ERR2_HUMAN - dbPTM
ERR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERR2_HUMAN
UniProt AC O95718
Protein Name Steroid hormone receptor ERR2 {ECO:0000305}
Gene Name ESRRB {ECO:0000312|HGNC:HGNC:3473}
Organism Homo sapiens (Human).
Sequence Length 433
Subcellular Localization Nucleus . Cytoplasm . Chromosome .
Protein Description Isoform 3: Transcription factor that binds a canonical ESRRB recognition (ERRE) sequence 5'TCAAGGTCA-3' localized on promoter and enhancer of targets genes regulating their expression or their transcription activity. [PubMed: 17920186]
Protein Sequence MSSDDRHLGSSCGSFIKTEPSSPSSGIDALSHHSPSGSSDASGGFGLALGTHANGLDSPPMFAGAGLGGTPCRKSYEDCASGIMEDSAIKCEYMLNAIPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRLDSESSPYLSLQISPPAKKPLTKIVSYLLVAEPDKLYAMPPPGMPEGDIKALTTLCDLADRELVVIIGWAKHIPGFSSLSLGDQMSLLQSAWMEILILGIVYRSLPYDDKLVYAEDYIMDEEHSRLAGLLELYRAILQLVRRYKKLKVEKEEFVTLKALALANSDSMYIEDLEAVQKLQDLLHEALQDYELSQRHEEPWRTGKLLLTLPLLRQTAAKAVQHFYSVKLQGKVPMHKLFLEMLEAKV
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
14PhosphorylationHLGSSCGSFIKTEPS
CCCCCCCCCEECCCC		28.2924719451
111PhosphorylationLVCGDIASGYHYGVA
EECCCCCCCCCCCHH		39.9724275569
119PhosphorylationGYHYGVASCEACKAF
CCCCCHHCHHHHHHH		15.3024275569
170AcetylationCLKVGMLKEGVRLDR
HHHHCCCCCCCCHHH		43.4612654415
238AcetylationGMPEGDIKALTTLCD
CCCCCHHHHHHHHHH		41.9220167786
343PhosphorylationVEKEEFVTLKALALA
CCHHHHHHHHHHHHH		28.0620068231
352PhosphorylationKALALANSDSMYIED
HHHHHHCCCCCHHHH		26.0020068231
354PhosphorylationLALANSDSMYIEDLE
HHHHCCCCCHHHHHH		17.2020068231
356PhosphorylationLANSDSMYIEDLEAV
HHCCCCCHHHHHHHH		12.7120068231
395PhosphorylationRTGKLLLTLPLLRQT
HHCHHHHHHHHHHHH		26.7120068231
448Phosphorylation----------------------
----------------------		30.64-
448 (in isoform 1)Phosphorylation-30.64-
478 (in isoform 1)Phosphorylation-50.6726471730
479 (in isoform 1)Phosphorylation-35.1626471730
493Phosphorylation-------------------------------------------------------------------
-------------------------------------------------------------------		24.5924732914
493 (in isoform 1)Phosphorylation-24.5924732914
494 (in isoform 1)Phosphorylation-41.7824732914
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 ERR2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERR2_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 ERR2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
1433T_HUMANYWHAQphysical
24189400
2AAA_HUMANPPP2R1Aphysical
24189400
4F2_HUMANSLC3A2physical
24189400
ACSL3_HUMANACSL3physical
24189400
ADT2_HUMANSLC25A5physical
24189400
ADT3_HUMANSLC25A6physical
24189400
ANXA2_HUMANANXA2physical
24189400
AT1A1_HUMANATP1A1physical
24189400
AT2A2_HUMANATP2A2physical
24189400
AT2A3_HUMANATP2A3physical
24189400
ATD3A_HUMANATAD3Aphysical
24189400
ATPA_HUMANATP5A1physical
24189400
ATPG_HUMANATP5C1physical
24189400
CALX_HUMANCANXphysical
24189400
CDC37_HUMANCDC37physical
24189400
CH60_HUMANHSPD1physical
24189400
DHCR7_HUMANDHCR7physical
24189400
DJC10_HUMANDNAJC10physical
24189400
DNJA1_HUMANDNAJA1physical
24189400
DNJA2_HUMANDNAJA2physical
24189400
DNJB2_HUMANDNAJB2physical
24189400
DNJB6_HUMANDNAJB6physical
24189400
DNJB8_HUMANDNAJB8physical
24189400
EF1A1_HUMANEEF1A1physical
24189400
EF1A2_HUMANEEF1A2physical
24189400
EFTU_HUMANTUFMphysical
24189400
EGFR_HUMANEGFRphysical
24189400
ERBB2_HUMANERBB2physical
24189400
ERD22_HUMANKDELR2physical
24189400
ERRFI_HUMANERRFI1physical
24189400
G3P_HUMANGAPDHphysical
24189400
GBB1_HUMANGNB1physical
24189400
GBB2_HUMANGNB2physical
24189400
GBB3_HUMANGNB3physical
24189400
GBB4_HUMANGNB4physical
24189400
GFAP_HUMANGFAPphysical
24189400
GRB2_HUMANGRB2physical
24189400
GRP75_HUMANHSPA9physical
24189400
GRP78_HUMANHSPA5physical
24189400
HACD3_HUMANPTPLAD1physical
24189400
HNRH1_HUMANHNRNPH1physical
24189400
HNRH2_HUMANHNRNPH2physical
24189400
HNRPF_HUMANHNRNPFphysical
24189400
HS90A_HUMANHSP90AA1physical
24189400
HS90B_HUMANHSP90AB1physical
24189400
HSP7C_HUMANHSPA8physical
24189400
LPPRC_HUMANLRPPRCphysical
24189400
MGST1_HUMANMGST1physical
24189400
MPCP_HUMANSLC25A3physical
24189400
NDUA4_HUMANNDUFA4physical
24189400
PHB_HUMANPHBphysical
24189400
PHB2_HUMANPHB2physical
24189400
PKDRE_HUMANPKDREJphysical
24189400
PKP2_HUMANPKP2physical
24189400
PP2AA_HUMANPPP2CAphysical
24189400
PP2AB_HUMANPPP2CBphysical
24189400
RL23_HUMANRPL23physical
24189400
RS14_HUMANRPS14physical
24189400
RS16_HUMANRPS16physical
24189400
RS2_HUMANRPS2physical
24189400
RS27_HUMANRPS27physical
24189400
RS27A_HUMANRPS27Aphysical
24189400
RS27L_HUMANRPS27Lphysical
24189400
RS3_HUMANRPS3physical
24189400
S10AE_HUMANS100A14physical
24189400
S10AG_HUMANS100A16physical
24189400
S39A7_HUMANSLC39A7physical
24189400
S61A1_HUMANSEC61A1physical
24189400
SGPL1_HUMANSGPL1physical
24189400
SLIRP_HUMANSLIRPphysical
24189400
SPTN4_HUMANSPTBN4physical
24189400
SSRA_HUMANSSR1physical
24189400
TBA1B_HUMANTUBA1Bphysical
24189400
TBA1C_HUMANTUBA1Cphysical
24189400
TBB5_HUMANTUBBphysical
24189400
TFR1_HUMANTFRCphysical
24189400
THEM6_HUMANTHEM6physical
24189400
TIM21_HUMANTIMM21physical
24189400
TIM50_HUMANTIMM50physical
24189400
TMM33_HUMANTMEM33physical
24189400
TNAP2_HUMANTNFAIP2physical
24189400
TXTP_HUMANSLC25A1physical
24189400
UBS3B_HUMANUBASH3Bphysical
24189400
VAPA_HUMANVAPAphysical
24189400
VAPB_HUMANVAPBphysical
24189400
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608565Deafness, autosomal recessive, 35 (DFNB35)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERR2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-395, AND MASSSPECTROMETRY.

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