PRP8_MOUSE - dbPTM
PRP8_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRP8_MOUSE
UniProt AC Q99PV0
Protein Name Pre-mRNA-processing-splicing factor 8
Gene Name Prpf8
Organism Mus musculus (Mouse).
Sequence Length 2335
Subcellular Localization Nucleus speckle .
Protein Description Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for the assembly of the U4/U6-U5 tri-snRNP complex. Functions as scaffold that positions spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so that splicing can occur. Interacts with both the 5' and the 3' splice site..
Protein Sequence MAGVFPYRGPGNPVPGPLAPLPDYMSEEKLQEKARKWQQLQAKRYAEKRKFGFVDAQKEDMPPEHVRKIIRDHGDMTNRKFRHDKRVYLGALKYMPHAVLKLLENMPMPWEQIRDVPVLYHITGAISFVNEIPWVIEPVYISQWGSMWIMMRREKRDRRHFKRMRFPPFDDEEPPLDYADNILDVEPLEAIQLELDPEEDAPVLDWFYDHQPLRDSRKYVNGSTYQRWQFTLPMMSTLYRLANQLLTDLVDDNYFYLFDLKAFFTSKALNMAIPGGPKFEPLVRDINLQDEDWNEFNDINKIIIRQPIRTEYKIAFPYLYNNLPHHVHLTWYHTPNVVFIKTEDPDLPAFYFDPLINPISHRHSVKSQEPLPDDDEEFELPEFVEPFLKDTPLYTDNTANGIALLWAPRPFNLRSGRTRRALDIPLVKNWYREHCPAGQPVKVRVSYQKLLKYYVLNALKHRPPKAQKKRYLFRSFKATKFFQSTKLDWVEVGLQVCRQGYNMLNLLIHRKNLNYLHLDYNFNLKPVKTLTTKERKKSRFGNAFHLCREVLRLTKLVVDSHVQYRLGNVDAFQLADGLQYIFAHVGQLTGMYRYKYKLMRQIRMCKDLKHLIYYRFNTGPVGKGPGCGFWAAGWRVWLFFMRGITPLLERWLGNLLARQFEGRHSKGVAKTVTKQRVESHFDLELRAAVMHDILDMMPEGIKQNKARTILQHLSEAWRCWKANIPWKVPGLPTPIENMILRYVKAKADWWTNTAHYNRERIRRGATVDKTVCKKNLGRLTRLYLKAEQERQHNYLKDGPYITAEEAVAVYTTTVHWLESRRFSPIPFPPLSYKHDTKLLILALERLKEAYSVKSRLNQSQREELGLIEQAYDNPHEALSRIKRHLLTQRAFKEVGIEFMDLYSHLVPVYDVEPLEKITDAYLDQYLWYEADKRRLFPPWIKPADTEPPPLLVYKWCQGINNLQDVWETSEGECNVMLESRFEKMYEKIDLTLLNRLLRLIVDHNIADYMTAKNNVVINYKDMNHTNSYGIIRGLQFASFIVQYYGLVMDLLVLGLHRASEMAGPPQMPNDFLSFQDIATEAAHPIRLFCRYIDRIHIFFRFTADEARDLIQRYLTEHPDPNNENIVGYNNKKCWPRDARMRLMKHDVNLGRAVFWDIKNRLPRSVTTVQWENSFVSVYSKDNPNLLFNMCGFECRILPKCRTSYEEFTHKDGVWNLQNEVTKERTAQCFLRVDDESMQRFHNRVRQILMASGSTTFTKIVNKWNTALIGLMTYFREAVVNTQELLDLLVKCENKIQTRIKIGLNSKMPSRFPPVVFYTPKELGGLGMLSMGHVLIPQSDLRWSKQTDVGITHFRSGMSHEEDQLIPNLYRYIQPWESEFIDSQRVWAEYALKRQEAIAQNRRLTLEDLEDSWDRGIPRINTLFQKDRHTLAYDKGWRVRTDFKQYQVLKQNPFWWTHQRHDGKLWNLNNYRTDMIQALGGVEGILEHTLFKGTYFPTWEGLFWEKASGFEESMKWKKLTNAQRSGLNQIPNRRFTLWWSPTINRANVYVGFQVQLDLTGIFMHGKIPTLKISLIQIFRAHLWQKIHESIVMDLCQVFDQELDALEIETVQKETIHPRKSYKMNSSCADILLFASYKWNVSRPSLLADSKDVMDSTTTQKYWIDIQLRWGDYDSHDIERYARAKFLDYTTDNMSIYPSPTGVLIAIDLAYNLHSAYGNWFPGSKPLIQQAMAKIMKANPALYVLRERIRKGLQLYSSEPTEPYLSSQNYGELFSNQIIWFVDDTNVYRVTIHKTFEGNLTTKPINGAIFIFNPRTGQLFLKIIHTSVWAGQKRLGQLAKWKTAEEVAALIRSLPVEEQPKQIIVTRKGMLDPLEVHLLDFPNIVIKGSELQLPFQACLKVEKFGDLILKATEPQMVLFNLYDDWLKTISSYTAFSRLILILRALHVNNDRAKVILKPDKTTVTEPHHIWPTLTDEEWIKVEVQLKDLILADYGKKNNVNVASLTQSEIRDIILGMEISAPSQQRQQIAEIEKQTKEQSQLTATQTRTVNKHGDEIITSTTSNYETQTFSSKTEWRVRAISAANLHLRTNHIYVSSDDIKETGYTYILPKNVLKKFICISDLRAQIAGYLYGVSPPDNPQVKEIRCIVMVPQWGTHQTVHLPSQLPQHEYLKEMEPLGWIHTQPNESPQLSPQDVTTHAKIMADNPSWDGEKTIIITCSFTPGSCTLTAYKLTPSGYEWGRQNTDKGNNPKGYLPSHYERVQMLLSDRFLGFFMVPAQSSWNYNFMGVRHDPNMKYELQLANPKEFYHEVHRPSHFLNFALLQEGEVYSADREDLYA
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
2Acetylation------MAGVFPYRG
------CCCCCCCCC		33.87-
43UbiquitinationKWQQLQAKRYAEKRK
HHHHHHHHHHHHHHC		32.7422790023
218UbiquitinationQPLRDSRKYVNGSTY
CCCCCCCCCCCCCCC		58.4622790023
267UbiquitinationLKAFFTSKALNMAIP
HHHHHHHHHHHCCCC		54.5622790023
278UbiquitinationMAIPGGPKFEPLVRD
CCCCCCCCCHHCCCC		66.6822790023
366UbiquitinationISHRHSVKSQEPLPD
CCCCCCCCCCCCCCC		49.8122790023
428UbiquitinationALDIPLVKNWYREHC
CCCCCHHHCHHHHHC		49.8222790023
452AcetylationVSYQKLLKYYVLNAL
EEHHHHHHHHHHHHH		45.0022826441
609AcetylationIRMCKDLKHLIYYRF
HHCCCCCCHHHEEEC		46.6422826441
679PhosphorylationVTKQRVESHFDLELR
CHHHHHHHHCCHHHH		26.9625338131
702UbiquitinationDMMPEGIKQNKARTI
HHCCHHHHHHHHHHH		59.6922790023
708PhosphorylationIKQNKARTILQHLSE
HHHHHHHHHHHHHHH		30.79-
746UbiquitinationILRYVKAKADWWTNT
HHHHHHHHCCCCCCC		40.9522790023
785UbiquitinationRLTRLYLKAEQERQH
HHHHHHHHHHHHHHC		36.00-
819PhosphorylationTTVHWLESRRFSPIP
EEHHHHHHCCCCCCC		26.96-
859PhosphorylationVKSRLNQSQREELGL
HHHHCCHHHHHHHCH		30.08-
1020UbiquitinationNNVVINYKDMNHTNS
CCEEEEECCCCCCCC		46.1122790023
1158UbiquitinationRAVFWDIKNRLPRSV
HHHHHHHHHCCCCCE		33.2822790023
1210UbiquitinationSYEEFTHKDGVWNLQ
CHHHHCCCCCCHHCC		53.7922790023
1272PhosphorylationTALIGLMTYFREAVV
HHHHHHHHHHHHHHC		25.26-
1273PhosphorylationALIGLMTYFREAVVN
HHHHHHHHHHHHHCC		6.15-
1300UbiquitinationNKIQTRIKIGLNSKM
CHHCHHEECCCCCCC		27.6822790023
1318PhosphorylationFPPVVFYTPKELGGL
CCCEEEECCHHHCCC		19.2014729942
1344UbiquitinationQSDLRWSKQTDVGIT
HHHCCHHHCCCCCCC		50.7022790023
1355PhosphorylationVGITHFRSGMSHEED
CCCCEECCCCCCCHH		37.5930635358
1358PhosphorylationTHFRSGMSHEEDQLI
CEECCCCCCCHHCCC		31.1330635358
1392UbiquitinationVWAEYALKRQEAIAQ
HHHHHHHHHHHHHHH		43.8122790023
1404PhosphorylationIAQNRRLTLEDLEDS
HHHCCCCCHHHHHHH		26.7027600695
1411PhosphorylationTLEDLEDSWDRGIPR
CHHHHHHHHHCCCCH		22.8528066266
1425"N6,N6-dimethyllysine"RINTLFQKDRHTLAY
HHHHHHHCCCCCCCC		49.77-
1425UbiquitinationRINTLFQKDRHTLAY
HHHHHHHCCCCCCCC		49.7722790023
1425MethylationRINTLFQKDRHTLAY
HHHHHHHCCCCCCCC		49.77-
1434UbiquitinationRHTLAYDKGWRVRTD
CCCCCCCCCCEEECC		47.9322790023
1443UbiquitinationWRVRTDFKQYQVLKQ
CEEECCHHHHHHHHC		51.4022790023
1463AcetylationTHQRHDGKLWNLNNY
EEECCCCEEEECCHH		57.2822826441
1524PhosphorylationKLTNAQRSGLNQIPN
HHHHHHHCCCCCCCC		35.2429176673
1735UbiquitinationQAMAKIMKANPALYV
HHHHHHHHHCHHHHH		48.7822790023
1831UbiquitinationTSVWAGQKRLGQLAK
HHHHCCCHHHHHHCC		48.9922790023
1840UbiquitinationLGQLAKWKTAEEVAA
HHHHCCCCCHHHHHH		36.8322790023
1851PhosphorylationEVAALIRSLPVEEQP
HHHHHHHCCCCCCCC		29.99-
1925UbiquitinationNLYDDWLKTISSYTA
ECHHHHHHHHHHHHH		39.29-
1993UbiquitinationLILADYGKKNNVNVA
HHHHHHCCCCCCCHH		46.2122790023
2031UbiquitinationQQIAEIEKQTKEQSQ
HHHHHHHHHHHHHHC		69.7722790023
2034UbiquitinationAEIEKQTKEQSQLTA
HHHHHHHHHHHCCCC		51.7922790023
2037PhosphorylationEKQTKEQSQLTATQT
HHHHHHHHCCCCEEE		28.4025338131
2042PhosphorylationEQSQLTATQTRTVNK
HHHCCCCEEEEECCC		25.8217525332
2044PhosphorylationSQLTATQTRTVNKHG
HCCCCEEEEECCCCC		24.7720139300
2059PhosphorylationDEIITSTTSNYETQT
CEEEEECCCCCCEEC		18.1025367039
2060PhosphorylationEIITSTTSNYETQTF
EEEEECCCCCCEECC		37.1925367039
2062PhosphorylationITSTTSNYETQTFSS
EEECCCCCCEECCCC		21.8125367039
2066PhosphorylationTSNYETQTFSSKTEW
CCCCCEECCCCCCCH		32.6725367039
2079PhosphorylationEWRVRAISAANLHLR
CHHHHHHHHCCCEEE		21.9726824392
2087PhosphorylationAANLHLRTNHIYVSS
HCCCEEEECEEEEEH		37.1925367039
2091PhosphorylationHLRTNHIYVSSDDIK
EEEECEEEEEHHHHH		6.1725367039
2093PhosphorylationRTNHIYVSSDDIKET
EECEEEEEHHHHHHH		15.8625367039
2094PhosphorylationTNHIYVSSDDIKETG
ECEEEEEHHHHHHHC		29.2925367039
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 PRP8_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRP8_MOUSE !!
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 PRP8_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRP6_HUMANPRPF6physical
20360068
SMD3_HUMANSNRPD3physical
20360068
CDC5L_HUMANCDC5Lphysical
20360068
TSSC4_HUMANTSSC4physical
20360068
SNUT2_HUMANUSP39physical
20360068
PRP31_HUMANPRPF31physical
20360068
RSRC1_HUMANRSRC1physical
20360068
AAR2_HUMANAAR2physical
20360068
PRPF3_HUMANPRPF3physical
20360068
PRP16_HUMANDHX38physical
20360068
SNUT1_HUMANSART1physical
20360068
TFP11_HUMANTFIP11physical
20360068
CRNL1_HUMANCRNKL1physical
20360068
PRP8_HUMANPRPF8physical
20360068
RUXG_HUMANSNRPGphysical
20360068
TLS1_HUMANC9orf78physical
20360068
U5S1_HUMANEFTUD2physical
20360068
PRP4_HUMANPRPF4physical
20360068
SNW1_HUMANSNW1physical
20360068
CWC15_HUMANCWC15physical
20360068
DHX35_HUMANDHX35physical
20360068
U520_HUMANSNRNP200physical
20360068
PPIL1_HUMANPPIL1physical
20360068
SNR40_HUMANSNRNP40physical
20360068
RUVB2_HUMANRUVBL2physical
20360068
ECD_HUMANECDphysical
20360068
SYF1_HUMANXAB2physical
20360068
PLRG1_HUMANPLRG1physical
20360068
LSM4_HUMANLSM4physical
20360068
CCD12_HUMANCCDC12physical
20360068
CD2B2_HUMANCD2BP2physical
20360068
RUXE_HUMANSNRPEphysical
20360068
SPF27_HUMANBCAS2physical
20360068
NCDN_HUMANNCDNphysical
20360068
SYF2_HUMANSYF2physical
20360068
RSMB_HUMANSNRPBphysical
20360068
PPIE_HUMANPPIEphysical
20360068
RUVB1_HUMANRUVBL1physical
20360068
EAPP_HUMANEAPPphysical
20360068
ZNHI2_HUMANZNHIT2physical
20360068
SMD1_HUMANSNRPD1physical
20360068
AQR_HUMANAQRphysical
20360068
PRP19_HUMANPRPF19physical
20360068
LSM8_HUMANLSM8physical
20360068
PPIH_HUMANPPIHphysical
20360068
DHX15_HUMANDHX15physical
20360068
SMD2_HUMANSNRPD2physical
20360068
PAXB1_HUMANPAXBP1physical
20360068
TTC27_HUMANTTC27physical
20360068
DDX23_HUMANDDX23physical
20360068
NH2L1_HUMANNHP2L1physical
20360068
SNR27_HUMANSNRNP27physical
20360068
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRP8_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2042, AND MASSSPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1318, AND MASSSPECTROMETRY.

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