COT2_HUMAN - dbPTM
COT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COT2_HUMAN
UniProt AC P24468
Protein Name COUP transcription factor 2
Gene Name NR2F2
Organism Homo sapiens (Human).
Sequence Length 414
Subcellular Localization Nucleus.
Protein Description Ligand-activated transcription factor. Activated by high concentrations of 9-cis-retinoic acid and all-trans-retinoic acid, but not by dexamethasone, cortisol or progesterone (in vitro). Regulation of the apolipoprotein A-I gene transcription. Binds to DNA site A..
Protein Sequence MAMVVSTWRDPQDEVPGSQGSQASQAPPVPGPPPGAPHTPQTPGQGGPASTPAQTAAGGQGGPGGPGSDKQQQQQHIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLSYTCRANRNCPIDQHHRNQCQYCRLKKCLKVGMRREAVQRGRMPPTQPTHGQFALTNGDPLNCHSYLSGYISLLLRAEPYPTSRFGSQCMQPNNIMGIENICELAARMLFSAVEWARNIPFFPDLQITDQVALLRLTWSELFVLNAAQCSMPLHVAPLLAAAGLHASPMSADRVVAFMDHIRIFQEQVEKLKALHVDSAEYSCLKAIVLFTSDACGLSDVAHVESLQEKSQCALEEYVRSQYPNQPTRFGKLLLRLPSLRTVSSSVIEQLFFVRLVGKTPIETLIRDMLLSGSSFNWPYMAIQ
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
7Phosphorylation-MAMVVSTWRDPQDE
-CCCEEEEECCCCCC
16.9524719451
39PhosphorylationPPPGAPHTPQTPGQG
CCCCCCCCCCCCCCC
18.9424275569
50PhosphorylationPGQGGPASTPAQTAA
CCCCCCCCCHHCCCC
37.7524275569
51PhosphorylationGQGGPASTPAQTAAG
CCCCCCCCHHCCCCC
25.4214702039
55PhosphorylationPASTPAQTAAGGQGG
CCCCHHCCCCCCCCC
22.1524275569
89UbiquitinationCGDKSSGKHYGQFTC
ECCCCCCCEEEEEEC
35.28-
112PhosphorylationRSVRRNLSYTCRANR
HHHHHHHHHHHCCCC
23.1921712546
133PhosphorylationHHRNQCQYCRLKKCL
HHHCHHHHHHHHHHH
6.2828152594
141MethylationCRLKKCLKVGMRREA
HHHHHHHHHCCHHHH
46.33-
148UbiquitinationKVGMRREAVQRGRMP
HHCCHHHHHHCCCCC
10.8421890473
168UbiquitinationHGQFALTNGDPLNCH
CCCEECCCCCCCCCH
54.4421890473
236UbiquitinationNIPFFPDLQITDQVA
CCCCCCCCCCCCHHH
3.9521890473
256UbiquitinationWSELFVLNAAQCSMP
HHHHHHHHHHHCCCC
28.1121890473
301UbiquitinationIFQEQVEKLKALHVD
HHHHHHHHHHHCCCC
57.3321890473
301UbiquitinationIFQEQVEKLKALHVD
HHHHHHHHHHHCCCC
57.3321890473
348PhosphorylationSQCALEEYVRSQYPN
HHHHHHHHHHHHCCC
7.56-
362UbiquitinationNQPTRFGKLLLRLPS
CCCCHHHHHHHHCCC
33.00-
369PhosphorylationKLLLRLPSLRTVSSS
HHHHHCCCCCCCCHH
34.7724719451
374PhosphorylationLPSLRTVSSSVIEQL
CCCCCCCCHHHHHHH
19.1122210691
375PhosphorylationPSLRTVSSSVIEQLF
CCCCCCCHHHHHHHH
25.0422210691
389UbiquitinationFFVRLVGKTPIETLI
HHHHHHCCCCHHHHH
43.5821890473
389UbiquitinationFFVRLVGKTPIETLI
HHHHHHCCCCHHHHH
43.5821890473
394PhosphorylationVGKTPIETLIRDMLL
HCCCCHHHHHHHHHH
28.3622210691

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 COT2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COT2_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 COT2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HDAC1_HUMANHDAC1physical
10704340
HDAC1_HUMANHDAC1genetic
10704340
NR2F6_HUMANNR2F6physical
10318855
TRIP4_HUMANTRIP4physical
20211142
GCR_HUMANNR3C1physical
14739255
SETD7_HUMANSETD7physical
21988832
COT2_HUMANNR2F2physical
23975195
BC11A_HUMANBCL11Aphysical
23975195
RPGR_HUMANRPGRphysical
28514442
AKT1_HUMANAKT1physical
28514442
NR2F6_HUMANNR2F6physical
28514442
VTDB_HUMANGCphysical
28514442
AKT2_HUMANAKT2physical
28514442
SHPK_HUMANSHPKphysical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of COT2_HUMAN

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Related Literatures of Post-Translational Modification

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