TRIM3_HUMAN - dbPTM
TRIM3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRIM3_HUMAN
UniProt AC O75382
Protein Name Tripartite motif-containing protein 3
Gene Name TRIM3
Organism Homo sapiens (Human).
Sequence Length 744
Subcellular Localization Cytoplasm. Early endosome . Golgi apparatus, trans-Golgi network . Cell projection, dendrite .
Protein Description Probably involved in vesicular trafficking via its association with the CART complex. [PubMed: 15772161 The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation]
Protein Sequence MAKREDSPGPEVQPMDKQFLVCSICLDRYQCPKVLPCLHTFCERCLQNYIPAQSLTLSCPVCRQTSILPEQGVSALQNNFFISSLMEAMQQAPDGAHDPEDPHPLSVVAGRPLSCPNHEGKTMEFYCEACETAMCGECRAGEHREHGTVLLRDVVEQHKAALQRQLEAVRGRLPQLSAAIALVGGISQQLQERKAEALAQISAAFEDLEQALQQRKQALVSDLETICGAKQKVLQSQLDTLRQGQEHIGSSCSFAEQALRLGSAPEVLLVRKHMRERLAALAAQAFPERPHENAQLELVLEVDGLRRSVLNLGALLTTSATAHETVATGEGLRQALVGQPASLTVTTKDKDGRLVRTGSAELRAEITGPDGTRLPVPVVDHKNGTYELVYTARTEGELLLSVLLYGQPVRGSPFRVRALRPGDLPPSPDDVKRRVKSPGGPGSHVRQKAVRRPSSMYSTGGKRKDNPIEDELVFRVGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRWVSIFSPEGKFKTKIGAGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSAEPLYGPQGLALTSDGHVVVADAGNHCFKAYRYLQ
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
2Acetylation------MAKREDSPG
------CCCCCCCCC		21.4419413330
7Phosphorylation-MAKREDSPGPEVQP
-CCCCCCCCCCCCCC		27.3129255136
23PhosphorylationDKQFLVCSICLDRYQ
CCCEEEEEHHHHHHC		14.6221406692
159UbiquitinationRDVVEQHKAALQRQL
HHHHHHHHHHHHHHH		34.74-
202PhosphorylationAEALAQISAAFEDLE
HHHHHHHHHHHHHHH		11.06-
216UbiquitinationEQALQQRKQALVSDL
HHHHHHHHHHHHHHH		35.27-
342PhosphorylationALVGQPASLTVTTKD
HHCCCCCEEEEEEEC		31.1228857561
344PhosphorylationVGQPASLTVTTKDKD
CCCCCEEEEEEECCC		17.2028857561
346PhosphorylationQPASLTVTTKDKDGR
CCCEEEEEEECCCCC		23.9330177828
347PhosphorylationPASLTVTTKDKDGRL
CCEEEEEEECCCCCE		32.6725690035
357PhosphorylationKDGRLVRTGSAELRA
CCCCEEECCCCEEEE		28.1928348404
359PhosphorylationGRLVRTGSAELRAEI
CCEEECCCCEEEEEE		20.2522964224
412PhosphorylationYGQPVRGSPFRVRAL
HCCCCCCCCEEEEEC		15.4224719451
427PhosphorylationRPGDLPPSPDDVKRR
CCCCCCCCHHHHHHH		38.7330266825
437PhosphorylationDVKRRVKSPGGPGSH
HHHHHCCCCCCCCHH		26.3930266825
443PhosphorylationKSPGGPGSHVRQKAV
CCCCCCCHHHHHHHH		23.1826055452
454PhosphorylationQKAVRRPSSMYSTGG
HHHHCCCHHHCCCCC		26.4023882029
455PhosphorylationKAVRRPSSMYSTGGK
HHHCCCHHHCCCCCC		25.1521712546
457PhosphorylationVRRPSSMYSTGGKRK
HCCCHHHCCCCCCCC		12.6723403867
458PhosphorylationRRPSSMYSTGGKRKD
CCCHHHCCCCCCCCC		16.3721712546
459PhosphorylationRPSSMYSTGGKRKDN
CCHHHCCCCCCCCCC		32.2523403867
483UbiquitinationVGSRGREKGEFTNLQ
ECCCCCCCCCCCCCC		63.48-
487PhosphorylationGREKGEFTNLQGVSA
CCCCCCCCCCCCCCC		30.6222210691
497PhosphorylationQGVSAASSGRIVVAD
CCCCCCCCCCEEEEC		27.6222210691
529PhosphorylationRFGVRGRSPGQLQRP
EEECCCCCCCCCCCC		35.8824719451
537PhosphorylationPGQLQRPTGVAVDTN
CCCCCCCCEEEECCC		46.6128102081
579UbiquitinationAGRLMGPKGVAVDRN
CCCCCCCCEEEECCC		61.36-
615MethylationLVGRFGGRGATDRHF
EEEEECCCCCCCCCC		31.77115918957
639PhosphorylationNKNEIVVTDFHNHSV
CCCCEEEEECCCCEE		23.27-
649PhosphorylationHNHSVKVYSADGEFL
CCCEEEEEECCCCEE		7.7623403867
650PhosphorylationNHSVKVYSADGEFLF
CCEEEEEECCCCEEE		23.9123403867
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 TRIM3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRIM3_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 TRIM3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRIM3_HUMANTRIM3physical
11331580
ACTN4_HUMANACTN4physical
10673389
UB2D4_HUMANUBE2D4physical
21143188
ACTN4_HUMANACTN4physical
15772161
MYO5A_HUMANMYO5Aphysical
15772161
ODPA_HUMANPDHA1physical
26344197
CDN1A_HUMANCDKN1Aphysical
24393003
UB2D1_HUMANUBE2D1physical
24393003
UB2D2_HUMANUBE2D2physical
24393003
UB2E1_HUMANUBE2E1physical
24393003
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 TRIM3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-7, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443, AND MASSSPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-7, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASSSPECTROMETRY.
"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-437, AND MASSSPECTROMETRY.

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