NR1I2_HUMAN - dbPTM
NR1I2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NR1I2_HUMAN
UniProt AC O75469
Protein Name Nuclear receptor subfamily 1 group I member 2
Gene Name NR1I2
Organism Homo sapiens (Human).
Sequence Length 434
Subcellular Localization Nucleus .
Protein Description Nuclear receptor that binds and is activated by variety of endogenous and xenobiotic compounds. Transcription factor that activates the transcription of multiple genes involved in the metabolism and secretion of potentially harmful xenobiotics, drugs and endogenous compounds. Activated by the antibiotic rifampicin and various plant metabolites, such as hyperforin, guggulipid, colupulone, and isoflavones. Response to specific ligands is species-specific. Activated by naturally occurring steroids, such as pregnenolone and progesterone. Binds to a response element in the promoters of the CYP3A4 and ABCB1/MDR1 genes..
Protein Sequence MEVRPKESWNHADFVHCEDTESVPGKPSVNADEEVGGPQICRVCGDKATGYHFNVMTCEGCKGFFRRAMKRNARLRCPFRKGACEITRKTRRQCQACRLRKCLESGMKKEMIMSDEAVEERRALIKRKKSERTGTQPLGVQGLTEEQRMMIRELMDAQMKTFDTTFSHFKNFRLPGVLSSGCELPESLQAPSREEAAKWSQVRKDLCSLKVSLQLRGEDGSVWNYKPPADSGGKEIFSLLPHMADMSTYMFKGIISFAKVISYFRDLPIEDQISLLKGAAFELCQLRFNTVFNAETGTWECGRLSYCLEDTAGGFQQLLLEPMLKFHYMLKKLQLHEEEYVLMQAISLFSPDRPGVLQHRVVDQLQEQFAITLKSYIECNRPQPAHRFLFLKIMAMLTELRSINAQHTQRLLRIQDIHPFATPLMQELFGITGS
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
8PhosphorylationMEVRPKESWNHADFV
CCCCCCCCCCCCCEE
39.0319617467
57PhosphorylationGYHFNVMTCEGCKGF
CCEEEEEECCCCHHH
11.7919171678
101UbiquitinationCQACRLRKCLESGMK
HHHHHHHHHHHHCCC
48.00-
109AcetylationCLESGMKKEMIMSDE
HHHHCCCHHHHCCHH
43.55108936999
114PhosphorylationMKKEMIMSDEAVEER
CCHHHHCCHHHHHHH
22.75-
133PhosphorylationKRKKSERTGTQPLGV
HHHHHCCCCCCCCCC
40.3027251275
135PhosphorylationKKSERTGTQPLGVQG
HHHCCCCCCCCCCCC
26.80-
167PhosphorylationKTFDTTFSHFKNFRL
HHCCCCHHHHCCCCC
26.39-
172PhosphorylationTFSHFKNFRLPGVLS
CHHHHCCCCCCCCCC
9.7627251275
200PhosphorylationREEAAKWSQVRKDLC
HHHHHHHHHHHHHHH
20.35-
208PhosphorylationQVRKDLCSLKVSLQL
HHHHHHHCCEEEEEE
38.2223684312
212PhosphorylationDLCSLKVSLQLRGED
HHHCCEEEEEECCCC
14.6023684312
221PhosphorylationQLRGEDGSVWNYKPP
EECCCCCCCEECCCC
35.96-
247PhosphorylationLPHMADMSTYMFKGI
HHHHCCCHHHHHHHH
19.5526074081
248PhosphorylationPHMADMSTYMFKGII
HHHCCCHHHHHHHHH
16.6226074081
249PhosphorylationHMADMSTYMFKGIIS
HHCCCHHHHHHHHHH
8.0126074081
256PhosphorylationYMFKGIISFAKVISY
HHHHHHHHHHHHHHH
19.7526074081
274PhosphorylationLPIEDQISLLKGAAF
CCHHHHHHHHHHHHH
23.2424719451
290PhosphorylationLCQLRFNTVFNAETG
HHCHHHCCEEECCCC
24.62-
305PhosphorylationTWECGRLSYCLEDTA
EEEECCEEEEEECCC
16.6719617467
350PhosphorylationMQAISLFSPDRPGVL
HHHHHHHCCCCCCCC
31.0518784074
408PhosphorylationRSINAQHTQRLLRIQ
HHCCHHHHHHHHHHH
11.8719617467
422PhosphorylationQDIHPFATPLMQELF
HHCCCCCHHHHHHHH
19.82-

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
114SPhosphorylationKinaseCDK2P24941
PSP
133TPhosphorylationKinaseCDK2P24941
PSP
135TPhosphorylationKinaseCDK2P24941
PSP
167SPhosphorylationKinaseCDK2P24941
PSP
200SPhosphorylationKinaseCDK2P24941
PSP
290TPhosphorylationKinaseCAMK2AQ9UQM7
PSP
350SPhosphorylationKinaseCDK2P24941
PSP
350SPhosphorylationKinaseVRK1Q99986
PSP
408TPhosphorylationKinasePRKCAP17252
GPS
-KUbiquitinationE3 ubiquitin ligaseUBR5O95071
PMID:24438055
-KUbiquitinationE3 ubiquitin ligaseRBCK1Q9BYM8
PMID:23160820

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NR1I2_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 NR1I2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NCOA1_HUMANNCOA1physical
12909012
ANM1_HUMANPRMT1physical
19144646
NCOR1_HUMANNCOR1physical
18978041
NCOA1_MOUSENcoa1physical
15610065
PRGC1_MOUSEPpargc1aphysical
15322103
PRGC1_HUMANPPARGC1Aphysical
15322103
ACTN2_HUMANACTN2physical
15604093
CHM1A_HUMANCHMP1Aphysical
15604093
RXRA_HUMANRXRAphysical
15604093
NUCB2_HUMANNUCB2physical
15604093
RXRG_HUMANRXRGphysical
15604093
PRGC1_HUMANPPARGC1Aphysical
15604093
RXRB_HUMANRXRBphysical
15604093
RXRA_HUMANRXRAphysical
23160820
NCOA1_HUMANNCOA1physical
23160820
NCOA2_HUMANNCOA2physical
23160820
HOIL1_HUMANRBCK1physical
23160820
NCOR2_HUMANNCOR2physical
16219912
NCOA3_HUMANNCOA3physical
16219912
CAB45_HUMANSDF4physical
21988832
AP2C_HUMANTFAP2Cphysical
21988832
NCOA1_HUMANNCOA1physical
12072427
NCOR2_HUMANNCOR2physical
12072427
UBR5_HUMANUBR5physical
24438055
DDB1_HUMANDDB1physical
24438055
RBBP7_HUMANRBBP7physical
24438055
DYRK2_HUMANDYRK2physical
24438055
PRS8_HUMANPSMC5physical
15604093
NCOA1_HUMANNCOA1physical
15604093
RXRB_HUMANRXRBphysical
23536728
P53_HUMANTP53physical
23536728
CEBPA_HUMANCEBPAphysical
20624854
NCOA1_HUMANNCOA1physical
18096694
NCOA1_HUMANNCOA1physical
16455805
HNF4A_HUMANHNF4Aphysical
16455805
PRGC1_HUMANPPARGC1Aphysical
16455805
HNF4A_HUMANHNF4Aphysical
15331348
NR5A2_HUMANNR5A2physical
15331348

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
DB01248Docetaxel
DB00530Erlotinib
DB00783Estradiol
DB00977Ethinyl Estradiol
DB01229Paclitaxel
DB01045Rifampicin
DB01220Rifaximin
DB08864Rilpivirine
DB00163Vitamin E
Regulatory Network of NR1I2_HUMAN

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Related Literatures of Post-Translational Modification

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