TRIM1_HUMAN - dbPTM
TRIM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRIM1_HUMAN
UniProt AC Q9UJV3
Protein Name Probable E3 ubiquitin-protein ligase MID2
Gene Name MID2
Organism Homo sapiens (Human).
Sequence Length 735
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. Microtubule-associated.
Protein Description May play a role in microtubule stabilization..
Protein Sequence MGESPASVVLNASGGLFSLKMETLESELTCPICLELFEDPLLLPCAHSLCFSCAHRILVSSCSSGESIEPITAFQCPTCRYVISLNHRGLDGLKRNVTLQNIIDRFQKASVSGPNSPSESRRERTYRPTTAMSSERIACQFCEQDPPRDAVKTCITCEVSYCDRCLRATHPNKKPFTSHRLVEPVPDTHLRGITCLDHENEKVNMYCVSDDQLICALCKLVGRHRDHQVASLNDRFEKLKQTLEMNLTNLVKRNSELENQMAKLIQICQQVEVNTAMHEAKLMEECDELVEIIQQRKQMIAVKIKETKVMKLRKLAQQVANCRQCLERSTVLINQAEHILKENDQARFLQSAKNIAERVAMATASSQVLIPDINFNDAFENFALDFSREKKLLEGLDYLTAPNPPSIREELCTASHDTITVHWISDDEFSISSYELQYTIFTGQANFISKSWCSWGLWPEIRKCKEAVSCSRLAGAPRGLYNSVDSWMIVPNIKQNHYTVHGLQSGTRYIFIVKAINQAGSRNSEPTRLKTNSQPFKLDPKMTHKKLKISNDGLQMEKDESSLKKSHTPERFSGTGCYGAAGNIFIDSGCHYWEVVMGSSTWYAIGIAYKSAPKNEWIGKNASSWVFSRCNSNFVVRHNNKEMLVDVPPHLKRLGVLLDYDNNMLSFYDPANSLHLHTFDVTFILPVCPTFTIWNKSLMILSGLPAPDFIDYPERQECNCRPQESPYVSGMKTCH
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
18PhosphorylationNASGGLFSLKMETLE
ECCCCEEEEEEEECC
31.9324719451
94UbiquitinationHRGLDGLKRNVTLQN
CCCCHHHHCCEEHHH
47.67-
98PhosphorylationDGLKRNVTLQNIIDR
HHHHCCEEHHHHHHH
26.6128450419
110PhosphorylationIDRFQKASVSGPNSP
HHHHHHHCCCCCCCC
24.6923403867
112PhosphorylationRFQKASVSGPNSPSE
HHHHHCCCCCCCCCH
46.1426055452
116PhosphorylationASVSGPNSPSESRRE
HCCCCCCCCCHHHHH
32.7021712546
118PhosphorylationVSGPNSPSESRRERT
CCCCCCCCHHHHHCC
48.2823403867
120PhosphorylationGPNSPSESRRERTYR
CCCCCCHHHHHCCCC
40.7623403867
169PhosphorylationCDRCLRATHPNKKPF
HHHHHHCCCCCCCCC
31.2829083192
177PhosphorylationHPNKKPFTSHRLVEP
CCCCCCCCCCCCCCC
31.9529083192
178PhosphorylationPNKKPFTSHRLVEPV
CCCCCCCCCCCCCCC
13.6429083192
242PhosphorylationRFEKLKQTLEMNLTN
HHHHHHHHHHHHHHH
24.0924505115
311AcetylationIKETKVMKLRKLAQQ
ECHHHHHHHHHHHHH
48.4019816947
398PhosphorylationKLLEGLDYLTAPNPP
HHHCCCCCCCCCCCC
15.8221394647
400PhosphorylationLEGLDYLTAPNPPSI
HCCCCCCCCCCCCCH
33.5629507054
469PhosphorylationRKCKEAVSCSRLAGA
HHHHHHHCHHHHCCC
17.2723403867
471PhosphorylationCKEAVSCSRLAGAPR
HHHHHCHHHHCCCCC
23.8723403867
498PhosphorylationPNIKQNHYTVHGLQS
CCCCCCCEEEEEECC
20.2924043423
499PhosphorylationNIKQNHYTVHGLQSG
CCCCCCEEEEEECCC
9.8524043423
505PhosphorylationYTVHGLQSGTRYIFI
EEEEEECCCCEEEEE
47.3724043423
507PhosphorylationVHGLQSGTRYIFIVK
EEEECCCCEEEEEEE
26.0824043423
530UbiquitinationNSEPTRLKTNSQPFK
CCCCCCCCCCCCCCC
42.23-
543PhosphorylationFKLDPKMTHKKLKIS
CCCCHHCCCCEEEEC
36.3523403867
550PhosphorylationTHKKLKISNDGLQME
CCCEEEECCCCCCCC
27.5522210691
623PhosphorylationEWIGKNASSWVFSRC
CCCCCCCCHHHHHCC
33.84-
725PhosphorylationCNCRPQESPYVSGMK
CCCCCCCCCCCCCCC
19.1126330541
727PhosphorylationCRPQESPYVSGMKTC
CCCCCCCCCCCCCCC
19.2726267517
729PhosphorylationPQESPYVSGMKTCH-
CCCCCCCCCCCCCC-
27.5926330541

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 TRIM1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRIM1_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 TRIM1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DYDC1_HUMANDYDC1physical
16189514
TRIM1_HUMANMID2physical
11331580
TRI18_HUMANMID1physical
11331580
TRIM1_HUMANMID2physical
11806752
TRI18_HUMANMID1physical
11806752
IGBP1_MOUSEIgbp1physical
11806752
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
TRI18_HUMANMID1physical
16434393
IGBP1_HUMANIGBP1physical
16434393
TRIM1_HUMANMID2physical
25416956
F107A_HUMANFAM107Aphysical
25416956
ISCU_HUMANISCUphysical
25416956
GORS2_HUMANGORASP2physical
25416956
PRP31_HUMANPRPF31physical
25416956
DIEXF_HUMANDIEXFphysical
25416956
SPG21_HUMANSPG21physical
25416956
UB2D4_HUMANUBE2D4physical
25416956
SYT17_HUMANSYT17physical
25416956
ATL4_HUMANADAMTSL4physical
25416956
CCHCR_HUMANCCHCR1physical
25416956
MGN2_HUMANMAGOHBphysical
25416956
F90A1_HUMANFAM90A1physical
25416956
RYDEN_HUMANC19orf66physical
25416956
TRPV6_HUMANTRPV6physical
25416956
RCOR3_HUMANRCOR3physical
25416956
UN45A_HUMANUNC45Aphysical
25416956
F214A_HUMANFAM214Aphysical
25416956
PPL13_HUMANLGALS14physical
25416956
TRI54_HUMANTRIM54physical
25416956
CBX8_HUMANCBX8physical
25416956
ZN250_HUMANZNF250physical
25416956
DMRT3_HUMANDMRT3physical
25416956
M1IP1_HUMANMID1IP1physical
25416956
GMCL1_HUMANGMCL1physical
25416956
MET17_HUMANMETTL17physical
25416956
AEN_HUMANAENphysical
25416956
OTUB2_HUMANOTUB2physical
25416956
SCNM1_HUMANSCNM1physical
25416956
ZFY21_HUMANZFYVE21physical
25416956
LENG1_HUMANLENG1physical
25416956
ZC21C_HUMANZC2HC1Cphysical
25416956
PTCD2_HUMANPTCD2physical
25416956
UBTD1_HUMANUBTD1physical
25416956
FXL18_HUMANFBXL18physical
25416956
TSG10_HUMANTSGA10physical
25416956
K1683_HUMANKIAA1683physical
25416956
THAP7_HUMANTHAP7physical
25416956
ATRIP_HUMANATRIPphysical
25416956
F161A_HUMANFAM161Aphysical
25416956
UTP23_HUMANUTP23physical
25416956
BRM1L_HUMANBRMS1Lphysical
25416956
ZGPAT_HUMANZGPATphysical
25416956
ZN587_HUMANZNF587physical
25416956
FBF1_HUMANFBF1physical
25416956
DGC6L_HUMANDGCR6Lphysical
25416956
CC120_HUMANCCDC120physical
25416956
SNP47_HUMANSNAP47physical
25416956
FRMD6_HUMANFRMD6physical
25416956
ZN440_HUMANZNF440physical
25416956
ZN792_HUMANZNF792physical
25416956
RP25L_HUMANRPP25Lphysical
25416956
ZN785_HUMANZNF785physical
25416956
CCD42_HUMANCCDC42physical
25416956
ZN417_HUMANZNF417physical
25416956
S2548_HUMANSLC25A48physical
25416956
ZN564_HUMANZNF564physical
25416956
PPR18_HUMANPPP1R18physical
25416956
SPA24_HUMANSPATA24physical
25416956
BCL6B_HUMANBCL6Bphysical
25416956
CE57L_HUMANCEP57L1physical
25416956
TRI42_HUMANTRIM42physical
25416956
BRCA1_HUMANBRCA1physical
25184681
COX5B_HUMANCOX5Bphysical
21516116
DCX_HUMANDCXphysical
21516116
CE57L_HUMANCEP57L1physical
21516116
ZN774_HUMANZNF774physical
21516116
UB2D4_HUMANUBE2D4physical
21516116
TSG10_HUMANTSGA10physical
21516116
K1683_HUMANKIAA1683physical
21516116
TM14B_HUMANTMEM14Bphysical
21516116
TCAF1_HUMANFAM115Aphysical
21516116
ZNF24_HUMANZNF24physical
21516116
TRI18_HUMANMID1physical
26748699
SPAG5_HUMANSPAG5physical
26748699
TBB5_HUMANTUBBphysical
26748699
TBA1B_HUMANTUBA1Bphysical
26748699
TBB4B_HUMANTUBB4Bphysical
26748699
CE128_HUMANCEP128physical
26748699
ASPM_HUMANASPMphysical
26748699
PSMD3_HUMANPSMD3physical
26748699
PRS7_HUMANPSMC2physical
26748699
PSD11_HUMANPSMD11physical
26748699
PSMD2_HUMANPSMD2physical
26748699
PSB5_HUMANPSMB5physical
26748699
LNX1_HUMANLNX1physical
29121065

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300928Mental retardation, X-linked 101 (MRX101)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRIM1_HUMAN

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Related Literatures of Post-Translational Modification

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