EDRF1_HUMAN - dbPTM
EDRF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EDRF1_HUMAN
UniProt AC Q3B7T1
Protein Name Erythroid differentiation-related factor 1
Gene Name EDRF1
Organism Homo sapiens (Human).
Sequence Length 1238
Subcellular Localization Nucleus .
Protein Description Transcription factor involved in erythroid differentiation. Involved in transcriptional activation of the globin gene..
Protein Sequence MGDAKEAGAEGPPAGAAARGGLSLLSQGESEESSAQGSALFLGGNEVKSRAVVKYSSAPPRTAFARLEEKTDLKLPPANWLRESAKLGPAGTTILGNSKKSKPFSSFGMAYDFIDSVGNDVDVVSDSENIKKLLKIPYSKSHVSMAVHRIGRTLLLDELDIQELFMRSSQTGDWTWLKEFYQRLIDQKWQRKKKSKEHWYQKAILSKFLYYSINGDGAAQPVSSTAEQQESSSSDQTNDSEGASWPAPFEMPSSVSEDPSASSQGSEPLEPSYIVGHVASAPKEQNLITLFNDGEHSQGLKNDFVRNILWTFEDIHMLVGSNMPIFGGGRYPAVSLRLRDNNKPINVLTGIDYWLDNLICNVPELVMCFHVNGIVQKYEMIKTEEIPNLENSNFSTKVIKDIAQNILSFLKSNCTKEGHTYWLFKASGSDIVKLYDLTTLCEETEDKYQNPFTMPVAILLYKVACNMMMKKNQNKKHYGTIRTLLLNCLKLLDKSRHPQIIASANYMLSELFQLDEPKKEENSESPLNENSDESYSEEEEEMPDSDENGSYSTSSDPSDDSKAVAIIKSVGELSVPEKYKSIHQIRPSCAFPVCHDTEERCRLVLSYVLEGLKSVDSSIKKESDLPAADPSTPIPLKYEDESSRGGPEGLEKQMALFLDKMGSLQKGNYSSQSGMIPGSWQHKMKLQLILKSSKAYYVLSDAAMSLQKYGRALRYIKLALQSHDTYCCLCTNMLSEVLLFLSQYLTLCGDIQLMLAQNANNRAAHLEEFHYQTKEDQEILHSLHRESSCQGFAWATDLSTDLESQLSVSCKCYEAANEILQFSDLKSQNPEHYVQVLKRMGNIRNEIGVFYMNQAAALQSERLVSKSVSAAEQQLWKKSFSCFEKGIHNFESIEDATNAALLLCNTGRLMRICAQAHCGAGDELKREFSPEEGLYYNKAIDYYLKALRSLGTRDIHPAVWDSVNWELSTTYFTMATLQQDYAPLSRKAQEQIEKEVSEAMMKSLKYCDVDSVSARQPLCQYRAATIHHRLASMYHSCLRNQVGDEHLRKQHRVLADLHYSKAAKLFQLLKDAPCELLRVQLERVAFAEFQMTSQNSNVGKLKTLSGALDIMVRTEHAFQLIQKELIEEFGQPKSGDAAAAADASPSLNREEVMKLLSIFESRLSFLLLQSIKLLSSTKKKTSNNIEDDTILKTNKHIYSQLLRATANKTATLLERINVIVHLLGQLAAGSAASSNAVQ
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
5Ubiquitination---MGDAKEAGAEGP
---CCCHHHCCCCCC
53.4924816145
23PhosphorylationAAARGGLSLLSQGES
HHHHHHHHHHCCCCC
30.4530624053
26PhosphorylationRGGLSLLSQGESEES
HHHHHHHCCCCCCCC
41.2430624053
30PhosphorylationSLLSQGESEESSAQG
HHHCCCCCCCCCCCC
54.1930624053
33PhosphorylationSQGESEESSAQGSAL
CCCCCCCCCCCCCEE
27.2430624053
34PhosphorylationQGESEESSAQGSALF
CCCCCCCCCCCCEEE
28.0830624053
38PhosphorylationEESSAQGSALFLGGN
CCCCCCCCEEEECCC
15.0930624053
99AcetylationTTILGNSKKSKPFSS
CEECCCCCCCCCCCC
66.137481415
102AcetylationLGNSKKSKPFSSFGM
CCCCCCCCCCCCCCH
59.997481425
106PhosphorylationKKSKPFSSFGMAYDF
CCCCCCCCCCHHHHH
26.63-
135UbiquitinationENIKKLLKIPYSKSH
HHHHHHHCCCCCHHH
52.66-
168PhosphorylationIQELFMRSSQTGDWT
HHHHHHHHCCCCCCH
18.2725219547
169PhosphorylationQELFMRSSQTGDWTW
HHHHHHHCCCCCCHH
22.7725219547
171PhosphorylationLFMRSSQTGDWTWLK
HHHHHCCCCCCHHHH
38.7725219547
175PhosphorylationSSQTGDWTWLKEFYQ
HCCCCCCHHHHHHHH
26.1725219547
178 (in isoform 3)Ubiquitination-37.0221890473
178 (in isoform 1)Ubiquitination-37.0221890473
178 (in isoform 4)Ubiquitination-37.0221890473
178UbiquitinationTGDWTWLKEFYQRLI
CCCCHHHHHHHHHHH
37.0221890473
178 (in isoform 5)Ubiquitination-37.0221890473
181PhosphorylationWTWLKEFYQRLIDQK
CHHHHHHHHHHHHHH
8.2025219547
188AcetylationYQRLIDQKWQRKKKS
HHHHHHHHHHHHHHC
41.367975581
192AcetylationIDQKWQRKKKSKEHW
HHHHHHHHHHCHHHH
49.837975591
196UbiquitinationWQRKKKSKEHWYQKA
HHHHHHCHHHHHHHH
63.5829967540
301 (in isoform 3)Ubiquitination-62.3821890473
301UbiquitinationGEHSQGLKNDFVRNI
CCCCHHHCCHHHHHH
62.3821906983
301 (in isoform 4)Ubiquitination-62.3821890473
301 (in isoform 1)Ubiquitination-62.3821890473
340UbiquitinationAVSLRLRDNNKPINV
EEEEEECCCCCCCEE
68.5923000965
343UbiquitinationLRLRDNNKPINVLTG
EEECCCCCCCEEECC
54.2321890473
363UbiquitinationDNLICNVPELVMCFH
HHHHCCCCHHHHHEE
18.4032015554
363 (in isoform 5)Ubiquitination-18.4021890473
383PhosphorylationQKYEMIKTEEIPNLE
HEEEEEECCCCCCCC
28.1129888752
392PhosphorylationEIPNLENSNFSTKVI
CCCCCCCCCCCHHHH
29.8529888752
395PhosphorylationNLENSNFSTKVIKDI
CCCCCCCCHHHHHHH
31.4129888752
396PhosphorylationLENSNFSTKVIKDIA
CCCCCCCHHHHHHHH
25.7829888752
397 (in isoform 3)Ubiquitination-40.5421890473
397 (in isoform 4)Ubiquitination-40.5421890473
397 (in isoform 1)Ubiquitination-40.5421890473
397UbiquitinationENSNFSTKVIKDIAQ
CCCCCCHHHHHHHHH
40.5421906983
408PhosphorylationDIAQNILSFLKSNCT
HHHHHHHHHHHHCCC
25.4124719451
448PhosphorylationCEETEDKYQNPFTMP
CHHCCCHHCCCCHHH
26.33-
453PhosphorylationDKYQNPFTMPVAILL
CHHCCCCHHHHHHHH
23.09-
544UbiquitinationEEEEEMPDSDENGSY
HHHHCCCCCCCCCCC
68.3729967540
578UbiquitinationGELSVPEKYKSIHQI
HHCCCCHHHHCHHHC
52.4929967540
603 (in isoform 5)Ubiquitination-5.3521890473
603UbiquitinationDTEERCRLVLSYVLE
CHHHHHHHHHHHHHH
5.3529967540
618UbiquitinationGLKSVDSSIKKESDL
HHHHCCHHCCHHCCC
33.6829967540
631PhosphorylationDLPAADPSTPIPLKY
CCCCCCCCCCCCCCC
47.5727273156
632PhosphorylationLPAADPSTPIPLKYE
CCCCCCCCCCCCCCC
30.5321815630
632UbiquitinationLPAADPSTPIPLKYE
CCCCCCCCCCCCCCC
30.5329967540
637UbiquitinationPSTPIPLKYEDESSR
CCCCCCCCCCCCCCC
41.0421906983
637 (in isoform 1)Ubiquitination-41.0421890473
637 (in isoform 3)Ubiquitination-41.0421890473
642PhosphorylationPLKYEDESSRGGPEG
CCCCCCCCCCCCCCH
37.3425627689
643PhosphorylationLKYEDESSRGGPEGL
CCCCCCCCCCCCCHH
32.6625627689
644MethylationKYEDESSRGGPEGLE
CCCCCCCCCCCCHHH
64.47-
652UbiquitinationGGPEGLEKQMALFLD
CCCCHHHHHHHHHHH
50.8729967540
657UbiquitinationLEKQMALFLDKMGSL
HHHHHHHHHHHHCCC
6.3523000965
660 (in isoform 5)Ubiquitination-47.5121890473
660UbiquitinationQMALFLDKMGSLQKG
HHHHHHHHHCCCCCC
47.5121890473
666UbiquitinationDKMGSLQKGNYSSQS
HHHCCCCCCCCCCCC
55.1829967540
691UbiquitinationMKLQLILKSSKAYYV
HHHHHHHHCCCCCHH
45.7723000965
694UbiquitinationQLILKSSKAYYVLSD
HHHHHCCCCCHHHHH
47.7223000965
694 (in isoform 3)Ubiquitination-47.7221890473
694 (in isoform 1)Ubiquitination-47.7221890473
696PhosphorylationILKSSKAYYVLSDAA
HHHCCCCCHHHHHHH
9.6118083107
697PhosphorylationLKSSKAYYVLSDAAM
HHCCCCCHHHHHHHH
10.3618083107
715PhosphorylationKYGRALRYIKLALQS
HHHHHHHHHHHHHHC
11.8518083107
771PhosphorylationAHLEEFHYQTKEDQE
HHHHHHHCCCHHHHH
24.1727642862
774UbiquitinationEEFHYQTKEDQEILH
HHHHCCCHHHHHHHH
43.71-
792UbiquitinationRESSCQGFAWATDLS
HHCCCCCEEEEECCC
1.8029967540
826UbiquitinationILQFSDLKSQNPEHY
HHHHHHHHHCCHHHH
55.7929967540
843UbiquitinationVLKRMGNIRNEIGVF
HHHHHCCHHHHHHEE
4.0829967540
877UbiquitinationAAEQQLWKKSFSCFE
HHHHHHHHHHHHHHH
47.3229967540
891UbiquitinationEKGIHNFESIEDATN
HHCCCCCCCHHHHHH
57.0029967540
904UbiquitinationTNAALLLCNTGRLMR
HHHHHHHHHHHHHHH
4.2929967540
925UbiquitinationCGAGDELKREFSPEE
CCCCHHHHHCCCCCC
48.0829967540
938UbiquitinationEEGLYYNKAIDYYLK
CCCCHHHHHHHHHHH
30.5129967540
1006PhosphorylationAMMKSLKYCDVDSVS
HHHHHCCCCCCCCCC
10.12-
1011PhosphorylationLKYCDVDSVSARQPL
CCCCCCCCCCCCCCH
20.16-
1013PhosphorylationYCDVDSVSARQPLCQ
CCCCCCCCCCCCHHH
22.99-
1021PhosphorylationARQPLCQYRAATIHH
CCCCHHHHHHHHHHH
10.96-
1134PhosphorylationEEFGQPKSGDAAAAA
HHHCCCCCCCHHHHC
48.8923403867
1144PhosphorylationAAAAADASPSLNREE
HHHHCCCCCCCCHHH
18.6423403867
1146PhosphorylationAAADASPSLNREEVM
HHCCCCCCCCHHHHH
35.4624719451
1153SulfoxidationSLNREEVMKLLSIFE
CCCHHHHHHHHHHHH
2.6121406390
1158 (in isoform 5)Ubiquitination-4.4721890473
1192 (in isoform 1)Ubiquitination-46.3221890473
1192UbiquitinationIEDDTILKTNKHIYS
CCCCHHHHHCHHHHH
46.322190698

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 EDRF1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EDRF1_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 EDRF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYCE1_HUMANSYCE1physical
25416956
FYB2_HUMANC1orf168physical
27173435
I2BP1_HUMANIRF2BP1physical
27173435

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 EDRF1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP