NR4A1_HUMAN - dbPTM
NR4A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NR4A1_HUMAN
UniProt AC P22736
Protein Name Nuclear receptor subfamily 4 group A member 1
Gene Name NR4A1
Organism Homo sapiens (Human).
Sequence Length 598
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Orphan nuclear receptor. May act concomitantly with NURR1 in regulating the expression of delayed-early genes during liver regeneration. Binds the NGFI-B response element (NBRE) 5'-AAAAGGTCA-3' (By similarity). May inhibit NF-kappa-B transactivation of IL2. Participates in energy homeostasis by sequestrating the kinase STK11 in the nucleus, thereby attenuating cytoplasmic AMPK activation..
Protein Sequence MPCIQAQYGTPAPSPGPRDHLASDPLTPEFIKPTMDLASPEAAPAAPTALPSFSTFMDGYTGEFDTFLYQLPGTVQPCSSASSSASSTSSSSATSPASASFKFEDFQVYGCYPGPLSGPVDEALSSSGSDYYGSPCSAPSPSTPSFQPPQLSPWDGSFGHFSPSQTYEGLRAWTEQLPKASGPPQPPAFFSFSPPTGPSPSLAQSPLKLFPSQATHQLGEGESYSMPTAFPGLAPTSPHLEGSGILDTPVTSTKARSGAPGGSEGRCAVCGDNASCQHYGVRTCEGCKGFFKRTVQKNAKYICLANKDCPVDKRRRNRCQFCRFQKCLAVGMVKEVVRTDSLKGRRGRLPSKPKQPPDASPANLLTSLVRAHLDSGPSTAKLDYSKFQELVLPHFGKEDAGDVQQFYDLLSGSLEVIRKWAEKIPGFAELSPADQDLLLESAFLELFILRLAYRSKPGEGKLIFCSGLVLHRLQCARGFGDWIDSILAFSRSLHSLLVDVPAFACLSALVLITDRHGLQEPRRVEELQNRIASCLKEHVAAVAGEPQPASCLSRLLGKLPELRTLCTQGLQRIFYLKLEDLVPPPPIIDKIFMDTLPF
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
8PhosphorylationMPCIQAQYGTPAPSP
CCCEECCCCCCCCCC
26.4426270265
10PhosphorylationCIQAQYGTPAPSPGP
CEECCCCCCCCCCCC
16.0225159151
14PhosphorylationQYGTPAPSPGPRDHL
CCCCCCCCCCCCCCC
44.5925159151
23PhosphorylationGPRDHLASDPLTPEF
CCCCCCCCCCCCHHH
46.2325159151
27PhosphorylationHLASDPLTPEFIKPT
CCCCCCCCHHHHCCC
26.5925159151
48PhosphorylationEAAPAAPTALPSFST
CCCCCCCCCCCCCCH
35.78-
52PhosphorylationAAPTALPSFSTFMDG
CCCCCCCCCCHHHCC
32.45-
54PhosphorylationPTALPSFSTFMDGYT
CCCCCCCCHHHCCCC
25.69-
55PhosphorylationTALPSFSTFMDGYTG
CCCCCCCHHHCCCCC
22.44-
60PhosphorylationFSTFMDGYTGEFDTF
CCHHHCCCCCEEEEE
13.80-
61PhosphorylationSTFMDGYTGEFDTFL
CHHHCCCCCEEEEEE
35.45-
95PhosphorylationTSSSSATSPASASFK
CCCCCCCCCCEECEE
20.4122002310
100PhosphorylationATSPASASFKFEDFQ
CCCCCEECEEECCEE
26.8624719451
102SumoylationSPASASFKFEDFQVY
CCCEECEEECCEEEE
45.40-
140PhosphorylationGSPCSAPSPSTPSFQ
CCCCCCCCCCCCCCC
31.0622002310
143PhosphorylationCSAPSPSTPSFQPPQ
CCCCCCCCCCCCCCC
26.7422234305
152PhosphorylationSFQPPQLSPWDGSFG
CCCCCCCCCCCCCCC
20.78-
174PhosphorylationYEGLRAWTEQLPKAS
HHHHHHHHHHCCCCC
16.9328555341
191PhosphorylationPQPPAFFSFSPPTGP
CCCCCEEECCCCCCC
20.5428102081
193PhosphorylationPPAFFSFSPPTGPSP
CCCEEECCCCCCCCC
28.8625159151
196PhosphorylationFFSFSPPTGPSPSLA
EEECCCCCCCCCCHH
66.1721712546
199PhosphorylationFSPPTGPSPSLAQSP
CCCCCCCCCCHHCCC
28.5925850435
201PhosphorylationPPTGPSPSLAQSPLK
CCCCCCCCHHCCCCC
40.4518691976
205PhosphorylationPSPSLAQSPLKLFPS
CCCCHHCCCCCCCCC
26.9625850435
214PhosphorylationLKLFPSQATHQLGEG
CCCCCCCCCCCCCCC
16.0424719451
218PhosphorylationPSQATHQLGEGESYS
CCCCCCCCCCCCCCC
5.3827251275
236PhosphorylationAFPGLAPTSPHLEGS
CCCCCCCCCCCCCCC
49.6526074081
237PhosphorylationFPGLAPTSPHLEGSG
CCCCCCCCCCCCCCC
14.8426074081
243PhosphorylationTSPHLEGSGILDTPV
CCCCCCCCCCCCCCC
17.1828348404
257PhosphorylationVTSTKARSGAPGGSE
CCCCCCCCCCCCCCC
44.13-
263PhosphorylationRSGAPGGSEGRCAVC
CCCCCCCCCCCEEEC
42.6721712546
279PhosphorylationDNASCQHYGVRTCEG
CCCCCCCCCCCCCCC
7.46-
283PhosphorylationCQHYGVRTCEGCKGF
CCCCCCCCCCCCCCH
16.71-
288AcetylationVRTCEGCKGFFKRTV
CCCCCCCCCHHHHHH
70.3926051181
300SumoylationRTVQKNAKYICLANK
HHHHHCCCEEEECCC
44.54-
300SumoylationRTVQKNAKYICLANK
HHHHHCCCEEEECCC
44.54-
300UbiquitinationRTVQKNAKYICLANK
HHHHHCCCEEEECCC
44.54-
300AcetylationRTVQKNAKYICLANK
HHHHHCCCEEEECCC
44.5426051181
307UbiquitinationKYICLANKDCPVDKR
CEEEECCCCCCCCHH
55.91-
307AcetylationKYICLANKDCPVDKR
CEEEECCCCCCCCHH
55.9126051181
339PhosphorylationMVKEVVRTDSLKGRR
CEEEEEECCCCCCCC
20.5228102081
341PhosphorylationKEVVRTDSLKGRRGR
EEEEECCCCCCCCCC
31.2228355574
351PhosphorylationGRRGRLPSKPKQPPD
CCCCCCCCCCCCCCC
67.2122322096
360PhosphorylationPKQPPDASPANLLTS
CCCCCCCCHHHHHHH
31.7422322096
364PhosphorylationPDASPANLLTSLVRA
CCCCHHHHHHHHHHH
6.3224719451
381SumoylationDSGPSTAKLDYSKFQ
HCCCCCCCCCHHHHH
41.81-
381UbiquitinationDSGPSTAKLDYSKFQ
HCCCCCCCCCHHHHH
41.8121906983
381SumoylationDSGPSTAKLDYSKFQ
HCCCCCCCCCHHHHH
41.81-
386UbiquitinationTAKLDYSKFQELVLP
CCCCCHHHHHHHHCC
44.85-
431PhosphorylationIPGFAELSPADQDLL
CCCCCCCCHHHHHHH
15.0022002310
558UbiquitinationCLSRLLGKLPELRTL
HHHHHHCCCHHHHHH
61.92-

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
95SPhosphorylationKinaseMAPK8P45983
GPS
95SPhosphorylationKinaseJNK-SUBFAMILY-GPS
152SPhosphorylationKinaseCSNK2A1P68400
GPS
341SPhosphorylationKinasePKA-Uniprot
351SPhosphorylationKinaseAKT1P31749
PSP
351SPhosphorylationKinaseAKT1P31750
PSP
351SPhosphorylationKinaseAKT-FAMILY-GPS
351SPhosphorylationKinasePKB_GROUP-PhosphoELM
431SPhosphorylationKinaseMAPK1P28482
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
351SPhosphorylation

17360704

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 NR4A1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
G45IP_HUMANGADD45GIP1physical
15459248
BCL2_HUMANBCL2physical
14980220
RXRA_HUMANRXRAphysical
14980220
NCOA3_HUMANNCOA3physical
12082103
NCOA1_HUMANNCOA1physical
12082103
EP300_HUMANEP300physical
12082103
KAT2B_HUMANKAT2Bphysical
12082103
RXRG_HUMANRXRGphysical
12082103
FXYD3_HUMANFXYD3physical
16169070
PML_HUMANPMLphysical
12032831
VHL_HUMANVHLphysical
18305400
HIF1A_HUMANHIF1Aphysical
18305400
P53_HUMANTP53physical
17139261
CHD4_HUMANCHD4physical
19321449
TOP2A_HUMANTOP2Aphysical
19321449
PELP1_HUMANPELP1physical
19321449
SMRC1_HUMANSMARCC1physical
19321449
MBB1A_HUMANMYBBP1Aphysical
19321449
MTA2_HUMANMTA2physical
19321449
TIF1B_HUMANTRIM28physical
19321449
SMCE1_HUMANSMARCE1physical
19321449
TMOD3_HUMANTMOD3physical
19321449
EF1A1_HUMANEEF1A1physical
19321449
HDAC6_HUMANHDAC6physical
19321449
DPOA2_HUMANPOLA2physical
21900206
HES1_HUMANHES1physical
21900206
ROBO2_HUMANROBO2physical
21900206
GCR_HUMANNR3C1physical
21900206
ZN579_HUMANZNF579physical
21900206
HS90B_HUMANHSP90AB1physical
21900206
MED31_HUMANMED31physical
21900206
RL7_HUMANRPL7physical
21900206
RTN4_HUMANRTN4physical
21900206
BBS10_HUMANBBS10physical
21900206
NACAD_HUMANNACADphysical
21900206
ZN331_HUMANZNF331physical
21900206
PRDX4_HUMANPRDX4physical
21900206
GLOD4_HUMANGLOD4physical
21900206
ROA2_HUMANHNRNPA2B1physical
21900206
ITF2_HUMANTCF4physical
21900206
CHD3_HUMANCHD3physical
21900206
KAIN_HUMANSERPINA4physical
21900206
FAF1_HUMANFAF1physical
21900206
CXCL7_HUMANPPBPphysical
21900206
CTNB1_HUMANCTNNB1physical
21986938
RXRA_HUMANRXRAphysical
17761950
STAT3_HUMANSTAT3physical
21988832
SGT1_HUMANSUGT1physical
21988832
RBL1_HUMANRBL1physical
21988832
IC1_HUMANSERPING1physical
21988832
SMAD3_HUMANSMAD3physical
21988832
PPM1A_HUMANPPM1Aphysical
21988832
PRDX6_HUMANPRDX6physical
21988832
PRDX4_HUMANPRDX4physical
21988832
SOCS4_HUMANSOCS4physical
21988832
TBB4A_HUMANTUBB4Aphysical
20195357
CUTA_HUMANCUTAphysical
20195357
AKIB1_HUMANANKIB1physical
20195357
VASP_HUMANVASPphysical
20195357
PGBD1_HUMANPGBD1physical
25416956
LONF1_HUMANLONRF1physical
25416956
KR101_HUMANKRTAP10-1physical
25416956
RXRA_HUMANRXRAphysical
7705655
KS6A5_HUMANRPS6KA5physical
25241761
SMAD7_HUMANSMAD7physical
24584437
RNF12_HUMANRLIMphysical
24584437
RN111_HUMANRNF111physical
24584437
AXIN2_HUMANAXIN2physical
24584437
MIDN_HUMANMIDNphysical
28514442
ACD11_HUMANACAD11physical
28514442
TMTC4_HUMANTMTC4physical
28514442
GRK6_HUMANGRK6physical
28514442

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 NR4A1_HUMAN

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Related Literatures of Post-Translational Modification

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