MEX3C_HUMAN - dbPTM
MEX3C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MEX3C_HUMAN
UniProt AC Q5U5Q3
Protein Name RNA-binding E3 ubiquitin-protein ligase MEX3C
Gene Name MEX3C
Organism Homo sapiens (Human).
Sequence Length 659
Subcellular Localization Cytoplasm . Nucleus . Predominantly expressed in the cytoplasm and shuttles between the cytoplasm and the nucleus through the CRM1 export pathway. May act as suppressor of replication stress and chromosome missegregation.
Protein Description E3 ubiquitin ligase responsible for the post-transcriptional regulation of common HLA-A allotypes. Binds to the 3' UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation..
Protein Sequence MPSGSSAALALAAAPAPLPQPPPPPPPPPPPLPPPSGGPELEGDGLLLRERLAALGLDDPSPAEPGAPALRAPAAAAQGQARRAAELSPEERAPPGRPGAPEAAELELEEDEEEGEEAELDGDLLEEEELEEAEEEDRSSLLLLSPPAATASQTQQIPGGSLGSVLLPAARFDAREAAAAAAAAGVLYGGDDAQGMMAAMLSHAYGPGGCGAAAAALNGEQAALLRRKSVNTTECVPVPSSEHVAEIVGRQGCKIKALRAKTNTYIKTPVRGEEPIFVVTGRKEDVAMAKREILSAAEHFSMIRASRNKNGPALGGLSCSPNLPGQTTVQVRVPYRVVGLVVGPKGATIKRIQQQTHTYIVTPSRDKEPVFEVTGMPENVDRAREEIEMHIAMRTGNYIELNEENDFHYNGTDVSFEGGTLGSAWLSSNPVPPSRARMISNYRNDSSSSLGSGSTDSYFGSNRLADFSPTSPFSTGNFWFGDTLPSVGSEDLAVDSPAFDSLPTSAQTIWTPFEPVNPLSGFGSDPSGNMKTQRRGSQPSTPRLSPTFPESIEHPLARRVRSDPPSTGNHVGLPIYIPAFSNGTNSYSSSNGGSTSSSPPESRRKHDCVICFENEVIAALVPCGHNLFCMECANKICEKRTPSCPVCQTAVTQAIQIHS
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
61PhosphorylationALGLDDPSPAEPGAP
HCCCCCCCCCCCCCC		43.6829978859
88PhosphorylationARRAAELSPEERAPP
HHHHHHCCHHHCCCC		23.0529255136
139PhosphorylationEAEEEDRSSLLLLSP
HHHHHHHHCEEEECC		37.3525850435
140PhosphorylationAEEEDRSSLLLLSPP
HHHHHHHCEEEECCC		24.7525850435
145PhosphorylationRSSLLLLSPPAATAS
HHCEEEECCCCCCCC		28.8925850435
150PhosphorylationLLSPPAATASQTQQI
EECCCCCCCCCCCCC		29.0227732954
152PhosphorylationSPPAATASQTQQIPG
CCCCCCCCCCCCCCC		29.4327732954
154PhosphorylationPAATASQTQQIPGGS
CCCCCCCCCCCCCCC		21.6827732954
228UbiquitinationQAALLRRKSVNTTEC
HHHHHHCCCCCCCCC		52.9329967540
229PhosphorylationAALLRRKSVNTTECV
HHHHHCCCCCCCCCE		20.8429255136
232PhosphorylationLRRKSVNTTECVPVP
HHCCCCCCCCCEECC		23.0929255136
233PhosphorylationRRKSVNTTECVPVPS
HCCCCCCCCCEECCC		23.3729255136
240PhosphorylationTECVPVPSSEHVAEI
CCCEECCCHHHHHHH		48.9029255136
241PhosphorylationECVPVPSSEHVAEIV
CCEECCCHHHHHHHH		26.1729255136
261UbiquitinationKIKALRAKTNTYIKT
EEEEEEECCCCEEEC		35.5527667366
262PhosphorylationIKALRAKTNTYIKTP
EEEEEECCCCEEECC		31.6328152594
264PhosphorylationALRAKTNTYIKTPVR
EEEECCCCEEECCCC		31.6828152594
265PhosphorylationLRAKTNTYIKTPVRG
EEECCCCEEECCCCC		11.5128152594
267UbiquitinationAKTNTYIKTPVRGEE
ECCCCEEECCCCCCC		36.04-
268PhosphorylationKTNTYIKTPVRGEEP
CCCCEEECCCCCCCC		19.9125159151
301PhosphorylationLSAAEHFSMIRASRN
HHHHHHHHHHHHHCC		18.4029396449
306PhosphorylationHFSMIRASRNKNGPA
HHHHHHHHCCCCCCC		26.9129396449
309UbiquitinationMIRASRNKNGPALGG
HHHHHCCCCCCCCCC		63.2729967540
318PhosphorylationGPALGGLSCSPNLPG
CCCCCCCCCCCCCCC		18.8025850435
320PhosphorylationALGGLSCSPNLPGQT
CCCCCCCCCCCCCCE		17.2828348404
345UbiquitinationVGLVVGPKGATIKRI
EEEEECCCCHHHHHH		56.0732142685
348PhosphorylationVVGPKGATIKRIQQQ
EECCCCHHHHHHHHC		35.38-
358PhosphorylationRIQQQTHTYIVTPSR
HHHHCCCEEEECCCC		20.5229759185
362PhosphorylationQTHTYIVTPSRDKEP
CCCEEEECCCCCCCC		13.1429759185
367UbiquitinationIVTPSRDKEPVFEVT
EECCCCCCCCCEEEE		63.9122817900
446PhosphorylationISNYRNDSSSSLGSG
HHHCCCCCCCCCCCC		35.3530576142
447PhosphorylationSNYRNDSSSSLGSGS
HHCCCCCCCCCCCCC		27.1527251275
448PhosphorylationNYRNDSSSSLGSGST
HCCCCCCCCCCCCCC		33.2730576142
448O-linked_GlycosylationNYRNDSSSSLGSGST
HCCCCCCCCCCCCCC		33.27OGP
449O-linked_GlycosylationYRNDSSSSLGSGSTD
CCCCCCCCCCCCCCC		38.40OGP
449PhosphorylationYRNDSSSSLGSGSTD
CCCCCCCCCCCCCCC		38.4026471730
452O-linked_GlycosylationDSSSSLGSGSTDSYF
CCCCCCCCCCCCCCC		34.56OGP
452PhosphorylationDSSSSLGSGSTDSYF
CCCCCCCCCCCCCCC		34.5628348404
454O-linked_GlycosylationSSSLGSGSTDSYFGS
CCCCCCCCCCCCCCC		30.64OGP
454PhosphorylationSSSLGSGSTDSYFGS
CCCCCCCCCCCCCCC		30.6427251275
455PhosphorylationSSLGSGSTDSYFGSN
CCCCCCCCCCCCCCC		32.2722210691
470PhosphorylationRLADFSPTSPFSTGN
CCCCCCCCCCCCCCC		48.0826074081
471PhosphorylationLADFSPTSPFSTGNF
CCCCCCCCCCCCCCC		27.6026074081
537PhosphorylationMKTQRRGSQPSTPRL
CCCCCCCCCCCCCCC		36.7930266825
540PhosphorylationQRRGSQPSTPRLSPT
CCCCCCCCCCCCCCC		43.3230266825
541PhosphorylationRRGSQPSTPRLSPTF
CCCCCCCCCCCCCCC		21.0727273156
545PhosphorylationQPSTPRLSPTFPESI
CCCCCCCCCCCCHHC		24.1529255136
547PhosphorylationSTPRLSPTFPESIEH
CCCCCCCCCCHHCCC		48.7430266825
551PhosphorylationLSPTFPESIEHPLAR
CCCCCCHHCCCHHHH		33.2523927012
576PhosphorylationNHVGLPIYIPAFSNG
CCCCCCEEEECCCCC		10.0224248375
587PhosphorylationFSNGTNSYSSSNGGS
CCCCCCCCCCCCCCC		18.0324248375
588PhosphorylationSNGTNSYSSSNGGST
CCCCCCCCCCCCCCC		27.4124248375
594PhosphorylationYSSSNGGSTSSSPPE
CCCCCCCCCCCCCCH		26.8924248375
595PhosphorylationSSSNGGSTSSSPPES
CCCCCCCCCCCCCHH		35.5824248375
596PhosphorylationSSNGGSTSSSPPESR
CCCCCCCCCCCCHHH		30.4324248375
597PhosphorylationSNGGSTSSSPPESRR
CCCCCCCCCCCHHHC		47.1324248375
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 MEX3C_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MEX3C_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 MEX3C_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBP7_HUMANUSP7physical
22863774
PABP1_HUMANPABPC1physical
18779327
DSRAD_HUMANADARphysical
26471122
AIFM1_HUMANAIFM1physical
26471122
AP2A1_HUMANAP2A1physical
26471122
AP2A2_HUMANAP2A2physical
26471122
AP2B1_HUMANAP2B1physical
26471122
ATD3A_HUMANATAD3Aphysical
26471122
ATX2L_HUMANATXN2Lphysical
26471122
BMS1_HUMANBMS1physical
26471122
C1TC_HUMANMTHFD1physical
26471122
PYR1_HUMANCADphysical
26471122
CCAR2_HUMANCCAR2physical
26471122
CNOT1_HUMANCNOT1physical
26471122
CNOT3_HUMANCNOT3physical
26471122
DHX37_HUMANDHX37physical
26471122
PRKDC_HUMANPRKDCphysical
26471122
EF1A1_HUMANEEF1A1physical
26471122
EIF3A_HUMANEIF3Aphysical
26471122
GGYF2_HUMANGIGYF2physical
26471122
GLE1_HUMANGLE1physical
26471122
GTPB1_HUMANGTPBP1physical
26471122
HNRL2_HUMANHNRNPUL2physical
26471122
GRP78_HUMANHSPA5physical
26471122
ILF3_HUMANILF3physical
26471122
LENG8_HUMANLENG8physical
26471122
LPPRC_HUMANLRPPRCphysical
26471122
MARK3_HUMANMARK3physical
26471122
RT30_HUMANMRPS30physical
26471122
MYCB2_HUMANMYCBP2physical
26471122
MYO1C_HUMANMYO1Cphysical
26471122
NOL6_HUMANNOL6physical
26471122
NUFP2_HUMANNUFIP2physical
26471122
NXF1_HUMANNXF1physical
26471122
RPOM_HUMANPOLRMTphysical
26471122
PRP6_HUMANPRPF6physical
26471122
PRP8_HUMANPRPF8physical
26471122
RBM19_HUMANRBM19physical
26471122
SAFB2_HUMANSAFB2physical
26471122
TIF1B_HUMANTRIM28physical
26471122
WDR6_HUMANWDR6physical
26471122
ZCCHV_HUMANZC3HAV1physical
26471122
ZN574_HUMANZNF574physical
26471122
CNOT7_HUMANCNOT7physical
26471122
PAN2_HUMANPAN2physical
26471122
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 MEX3C_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory