PRP6_HUMAN - dbPTM
PRP6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRP6_HUMAN
UniProt AC O94906
Protein Name Pre-mRNA-processing factor 6
Gene Name PRPF6
Organism Homo sapiens (Human).
Sequence Length 941
Subcellular Localization Nucleus, nucleoplasm. Nucleus speckle. Localized in splicing speckles.
Protein Description Involved in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex, one of the building blocks of the spliceosome. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation..
Protein Sequence MNKKKKPFLGMPAPLGYVPGLGRGATGFTTRSDIGPARDANDPVDDRHAPPGKRTVGDQMKKNQAADDDDEDLNDTNYDEFNGYAGSLFSSGPYEKDDEEADAIYAALDKRMDERRKERREQREKEEIEKYRMERPKIQQQFSDLKRKLAEVTEEEWLSIPEVGDARNKRQRNPRYEKLTPVPDSFFAKHLQTGENHTSVDPRQTQFGGLNTPYPGGLNTPYPGGMTPGLMTPGTGELDMRKIGQARNTLMDMRLSQVSDSVSGQTVVDPKGYLTDLNSMIPTHGGDINDIKKARLLLKSVRETNPHHPPAWIASARLEEVTGKLQVARNLIMKGTEMCPKSEDVWLEAARLQPGDTAKAVVAQAVRHLPQSVRIYIRAAELETDIRAKKRVLRKALEHVPNSVRLWKAAVELEEPEDARIMLSRAVECCPTSVELWLALARLETYENARKVLNKARENIPTDRHIWITAAKLEEANGNTQMVEKIIDRAITSLRANGVEINREQWIQDAEECDRAGSVATCQAVMRAVIGIGIEEEDRKHTWMEDADSCVAHNALECARAIYAYALQVFPSKKSVWLRAAYFEKNHGTRESLEALLQRAVAHCPKAEVLWLMGAKSKWLAGDVPAARSILALAFQANPNSEEIWLAAVKLESENDEYERARRLLAKARSSAPTARVFMKSVKLEWVQDNIRAAQDLCEEALRHYEDFPKLWMMKGQIEEQKEMMEKAREAYNQGLKKCPHSTPLWLLLSRLEEKIGQLTRARAILEKSRLKNPKNPGLWLESVRLEYRAGLKNIANTLMAKALQECPNSGILWSEAIFLEARPQRRTKSVDALKKCEHDPHVLLAVAKLFWSQRKITKAREWFHRTVKIDSDLGDAWAFFYKFELQHGTEEQQEEVRKRCESAEPRHGELWCAVSKDIANWQKKIGDILRLVAGRIKNTF
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
17PhosphorylationGMPAPLGYVPGLGRG
CCCCCCCCCCCCCCC		15.9120068231
23DimethylationGYVPGLGRGATGFTT
CCCCCCCCCCCCCCC		36.29-
23MethylationGYVPGLGRGATGFTT
CCCCCCCCCCCCCCC		36.2924384299
26PhosphorylationPGLGRGATGFTTRSD
CCCCCCCCCCCCHHH		35.3418452278
30PhosphorylationRGATGFTTRSDIGPA
CCCCCCCCHHHCCCC		26.3918452278
31MethylationGATGFTTRSDIGPAR
CCCCCCCHHHCCCCC		29.31115383813
32PhosphorylationATGFTTRSDIGPARD
CCCCCCHHHCCCCCC		31.3318452278
47MethylationANDPVDDRHAPPGKR
CCCCCCCCCCCCCCC		24.33115489023
61AcetylationRTVGDQMKKNQAADD
CCHHHHHHHCCCCCC		42.8325953088
105PhosphorylationDEEADAIYAALDKRM
HHHHHHHHHHHHHHH		6.3728674419
110UbiquitinationAIYAALDKRMDERRK
HHHHHHHHHHHHHHH		50.9329967540
125UbiquitinationERREQREKEEIEKYR
HHHHHHHHHHHHHHH		63.9424816145
137UbiquitinationKYRMERPKIQQQFSD
HHHHHCHHHHHHHHH		60.4124816145
143PhosphorylationPKIQQQFSDLKRKLA
HHHHHHHHHHHHHHH		37.3830266825
146SumoylationQQQFSDLKRKLAEVT
HHHHHHHHHHHHHCC		53.10-
1462-HydroxyisobutyrylationQQQFSDLKRKLAEVT
HHHHHHHHHHHHHCC		53.10-
146AcetylationQQQFSDLKRKLAEVT
HHHHHHHHHHHHHCC		53.1027452117
146MethylationQQQFSDLKRKLAEVT
HHHHHHHHHHHHHCC		53.10110872609
146SumoylationQQQFSDLKRKLAEVT
HHHHHHHHHHHHHCC		53.10-
146UbiquitinationQQQFSDLKRKLAEVT
HHHHHHHHHHHHHCC		53.1033845483
153PhosphorylationKRKLAEVTEEEWLSI
HHHHHHCCHHHHHCC		29.23-
176PhosphorylationKRQRNPRYEKLTPVP
CCCCCCCCHHCCCCC		20.7622210691
178UbiquitinationQRNPRYEKLTPVPDS
CCCCCCHHCCCCCCC		49.0421890473
178UbiquitinationQRNPRYEKLTPVPDS
CCCCCCHHCCCCCCC		49.0421890473
178SumoylationQRNPRYEKLTPVPDS
CCCCCCHHCCCCCCC		49.04-
178SumoylationQRNPRYEKLTPVPDS
CCCCCCHHCCCCCCC		49.04-
178UbiquitinationQRNPRYEKLTPVPDS
CCCCCCHHCCCCCCC		49.0423000965
180PhosphorylationNPRYEKLTPVPDSFF
CCCCHHCCCCCCCHH		33.0528555341
189UbiquitinationVPDSFFAKHLQTGEN
CCCCHHHHHCCCCCC		39.43-
193PhosphorylationFFAKHLQTGENHTSV
HHHHHCCCCCCCCCC		53.4728555341
198PhosphorylationLQTGENHTSVDPRQT
CCCCCCCCCCCCCCC		41.8628555341
199PhosphorylationQTGENHTSVDPRQTQ
CCCCCCCCCCCCCCC		19.5728555341
205PhosphorylationTSVDPRQTQFGGLNT
CCCCCCCCCCCCCCC		27.4323532336
212PhosphorylationTQFGGLNTPYPGGLN
CCCCCCCCCCCCCCC		29.2825159151
214PhosphorylationFGGLNTPYPGGLNTP
CCCCCCCCCCCCCCC		16.6925159151
220PhosphorylationPYPGGLNTPYPGGMT
CCCCCCCCCCCCCCC		29.2824043423
222PhosphorylationPGGLNTPYPGGMTPG
CCCCCCCCCCCCCCC		16.6923532336
227PhosphorylationTPYPGGMTPGLMTPG
CCCCCCCCCCCCCCC		19.9228348404
232PhosphorylationGMTPGLMTPGTGELD
CCCCCCCCCCCCCCC		24.4924043423
235PhosphorylationPGLMTPGTGELDMRK
CCCCCCCCCCCCHHH		28.7824043423
256PhosphorylationTLMDMRLSQVSDSVS
HHHHHHHHHCCCCCC		20.4023663014
259PhosphorylationDMRLSQVSDSVSGQT
HHHHHHCCCCCCCCE		19.2823663014
261PhosphorylationRLSQVSDSVSGQTVV
HHHHCCCCCCCCEEE		15.6321955146
263PhosphorylationSQVSDSVSGQTVVDP
HHCCCCCCCCEEECC		29.1830266825
266PhosphorylationSDSVSGQTVVDPKGY
CCCCCCCEEECCCCC		26.4830266825
271UbiquitinationGQTVVDPKGYLTDLN
CCEEECCCCCCCCHH		56.5829967540
273PhosphorylationTVVDPKGYLTDLNSM
EEECCCCCCCCHHHC		16.7430266825
275PhosphorylationVDPKGYLTDLNSMIP
ECCCCCCCCHHHCCC		29.9223401153
279PhosphorylationGYLTDLNSMIPTHGG
CCCCCHHHCCCCCCC		25.9430266825
283PhosphorylationDLNSMIPTHGGDIND
CHHHCCCCCCCCHHH		23.4123663014
292AcetylationGGDINDIKKARLLLK
CCCHHHHHHHHHHHH		43.1525953088
3242-HydroxyisobutyrylationRLEEVTGKLQVARNL
CHHHHHCHHHHHHHH		26.78-
324AcetylationRLEEVTGKLQVARNL
CHHHHHCHHHHHHHH		26.7825953088
324UbiquitinationRLEEVTGKLQVARNL
CHHHHHCHHHHHHHH		26.7824816145
341SumoylationKGTEMCPKSEDVWLE
HCCCCCCCCHHCHHH		62.64-
341AcetylationKGTEMCPKSEDVWLE
HCCCCCCCCHHCHHH		62.6426051181
341SumoylationKGTEMCPKSEDVWLE
HCCCCCCCCHHCHHH		62.64-
341UbiquitinationKGTEMCPKSEDVWLE
HCCCCCCCCHHCHHH		62.6429967540
351MethylationDVWLEAARLQPGDTA
HCHHHHHCCCCCCHH		40.69115489031
357PhosphorylationARLQPGDTAKAVVAQ
HCCCCCCHHHHHHHH		35.65-
372PhosphorylationAVRHLPQSVRIYIRA
HHHHCCHHHEEEEHH		16.07-
395UbiquitinationAKKRVLRKALEHVPN
HHHHHHHHHHHCCCC		53.8424816145
408UbiquitinationPNSVRLWKAAVELEE
CCHHHHHHHHHHCCC		30.9321906983
464MethylationRENIPTDRHIWITAA
HHCCCCCCCEEEEEH		26.18115489015
472UbiquitinationHIWITAAKLEEANGN
CEEEEEHHHHHHCCC		54.7021963094
482SulfoxidationEANGNTQMVEKIIDR
HHCCCHHHHHHHHHH		3.8521406390
485AcetylationGNTQMVEKIIDRAIT
CCHHHHHHHHHHHHH		33.2926051181
485UbiquitinationGNTQMVEKIIDRAIT
CCHHHHHHHHHHHHH		33.29-
512UbiquitinationQWIQDAEECDRAGSV
HHHCCHHHHCCCCCH		43.3624816145
518PhosphorylationEECDRAGSVATCQAV
HHHCCCCCHHHHHHH		13.9521406692
521PhosphorylationDRAGSVATCQAVMRA
CCCCCHHHHHHHHHH		11.7321406692
526SulfoxidationVATCQAVMRAVIGIG
HHHHHHHHHHHHCCC		2.2621406390
542PhosphorylationEEEDRKHTWMEDADS
CHHHHCCCCCCCHHH		29.5520873877
543UbiquitinationEEDRKHTWMEDADSC
HHHHCCCCCCCHHHH		6.4621890473
545UbiquitinationDRKHTWMEDADSCVA
HHCCCCCCCHHHHHH		41.4221890473
549PhosphorylationTWMEDADSCVAHNAL
CCCCCHHHHHHHHHH		16.5320873877
563PhosphorylationLECARAIYAYALQVF
HHHHHHHHHHHHHHC		7.8022817900
565PhosphorylationCARAIYAYALQVFPS
HHHHHHHHHHHHCCC		7.2922817900
573AcetylationALQVFPSKKSVWLRA
HHHHCCCCCHHHHHH		49.6726051181
573UbiquitinationALQVFPSKKSVWLRA
HHHHCCCCCHHHHHH		49.67-
574UbiquitinationLQVFPSKKSVWLRAA
HHHCCCCCHHHHHHH		55.36-
5852-HydroxyisobutyrylationLRAAYFEKNHGTRES
HHHHHHHHHCCCHHH		44.33-
585AcetylationLRAAYFEKNHGTRES
HHHHHHHHHCCCHHH		44.3319608861
585UbiquitinationLRAAYFEKNHGTRES
HHHHHHHHHCCCHHH		44.3333845483
606AcetylationRAVAHCPKAEVLWLM
HHHHCCCHHHHHHHH		63.6726051181
606UbiquitinationRAVAHCPKAEVLWLM
HHHHCCCHHHHHHHH		63.67-
607UbiquitinationAVAHCPKAEVLWLMG
HHHCCCHHHHHHHHC		9.4027667366
616UbiquitinationVLWLMGAKSKWLAGD
HHHHHCCCCCHHCCC		47.0021890473
616UbiquitinationVLWLMGAKSKWLAGD
HHHHHCCCCCHHCCC		47.0021890473
616AcetylationVLWLMGAKSKWLAGD
HHHHHCCCCCHHCCC		47.0025953088
616UbiquitinationVLWLMGAKSKWLAGD
HHHHHCCCCCHHCCC		47.0021906983
618UbiquitinationWLMGAKSKWLAGDVP
HHHCCCCCHHCCCCH		45.5821890473
618UbiquitinationWLMGAKSKWLAGDVP
HHHCCCCCHHCCCCH		45.5821890473
618SumoylationWLMGAKSKWLAGDVP
HHHCCCCCHHCCCCH		45.58-
618AcetylationWLMGAKSKWLAGDVP
HHHCCCCCHHCCCCH		45.5826822725
618SumoylationWLMGAKSKWLAGDVP
HHHCCCCCHHCCCCH		45.58-
618UbiquitinationWLMGAKSKWLAGDVP
HHHCCCCCHHCCCCH		45.5821906983
650SumoylationEIWLAAVKLESENDE
HHHEEEEEECCCCHH		41.64-
653PhosphorylationLAAVKLESENDEYER
EEEEEECCCCHHHHH		52.73-
658PhosphorylationLESENDEYERARRLL
ECCCCHHHHHHHHHH		17.3627642862
680UbiquitinationPTARVFMKSVKLEWV
CCHHHHHHHHCHHHH		40.4027667366
683SumoylationRVFMKSVKLEWVQDN
HHHHHHHCHHHHHHH		48.02-
683SumoylationRVFMKSVKLEWVQDN
HHHHHHHCHHHHHHH		48.02-
683UbiquitinationRVFMKSVKLEWVQDN
HHHHHHHCHHHHHHH		48.02-
699UbiquitinationRAAQDLCEEALRHYE
HHHHHHHHHHHHHCC		54.3122817900
702UbiquitinationQDLCEEALRHYEDFP
HHHHHHHHHHCCCCH		3.8221890473
703MethylationDLCEEALRHYEDFPK
HHHHHHHHHCCCCHH		37.07115489007
705PhosphorylationCEEALRHYEDFPKLW
HHHHHHHCCCCHHHH		15.68-
710UbiquitinationRHYEDFPKLWMMKGQ
HHCCCCHHHHHHCCC		55.5729967540
715SumoylationFPKLWMMKGQIEEQK
CHHHHHHCCCHHHHH		31.40-
715SumoylationFPKLWMMKGQIEEQK
CHHHHHHCCCHHHHH		31.40-
715UbiquitinationFPKLWMMKGQIEEQK
CHHHHHHCCCHHHHH		31.4032015554
722SumoylationKGQIEEQKEMMEKAR
CCCHHHHHHHHHHHH		51.35-
722AcetylationKGQIEEQKEMMEKAR
CCCHHHHHHHHHHHH		51.3526051181
722SumoylationKGQIEEQKEMMEKAR
CCCHHHHHHHHHHHH		51.35-
722UbiquitinationKGQIEEQKEMMEKAR
CCCHHHHHHHHHHHH		51.3529967540
7272-HydroxyisobutyrylationEQKEMMEKAREAYNQ
HHHHHHHHHHHHHHH		34.54-
727AcetylationEQKEMMEKAREAYNQ
HHHHHHHHHHHHHHH		34.5426051181
727UbiquitinationEQKEMMEKAREAYNQ
HHHHHHHHHHHHHHH		34.5429967540
737AcetylationEAYNQGLKKCPHSTP
HHHHHHHHCCCCCCH		60.1925953088
737UbiquitinationEAYNQGLKKCPHSTP
HHHHHHHHCCCCCCH		60.1929967540
738UbiquitinationAYNQGLKKCPHSTPL
HHHHHHHCCCCCCHH		59.0329967540
755AcetylationLLSRLEEKIGQLTRA
HHHHHHHHHHHHHHH		42.6426051181
755UbiquitinationLLSRLEEKIGQLTRA
HHHHHHHHHHHHHHH		42.6429967540
7682-HydroxyisobutyrylationRARAILEKSRLKNPK
HHHHHHHHHCCCCCC		37.11-
768UbiquitinationRARAILEKSRLKNPK
HHHHHHHHHCCCCCC		37.1129967540
772UbiquitinationILEKSRLKNPKNPGL
HHHHHCCCCCCCCCC		70.8222817900
775UbiquitinationKSRLKNPKNPGLWLE
HHCCCCCCCCCCHHH		82.3421890473
775UbiquitinationKSRLKNPKNPGLWLE
HHCCCCCCCCCCHHH		82.3421890473
775UbiquitinationKSRLKNPKNPGLWLE
HHCCCCCCCCCCHHH		82.3422817900
783PhosphorylationNPGLWLESVRLEYRA
CCCCHHHHHHHHHHH		15.4621712546
793UbiquitinationLEYRAGLKNIANTLM
HHHHHHHHHHHHHHH		45.44-
798PhosphorylationGLKNIANTLMAKALQ
HHHHHHHHHHHHHHH		14.6421406692
800SulfoxidationKNIANTLMAKALQEC
HHHHHHHHHHHHHHC		3.1921406390
828O-linked_GlycosylationEARPQRRTKSVDALK
HCCCCCCCCCHHHHH		29.8430379171
829AcetylationARPQRRTKSVDALKK
CCCCCCCCCHHHHHH		46.8223749302
829UbiquitinationARPQRRTKSVDALKK
CCCCCCCCCHHHHHH		46.8229967540
836UbiquitinationKSVDALKKCEHDPHV
CCHHHHHHCCCCHHH		45.7833845483
853PhosphorylationAVAKLFWSQRKITKA
HHHHHHHHHHHHHHH		16.8722673903
858PhosphorylationFWSQRKITKAREWFH
HHHHHHHHHHHHHHH		22.9922673903
883SumoylationDAWAFFYKFELQHGT
HHHHHHHHHHCCCCC		27.49-
917AcetylationELWCAVSKDIANWQK
CCCEECCHHHHHHHH		46.7026051181
917UbiquitinationELWCAVSKDIANWQK
CCCEECCHHHHHHHH		46.7029967540
924UbiquitinationKDIANWQKKIGDILR
HHHHHHHHHHHHHHH		37.6629967540
925UbiquitinationDIANWQKKIGDILRL
HHHHHHHHHHHHHHH		36.5029967540
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 PRP6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRP6_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 PRP6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TXN4B_HUMANTXNL4Bphysical
15161931
TIM44_HUMANTIMM44physical
10848612
PRP6_HUMANPRPF6physical
10848612
1433B_HUMANYWHABphysical
10848612
ANDR_HUMANARphysical
12039962
PRP31_HUMANPRPF31physical
16723661
SNUT1_HUMANSART1physical
16723661
TXN4A_HUMANTXNL4Aphysical
16723661
PRP6_HUMANPRPF6physical
16723661
U5S1_HUMANEFTUD2physical
16723661
U520_HUMANSNRNP200physical
16723661
PRP8_HUMANPRPF8physical
16723661
PRPF3_HUMANPRPF3physical
16723661
PRP8_HUMANPRPF8physical
22939629
U520_HUMANSNRNP200physical
22939629
SMD1_HUMANSNRPD1physical
22939629
SMD3_HUMANSNRPD3physical
22939629
SF3B3_HUMANSF3B3physical
22939629
SMD2_HUMANSNRPD2physical
22939629
RU2A_HUMANSNRPA1physical
22939629
SRSF7_HUMANSRSF7physical
22939629
U2AF1_HUMANU2AF1physical
22939629
SRSF5_HUMANSRSF5physical
22939629
PRPF3_HUMANPRPF3physical
22939629
U2AF2_HUMANU2AF2physical
22939629
SNUT1_HUMANSART1physical
22939629
SRRM2_HUMANSRRM2physical
22939629
SAP18_HUMANSAP18physical
22939629
SON_HUMANSONphysical
22939629
TPBG_HUMANTPBGphysical
22939629
TR150_HUMANTHRAP3physical
22939629
RS13_HUMANRPS13physical
22939629
RS24_HUMANRPS24physical
22939629
RBM14_HUMANRBM14physical
22939629
SP16H_HUMANSUPT16Hphysical
22939629
TRA2A_HUMANTRA2Aphysical
22939629
ZN326_HUMANZNF326physical
22939629
SRRM2_HUMANSRRM2physical
22365833
PRP31_HUMANPRPF31physical
22365833
RED_HUMANIKphysical
22365833
CD2B2_HUMANCD2BP2physical
22365833
CD2B2_HUMANCD2BP2physical
26344197
U5S1_HUMANEFTUD2physical
26344197
LC7L2_HUMANLUC7L2physical
26344197
PRP19_HUMANPRPF19physical
26344197
PRPF3_HUMANPRPF3physical
26344197
PRP31_HUMANPRPF31physical
26344197
PRP4_HUMANPRPF4physical
26344197
PRP8_HUMANPRPF8physical
26344197
SNUT1_HUMANSART1physical
26344197
SF3A3_HUMANSF3A3physical
26344197
U520_HUMANSNRNP200physical
26344197
SMD1_HUMANSNRPD1physical
26344197
SMD2_HUMANSNRPD2physical
26344197
TXN4A_HUMANTXNL4Aphysical
28514442
U520_HUMANSNRNP200physical
27173435
SMU1_HUMANSMU1physical
27173435
RIOK1_HUMANRIOK1physical
27173435
U5S1_HUMANEFTUD2physical
27173435
CD2B2_HUMANCD2BP2physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613983Retinitis pigmentosa 60 (RP60)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRP6_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-585, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-266; THR-275 ANDSER-279, AND MASS SPECTROMETRY.

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