, syndromic, 14 (MRXS14)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of REN3B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-169, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-169, AND MASSSPECTROMETRY.

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