TREF1_HUMAN - dbPTM
TREF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TREF1_HUMAN
UniProt AC Q96PN7
Protein Name Transcriptional-regulating factor 1
Gene Name TRERF1
Organism Homo sapiens (Human).
Sequence Length 1200
Subcellular Localization Nucleus .
Protein Description Binds DNA and activates transcription of CYP11A1. Interaction with CREBBP and EP300 results in a synergistic transcriptional activation of CYP11A1..
Protein Sequence MGDQQLYKTNHVAHGSENLFYQQPPLGVHSGLNHNYGNAVTGGGMDAPQASPISPHFPQDTRDGLGLPVGSKNLGQMDTSRQGGWGSHAGPGNHVQLRGNLANSNMMWGAPAQAEPTDGYQYTYSQASEIRTQKLTSGVLHKLDSFTQVFANQNLRIQVNNMAQVLHTQSAVMDGAPDSALRQLLSQKPMEPPAPAIPSRYQQVPQQPHPGFTGGLSKPALQVGQHPTQGHLYYDYQQPLAQVPVQGGQPLQAPQMLSQHMQQMQQHQYYPPQQQQQAGQQRISMQEIQTQPQQIRPSQPQPPPQQQQPQQLQLQQRQGSMQIPQYYQPQPMMQHLQEQQQQQMHLQPPSYHRDPHQYTPEQAHTVQLIPLGSMSQYYYQEPQQPYSHPLYQQSHLSQHQQREDSQLKTYSSDRQAQAMLSSHGDLGPPDTGMGDPASSDLTRVSSTLPHRPLLSPSGIHLNNMGPQHQQLSPSAMWPQMHLPDGRAQPGSPESSGQPKGAFGEQFDAKNKLTCSICLKEFKNLPALNGHMRSHGGMRASPNLKQEEGEKVLPPQPQPPLPPPPPPPPPPQLPPEAESLTPMVMPVSVPVKLLPPKPSSQGFTNSTVAAPSARDKPASSMSDDEMPVLEIPRKHQPSVPKAEEPLKTVQEKKKFRHRPEPLFIPPPPSYNPNPAASYSGATLYQSQLRSPRVLGDHLLLDPTHELPPYTPPPMLSPVRQGSGLFSNVLISGHGPGAHPQLPLTPLTPTPRVLLCRSNSIDGSNVTVTPGPGEQTVDVEPRINIGLRFQAEIPELQDISALAQDTHKATLVWKPWPELENHDLQQRVENLLNLCCSSALPGGGTNSEFALHSLFEAKGDVMVALEMLLLRKPVRLKCHPLANYHYAGSDKWTSLERKLFNKALATYSKDFIFVQKMVKSKTVAQCVEYYYTWKKIMRLGRKHRTRLAEIIDDCVTSEEEEELEEEEEEDPEEDRKSTKEEESEVPKSPEPPPVPVLAPTEGPPLQALGQPSGSFICEMPNCGAVFSSRQALNGHARIHGGTNQVTKARGAIPSGKQKPGGTQSGYCSVKSSPSHSTTSGETDPTTIFPCKECGKVFFKIKSRNAHMKTHRQQEEQQRQKAQKAAFAAEMAATIERTTGPVGAPGLLPLDQLSLIKPIKDVDILDDDVVQQLGGVMEEAEVVDTDLLLDDQDSVLLQGDAEL
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
27 (in isoform 2)Ubiquitination-22.3621890473
27 (in isoform 3)Ubiquitination-22.3621890473
41PhosphorylationHNYGNAVTGGGMDAP
CCCCCCCCCCCCCCC
27.9128348404
51PhosphorylationGMDAPQASPISPHFP
CCCCCCCCCCCCCCC
19.9526074081
54PhosphorylationAPQASPISPHFPQDT
CCCCCCCCCCCCCCC
18.7326074081
72SumoylationLGLPVGSKNLGQMDT
CCCCCCCCCCCCCCC
50.71-
72SumoylationLGLPVGSKNLGQMDT
CCCCCCCCCCCCCCC
50.71-
72UbiquitinationLGLPVGSKNLGQMDT
CCCCCCCCCCCCCCC
50.71-
104PhosphorylationLRGNLANSNMMWGAP
EECCCCCCCCCCCCC
22.0930576142
120PhosphorylationQAEPTDGYQYTYSQA
CCCCCCCCCEEECCH
10.9330576142
122PhosphorylationEPTDGYQYTYSQASE
CCCCCCCEEECCHHH
10.1220090780
134UbiquitinationASEIRTQKLTSGVLH
HHHHHHCCCCHHHHH
53.79-
136PhosphorylationEIRTQKLTSGVLHKL
HHHHCCCCHHHHHHH
30.3927251275
137PhosphorylationIRTQKLTSGVLHKLD
HHHCCCCHHHHHHHH
37.0227251275
145PhosphorylationGVLHKLDSFTQVFAN
HHHHHHHHHHHHHCC
40.4027080861
147PhosphorylationLHKLDSFTQVFANQN
HHHHHHHHHHHCCCC
27.9827080861
188AcetylationLRQLLSQKPMEPPAP
HHHHHCCCCCCCCCC
42.8526051181
188UbiquitinationLRQLLSQKPMEPPAP
HHHHHCCCCCCCCCC
42.8521906983
188 (in isoform 1)Ubiquitination-42.8521890473
188 (in isoform 4)Ubiquitination-42.8521890473
188 (in isoform 5)Ubiquitination-42.8521890473
379 (in isoform 2)Phosphorylation-11.06-
379 (in isoform 3)Phosphorylation-11.06-
408UbiquitinationQREDSQLKTYSSDRQ
HHHHHHHHHHCHHHH
37.47-
421PhosphorylationRQAQAMLSSHGDLGP
HHHHHHHHHCCCCCC
13.7522210691
422PhosphorylationQAQAMLSSHGDLGPP
HHHHHHHHCCCCCCC
27.7722210691
445PhosphorylationSSDLTRVSSTLPHRP
CCCCCEECCCCCCCC
17.8327251275
446PhosphorylationSDLTRVSSTLPHRPL
CCCCEECCCCCCCCC
30.9827251275
447PhosphorylationDLTRVSSTLPHRPLL
CCCEECCCCCCCCCC
36.4827251275
455PhosphorylationLPHRPLLSPSGIHLN
CCCCCCCCCCCCCCC
25.3828348404
457PhosphorylationHRPLLSPSGIHLNNM
CCCCCCCCCCCCCCC
47.1827251275
472PhosphorylationGPQHQQLSPSAMWPQ
CHHCCCCCHHHCCCC
16.6927251275
474PhosphorylationQHQQLSPSAMWPQMH
HCCCCCHHHCCCCCC
27.6428348404
491PhosphorylationDGRAQPGSPESSGQP
CCCCCCCCCCCCCCC
31.9823401153
494PhosphorylationAQPGSPESSGQPKGA
CCCCCCCCCCCCCCC
43.0630266825
495PhosphorylationQPGSPESSGQPKGAF
CCCCCCCCCCCCCCC
39.5230266825
509SumoylationFGEQFDAKNKLTCSI
CCCCCCCCCCEEEEE
57.36-
509AcetylationFGEQFDAKNKLTCSI
CCCCCCCCCCEEEEE
57.3625953088
509SumoylationFGEQFDAKNKLTCSI
CCCCCCCCCCEEEEE
57.36-
519AcetylationLTCSICLKEFKNLPA
EEEEEHHHHHCCCCH
57.6126051181
522SumoylationSICLKEFKNLPALNG
EEHHHHHCCCCHHCC
59.68-
522SumoylationSICLKEFKNLPALNG
EEHHHHHCCCCHHCC
59.68-
540PhosphorylationSHGGMRASPNLKQEE
CCCCCCCCCCCCHHH
12.1725849741
540 (in isoform 4)Phosphorylation-12.17-
540 (in isoform 5)Phosphorylation-12.17-
544SumoylationMRASPNLKQEEGEKV
CCCCCCCCHHHCCCC
63.40-
544SumoylationMRASPNLKQEEGEKV
CCCCCCCCHHHCCCC
63.40-
568 (in isoform 2)Ubiquitination-60.0021890473
568 (in isoform 3)Ubiquitination-60.0021890473
603PhosphorylationKPSSQGFTNSTVAAP
CCCCCCCCCCCCCCC
34.7728555341
618PhosphorylationSARDKPASSMSDDEM
CCCCCCCCCCCCCCC
34.7930266825
619PhosphorylationARDKPASSMSDDEMP
CCCCCCCCCCCCCCC
25.1430266825
621PhosphorylationDKPASSMSDDEMPVL
CCCCCCCCCCCCCEE
43.8130266825
633AcetylationPVLEIPRKHQPSVPK
CEEECCCCCCCCCCC
41.03-
637PhosphorylationIPRKHQPSVPKAEEP
CCCCCCCCCCCCCCC
44.47-
640SumoylationKHQPSVPKAEEPLKT
CCCCCCCCCCCCCCH
67.29-
640AcetylationKHQPSVPKAEEPLKT
CCCCCCCCCCCCCCH
67.29-
640SumoylationKHQPSVPKAEEPLKT
CCCCCCCCCCCCCCH
67.29-
646AcetylationPKAEEPLKTVQEKKK
CCCCCCCCHHHHHHC
58.3225953088
676PhosphorylationYNPNPAASYSGATLY
CCCCCCCCCCCCEEE
23.1823401153
677PhosphorylationNPNPAASYSGATLYQ
CCCCCCCCCCCEEEH
13.3428152594
678PhosphorylationPNPAASYSGATLYQS
CCCCCCCCCCEEEHH
21.3228152594
681PhosphorylationAASYSGATLYQSQLR
CCCCCCCEEEHHHCC
29.5328152594
683PhosphorylationSYSGATLYQSQLRSP
CCCCCEEEHHHCCCC
11.1928152594
685PhosphorylationSGATLYQSQLRSPRV
CCCEEEHHHCCCCCC
20.0228152594
689PhosphorylationLYQSQLRSPRVLGDH
EEHHHCCCCCCCCCC
26.1728464451
702PhosphorylationDHLLLDPTHELPPYT
CCCCCCCCCCCCCCC
27.8728450419
708PhosphorylationPTHELPPYTPPPMLS
CCCCCCCCCCCCCCC
29.9130108239
709PhosphorylationTHELPPYTPPPMLSP
CCCCCCCCCCCCCCC
34.7821712546
715PhosphorylationYTPPPMLSPVRQGSG
CCCCCCCCCCCCCCC
18.3322617229
721PhosphorylationLSPVRQGSGLFSNVL
CCCCCCCCCCCCCEE
24.8020068231
725PhosphorylationRQGSGLFSNVLISGH
CCCCCCCCCEEEECC
30.9520068231
729 (in isoform 4)Ubiquitination-3.9521890473
729 (in isoform 5)Ubiquitination-3.9521890473
730PhosphorylationLFSNVLISGHGPGAH
CCCCEEEECCCCCCC
22.1526657352
743PhosphorylationAHPQLPLTPLTPTPR
CCCCCCCCCCCCCCE
17.8227273156
746PhosphorylationQLPLTPLTPTPRVLL
CCCCCCCCCCCEEEE
26.7327273156
748PhosphorylationPLTPLTPTPRVLLCR
CCCCCCCCCEEEEEE
20.6327273156
756PhosphorylationPRVLLCRSNSIDGSN
CEEEEEECCCCCCCC
33.6530278072
758PhosphorylationVLLCRSNSIDGSNVT
EEEEECCCCCCCCCE
24.2530278072
762PhosphorylationRSNSIDGSNVTVTPG
ECCCCCCCCCEECCC
25.1223927012
765PhosphorylationSIDGSNVTVTPGPGE
CCCCCCCEECCCCCC
23.9423927012
767PhosphorylationDGSNVTVTPGPGEQT
CCCCCEECCCCCCCE
17.1123927012
774PhosphorylationTPGPGEQTVDVEPRI
CCCCCCCEEECCCCC
17.8623927012
812UbiquitinationHKATLVWKPWPELEN
CHHEEEEECCHHHCC
29.7121890473
812 (in isoform 1)Ubiquitination-29.7121890473
892PhosphorylationAGSDKWTSLERKLFN
CCCCCCCHHHHHHHH
27.41-
907AcetylationKALATYSKDFIFVQK
HHHHHHCCCEEEEHH
46.3619821629
914AcetylationKDFIFVQKMVKSKTV
CCEEEEHHHHCCCCH
40.1224885407
917AcetylationIFVQKMVKSKTVAQC
EEEHHHHCCCCHHHH
42.6119821639
954PhosphorylationEIIDDCVTSEEEEEL
HHHHHHCCCHHHHHH
36.4330576142
955PhosphorylationIIDDCVTSEEEEELE
HHHHHCCCHHHHHHH
23.7130576142
975PhosphorylationDPEEDRKSTKEEESE
CCHHHHHCHHHHHCC
45.6825159151
976PhosphorylationPEEDRKSTKEEESEV
CHHHHHCHHHHHCCC
45.5727251275
981PhosphorylationKSTKEEESEVPKSPE
HCHHHHHCCCCCCCC
47.3622985185
986PhosphorylationEESEVPKSPEPPPVP
HHCCCCCCCCCCCCC
28.5523879269
1040PhosphorylationHARIHGGTNQVTKAR
CCEECCCCCHHHCCC
27.3730108239
1044PhosphorylationHGGTNQVTKARGAIP
CCCCCHHHCCCCCCC
14.8230108239
1052PhosphorylationKARGAIPSGKQKPGG
CCCCCCCCCCCCCCC
53.1324719451
1054AcetylationRGAIPSGKQKPGGTQ
CCCCCCCCCCCCCCC
60.5325953088
1056AcetylationAIPSGKQKPGGTQSG
CCCCCCCCCCCCCCC
49.4626051181
1062PhosphorylationQKPGGTQSGYCSVKS
CCCCCCCCCEEEEEC
31.4127794612
1064PhosphorylationPGGTQSGYCSVKSSP
CCCCCCCEEEEECCC
6.1827794612
1066PhosphorylationGTQSGYCSVKSSPSH
CCCCCEEEEECCCCC
24.8925056879
1069PhosphorylationSGYCSVKSSPSHSTT
CCEEEEECCCCCCCC
45.3823401153
1070PhosphorylationGYCSVKSSPSHSTTS
CEEEEECCCCCCCCC
25.3823927012
1072PhosphorylationCSVKSSPSHSTTSGE
EEEECCCCCCCCCCC
31.8323927012
1074PhosphorylationVKSSPSHSTTSGETD
EECCCCCCCCCCCCC
37.4025159151
1075PhosphorylationKSSPSHSTTSGETDP
ECCCCCCCCCCCCCC
21.4023927012
1076PhosphorylationSSPSHSTTSGETDPT
CCCCCCCCCCCCCCC
37.4423927012
1077PhosphorylationSPSHSTTSGETDPTT
CCCCCCCCCCCCCCC
34.4223927012
1080PhosphorylationHSTTSGETDPTTIFP
CCCCCCCCCCCCEEE
51.2925394399
1083PhosphorylationTSGETDPTTIFPCKE
CCCCCCCCCEEECCH
35.0223927012
1084PhosphorylationSGETDPTTIFPCKEC
CCCCCCCCEEECCHH
26.4723927012
1089AcetylationPTTIFPCKECGKVFF
CCCEEECCHHCCEEE
57.1726051181
1151PhosphorylationLLPLDQLSLIKPIKD
EEEHHHHHHCCCCCC
23.5524719451
1154AcetylationLDQLSLIKPIKDVDI
HHHHHHCCCCCCCCC
46.0819608861

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 TREF1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TREF1_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 TREF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STF1_HUMANNR5A1physical
12101186
TDIF1_HUMANDNTTIP1physical
21258344
HDAC1_HUMANHDAC1physical
21258344

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 TREF1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, AND MASSSPECTROMETRY.
"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 THR-767, AND MASSSPECTROMETRY.

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