RC3H2_HUMAN - dbPTM
RC3H2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RC3H2_HUMAN
UniProt AC Q9HBD1
Protein Name Roquin-2
Gene Name RC3H2
Organism Homo sapiens (Human).
Sequence Length 1191
Subcellular Localization Cytoplasm, P-body. During stress, such as that induced by arsenite, localizes to cytosolic stress granules. Localization to stress granules, but not to P-bodies, depends upon the RING-type zinc finger.
Protein Description Post-transcriptional repressor of mRNAs containing a conserved stem loop motif, called constitutive decay element (CDE), which is often located in the 3'-UTR, as in HMGXB3, ICOS, IER3, NFKBID, NFKBIZ, PPP1R10, TNF and in many more mRNAs. Binds to CDE and promotes mRNA deadenylation and degradation. This process does not involve miRNAs. In follicular helper T (Tfh) cells, represses of ICOS and TNFRSF4 expression, thus preventing spontaneous Tfh cell differentiation, germinal center B-cell differentiation in the absence of immunization and autoimmunity. In resting or LPS-stimulated macrophages, controls inflammation by suppressing TNF expression. Also recognizes CDE in its own mRNA and in that of paralogous RC3H1, possibly leading to feedback loop regulation (By similarity). miRNA-binding protein that regulates microRNA homeostasis. Enhances DICER-mediated processing of pre-MIR146a but reduces mature MIR146a levels through an increase of 3' end uridylation. Both inhibits ICOS mRNA expression and they may act together to exert the suppression. [PubMed: 25697406 Acts as a ubiquitin E3 ligase. Pairs with E2 enzymes UBE2B, UBE2D2, UBE2E2, UBE2E3, UBE2G2, UBE2K and UBE2Q2 and produces polyubiquitin chains]
Protein Sequence MPVQAAQWTEFLSCPICYNEFDENVHKPISLGCSHTVCKTCLNKLHRKACPFDQTAINTDIDVLPVNFALLQLVGAQVPDHQSIKLSNLGENKHYEVAKKCVEDLALYLKPLSGGKGVASLNQSALSRPMQRKLVTLVNCQLVEEEGRVRAMRAARSLGERTVTELILQHQNPQQLSANLWAAVRARGCQFLGPAMQEEALKLVLLALEDGSALSRKVLVLFVVQRLEPRFPQASKTSIGHVVQLLYRASCFKVTKRDEDSSLMQLKEEFRSYEALRREHDAQIVHIAMEAGLRISPEQWSSLLYGDLAHKSHMQSIIDKLQSPESFAKSVQELTIVLQRTGDPANLNRLRPHLELLANIDPNPDAVSPTWEQLENAMVAVKTVVHGLVDFIQNYSRKGHETPQPQPNSKYKTSMCRDLRQQGGCPRGTNCTFAHSQEELEKYRLRNKKINATVRTFPLLNKVGVNNTVTTTAGNVISVIGSTETTGKIVPSTNGISNAENSVSQLISRSTDSTLRALETVKKVGKVGANGQNAAGPSADSVTENKIGSPPKTPVSNVAATSAGPSNVGTELNSVPQKSSPFLTRVPVYPPHSENIQYFQDPRTQIPFEVPQYPQTGYYPPPPTVPAGVAPCVPRFVRSNNVPESSLPPASMPYADHYSTFSPRDRMNSSPYQPPPPQPYGPVPPVPSGMYAPVYDSRRIWRPPMYQRDDIIRSNSLPPMDVMHSSVYQTSLRERYNSLDGYYSVACQPPSEPRTTVPLPREPCGHLKTSCEEQIRRKPDQWAQYHTQKAPLVSSTLPVATQSPTPPSPLFSVDFRADFSESVSGTKFEEDHLSHYSPWSCGTIGSCINAIDSEPKDVIANSNAVLMDLDSGDVKRRVHLFETQRRTKEEDPIIPFSDGPIISKWGAISRSSRTGYHTTDPVQATASQGSATKPISVSDYVPYVNAVDSRWSSYGNEATSSAHYVERDRFIVTDLSGHRKHSSTGDLLSLELQQAKSNSLLLQREANALAMQQKWNSLDEGRHLTLNLLSKEIELRNGELQSDYTEDATDTKPDRDIELELSALDTDEPDGQSEPIEEILDIQLGISSQNDQLLNGMAVENGHPVQQHQKEPPKQKKQSLGEDHVILEEQKTILPVTSCFSQPLPVSISNASCLPITTSVSAGNLILKTHVMSEDKNDFLKPVANGKMVNS
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
120PhosphorylationSGGKGVASLNQSALS
CCCCCHHHCCHHHHC		26.0024719451
212PhosphorylationLLALEDGSALSRKVL
HHHHCCCCHHHHHHH		38.0623403867
215PhosphorylationLEDGSALSRKVLVLF
HCCCCHHHHHHHHHH		29.7623403867
250PhosphorylationVQLLYRASCFKVTKR
HHHHHHHHCEECEEC		15.8719413330
453PhosphorylationRNKKINATVRTFPLL
HCCCCCCEEECHHCC		13.1620363803
471O-linked_GlycosylationGVNNTVTTTAGNVIS
CCCCCEEECCCCEEE		15.4330059200
472O-linked_GlycosylationVNNTVTTTAGNVISV
CCCCEEECCCCEEEE		24.1730059200
497O-linked_GlycosylationVPSTNGISNAENSVS
CCCCCCCCCCCHHHH		31.2430059200
514PhosphorylationISRSTDSTLRALETV
HHCCHHHHHHHHHHH		24.07-
549PhosphorylationVTENKIGSPPKTPVS
CCCCCCCCCCCCCCC		41.3125159151
553PhosphorylationKIGSPPKTPVSNVAA
CCCCCCCCCCCCCCC		34.4025159151
556PhosphorylationSPPKTPVSNVAATSA
CCCCCCCCCCCCCCC		27.1323927012
561PhosphorylationPVSNVAATSAGPSNV
CCCCCCCCCCCCCCC		14.9023927012
562PhosphorylationVSNVAATSAGPSNVG
CCCCCCCCCCCCCCC		26.8823403867
566PhosphorylationAATSAGPSNVGTELN
CCCCCCCCCCCCCCC		43.1423403867
579PhosphorylationLNSVPQKSSPFLTRV
CCCCCCCCCCCEECC		37.6927251275
580PhosphorylationNSVPQKSSPFLTRVP
CCCCCCCCCCEECCC		27.0621815630
584PhosphorylationQKSSPFLTRVPVYPP
CCCCCCEECCCCCCC		29.9624719451
593O-linked_GlycosylationVPVYPPHSENIQYFQ
CCCCCCCCCCCCCCC		37.8030059200
662PhosphorylationADHYSTFSPRDRMNS
CCCCCCCCCCCCCCC		21.0824719451
666MethylationSTFSPRDRMNSSPYQ
CCCCCCCCCCCCCCC		27.7130762627
666DimethylationSTFSPRDRMNSSPYQ
CCCCCCCCCCCCCCC		27.71-
669PhosphorylationSPRDRMNSSPYQPPP
CCCCCCCCCCCCCCC		24.2828555341
670PhosphorylationPRDRMNSSPYQPPPP
CCCCCCCCCCCCCCC		23.7128555341
691PhosphorylationPPVPSGMYAPVYDSR
CCCCCCCCCCCCCCC		15.98-
714PhosphorylationQRDDIIRSNSLPPMD
CCCHHHHCCCCCCHH		21.9928348404
716PhosphorylationDDIIRSNSLPPMDVM
CHHHHCCCCCCHHHC		43.4228348404
726O-linked_GlycosylationPMDVMHSSVYQTSLR
CHHHCCCHHHHHHHH		15.3430059200
736PhosphorylationQTSLRERYNSLDGYY
HHHHHHHHHHCCCEE		12.3529978859
738PhosphorylationSLRERYNSLDGYYSV
HHHHHHHHCCCEEEE		20.9229978859
742PhosphorylationRYNSLDGYYSVACQP
HHHHCCCEEEEEECC		7.7027642862
743PhosphorylationYNSLDGYYSVACQPP
HHHCCCEEEEEECCC		11.3827642862
755O-linked_GlycosylationQPPSEPRTTVPLPRE
CCCCCCCCCCCCCCC		42.7530059200
768MethylationREPCGHLKTSCEEQI
CCCCCCCCCCHHHHH		32.49115973179
778UbiquitinationCEEQIRRKPDQWAQY
HHHHHHHCHHHHHHH		43.00-
794PhosphorylationTQKAPLVSSTLPVAT
HCCCCCEECCCCCCC		25.8627732954
795PhosphorylationQKAPLVSSTLPVATQ
CCCCCEECCCCCCCC		26.8727732954
796PhosphorylationKAPLVSSTLPVATQS
CCCCEECCCCCCCCC		27.8127732954
801PhosphorylationSSTLPVATQSPTPPS
ECCCCCCCCCCCCCC		29.7929255136
803PhosphorylationTLPVATQSPTPPSPL
CCCCCCCCCCCCCCC		26.7929255136
805PhosphorylationPVATQSPTPPSPLFS
CCCCCCCCCCCCCEE		53.7529255136
808PhosphorylationTQSPTPPSPLFSVDF
CCCCCCCCCCEEEEE		35.1229255136
812PhosphorylationTPPSPLFSVDFRADF
CCCCCCEEEEEECCC		28.5829255136
834PhosphorylationKFEEDHLSHYSPWSC
CCCCCCHHHCCCCCC		19.5725627689
837PhosphorylationEDHLSHYSPWSCGTI
CCCHHHCCCCCCHHH		17.9225627689
871PhosphorylationAVLMDLDSGDVKRRV
CEEEECCCCCHHHHE		44.1624719451
875UbiquitinationDLDSGDVKRRVHLFE
ECCCCCHHHHEEHHH		38.95-
883O-linked_GlycosylationRRVHLFETQRRTKEE
HHEEHHHHCCCCCCC		21.7530059200
887O-linked_GlycosylationLFETQRRTKEEDPII
HHHHCCCCCCCCCCC		45.0230059200
888UbiquitinationFETQRRTKEEDPIIP
HHHCCCCCCCCCCCC		58.24-
897O-linked_GlycosylationEDPIIPFSDGPIISK
CCCCCCCCCCCCEEC		35.9830059200
903O-linked_GlycosylationFSDGPIISKWGAISR
CCCCCCEECCCCCCC		24.0730059200
909O-linked_GlycosylationISKWGAISRSSRTGY
EECCCCCCCCCCCCC		26.1030059200
932PhosphorylationTASQGSATKPISVSD
CCCCCCCCCCCCHHH		38.7628555341
954PhosphorylationVDSRWSSYGNEATSS
ECCCHHHCCCCCCCC		20.6029978859
959PhosphorylationSSYGNEATSSAHYVE
HHCCCCCCCCCEEEE		19.6228796482
960PhosphorylationSYGNEATSSAHYVER
HCCCCCCCCCEEEEC		32.3528796482
960O-linked_GlycosylationSYGNEATSSAHYVER
HCCCCCCCCCEEEEC		32.3530059200
961PhosphorylationYGNEATSSAHYVERD
CCCCCCCCCEEEECC		18.0828796482
964PhosphorylationEATSSAHYVERDRFI
CCCCCCEEEECCEEE		12.0628796482
976PhosphorylationRFIVTDLSGHRKHSS
EEEEECCCCCCCCCC		35.0528555341
982PhosphorylationLSGHRKHSSTGDLLS
CCCCCCCCCCCCHHH		32.4123401153
983PhosphorylationSGHRKHSSTGDLLSL
CCCCCCCCCCCHHHH		35.8123927012
984PhosphorylationGHRKHSSTGDLLSLE
CCCCCCCCCCHHHHH		37.4225159151
989PhosphorylationSSTGDLLSLELQQAK
CCCCCHHHHHHHHHH		27.3923403867
996UbiquitinationSLELQQAKSNSLLLQ
HHHHHHHHCCCHHHH		45.92-
999PhosphorylationLQQAKSNSLLLQREA
HHHHHCCCHHHHHHH		27.7322985185
1014UbiquitinationNALAMQQKWNSLDEG
HHHHHHHHHHHCHHC		31.30-
1017PhosphorylationAMQQKWNSLDEGRHL
HHHHHHHHCHHCHHH		35.7621815630
1030PhosphorylationHLTLNLLSKEIELRN
HHHHHHHHHHHHHHC		31.2628555341
1031UbiquitinationLTLNLLSKEIELRNG
HHHHHHHHHHHHHCC		63.78-
1044PhosphorylationNGELQSDYTEDATDT
CCCCCCCCCCCCCCC		19.7827642862
1119PhosphorylationPPKQKKQSLGEDHVI
CCHHHCCCCCCCCEE		47.4229255136
1168UbiquitinationSAGNLILKTHVMSED
CCCCEEEEEECCCCC		29.59-
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
-KUbiquitinationE3 ubiquitin ligaseKLHL6Q8WZ60
PMID:29695787
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RC3H2_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 RC3H2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRIM8_HUMANTRIM8physical
22493164
RC3H2_HUMANRC3H2physical
26489670
UBC_HUMANUBCphysical
26489670
UB2E2_HUMANUBE2E2physical
26489670
UB2E3_HUMANUBE2E3physical
26489670
UBE2K_HUMANUBE2Kphysical
26489670
UB2Q2_HUMANUBE2Q2physical
26489670
UBE2B_HUMANUBE2Bphysical
26489670
UB2D2_HUMANUBE2D2physical
26489670
UB2G2_HUMANUBE2G2physical
26489670
UBE2N_HUMANUBE2Nphysical
26489670
UB2V1_HUMANUBE2V1physical
26489670
UB2V2_HUMANUBE2V2physical
26489670
CP19A_HUMANCYP19A1physical
28514442
ACTBL_HUMANACTBL2physical
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 RC3H2_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 SER-549, AND MASSSPECTROMETRY.

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