RTF1_HUMAN - dbPTM
RTF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RTF1_HUMAN
UniProt AC Q92541
Protein Name RNA polymerase-associated protein RTF1 homolog
Gene Name RTF1
Organism Homo sapiens (Human).
Sequence Length 710
Subcellular Localization Nucleus, nucleoplasm.
Protein Description Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Binds single-stranded DNA. Required for maximal induction of heat-shock genes. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of a SET1 complex (By similarity)..
Protein Sequence MRGRLCVGRAAAAAAAVAVPLAGGQEGSPGGGRRGSRGTTMVKKRKGRVVIDSDTEDSGSDENLDQELLSLAKRKRSDSEEKEPPVSQPAASSDSETSDSDDEWTFGSNKNKKKGKARKIEKKGTMKKQANKTASSGSSDKDSSAESSAPEEGEVSDSDSNSSSSSSDSDSSSEDEEFHDGYGEDLMGDEEDRARLEQMTEKEREQELFNRIEKREVLKRRFEIKKKLKTAKKKEKKEKKKKQEEEQEKKKLTQIQESQVTSHNKERRSKRDEKLDKKSQAMEELKAEREKRKNRTAELLAKKQPLKTSEVYSDDEEEEEDDKSSEKSDRSSRTSSSDEEEEKEEIPPKSQPVSLPEELNRVRLSRHKLERWCHMPFFAKTVTGCFVRIGIGNHNSKPVYRVAEITGVVETAKVYQLGGTRTNKGLQLRHGNDQRVFRLEFVSNQEFTESEFMKWKEAMFSAGMQLPTLDEINKKELSIKEALNYKFNDQDIEEIVKEKERFRKAPPNYAMKKTQLLKEKAMAEDLGDQDKAKQIQDQLNELEERAEALDRQRTKNISAISYINQRNREWNIVESEKALVAESHNMKNQQMDPFTRRQCKPTIVSNSRDPAVQAAILAQLNAKYGSGVLPDAPKEMSKGQGKDKDLNSKSASDLSEDLFKVHDFDVKIDLQVPSSESKALAITSKAPPAKDGAPRRSLNLEDYKKRRGLI
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
20PhosphorylationAAAAVAVPLAGGQEG
HHHHHHEECCCCCCC		13.5215302935
44TrimethylationRGTTMVKKRKGRVVI
CCCEEEEECCCCEEE		48.18-
44MethylationRGTTMVKKRKGRVVI
CCCEEEEECCCCEEE		48.1823644510
53PhosphorylationKGRVVIDSDTEDSGS
CCCEEECCCCCCCCC		35.0026503892
55PhosphorylationRVVIDSDTEDSGSDE
CEEECCCCCCCCCCC		45.7226503892
58PhosphorylationIDSDTEDSGSDENLD
ECCCCCCCCCCCCHH		33.6826503892
60PhosphorylationSDTEDSGSDENLDQE
CCCCCCCCCCCHHHH		45.7826503892
70PhosphorylationNLDQELLSLAKRKRS
CHHHHHHHHHHHHCC		38.6220873877
79PhosphorylationAKRKRSDSEEKEPPV
HHHHCCCCCCCCCCC		49.2328985074
92PhosphorylationPVSQPAASSDSETSD
CCCCCCCCCCCCCCC		36.4624461736
93PhosphorylationVSQPAASSDSETSDS
CCCCCCCCCCCCCCC		40.1924461736
95PhosphorylationQPAASSDSETSDSDD
CCCCCCCCCCCCCCC		44.7324461736
97PhosphorylationAASSDSETSDSDDEW
CCCCCCCCCCCCCCC		41.6124461736
98PhosphorylationASSDSETSDSDDEWT
CCCCCCCCCCCCCCC		30.9424461736
100PhosphorylationSDSETSDSDDEWTFG
CCCCCCCCCCCCCCC		46.8824461736
105PhosphorylationSDSDDEWTFGSNKNK
CCCCCCCCCCCCCCC		18.9724461736
133PhosphorylationMKKQANKTASSGSSD
HHHHCCCCCCCCCCC		31.4230619164
135PhosphorylationKQANKTASSGSSDKD
HHCCCCCCCCCCCCC		40.2330619164
136PhosphorylationQANKTASSGSSDKDS
HCCCCCCCCCCCCCC		39.9830619164
138PhosphorylationNKTASSGSSDKDSSA
CCCCCCCCCCCCCCC		36.9930619164
139PhosphorylationKTASSGSSDKDSSAE
CCCCCCCCCCCCCCC		52.8130619164
172PhosphorylationSSSDSDSSSEDEEFH
CCCCCCCCCCCHHCC		42.61-
173PhosphorylationSSDSDSSSEDEEFHD
CCCCCCCCCCHHCCC		53.68-
202UbiquitinationRLEQMTEKEREQELF
HHHHHCHHHHHHHHH		53.5624816145
202AcetylationRLEQMTEKEREQELF
HHHHHCHHHHHHHHH		53.5623749302
253PhosphorylationEQEKKKLTQIQESQV
HHHHHHHHHHHHHHH		32.2920068231
258PhosphorylationKLTQIQESQVTSHNK
HHHHHHHHHHHHCHH		17.3620068231
261PhosphorylationQIQESQVTSHNKERR
HHHHHHHHHCHHHHH		19.3420068231
262PhosphorylationIQESQVTSHNKERRS
HHHHHHHHCHHHHHH		26.6320068231
265AcetylationSQVTSHNKERRSKRD
HHHHHCHHHHHHHHH		47.3723749302
279PhosphorylationDEKLDKKSQAMEELK
HHHHHHHHHHHHHHH		28.9829214152
282SulfoxidationLDKKSQAMEELKAER
HHHHHHHHHHHHHHH		2.9721406390
286UbiquitinationSQAMEELKAEREKRK
HHHHHHHHHHHHHHH		52.0232015554
296PhosphorylationREKRKNRTAELLAKK
HHHHHHHHHHHHHHC		33.6028555341
302UbiquitinationRTAELLAKKQPLKTS
HHHHHHHHCCCCCCC		52.4922817900
302AcetylationRTAELLAKKQPLKTS
HHHHHHHHCCCCCCC		52.4925953088
303UbiquitinationTAELLAKKQPLKTSE
HHHHHHHCCCCCCCC		52.0922817900
307UbiquitinationLAKKQPLKTSEVYSD
HHHCCCCCCCCCCCC		57.6022817900
308PhosphorylationAKKQPLKTSEVYSDD
HHCCCCCCCCCCCCC		37.4928176443
309PhosphorylationKKQPLKTSEVYSDDE
HCCCCCCCCCCCCCC		24.3928176443
312PhosphorylationPLKTSEVYSDDEEEE
CCCCCCCCCCCCCCC		11.4330576142
313PhosphorylationLKTSEVYSDDEEEEE
CCCCCCCCCCCCCCC		43.7025159151
324PhosphorylationEEEEDDKSSEKSDRS
CCCCCCCCCCCCHHH		51.2120363803
325PhosphorylationEEEDDKSSEKSDRSS
CCCCCCCCCCCHHHC		55.5820363803
328PhosphorylationDDKSSEKSDRSSRTS
CCCCCCCCHHHCCCC		33.9226657352
331PhosphorylationSSEKSDRSSRTSSSD
CCCCCHHHCCCCCCH		29.2126657352
332PhosphorylationSEKSDRSSRTSSSDE
CCCCHHHCCCCCCHH		40.2326657352
337PhosphorylationRSSRTSSSDEEEEKE
HHCCCCCCHHHHHHH		49.1326437602
397AcetylationGIGNHNSKPVYRVAE
ECCCCCCCCEEEEEE		43.7626051181
400PhosphorylationNHNSKPVYRVAEITG
CCCCCCEEEEEEEEE		14.1128064214
413AcetylationTGVVETAKVYQLGGT
EEEEEEEEEEEECCC		49.2319608861
424UbiquitinationLGGTRTNKGLQLRHG
ECCCCCCCCCEEECC		61.46-
453SulfoxidationEFTESEFMKWKEAMF
CCCHHHHHHHHHHHH		4.4321406390
461PhosphorylationKWKEAMFSAGMQLPT
HHHHHHHHHCCCCCC		15.7229083192
478PhosphorylationEINKKELSIKEALNY
HHCHHHCCHHHHHCC		32.48-
4802-HydroxyisobutyrylationNKKELSIKEALNYKF
CHHHCCHHHHHCCCC		33.29-
480UbiquitinationNKKELSIKEALNYKF
CHHHCCHHHHHCCCC		33.2929967540
486UbiquitinationIKEALNYKFNDQDIE
HHHHHCCCCCHHHHH		36.3029967540
497UbiquitinationQDIEEIVKEKERFRK
HHHHHHHHHHHHHHC		69.5929967540
504AcetylationKEKERFRKAPPNYAM
HHHHHHHCCCCCHHH		63.637696083
504UbiquitinationKEKERFRKAPPNYAM
HHHHHHHCCCCCHHH		63.6329967540
512AcetylationAPPNYAMKKTQLLKE
CCCCHHHHHHHHHHH		44.4925953088
533UbiquitinationLGDQDKAKQIQDQLN
HCCHHHHHHHHHHHH		54.3929967540
555UbiquitinationALDRQRTKNISAISY
HHHHHHHCCHHHHHH		55.2429967540
558PhosphorylationRQRTKNISAISYINQ
HHHHCCHHHHHHHHH		29.0128555341
561PhosphorylationTKNISAISYINQRNR
HCCHHHHHHHHHHCC		21.4828796482
562PhosphorylationKNISAISYINQRNRE
CCHHHHHHHHHHCCC		9.5928796482
575PhosphorylationREWNIVESEKALVAE
CCCCCHHHHHHHHHH		33.24-
587UbiquitinationVAESHNMKNQQMDPF
HHHHHCCCCCCCCCC		57.8532015554
587MethylationVAESHNMKNQQMDPF
HHHHHCCCCCCCCCC		57.8524129315
591SulfoxidationHNMKNQQMDPFTRRQ
HCCCCCCCCCCHHCC		5.2121406390
600UbiquitinationPFTRRQCKPTIVSNS
CCHHCCCCCEEECCC		36.5424816145
624PhosphorylationLAQLNAKYGSGVLPD
HHHHHHHHCCCCCCC		17.7020068231
626PhosphorylationQLNAKYGSGVLPDAP
HHHHHHCCCCCCCCC		23.7320068231
634PhosphorylationGVLPDAPKEMSKGQG
CCCCCCCCHHCCCCC		68.7018669648
637PhosphorylationPDAPKEMSKGQGKDK
CCCCCHHCCCCCCCC		34.4218669648
648PhosphorylationGKDKDLNSKSASDLS
CCCCCCCCCCHHHHH		34.9729214152
649UbiquitinationKDKDLNSKSASDLSE
CCCCCCCCCHHHHHH		49.3032015554
650PhosphorylationDKDLNSKSASDLSED
CCCCCCCCHHHHHHH		32.5925159151
652PhosphorylationDLNSKSASDLSEDLF
CCCCCCHHHHHHHHH		46.2921712546
655PhosphorylationSKSASDLSEDLFKVH
CCCHHHHHHHHHHHH		33.7720873877
657PhosphorylationSASDLSEDLFKVHDF
CHHHHHHHHHHHHCC		54.7718669648
660UbiquitinationDLSEDLFKVHDFDVK
HHHHHHHHHHCCEEE		46.0529967540
674PhosphorylationKIDLQVPSSESKALA
EEEEECCCCCCCEEE		48.1330266825
675O-linked_GlycosylationIDLQVPSSESKALAI
EEEECCCCCCCEEEE		39.5630059200
675PhosphorylationIDLQVPSSESKALAI
EEEECCCCCCCEEEE		39.5630266825
677PhosphorylationLQVPSSESKALAITS
EECCCCCCCEEEEEC		25.7730266825
677O-linked_GlycosylationLQVPSSESKALAITS
EECCCCCCCEEEEEC		25.7730059200
678UbiquitinationQVPSSESKALAITSK
ECCCCCCCEEEEECC		43.2832015554
683PhosphorylationESKALAITSKAPPAK
CCCEEEEECCCCCCC		20.6826074081
684PhosphorylationSKALAITSKAPPAKD
CCEEEEECCCCCCCC		22.2526074081
685AcetylationKALAITSKAPPAKDG
CEEEEECCCCCCCCC		57.1525953088
685UbiquitinationKALAITSKAPPAKDG
CEEEEECCCCCCCCC		57.1532015554
697PhosphorylationKDGAPRRSLNLEDYK
CCCCCCCCCCHHHHH		23.9222167270
703PhosphorylationRSLNLEDYKKRRGLI
CCCCHHHHHHHHCCC		14.7229396449
704UbiquitinationSLNLEDYKKRRGLI-
CCCHHHHHHHHCCC-		52.7232015554
705UbiquitinationLNLEDYKKRRGLI--
CCHHHHHHHHCCC--		40.8924816145
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 RTF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RTF1_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 RTF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LEO1_HUMANLEO1physical
20178742
CDC73_HUMANCDC73physical
20178742
CTR9_HUMANCTR9physical
20178742
WDR61_HUMANWDR61physical
20178742
PAF1_HUMANPAF1physical
20178742
NEDD4_HUMANNEDD4physical
19953087
ECHA_HUMANHADHAphysical
20305087
ECHB_HUMANHADHBphysical
20305087
A4_HUMANAPPphysical
21832049
SP16H_HUMANSUPT16Hphysical
22939629
SSRP1_HUMANSSRP1physical
22939629
TRPM8_HUMANTRPM8physical
22939629
ERF1_HUMANETF1physical
22863883
STAT1_HUMANSTAT1physical
22863883
CHD1_HUMANCHD1physical
26344197
CTR9_HUMANCTR9physical
26344197
RL37_HUMANRPL37physical
26344197
SRRM2_HUMANSRRM2physical
26344197
SP16H_HUMANSUPT16Hphysical
26344197
SPT5H_HUMANSUPT5Hphysical
26344197
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 RTF1_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-413, 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 SER-697, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697, AND MASSSPECTROMETRY.

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