| UniProt ID | RC3H1_HUMAN | |
|---|---|---|
| UniProt AC | Q5TC82 | |
| Protein Name | Roquin-1 {ECO:0000305} | |
| Gene Name | RC3H1 {ECO:0000312|HGNC:HGNC:29434} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 1133 | |
| Subcellular Localization | Cytoplasm, P-body . Cytoplasmic granule . During stress, such as that induced by arsenite treatment, localizes to cytosolic stress granules (By similarity). 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, TNFRSF4 and in many more mRNAs. [PubMed: 25026078 Cleaves translationally inactive mRNAs harboring a stem-loop (SL), often located in their 3'-UTRs, during the early phase of inflammation in a helicase UPF1-independent manner (By similarity Binds to CDE and promotes mRNA deadenylation and degradation. This process does not involve miRNAs (By similarity 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 (By similarity In resting or LPS-stimulated macrophages, controls inflammation by suppressing TNF expression (By similarity Also recognizes CDE in its own mRNA and in that of paralogous RC3H2, possibly leading to feedback loop regulation (By similarity Recognizes and binds mRNAs containing an hexaloop stem-loop motif, called alternative decay element (ADE) (By similarity Able to interact with double-stranded RNA (dsRNA)] | |
| Protein Sequence | MPVQAPQWTDFLSCPICTQTFDETIRKPISLGCGHTVCKMCLNKLHRKACPFDQTTINTDIELLPVNSALLQLVGAQVPEQQPITLCSGVEDTKHYEEAKKCVEELALYLKPLSSARGVGLNSTTQSVLSRPMQRKLVTLVHCQLVEEEGRIRAMRAARSLGERTVTELILQHQNPQQLSSNLWAAVRARGCQFLGPAMQEEALKLVLLALEDGSALSRKVLVLFVVQRLEPRFPQASKTSIGHVVQLLYRASCFKVTKRDEDSSLMQLKEEFRTYEALRREHDSQIVQIAMEAGLRIAPDQWSSLLYGDQSHKSHMQSIIDKLQTPASFAQSVQELTIALQRTGDPANLNRLRPHLELLANIDPSPDAPPPTWEQLENGLVAVRTVVHGLVDYIQNHSKKGADQQQPPQHSKYKTYMCRDMKQRGGCPRGASCTFAHSQEELEKFRKMNKRLVPRRPLSASLGQLNEVGLPSAAILPDEGAVDLPSRKPPALPNGIVSTGNTVTQLIPRGTDPSYDSSLKPGKIDHLSSSAPGSPPDLLESVPKSISALPVNPHSIPPRGPADLPPMPVTKPLQMVPRGSQLYPAQQTDVYYQDPRGAAPPFEPAPYQQGMYYTPPPQCVSRFVRPPPSAPEPAPPYLDHYPPYLQERVVNSQYGTQPQQYPPIYPSHYDGRRVYPAPSYTREEIFRESPIPIEIPPAAVPSYVPESRERYQQIESYYPVAPHPTQIRPSYLREPPYSRLPPPPQPHPSLDELHRRRKEIMAQLEERKVISPPPFAPSPTLPPTFHPEEFLDEDLKVAGKYKGNDYSQYSPWSCDTIGSYIGTKDAKPKDVVAAGSVEMMNVESKGMRDQRLDLQRRAAETSDDDLIPFGDRPTVSRFGAISRTSKTIYQGAGPMQAMAPQGAPTKSINISDYSPYGTHGGWGASPYSPHQNIPSQGHFSERERISMSEVASHGKPLPSAEREQLRLELQQLNHQISQQTQLRGLEAVSNRLVLQREANTLAGQSQPPPPPPPKWPGMISSEQLSLELHQVEREIGKRTRELSMENQCSLDMKSKLNTSKQAENGQPEPQNKVPAEDLTLTFSDVPNGSALTQENISLLSNKTSSLNLSEDPEGGGDNNDSQRSGVTPSSAP | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 115 | Phosphorylation | LYLKPLSSARGVGLN HHHHCHHHCCCCCCC | 29.66 | - | |
| 127 | Phosphorylation | GLNSTTQSVLSRPMQ CCCHHHHHHHCCHHH | 23.96 | - | |
| 130 | Phosphorylation | STTQSVLSRPMQRKL HHHHHHHCCHHHHHH | 31.98 | - | |
| 136 | Malonylation | LSRPMQRKLVTLVHC HCCHHHHHHHHHHHH | 30.34 | 26320211 | |
| 165 | Phosphorylation | ARSLGERTVTELILQ HHHHCCHHHHHHHHH | 27.72 | 28270605 | |
| 167 | Phosphorylation | SLGERTVTELILQHQ HHCCHHHHHHHHHCC | 25.18 | 28270605 | |
| 180 | Phosphorylation | HQNPQQLSSNLWAAV CCCHHHHHHHHHHHH | 16.91 | 28270605 | |
| 181 | Phosphorylation | QNPQQLSSNLWAAVR CCHHHHHHHHHHHHH | 44.53 | 28270605 | |
| 215 | Phosphorylation | LLALEDGSALSRKVL HHHHCCCCHHHHHHH | 38.06 | 23403867 | |
| 218 | Phosphorylation | LEDGSALSRKVLVLF HCCCCHHHHHHHHHH | 29.76 | 23403867 | |
| 239 | Acetylation | PRFPQASKTSIGHVV CCCCCCCCCHHHHHH | 49.67 | 19413330 | |
| 253 | Phosphorylation | VQLLYRASCFKVTKR HHHHHHHHCEECEEC | 15.87 | 19413330 | |
| 326 | Phosphorylation | SIIDKLQTPASFAQS HHHHHHHCHHHHHHH | 31.12 | - | |
| 433 | Phosphorylation | GGCPRGASCTFAHSQ CCCCCCCCCCCCCCH | 19.26 | 28857561 | |
| 460 | Phosphorylation | LVPRRPLSASLGQLN CCCCCCCCCCHHCCC | 20.63 | 30266825 | |
| 462 | Phosphorylation | PRRPLSASLGQLNEV CCCCCCCCHHCCCCC | 29.65 | 30266825 | |
| 473 | Phosphorylation | LNEVGLPSAAILPDE CCCCCCCCCEECCCC | 35.06 | 27732954 | |
| 487 | Phosphorylation | EGAVDLPSRKPPALP CCCCCCCCCCCCCCC | 61.30 | 27080861 | |
| 500 | Phosphorylation | LPNGIVSTGNTVTQL CCCCEECCCCCEEEC | 24.45 | 28555341 | |
| 512 | Phosphorylation | TQLIPRGTDPSYDSS EECCCCCCCCCCCCC | 46.12 | 23312004 | |
| 515 | Phosphorylation | IPRGTDPSYDSSLKP CCCCCCCCCCCCCCC | 44.36 | 23312004 | |
| 516 | Phosphorylation | PRGTDPSYDSSLKPG CCCCCCCCCCCCCCC | 25.82 | 23312004 | |
| 518 | Phosphorylation | GTDPSYDSSLKPGKI CCCCCCCCCCCCCCC | 29.36 | 23312004 | |
| 519 | Phosphorylation | TDPSYDSSLKPGKID CCCCCCCCCCCCCCC | 37.20 | 23312004 | |
| 529 | Phosphorylation | PGKIDHLSSSAPGSP CCCCCCCCCCCCCCC | 20.87 | 30266825 | |
| 530 | Phosphorylation | GKIDHLSSSAPGSPP CCCCCCCCCCCCCCH | 36.56 | 30266825 | |
| 531 | Phosphorylation | KIDHLSSSAPGSPPD CCCCCCCCCCCCCHH | 34.80 | 30266825 | |
| 535 | Phosphorylation | LSSSAPGSPPDLLES CCCCCCCCCHHHHHH | 32.00 | 29255136 | |
| 542 | Phosphorylation | SPPDLLESVPKSISA CCHHHHHHCCCCCCC | 43.63 | 23403867 | |
| 556 | Phosphorylation | ALPVNPHSIPPRGPA CCCCCCCCCCCCCCC | 37.74 | 24719451 | |
| 589 | Phosphorylation | QLYPAQQTDVYYQDP CCCCCCCCCEECCCC | 18.49 | 28796482 | |
| 592 | Phosphorylation | PAQQTDVYYQDPRGA CCCCCCEECCCCCCC | 9.75 | 28796482 | |
| 593 | Phosphorylation | AQQTDVYYQDPRGAA CCCCCEECCCCCCCC | 13.29 | 28796482 | |
| 597 | Methylation | DVYYQDPRGAAPPFE CEECCCCCCCCCCCC | 56.52 | 80702553 | |
| 623 | Methylation | PPPQCVSRFVRPPPS CCCCHHHCCCCCCCC | 17.43 | 115386963 | |
| 662 | Phosphorylation | YGTQPQQYPPIYPSH CCCCCCCCCCCCCCC | 13.01 | 20090780 | |
| 690 | Phosphorylation | REEIFRESPIPIEIP HHHHHHCCCCCCCCC | 24.71 | 28122231 | |
| 717 | Phosphorylation | ERYQQIESYYPVAPH HHHHHHHHHCCCCCC | 31.43 | 23401153 | |
| 718 | Phosphorylation | RYQQIESYYPVAPHP HHHHHHHHCCCCCCC | 10.05 | 23401153 | |
| 719 | Phosphorylation | YQQIESYYPVAPHPT HHHHHHHCCCCCCCC | 10.66 | 23401153 | |
| 726 | Phosphorylation | YPVAPHPTQIRPSYL CCCCCCCCCCCHHHH | 33.33 | 23401153 | |
| 729 | Methylation | APHPTQIRPSYLREP CCCCCCCCHHHHCCC | 12.32 | 20680375 | |
| 729 | Dimethylation | APHPTQIRPSYLREP CCCCCCCCHHHHCCC | 12.32 | - | |
| 731 | Phosphorylation | HPTQIRPSYLREPPY CCCCCCHHHHCCCCC | 27.27 | 23401153 | |
| 732 | Phosphorylation | PTQIRPSYLREPPYS CCCCCHHHHCCCCCC | 16.68 | 23401153 | |
| 734 | Methylation | QIRPSYLREPPYSRL CCCHHHHCCCCCCCC | 46.25 | 20680377 | |
| 740 | Methylation | LREPPYSRLPPPPQP HCCCCCCCCCCCCCC | 45.42 | 115490951 | |
| 750 | Phosphorylation | PPPQPHPSLDELHRR CCCCCCCCHHHHHHH | 45.47 | 28787133 | |
| 772 | Phosphorylation | LEERKVISPPPFAPS HHHCCCCCCCCCCCC | 34.05 | 29255136 | |
| 779 | Phosphorylation | SPPPFAPSPTLPPTF CCCCCCCCCCCCCCC | 27.38 | 29255136 | |
| 781 | Phosphorylation | PPFAPSPTLPPTFHP CCCCCCCCCCCCCCH | 57.12 | 29255136 | |
| 785 | Phosphorylation | PSPTLPPTFHPEEFL CCCCCCCCCCHHHHC | 32.41 | 29255136 | |
| 808 | Phosphorylation | KYKGNDYSQYSPWSC CCCCCCCHHCCCCCC | 26.04 | - | |
| 810 | Phosphorylation | KGNDYSQYSPWSCDT CCCCCHHCCCCCCCC | 15.68 | - | |
| 811 | Phosphorylation | GNDYSQYSPWSCDTI CCCCHHCCCCCCCCC | 16.56 | 25159151 | |
| 862 | Phosphorylation | LQRRAAETSDDDLIP HHHHHHHCCCCCCCC | 32.50 | 30108239 | |
| 863 | Phosphorylation | QRRAAETSDDDLIPF HHHHHHCCCCCCCCC | 30.46 | 23927012 | |
| 875 | Phosphorylation | IPFGDRPTVSRFGAI CCCCCCCCHHHCCHH | 31.82 | 23927012 | |
| 877 | O-linked_Glycosylation | FGDRPTVSRFGAISR CCCCCCHHHCCHHCC | 25.11 | 30620550 | |
| 877 | Phosphorylation | FGDRPTVSRFGAISR CCCCCCHHHCCHHCC | 25.11 | 23927012 | |
| 885 | Phosphorylation | RFGAISRTSKTIYQG HCCHHCCCCCCCCCC | 27.99 | 27251275 | |
| 886 | Phosphorylation | FGAISRTSKTIYQGA CCHHCCCCCCCCCCC | 27.05 | 27251275 | |
| 888 | Phosphorylation | AISRTSKTIYQGAGP HHCCCCCCCCCCCCH | 25.37 | 21945579 | |
| 890 | Phosphorylation | SRTSKTIYQGAGPMQ CCCCCCCCCCCCHHH | 13.21 | 21945579 | |
| 906 | Phosphorylation | MAPQGAPTKSINISD CCCCCCCCCCEECCC | 36.57 | 27762562 | |
| 947 | Phosphorylation | FSERERISMSEVASH CCHHHCCCHHHHHHC | 23.60 | 28348404 | |
| 949 | Phosphorylation | ERERISMSEVASHGK HHHCCCHHHHHHCCC | 23.33 | 22210691 | |
| 953 | Phosphorylation | ISMSEVASHGKPLPS CCHHHHHHCCCCCCH | 37.64 | 25159151 | |
| 960 | Phosphorylation | SHGKPLPSAEREQLR HCCCCCCHHHHHHHH | 50.90 | 27174698 | |
| 1040 | Phosphorylation | EREIGKRTRELSMEN HHHHHHHHHHHHHHC | 31.79 | - | |
| 1044 | Phosphorylation | GKRTRELSMENQCSL HHHHHHHHHHCCCHH | 21.21 | 27251275 | |
| 1050 | Phosphorylation | LSMENQCSLDMKSKL HHHHCCCHHHHHHHH | 20.03 | 24719451 | |
| 1055 | Phosphorylation | QCSLDMKSKLNTSKQ CCHHHHHHHHCHHHH | 35.42 | 30576142 | |
| 1059 | Phosphorylation | DMKSKLNTSKQAENG HHHHHHCHHHHHHCC | 47.97 | 30576142 | |
| 1060 | Phosphorylation | MKSKLNTSKQAENGQ HHHHHCHHHHHHCCC | 23.00 | 30576142 | |
| 1104 | Phosphorylation | ISLLSNKTSSLNLSE HHHHHCCCCCCCCCC | 28.00 | 28348404 | |
| 1105 | Phosphorylation | SLLSNKTSSLNLSED HHHHCCCCCCCCCCC | 34.14 | 28348404 | |
| 1106 | Phosphorylation | LLSNKTSSLNLSEDP HHHCCCCCCCCCCCC | 26.89 | 28348404 | |
| 1110 | Phosphorylation | KTSSLNLSEDPEGGG CCCCCCCCCCCCCCC | 38.59 | - | |
| 1125 | Phosphorylation | DNNDSQRSGVTPSSA CCCCCCCCCCCCCCC | 29.94 | 23403867 | |
| 1128 | Phosphorylation | DSQRSGVTPSSAP-- CCCCCCCCCCCCC-- | 22.45 | 23403867 | |
| 1130 | Phosphorylation | QRSGVTPSSAP---- CCCCCCCCCCC---- | 29.75 | 23403867 | |
| 1131 | Phosphorylation | RSGVTPSSAP----- CCCCCCCCCC----- | 45.85 | 23403867 | |
| 1131 | O-linked_Glycosylation | RSGVTPSSAP----- CCCCCCCCCC----- | 45.85 | 30620550 |
| 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 RC3H1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RC3H1_HUMAN !! | ||||||
* 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 RC3H1_HUMAN !! | ||||||
| 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. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-535, 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 SER-530 AND SER-535, ANDMASS SPECTROMETRY. | |
