TRI18_HUMAN - dbPTM
TRI18_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI18_HUMAN
UniProt AC O15344
Protein Name E3 ubiquitin-protein ligase Midline-1
Gene Name MID1
Organism Homo sapiens (Human).
Sequence Length 667
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, spindle . Microtubule-associated. It is associated with microtubules throughout the cell cycle, co-localizing with cytoplasmic fibers in interphase and with the mitotic spindle and midbod
Protein Description Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination..
Protein Sequence METLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNESVESITAFQCPTCRHVITLSQRGLDGLKRNVTLQNIIDRFQKASVSGPNSPSETRRERAFDANTMTSAEKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEPIPDSHIRGLMCLEHEDEKVNMYCVTDDQLICALCKLVGRHRDHQVAALSERYDKLKQNLESNLTNLIKRNTELETLLAKLIQTCQHVEVNASRQEAKLTEECDLLIEIIQQRRQIIGTKIKEGKVMRLRKLAQQIANCKQCIERSASLISQAEHSLKENDHARFLQTAKNITERVSMATASSQVLIPEINLNDTFDTFALDFSREKKLLECLDYLTAPNPPTIREELCTASYDTITVHWTSDDEFSVVSYELQYTIFTGQANVVSLCNSADSWMIVPNIKQNHYTVHGLQSGTKYIFMVKAINQAGSRSSEPGKLKTNSQPFKLDPKSAHRKLKVSHDNLTVERDESSSKKSHTPERFTSQGSYGVAGNVFIDSGRHYWEVVISGSTWYAIGLAYKSAPKHEWIGKNSASWALCRCNNNWVVRHNSKEIPIEPAPHLRRVGILLDYDNGSIAFYDALNSIHLYTFDVAFAQPVCPTFTVWNKCLTIITGLPIPDHLDCTEQLP
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
64PhosphorylationPTCRHVITLSQRGLD
CCCCCEEEEHHHCCH		21.1929214152
66PhosphorylationCRHVITLSQRGLDGL
CCCEEEEHHHCCHHH		14.8020873877
68MethylationHVITLSQRGLDGLKR
CEEEEHHHCCHHHHH		44.24115483241
74UbiquitinationQRGLDGLKRNVTLQN
HHCCHHHHHCCCHHH		47.67-
78PhosphorylationDGLKRNVTLQNIIDR
HHHHHCCCHHHHHHH		26.6128450419
88UbiquitinationNIIDRFQKASVSGPN
HHHHHHHHHCCCCCC		39.66-
90PhosphorylationIDRFQKASVSGPNSP
HHHHHHHCCCCCCCC		24.6925463755
90 (in isoform 2)Phosphorylation-24.69-
92PhosphorylationRFQKASVSGPNSPSE
HHHHHCCCCCCCCCH		46.1429255136
92 (in isoform 2)Phosphorylation-46.14-
96PhosphorylationASVSGPNSPSETRRE
HCCCCCCCCCHHHHH		32.7029255136
96 (in isoform 2)Phosphorylation-32.70-
98 (in isoform 2)Phosphorylation-51.96-
98PhosphorylationVSGPNSPSETRRERA
CCCCCCCCHHHHHHH		51.9625463755
100PhosphorylationGPNSPSETRRERAFD
CCCCCCHHHHHHHCC		39.0925463755
110PhosphorylationERAFDANTMTSAEKV
HHHCCCCCCCCHHHH		24.4427470641
168PhosphorylationLIEPIPDSHIRGLMC
CCEECCCCCCCCEEE		18.5628857561
213PhosphorylationDHQVAALSERYDKLK
HHHHHHHHHHHHHHH		18.4625159151
216PhosphorylationVAALSERYDKLKQNL
HHHHHHHHHHHHHHH		17.2429214152
232 (in isoform 2)Ubiquitination-42.6421890473
232 (in isoform 1)Ubiquitination-42.6421890473
232UbiquitinationSNLTNLIKRNTELET
HHHHHHHHHHHHHHH		42.6421890473
266GlutathionylationEAKLTEECDLLIEII
HHHHHHHHHHHHHHH		3.4822555962
309PhosphorylationCKQCIERSASLISQA
HHHHHHHHHHHHHHH		14.9329978859
311PhosphorylationQCIERSASLISQAEH
HHHHHHHHHHHHHHH		27.7327422710
314PhosphorylationERSASLISQAEHSLK
HHHHHHHHHHHHHHC		28.7323312004
321UbiquitinationSQAEHSLKENDHARF
HHHHHHHCCCHHHHH		58.44-
333UbiquitinationARFLQTAKNITERVS
HHHHHHHHHHHHHHH		52.88-
378PhosphorylationKLLECLDYLTAPNPP
HHHHHHHHHCCCCCC		7.9422461510
474PhosphorylationNQAGSRSSEPGKLKT
HHCCCCCCCCCCCCC		46.8530576142
480UbiquitinationSSEPGKLKTNSQPFK
CCCCCCCCCCCCCCC		49.50-
481PhosphorylationSEPGKLKTNSQPFKL
CCCCCCCCCCCCCCC		51.0030576142
483PhosphorylationPGKLKTNSQPFKLDP
CCCCCCCCCCCCCCH		44.4530576142
500PhosphorylationAHRKLKVSHDNLTVE
HCCCCCCCCCCCEEE		24.4420873877
505PhosphorylationKVSHDNLTVERDESS
CCCCCCCEEECCCCC		26.9520873877
511PhosphorylationLTVERDESSSKKSHT
CEEECCCCCCCCCCC		44.1725159151
512PhosphorylationTVERDESSSKKSHTP
EEECCCCCCCCCCCC		44.0920873877
513PhosphorylationVERDESSSKKSHTPE
EECCCCCCCCCCCCC		54.0720873877
518PhosphorylationSSSKKSHTPERFTSQ
CCCCCCCCCCCCCCC		33.66-
523PhosphorylationSHTPERFTSQGSYGV
CCCCCCCCCCCCCEE		26.7628152594
524PhosphorylationHTPERFTSQGSYGVA
CCCCCCCCCCCCEEE		29.8128152594
527PhosphorylationERFTSQGSYGVAGNV
CCCCCCCCCEEEEEE		15.8628442448
528PhosphorylationRFTSQGSYGVAGNVF
CCCCCCCCEEEEEEE		23.5728152594
572PhosphorylationHEWIGKNSASWALCR
CCCCCCCCCCEEEEE		27.4520363803
590PhosphorylationNWVVRHNSKEIPIEP
CEEEEECCCCCCCCC		26.0728857561
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 TRI18_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI18_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 TRI18_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI18_HUMANMID1physical
11331580
TRIM1_HUMANMID2physical
11331580
TRI18_HUMANMID1physical
11806752
TRIM1_HUMANMID2physical
11806752
IGBP1_MOUSEIgbp1physical
11806752
TRI18_HUMANMID1physical
10400985
IGBP1_HUMANIGBP1physical
20092282
PP2AA_HUMANPPP2CAphysical
20092282
TRI18_HUMANMID1physical
21296087
UB2D1_HUMANUBE2D1physical
21296087
UB2D1_HUMANUBE2D1physical
21143188
UB2D2_HUMANUBE2D2physical
21143188
UB2D3_HUMANUBE2D3physical
21143188
UB2D4_HUMANUBE2D4physical
21143188
UB2E1_HUMANUBE2E1physical
21143188
UB2E2_HUMANUBE2E2physical
21143188
UB2E3_HUMANUBE2E3physical
21143188
UBE2N_HUMANUBE2Nphysical
21143188
IGBP1_HUMANIGBP1physical
11685209
TRIM1_HUMANMID2physical
16434393
IGBP1_HUMANIGBP1physical
16434393
IGBP1_HUMANIGBP1physical
22613722
PP2AA_HUMANPPP2CAphysical
22613722
HS90A_HUMANHSP90AA1physical
18172692
EF1A1_HUMANEEF1A1physical
18172692
ANXA2_HUMANANXA2physical
18172692
RS3_HUMANRPS3physical
18172692
RACK1_HUMANGNB2L1physical
18172692
NPM_HUMANNPM1physical
18172692
RS8_HUMANRPS8physical
18172692
PTPA_HUMANPPP2R4physical
15057556
UB2D2_HUMANUBE2D2physical
22613722
UB2D3_HUMANUBE2D3physical
22613722
M1IP1_HUMANMID1IP1physical
15070402
IGBP1_HUMANIGBP1physical
23740247
TRI18_HUMANMID1physical
22493164
PP2AA_HUMANPPP2CAphysical
25207814
UB2D1_HUMANUBE2D1physical
25207814
UB2D2_HUMANUBE2D2physical
25207814
UB2D3_HUMANUBE2D3physical
25207814
UB2E1_HUMANUBE2E1physical
25207814
TRI18_HUMANMID1physical
25207814
PTPA_HUMANPPP2R4physical
25207814
STK36_HUMANSTK36physical
25278022
UB2D1_HUMANUBE2D1physical
25278022
UB2D2_HUMANUBE2D2physical
25278022
UB2D3_HUMANUBE2D3physical
25278022
TRI18_HUMANMID1physical
25416956
PKN1_HUMANPKN1physical
25416956
UB2D1_HUMANUBE2D1physical
25416956
UB2D3_HUMANUBE2D3physical
25416956
UB2E2_HUMANUBE2E2physical
25416956
DYRK4_HUMANDYRK4physical
25416956
UB2E3_HUMANUBE2E3physical
25416956
TRIM1_HUMANMID2physical
25416956
GMCL1_HUMANGMCL1physical
25416956
OTUB2_HUMANOTUB2physical
25416956
UBTD1_HUMANUBTD1physical
25416956
TEANC_HUMANTCEANCphysical
25416956
UBC_HUMANUBCphysical
11685209
ANDR_HUMANARphysical
24913494
EFL1_HUMANEFTUD1physical
26344197
TRI18_HUMANMID1physical
21516116
UB2E2_HUMANUBE2E2physical
21516116
TRIM1_HUMANMID2physical
26748699
SPAG5_HUMANSPAG5physical
26748699
TBB5_HUMANTUBBphysical
26748699
TBA1B_HUMANTUBA1Bphysical
26748699
TBB4B_HUMANTUBB4Bphysical
26748699
PSMD3_HUMANPSMD3physical
26748699
PRS7_HUMANPSMC2physical
26748699
PSMD2_HUMANPSMD2physical
26748699
PSB5_HUMANPSMB5physical
26748699
PRS4_HUMANPSMC1physical
26748699
PSA1_HUMANPSMA1physical
26748699
PSB4_HUMANPSMB4physical
26748699
PSB1_HUMANPSMB1physical
26748699
PSMD7_HUMANPSMD7physical
26748699
PSDE_HUMANPSMD14physical
26748699
PSA6_HUMANPSMA6physical
26748699
PSB6_HUMANPSMB6physical
26748699
PRS10_HUMANPSMC6physical
26748699
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300000Opitz GBBB syndrome 1 (GBBB1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRI18_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-92; SER-96 ANDSER-98, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-98, AND MASSSPECTROMETRY.

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