ERG_HUMAN - dbPTM
ERG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERG_HUMAN
UniProt AC P11308
Protein Name Transcriptional regulator ERG
Gene Name ERG
Organism Homo sapiens (Human).
Sequence Length 486
Subcellular Localization Nucleus . Cytoplasm . Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Protein Description Transcriptional regulator. May participate in transcriptional regulation through the recruitment of SETDB1 histone methyltransferase and subsequent modification of local chromatin structure..
Protein Sequence MIQTVPDPAAHIKEALSVVSEDQSLFECAYGTPHLAKTEMTASSSSDYGQTSKMSPRVPQQDWLSQPPARVTIKMECNPSQVNGSRNSPDECSVAKGGKMVGSPDTVGMNYGSYMEEKHMPPPNMTTNERRVIVPADPTLWSTDHVRQWLEWAVKEYGLPDVNILLFQNIDGKELCKMTKDDFQRLTPSYNADILLSHLHYLRETPLPHLTSDDVDKALQNSPRLMHARNTGGAAFIFPNTSVYPEATQRITTRPDLPYEPPRRSAWTGHGHPTPQSKAAQPSPSTVPKTEDQRPQLDPYQILGPTSSRLANPGSGQIQLWQFLLELLSDSSNSSCITWEGTNGEFKMTDPDEVARRWGERKSKPNMNYDKLSRALRYYYDKNIMTKVHGKRYAYKFDFHGIAQALQPHPPESSLYKYPSDLPYMGSYHAHPQKMNFVAPHPPALPVTSSSFFAAPNPYWNSPTGGIYPNTRLPTSHMPSHLGTYY
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
4Phosphorylation----MIQTVPDPAAH
----CCCCCCCHHHH
24.0725159151
30PhosphorylationQSLFECAYGTPHLAK
HHHHHHCCCCCCCEE
32.9423532336
32PhosphorylationLFECAYGTPHLAKTE
HHHHCCCCCCCEEEE
8.54-
44PhosphorylationKTEMTASSSSDYGQT
EEEECCCCCCCCCCC
31.25-
45PhosphorylationTEMTASSSSDYGQTS
EEECCCCCCCCCCCC
25.41-
46PhosphorylationEMTASSSSDYGQTSK
EECCCCCCCCCCCCC
36.48-
48PhosphorylationTASSSSDYGQTSKMS
CCCCCCCCCCCCCCC
17.06-
51PhosphorylationSSSDYGQTSKMSPRV
CCCCCCCCCCCCCCC
26.4223403867
52PhosphorylationSSDYGQTSKMSPRVP
CCCCCCCCCCCCCCC
20.6223403867
55PhosphorylationYGQTSKMSPRVPQQD
CCCCCCCCCCCCCCH
17.1923403867
65PhosphorylationVPQQDWLSQPPARVT
CCCCHHHCCCCCEEE
36.0728387310
80PhosphorylationIKMECNPSQVNGSRN
EEEECCHHHCCCCCC
32.5422115753
81PhosphorylationKMECNPSQVNGSRNS
EEECCHHHCCCCCCC
33.67-
85PhosphorylationNPSQVNGSRNSPDEC
CHHHCCCCCCCCCCC
24.0823401153
88PhosphorylationQVNGSRNSPDECSVA
HCCCCCCCCCCCCCC
32.3923401153
93PhosphorylationRNSPDECSVAKGGKM
CCCCCCCCCCCCCEE
24.0615302935
96PhosphorylationPDECSVAKGGKMVGS
CCCCCCCCCCEECCC
67.07-
96AcetylationPDECSVAKGGKMVGS
CCCCCCCCCCEECCC
67.07112788003
99AcetylationCSVAKGGKMVGSPDT
CCCCCCCEECCCCCC
38.80112788001
103PhosphorylationKGGKMVGSPDTVGMN
CCCEECCCCCCCCCC
14.2723401153
106PhosphorylationKMVGSPDTVGMNYGS
EECCCCCCCCCCHHH
23.4923403867
111PhosphorylationPDTVGMNYGSYMEEK
CCCCCCCHHHHHHHH
9.8830301811
113PhosphorylationTVGMNYGSYMEEKHM
CCCCCHHHHHHHHCC
15.7930301811
114PhosphorylationVGMNYGSYMEEKHMP
CCCCHHHHHHHHCCC
12.2730301811
136 (in isoform 2)Phosphorylation-25.23-
222PhosphorylationVDKALQNSPRLMHAR
HHHHHHHCCCCCCCC
9.8423401153
235 (in isoform 1)Phosphorylation-11.01-
259PhosphorylationTTRPDLPYEPPRRSA
CCCCCCCCCCCCCCC
48.65-
283PhosphorylationQSKAAQPSPSTVPKT
CCCCCCCCCCCCCCC
21.2823403867
285PhosphorylationKAAQPSPSTVPKTED
CCCCCCCCCCCCCCC
46.5023403867
286PhosphorylationAAQPSPSTVPKTEDQ
CCCCCCCCCCCCCCC
44.1830301811
289SumoylationPSPSTVPKTEDQRPQ
CCCCCCCCCCCCCCC
61.2828112733
300PhosphorylationQRPQLDPYQILGPTS
CCCCCCCCCCCCCCC
14.0927642862
349PhosphorylationTNGEFKMTDPDEVAR
CCCEEEECCHHHHHH
44.9922591006
369PhosphorylationKSKPNMNYDKLSRAL
CCCCCCCHHHHHHHH
12.04-
371AcetylationKPNMNYDKLSRALRY
CCCCCHHHHHHHHHH
37.6922973553
382AcetylationALRYYYDKNIMTKVH
HHHHHHHCCCEEEEC
32.0522973553
387AcetylationYDKNIMTKVHGKRYA
HHCCCEEEECCEEEE
18.1722973553
413PhosphorylationLQPHPPESSLYKYPS
HCCCCCCCHHCCCCC
31.27-
427PhosphorylationSDLPYMGSYHAHPQK
CCCCCCCCCCCCCCC
9.3823401153

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
37SPhosphorylationKinaseCK1AP48729
PSP
38SPhosphorylationKinaseCK1AP48729
PSP
39SPhosphorylationKinaseCK1AP48729
PSP
44SPhosphorylationKinaseCSNK1A1P48729
GPS
45SPhosphorylationKinaseCSNK1A1P48729
GPS
46SPhosphorylationKinaseCSNK1A1P48729
GPS
96SPhosphorylationKinaseERK2P28482
PSP
103SPhosphorylationKinaseMAPK1P28482
GPS
215SPhosphorylationKinaseERK2P28482
PSP
222SPhosphorylationKinaseMAPK1P28482
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERG_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 ERG_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
JUN_HUMANJUNphysical
11278640
ANDR_HUMANARphysical
20478527
HSP74_HUMANHSPA4physical
21183741
HSP7C_HUMANHSPA8physical
21183741
NEDD4_HUMANNEDD4physical
21463633
PRKDC_HUMANPRKDCphysical
21575865
XRCC5_HUMANXRCC5physical
21575865
XRCC6_HUMANXRCC6physical
21575865
PARP1_HUMANPARP1physical
21575865
XRCC4_HUMANXRCC4physical
21575865
NDKA_HUMANNME1physical
21575865
DDX3X_HUMANDDX3Xphysical
21575865
HSP7C_HUMANHSPA8physical
21575865
PCBP1_HUMANPCBP1physical
21575865
ROA2_HUMANHNRNPA2B1physical
21575865
DDX5_HUMANDDX5physical
21575865
RO52_HUMANTRIM21physical
21575865
TPM1_HUMANTPM1physical
21575865
HNRPM_HUMANHNRNPMphysical
21575865
IF2A_HUMANEIF2S1physical
21575865
RLA0_HUMANRPLP0physical
21575865
PRP8_HUMANPRPF8physical
21575865
RL7A_HUMANRPL7Aphysical
21575865
HNRDL_HUMANHNRNPDLphysical
21575865
TBB5_HUMANTUBBphysical
21575865
PYR1_HUMANCADphysical
21575865
ACTB_HUMANACTBphysical
21575865
ATPA_HUMANATP5A1physical
21575865
RS18_HUMANRPS18physical
21575865
HNRPU_HUMANHNRNPUphysical
21575865
SPTN1_HUMANSPTAN1physical
21575865
A4_HUMANAPPphysical
21832049
USP9X_HUMANUSP9Xphysical
24591637
ACTB_HUMANACTBphysical
24591637
DSRAD_HUMANADARphysical
24591637
CDC5L_HUMANCDC5Lphysical
24591637
CLH1_HUMANCLTCphysical
24591637
DDX21_HUMANDDX21physical
24591637
DDX23_HUMANDDX23physical
24591637
DKC1_HUMANDKC1physical
24591637
EF1A2_HUMANEEF1A2physical
24591637
ELAV1_HUMANELAVL1physical
24591637
FBRL_HUMANFBLphysical
24591637
ROA1_HUMANHNRNPA1physical
24591637
ROA2_HUMANHNRNPA2B1physical
24591637
ROAA_HUMANHNRNPABphysical
24591637
HNRPC_HUMANHNRNPCphysical
24591637
HNRPD_HUMANHNRNPDphysical
24591637
HNRPF_HUMANHNRNPFphysical
24591637
HNRH1_HUMANHNRNPH1physical
24591637
HNRH3_HUMANHNRNPH3physical
24591637
HNRPU_HUMANHNRNPUphysical
24591637
HNRL1_HUMANHNRNPUL1physical
24591637
HNRL2_HUMANHNRNPUL2physical
24591637
HNRDL_HUMANHNRNPDLphysical
24591637
CH60_HUMANHSPD1physical
24591637
ILF2_HUMANILF2physical
24591637
ILF3_HUMANILF3physical
24591637
LANC1_HUMANLANCL1physical
24591637
MATR3_HUMANMATR3physical
24591637
NUCL_HUMANNCLphysical
24591637
NOLC1_HUMANNOLC1physical
24591637
NONO_HUMANNONOphysical
24591637
NPM_HUMANNPM1physical
24591637
NUMA1_HUMANNUMA1physical
24591637
PARP1_HUMANPARP1physical
24591637
PCBP1_HUMANPCBP1physical
24591637
RPB1_HUMANPOLR2Aphysical
24591637
PRKDC_HUMANPRKDCphysical
24591637
PR40A_HUMANPRPF40Aphysical
24591637
PRP8_HUMANPRPF8physical
24591637
PUF60_HUMANPUF60physical
24591637
RCC2_HUMANRCC2physical
24591637
RLA0_HUMANRPLP0physical
24591637
SF3B1_HUMANSF3B1physical
24591637
SF3B2_HUMANSF3B2physical
24591637
SF3B3_HUMANSF3B3physical
24591637
SFPQ_HUMANSFPQphysical
24591637
U520_HUMANSNRNP200physical
24591637
SYN1_HUMANSYN1physical
24591637
TOP1_HUMANTOP1physical
24591637
TOP2B_HUMANTOP2Bphysical
24591637
XRN2_HUMANXRN2physical
24591637
CUL3_HUMANCUL3physical
26344095
SPOP_HUMANSPOPphysical
26344095
SPOP_HUMANSPOPphysical
26344096
TRI25_HUMANTRIM25physical
27626314
UBR5_HUMANUBR5physical
27626314
TRI33_HUMANTRIM33physical
27626314
RING1_HUMANRING1physical
27626314
UBR4_HUMANUBR4physical
27626314
RING2_HUMANRNF2physical
27626314
TRIPC_HUMANTRIP12physical
27626314
HUWE1_HUMANHUWE1physical
27626314
CHIP_HUMANSTUB1physical
27626314
UHRF1_HUMANUHRF1physical
27626314
HERC2_HUMANHERC2physical
27626314
BRD2_HUMANBRD2physical
28805820
BRD3_HUMANBRD3physical
28805820
BRD4_HUMANBRD4physical
28805820

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612219Ewing sarcoma (ES)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERG_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-93, AND MASSSPECTROMETRY.

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