CTR9_MOUSE - dbPTM
CTR9_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTR9_MOUSE
UniProt AC Q62018
Protein Name RNA polymerase-associated protein CTR9 homolog
Gene Name Ctr9
Organism Mus musculus (Mouse).
Sequence Length 1173
Subcellular Localization Nucleus speckle .
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. 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. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription (By similarity). 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 the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway; may regulate DNA-association of STAT3..
Protein Sequence MSRGSIEIPLRDTDEVIELDFDQLPEGDEVISILKQEHTQLHIWIALALEYYKQGKTEEFVKLLEAARIDGNLDYRDHEKDQMTCLDTLAAYYVQQARKEKNKDNKKDLITQATLLYTMADKIIMYDQNHLLGRACFCLLEGDKMDQADAQFHFVLNQSPNNIPALLGKACISFNKKDYRGALAYYKKALRTNPGCPAEVRLGMGHCFVKLNKLEKARLAFSRALELNSKCVGALVGLAVLELNNKEADSIKNGVQLLSRAYTIDPSNPMVLNHLANHFFFKKDYSKVQHLALHAFHNTEVEAMQAESCYQLARSFHVQEDYDQAFQYYYQATQFASSSFVLPFFGLGQMYIYRGDKENASQCFEKVLKAYPNNYETMKILGSLYAASEDQEKRDIAKGHLKKVTEQYPDDVEAWIELAQILEQTDIQGALSAYGTATRILQEKVQADVPPEILNNVGALHFRLGNLGEAKKYFLASLDRAKAEAEHDEHYYNAISVTTSYNLARLYEAMCEFHEAEKLYKNILREHPNYVDCYLRLGAMARDKGNFYEASDWFKEALQINQDHPDAWSLIGNLHLAKQEWGPGQKKFERILKQPATQSDTYSMLALGNVWLQTLHQPTRDREKEKRHQDRALAIYKQVLRNDAKNLYAANGIGAVLAHKGYFREARDVFAQVREATADISDVWLNLAHIYVEQKQYISAVQMYENCLRKFYKHQNTEVVLYLARALFKCGKLQECKQTLLKARHVAPSDTVLMFNVALVLQRLATSVLKDEKSNLKEVLNAVKELELAHRYFSYLSKVGDKMRFDLALAASEARQCSDLLSQAQYHVARARKQDEEERELRAKQEQEKELLRQKLLKEQEEKRLREKEEQKKLLEQRAQYVEKTKNILMFTGETEATKEKKRGGGGGRRSKKGGEFDEFVNDDTDDDLPVSKKKKRRKGSGSEQEGEEEEGGERKKKRRRRPPKGEEGSEEEETENGPKPKKRRPPRAEKKKAPKPERLPPSMKGKIKSKAIISSSDDSSDEDKLKIADEGHPRNSNSDSDDDERPNRRASSESDSDDNQNKSGSEAGSPRRSGRQESDEDSDSDQPSRKRRRSGSEQSDNESVQSGRSPSGASENENDSRPASPSAESDHESEQGSDNEGSGQGSGNESEPEGSNNEASDRGSEHGSDDSD
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
2Phosphorylation------MSRGSIEIP
------CCCCCEEEE		57.5623984901
5Phosphorylation---MSRGSIEIPLRD
---CCCCCEEEECCC		18.8822982522
114PhosphorylationKDLITQATLLYTMAD
HHHHHHHHHHHHHHH		13.8929514104
118PhosphorylationTQATLLYTMADKIIM
HHHHHHHHHHHHHHH		13.0729514104
259PhosphorylationKNGVQLLSRAYTIDP
HHHHHHHHHCEECCC		24.3729550500
366UbiquitinationNASQCFEKVLKAYPN
HHHHHHHHHHHHCCC		32.3922790023
371PhosphorylationFEKVLKAYPNNYETM
HHHHHHHCCCCHHHH		12.6128576409
375PhosphorylationLKAYPNNYETMKILG
HHHCCCCHHHHHHHH		21.2928576409
377PhosphorylationAYPNNYETMKILGSL
HCCCCHHHHHHHHHH		17.2628576409
597PhosphorylationRILKQPATQSDTYSM
HHHCCCCCCCCCCHH		34.98-
599PhosphorylationLKQPATQSDTYSMLA
HCCCCCCCCCCHHHH		27.80-
697 (in isoform 2)Phosphorylation-12.1323140645
699 (in isoform 2)Phosphorylation-19.9023140645
705 (in isoform 2)Phosphorylation-35.8023140645
706 (in isoform 2)Phosphorylation-16.7923140645
804MethylationSKVGDKMRFDLALAA
HHHCHHHHHHHHHHH		27.8918962911
804DimethylationSKVGDKMRFDLALAA
HHHCHHHHHHHHHHH		27.89-
815DimethylationALAASEARQCSDLLS
HHHHHHHHHHHHHHH		33.71-
815MethylationALAASEARQCSDLLS
HHHHHHHHHHHHHHH		33.7118962919
818PhosphorylationASEARQCSDLLSQAQ
HHHHHHHHHHHHHHH		23.9725619855
911PhosphorylationGGGGGRRSKKGGEFD
CCCCCCCCCCCCCCC		37.0425777480
925PhosphorylationDEFVNDDTDDDLPVS
CHHCCCCCCCCCCCC		44.1627087446
932PhosphorylationTDDDLPVSKKKKRRK
CCCCCCCCCCCCCCC		36.5024925903
941PhosphorylationKKKRRKGSGSEQEGE
CCCCCCCCCCCCCCC		42.0325521595
943PhosphorylationKRRKGSGSEQEGEEE
CCCCCCCCCCCCCCC		37.4925521595
970PhosphorylationPPKGEEGSEEEETEN
CCCCCCCCHHHCCCC		45.1527087446
975PhosphorylationEGSEEEETENGPKPK
CCCHHHCCCCCCCCC		37.7225619855
1003PhosphorylationKPERLPPSMKGKIKS
CHHHCCHHHCCCCCE		31.0529895711
1015PhosphorylationIKSKAIISSSDDSSD
CCEEEEECCCCCCCC		20.0623429704
1016PhosphorylationKSKAIISSSDDSSDE
CEEEEECCCCCCCCH		27.6423429704
1017PhosphorylationSKAIISSSDDSSDED
EEEEECCCCCCCCHH		38.3523429704
1020PhosphorylationIISSSDDSSDEDKLK
EECCCCCCCCHHHHH		44.6823375375
1021PhosphorylationISSSDDSSDEDKLKI
ECCCCCCCCHHHHHH		52.6023375375
1037PhosphorylationDEGHPRNSNSDSDDD
CCCCCCCCCCCCCCC		38.7025521595
1039PhosphorylationGHPRNSNSDSDDDER
CCCCCCCCCCCCCCC		38.0125521595
1041PhosphorylationPRNSNSDSDDDERPN
CCCCCCCCCCCCCCC		42.6425521595
1057PhosphorylationRASSESDSDDNQNKS
HHCCCCCCCCCCCCC		57.0221183079
1066PhosphorylationDNQNKSGSEAGSPRR
CCCCCCCCCCCCCCC		31.2221183079
1070PhosphorylationKSGSEAGSPRRSGRQ
CCCCCCCCCCCCCCC		23.4522817900
1074PhosphorylationEAGSPRRSGRQESDE
CCCCCCCCCCCCCCC		39.3427087446
1079PhosphorylationRRSGRQESDEDSDSD
CCCCCCCCCCCCCCC		37.6525521595
1083PhosphorylationRQESDEDSDSDQPSR
CCCCCCCCCCCCCCH		36.6525521595
1085PhosphorylationESDEDSDSDQPSRKR
CCCCCCCCCCCCHHH		41.9425521595
1089PhosphorylationDSDSDQPSRKRRRSG
CCCCCCCCHHHHCCC		44.8129899451
1095PhosphorylationPSRKRRRSGSEQSDN
CCHHHHCCCCCCCCC		44.8830635358
1097PhosphorylationRKRRRSGSEQSDNES
HHHHCCCCCCCCCCC		33.4423684622
1100PhosphorylationRRSGSEQSDNESVQS
HCCCCCCCCCCCCCC		38.0522345495
1121PhosphorylationASENENDSRPASPSA
CCCCCCCCCCCCCCC		52.31-
1125PhosphorylationENDSRPASPSAESDH
CCCCCCCCCCCCCCC		23.28-
1130PhosphorylationPASPSAESDHESEQG
CCCCCCCCCCCCCCC		43.94-
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 CTR9_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTR9_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 CTR9_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAF1_MOUSEPaf1physical
19345177
CDC73_MOUSECdc73physical
19345177
LEO1_MOUSELeo1physical
19345177
WDR61_MOUSEWdr61physical
19345177
PABP1_MOUSEPabpc1physical
19345177
RUVB1_MOUSERuvbl1physical
19345177
RCOR2_MOUSERcor2physical
19345177
RUVB2_MOUSERuvbl2physical
19345177
SFPQ_MOUSESfpqphysical
19345177
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CTR9_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-941; SER-943;SER-970; SER-1037; SER-1039 AND SER-1041, AND MASS SPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1079; SER-1083 ANDSER-1085, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925 AND SER-970, ANDMASS SPECTROMETRY.
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, AND MASSSPECTROMETRY.

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