NR2E1_HUMAN - dbPTM
NR2E1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NR2E1_HUMAN
UniProt AC Q9Y466
Protein Name Nuclear receptor subfamily 2 group E member 1
Gene Name NR2E1
Organism Homo sapiens (Human).
Sequence Length 385
Subcellular Localization Nucleus .
Protein Description Orphan receptor that binds DNA as a monomer to hormone response elements (HRE) containing an extended core motif half-site sequence 5'-AAGGTCA-3' in which the 5' flanking nucleotides participate in determining receptor specificity (By similarity). May be required to pattern anterior brain differentiation. Involved in the regulation of retinal development and essential for vision. During retinogenesis, regulates PTEN-Cyclin D expression via binding to the promoter region of PTEN and suppressing its activity (By similarity). May be involved in retinoic acid receptor (RAR) regulation in retinal cells..
Protein Sequence MSKPAGSTSRILDIPCKVCGDRSSGKHYGVYACDGCSGFFKRSIRRNRTYVCKSGNQGGCPVDKTHRNQCRACRLKKCLEVNMNKDAVQHERGPRTSTIRKQVALYFRGHKEENGAAAHFPSAALPAPAFFTAVTQLEPHGLELAAVSTTPERQTLVSLAQPTPKYPHEVNGTPMYLYEVATESVCESAARLLFMSIKWAKSVPAFSTLSLQDQLMLLEDAWRELFVLGIAQWAIPVDANTLLAVSGMNGDNTDSQKLNKIISEIQALQEVVARFRQLRLDATEFACLKCIVTFKAVPTHSGSELRSFRNAAAIAALQDEAQLTLNSYIHTRYPTQPCRFGKLLLLLPALRSISPSTIEEVFFKKTIGNVPITRLLSDMYKSSDI
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------MSKPAGSTS
------CCCCCCCCC
47.5530631047
7Phosphorylation-MSKPAGSTSRILDI
-CCCCCCCCCEEEEE
25.8921955146
9PhosphorylationSKPAGSTSRILDIPC
CCCCCCCCEEEEEEE
21.01-
202PhosphorylationMSIKWAKSVPAFSTL
HHHHHHHCCCCCEEC
26.1130206219
207PhosphorylationAKSVPAFSTLSLQDQ
HHCCCCCEECCHHHH
30.4630206219
208PhosphorylationKSVPAFSTLSLQDQL
HCCCCCEECCHHHHH
17.5730206219
210PhosphorylationVPAFSTLSLQDQLML
CCCCEECCHHHHHHH
24.8730206219
299PhosphorylationVTFKAVPTHSGSELR
EEEEECCCCCCHHHH
23.2928348404
301PhosphorylationFKAVPTHSGSELRSF
EEECCCCCCHHHHHH
46.6318187866
357PhosphorylationLRSISPSTIEEVFFK
HHCCCHHHHHHHHCH
35.47-

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 NR2E1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NR2E1_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 NR2E1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZMYM2_HUMANZMYM2physical
18391013
GSE1_HUMANGSE1physical
18391013
RCOR1_HUMANRCOR1physical
18391013
HDAC1_HUMANHDAC1physical
18391013
HDAC2_HUMANHDAC2physical
18391013
KDM1A_HUMANKDM1Aphysical
18391013
HDAC3_HUMANHDAC3physical
17873065
HDAC5_HUMANHDAC5physical
17873065
SP1_HUMANSP1physical
20599619
BC11A_HUMANBCL11Aphysical
23975195
DCAF6_HUMANDCAF6physical
26186194
TNR6C_HUMANTNRC6Cphysical
26186194
RGPD5_HUMANRGPD5physical
26186194
IMDH1_HUMANIMPDH1physical
26186194
REN3B_HUMANUPF3Bphysical
26186194
CARME_HUMANC9orf41physical
26186194
GBB4_HUMANGNB4physical
26186194
ARL10_HUMANARL10physical
26186194
SUFU_HUMANSUFUphysical
26186194
TYB10_HUMANTMSB10physical
26186194
CIZ1_HUMANCIZ1physical
26186194
LYRIC_HUMANMTDHphysical
26186194
VRK3_HUMANVRK3physical
26186194
RPA43_HUMANTWISTNBphysical
26186194
DCAF6_HUMANDCAF6physical
28514442
SUFU_HUMANSUFUphysical
28514442
ARL10_HUMANARL10physical
28514442
TNR6C_HUMANTNRC6Cphysical
28514442
LYRIC_HUMANMTDHphysical
28514442
CARME_HUMANC9orf41physical
28514442
VRK3_HUMANVRK3physical
28514442
CIZ1_HUMANCIZ1physical
28514442
RGPD5_HUMANRGPD5physical
28514442
DDX5_HUMANDDX5physical
26965827
RNC_HUMANDROSHAphysical
26965827
DGCR8_HUMANDGCR8physical
26965827

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 NR2E1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND MASSSPECTROMETRY.

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