PRAME_HUMAN - dbPTM
PRAME_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRAME_HUMAN
UniProt AC P78395
Protein Name Melanoma antigen preferentially expressed in tumors {ECO:0000305}
Gene Name PRAME {ECO:0000312|HGNC:HGNC:9336}
Organism Homo sapiens (Human).
Sequence Length 509
Subcellular Localization Nucleus . Cell membrane .
Protein Description Functions as a transcriptional repressor, inhibiting the signaling of retinoic acid through the retinoic acid receptors RARA, RARB and RARG. Prevents retinoic acid-induced cell proliferation arrest, differentiation and apoptosis..
Protein Sequence MERRRLWGSIQSRYISMSVWTSPRRLVELAGQSLLKDEALAIAALELLPRELFPPLFMAAFDGRHSQTLKAMVQAWPFTCLPLGVLMKGQHLHLETFKAVLDGLDVLLAQEVRPRRWKLQVLDLRKNSHQDFWTVWSGNRASLYSFPEPEAAQPMTKKRKVDGLSTEAEQPFIPVEVLVDLFLKEGACDELFSYLIEKVKRKKNVLRLCCKKLKIFAMPMQDIKMILKMVQLDSIEDLEVTCTWKLPTLAKFSPYLGQMINLRRLLLSHIHASSYISPEKEEQYIAQFTSQFLSLQCLQALYVDSLFFLRGRLDQLLRHVMNPLETLSITNCRLSEGDVMHLSQSPSVSQLSVLSLSGVMLTDVSPEPLQALLERASATLQDLVFDECGITDDQLLALLPSLSHCSQLTTLSFYGNSISISALQSLLQHLIGLSNLTHVLYPVPLESYEDIHGTLHLERLAYLHARLRELLCELGRPSMVWLSANPCPHCGDRTFYDPEPILCPCFMPN
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
9PhosphorylationERRRLWGSIQSRYIS
CCHHHHHHHHHHEEH		13.0826434776
12PhosphorylationRLWGSIQSRYISMSV
HHHHHHHHHEEHHHC		25.9426434776
14PhosphorylationWGSIQSRYISMSVWT
HHHHHHHEEHHHCCC		11.5527174698
16PhosphorylationSIQSRYISMSVWTSP
HHHHHEEHHHCCCCH		8.9616179254
18PhosphorylationQSRYISMSVWTSPRR
HHHEEHHHCCCCHHH		14.0127174698
21PhosphorylationYISMSVWTSPRRLVE
EEHHHCCCCHHHHHH		27.0527174698
22PhosphorylationISMSVWTSPRRLVEL
EHHHCCCCHHHHHHH		10.7427174698
33PhosphorylationLVELAGQSLLKDEAL
HHHHHCCCCCCCHHH		34.4524719451
118UbiquitinationEVRPRRWKLQVLDLR
CCCCCCCEEEEEECC		27.51-
126UbiquitinationLQVLDLRKNSHQDFW
EEEEECCCCCCCCCE		70.83-
142PhosphorylationVWSGNRASLYSFPEP
EECCCCCEEECCCCH		25.3021945579
144PhosphorylationSGNRASLYSFPEPEA
CCCCCEEECCCCHHH		13.0321945579
145PhosphorylationGNRASLYSFPEPEAA
CCCCEEECCCCHHHC		39.3521945579
157UbiquitinationEAAQPMTKKRKVDGL
HHCCCCCCCCCCCCC		44.3121906983
158UbiquitinationAAQPMTKKRKVDGLS
HCCCCCCCCCCCCCC		48.57-
158AcetylationAAQPMTKKRKVDGLS
HCCCCCCCCCCCCCC		48.5712431373
184AcetylationVLVDLFLKEGACDEL
HHHHHHHHCCCCHHH		46.9312431381
198UbiquitinationLFSYLIEKVKRKKNV
HHHHHHHHHHCCCCH		46.17-
224UbiquitinationAMPMQDIKMILKMVQ
EEEHHHHHHHHHHHC		28.33-
251UbiquitinationWKLPTLAKFSPYLGQ
EECCCHHHHCHHHHH		49.87-
253PhosphorylationLPTLAKFSPYLGQMI
CCCHHHHCHHHHHHH		16.3626074081
255PhosphorylationTLAKFSPYLGQMINL
CHHHHCHHHHHHHHH		23.4326074081
345PhosphorylationDVMHLSQSPSVSQLS
CEEEHHCCCCHHHHH		18.7724400094
349PhosphorylationLSQSPSVSQLSVLSL
HHCCCCHHHHHEEEC		29.7324400094
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 PRAME_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRAME_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 PRAME_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUL2_HUMANCUL2physical
21822215
ELOC_HUMANTCEB1physical
21822215
ELOB_HUMANTCEB2physical
21822215
RBX1_HUMANRBX1physical
21822215
KDM1A_HUMANKDM1Aphysical
22912744
BAG2_HUMANBAG2physical
22912744
HNRPC_HUMANHNRNPCphysical
22912744
UBL4A_HUMANUBL4Aphysical
22912744
RSMB_HUMANSNRPBphysical
22912744
RL10_HUMANRPL10physical
22912744
HNRH1_HUMANHNRNPH1physical
22912744
RFC4_HUMANRFC4physical
22912744
RL22_HUMANRPL22physical
22912744
PRS6B_HUMANPSMC4physical
22912744
HNRPM_HUMANHNRNPMphysical
22912744
HNRPF_HUMANHNRNPFphysical
22912744
RS13_HUMANRPS13physical
22912744
RBX1_HUMANRBX1physical
22912744
PRAME_HUMANPRAMEphysical
22912744
CUL2_HUMANCUL2physical
22912744
LAGE3_HUMANLAGE3physical
22912744
ELOC_HUMANTCEB1physical
22912744
ELOB_HUMANTCEB2physical
22912744
OSGEP_HUMANOSGEPphysical
22912744
PRPK_HUMANTP53RKphysical
22912744
TPRKB_HUMANTPRKBphysical
22912744
RARA_HUMANRARAphysical
16179254
ELOB_HUMANTCEB2physical
23460923
ELOC_HUMANTCEB1physical
23460923
CUL2_HUMANCUL2physical
23460923
H2B2E_HUMANHIST2H2BEphysical
23460923
H2A2C_HUMANHIST2H2ACphysical
23460923
H31T_HUMANHIST3H3physical
23460923
FXL12_HUMANFBXL12physical
24035498
UBC_HUMANUBCphysical
21822215
CSN2_HUMANCOPS2physical
26186194
CUL2_HUMANCUL2physical
26186194
NOL11_HUMANNOL11physical
26186194
EF1D_HUMANEEF1Dphysical
28514442
CUL2_HUMANCUL2physical
28514442
CC28B_HUMANCCDC28Bphysical
27173435
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 PRAME_HUMAN

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Related Literatures of Post-Translational Modification

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