Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Tripartite motif-containing protein 3  

UniProtKB / Swiss-Prot ID :  TRIM3_HUMAN

Gene Name (Synonyms) : 
TRIM3, BERP, RNF22, RNF97  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm (By similarity). Early endosome. 

Protein Function :  Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. 

Protein Sequence MAKREDSPGPEVQPMDKQFLVCSICLDRYQCPKVLPCLHTFCERCLQNYIPAQSLTLSCPVCRQTSILPE...
Predicted Secondary Structure CCCCCCCCCHHHHHHCHHCEEEEECCCCCCCCEECCCCCHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
298L -> R (in dbSNP:rs10128723). VAR_052124
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAKRED
---CCCCCC
21.44UniProtKB
Link-
7PhosphoserineKREDSPGPE
CCCCCCCHH
27.31HPRD
Link-
7PhosphoserineKREDSPGPE
CCCCCCCHH
27.31PhosphoELM
Link-
7PhosphoserineKREDSPGPE
CCCCCCCHH
27.31Phosphositeplus
Link-
7PhosphoserineKREDSPGPE
CCCCCCCHH
27.31SysPTM
Link-
7Phosphoserine.KREDSPGPE
CCCCCCCHH
27.31UniProtKB
Link-
23PhosphoserineFLVCSICLD
CEEEEECCC
14.62Phosphositeplus
Link-
437PhosphoserineRRVKSPGGP
CEEEECCCC
26.39HPRD
Link-
437PhosphoserineRRVKSPGGP
CEEEECCCC
26.39PhosphoELM
Link-
437PhosphoserineRRVKSPGGP
CEEEECCCC
26.39Phosphositeplus
Link-
437PhosphoserineRRVKSPGGP
CEEEECCCC
26.39SysPTM
Link-
437Phosphoserine.RRVKSPGGP
CEEEECCCC
26.39UniProtKB
Link-
443PhosphoserineGGPGSHVRQ
CCCCCCCCC
23.18Phosphositeplus
Link-
443Phosphoserine.GGPGSHVRQ
CCCCCCCCC
23.18UniProtKB
Link-
454PhosphoserineVRRPSSMYS
CEEEEEEEE
26.40Phosphositeplus
Link-
455PhosphoserineRRPSSMYST
EEEEEEEEE
25.15Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
MYO5A_HUMANin vivo
yeast 2-hybrid
HPRD:05690HPRD10391919
UBC1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:05690HPRD11513855
ACTN4_HUMANin vivo
yeast 2-hybrid
HPRD:05690HPRD10673389
TRIM3_HUMANyeast 2-hybridHPRD:05690HPRD11331580
ACTN4_HUMANENSP00000340797STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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.
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures