TRIM5_MACMU - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRIM5_MACMU
• UniProt AC: Q0PF16
• Protein Name: Tripartite motif-containing protein 5
• Gene Name: TRIM5
• Organism: Macaca mulatta (Rhesus macaque).
• Sequence Length: 497
• Subcellular Localization: Cytoplasm . Nucleus . Predominantly localizes in cytoplasmic bodies (PubMed:20357094, PubMed:22078707). Localization may be influenced by the coexpression of other TRIM proteins, hence partial nuclear localization is observed in the presence of TRIM2
• Protein Description: Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Restricts infection by human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV-agm). Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. [PubMed: 25127057 Also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction]
• Protein Sequence: MASGILLNVKEEVTCPICLELLTEPLSLHCGHSFCQACITANHKKSMLYKEGERSCPVCRISYQPENIQPNRHVANIVEKLREVKLSPEEGQKVDHCARHGEKLLLFCQEDSKVICWLCERSQEHRGHHTFLMEEVAQEYHVKLQTALEMLRQKQQEAEKLEADIREEKASWKIQIDYDKTNVSADFEQLREILDWEESNELQNLEKEEEDILKSLTKSETEMVQQTQYMRELISELEHRLQGSMMDLLQGVDGIIKRIENMTLKKPKTFHKNQRRVFRAPDLKGMLDMFRELTDARRYWVDVTLAPNNISHAVIAEDKRQVSSRNPQIMYQAPGTLFTFPSLTNFNYCTGVLGSQSITSGKHYWEVDVSKKSAWILGVCAGFQSDAMYNIEQNENYQPKYGYWVIGLQEGVKYSVFQDGSSHTPFAPFIVPLSVIICPDRVGVFVDYEACTVSFFNITNHGFLIYKFSQCSFSKPVFPYLNPRKCTVPMTLCSPSS

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
2	Acetylation	------MASGILLNV ------CCCCEEECC	19.23	-
87	Phosphorylation	KLREVKLSPEEGQKV HHHHCCCCHHHCCCC	25.25	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TRIM5_MACMU !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRIM5_MACMU !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TRIM5_MACMU !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRIM6_HUMAN	TRIM6	physical	21680743
TRI34_HUMAN	TRIM34	physical	21680743
TRIM5_MACMU	TRIM5	physical	21680743
HSP74_HUMAN	HSPA4	physical	20053985
FLOT1_HUMAN	FLOT1	physical	20810659
HSP74_HUMAN	HSPA4	physical	20810659
TBA1A_HUMAN	TUBA1A	physical	20810659
TRIM5_MACMU	TRIM5	physical	16808955
SQSTM_HUMAN	SQSTM1	physical	20357094
TRIM5_MACMU	TRIM5	physical	19656869
GAG_HV1H2	gag	physical	19656869
TRIM5_MACMU	TRIM5	physical	23637418
HSP7C_HUMAN	HSPA8	physical	20053985
SOCS1_HUMAN	SOCS1	physical	25310711

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.