TRIM5_HUMAN - dbPTM
TRIM5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRIM5_HUMAN
UniProt AC Q9C035
Protein Name Tripartite motif-containing protein 5
Gene Name TRIM5
Organism Homo sapiens (Human).
Sequence Length 493
Subcellular Localization Cytoplasm . Nucleus . Predominantly localizes in cytoplasmic bodies (PubMed:12878161, PubMed:20357094). 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 N-tropic murine leukemia virus (N-MLV), equine infectious anemia virus (EIAV), simian immunodeficiency virus of macaques (SIVmac), feline immunodeficiency virus (FIV), and bovine immunodeficiency virus (BIV). [PubMed: 17156811 Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2]
Protein Sequence MASGILVNVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDKGESSCPVCRISYQPENIRPNRHVANIVEKLREVKLSPEGQKVDHCARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLTEEVAREYQVKLQAALEMLRQKQQEAEELEADIREEKASWKTQIQYDKTNVLADFEQLRDILDWEESNELQNLEKEEEDILKSLTNSETEMVQQTQSLRELISDLEHRLQGSVMELLQGVDGVIKRTENVTLKKPETFPKNQRRVFRAPDLKGMLEVFRELTDVRRYWVDVTVAPNNISCAVISEDKRQVSSPKPQIIYGARGTRYQTFVNFNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVCAGFQPDAMCNIEKNENYQPKYGYWVIGLEEGVKCSAFQDSSFHTPSVPFIVPLSVIICPDRVGVFLDYEACTVSFFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCGVPMTLCSPSS
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------MASGILVNV
------CCCCEEEEC		19.2322223895
3Phosphorylation-----MASGILVNVK
-----CCCCEEEECC		25.6827251275
10SumoylationSGILVNVKEEVTCPI
CCEEEECCCCCCCCH		42.84-
10SumoylationSGILVNVKEEVTCPI
CCEEEECCCCCCCCH		42.84-
45UbiquitinationCLTANHKKSMLDKGE
HHHHCHHHHHHHCCC		33.28-
46PhosphorylationLTANHKKSMLDKGES
HHHCHHHHHHHCCCC		29.4028857561
50UbiquitinationHKKSMLDKGESSCPV
HHHHHHHCCCCCCCC		61.69-
79UbiquitinationHVANIVEKLREVKLS
HHHHHHHHHHCCCCC		41.7823000965
84UbiquitinationVEKLREVKLSPEGQK
HHHHHCCCCCCCCCC		38.1923000965
86PhosphorylationKLREVKLSPEGQKVD
HHHCCCCCCCCCCCC		18.3923401153
91UbiquitinationKLSPEGQKVDHCARH
CCCCCCCCCCHHHHC		61.5629967540
152UbiquitinationALEMLRQKQQEAEEL
HHHHHHHHHHHHHHH		47.7329967540
167UbiquitinationEADIREEKASWKTQI
HHHHHHHHHHHHHHE		42.8623503661
169PhosphorylationDIREEKASWKTQIQY
HHHHHHHHHHHHEEE		39.9224719451
171UbiquitinationREEKASWKTQIQYDK
HHHHHHHHHHEEECC		28.2323503661
171 (in isoform 2)Ubiquitination-28.23-
172PhosphorylationEEKASWKTQIQYDKT
HHHHHHHHHEEECCC		25.3329978859
176PhosphorylationSWKTQIQYDKTNVLA
HHHHHEEECCCCEEC		22.4929978859
178 (in isoform 2)Ubiquitination-36.7421890473
178 (in isoform 1)Ubiquitination-36.7421890473
178 (in isoform 3)Ubiquitination-36.7421906983
178 (in isoform 4)Ubiquitination-36.7421906983
178 (in isoform 5)Ubiquitination-36.7421906983
178UbiquitinationKTQIQYDKTNVLADF
HHHEEECCCCEECCH		36.7421906983
197PhosphorylationDILDWEESNELQNLE
HHHCHHHHHHHHHHH		24.8824275569
205UbiquitinationNELQNLEKEEEDILK
HHHHHHHHHHHHHHH		73.8529967540
212 (in isoform 5)Ubiquitination-43.6921906983
212 (in isoform 1)Ubiquitination-43.6921890473
212 (in isoform 2)Ubiquitination-43.6921890473
212 (in isoform 3)Ubiquitination-43.6921906983
212 (in isoform 4)Ubiquitination-43.6921906983
212UbiquitinationKEEEDILKSLTNSET
HHHHHHHHHHCCCHH		43.6921906983
255 (in isoform 1)Ubiquitination-51.3521890473
255UbiquitinationQGVDGVIKRTENVTL
HCCCCEEEECCCCCC		51.3521906983
255 (in isoform 4)Ubiquitination-51.3521906983
255 (in isoform 3)Ubiquitination-51.3521906983
255 (in isoform 2)Ubiquitination-51.3521890473
263UbiquitinationRTENVTLKKPETFPK
ECCCCCCCCCCCCCC		57.8429967540
264UbiquitinationTENVTLKKPETFPKN
CCCCCCCCCCCCCCC		51.7227667366
270UbiquitinationKKPETFPKNQRRVFR
CCCCCCCCCCCCEEC		62.6129967540
282UbiquitinationVFRAPDLKGMLEVFR
EECCCCHHHHHHHHH		50.0523000965
282 (in isoform 2)Ubiquitination-50.0521890473
282 (in isoform 3)Ubiquitination-50.0521906983
282 (in isoform 1)Ubiquitination-50.0521890473
282 (in isoform 4)Ubiquitination-50.0521906983
322PhosphorylationEDKRQVSSPKPQIIY
CCCCCCCCCCCEEEE		37.7828555341
324UbiquitinationKRQVSSPKPQIIYGA
CCCCCCCCCEEEEEC		52.0522817900
324 (in isoform 1)Ubiquitination-52.0521890473
324 (in isoform 2)Ubiquitination-52.0521890473
329PhosphorylationSPKPQIIYGARGTRY
CCCCEEEEECCCCCE		13.32-
367UbiquitinationYWEVDVSKKTAWILG
EEEEECCHHHHEEEH		54.7329967540
416PhosphorylationKCSAFQDSSFHTPSV
CCCCCCCCCCCCCCC		24.91-
465PhosphorylationGFLIYKFSHCSFSQP
EEEEEEEECCCCCCC		21.3126074081
468PhosphorylationIYKFSHCSFSQPVFP
EEEEECCCCCCCCCC		23.6226074081
470PhosphorylationKFSHCSFSQPVFPYL
EEECCCCCCCCCCCC		19.7926074081
476PhosphorylationFSQPVFPYLNPRKCG
CCCCCCCCCCCCCCC		13.9826074081
481UbiquitinationFPYLNPRKCGVPMTL
CCCCCCCCCCCCCEE		36.2822505724
490PhosphorylationGVPMTLCSPSS----
CCCCEEECCCC----		30.8121712546
492PhosphorylationPMTLCSPSS------
CCEEECCCC------		32.17-
493PhosphorylationMTLCSPSS-------
CEEECCCC-------		47.8521712546
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
-KUbiquitinationE3 ubiquitin ligaseTRIM21P19474
PMID:18312418
-KUbiquitinationE3 ubiquitin ligaseTRIM5Q9C035
PMID:18312418
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRIM5_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 TRIM5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRIM5_HUMANTRIM5physical
11331580
TRIM5_HUMANTRIM5physical
18312418
TRIM5_HUMANTRIM5physical
21734049
UBB_HUMANUBBphysical
22078707
PRS7_HUMANPSMC2physical
22078707
PSMD7_HUMANPSMD7physical
22078707
PRS6B_HUMANPSMC4physical
22078707
PRS8_HUMANPSMC5physical
22078707
M3K11_HUMANMAP3K11physical
22078707
TRIM5_HUMANTRIM5physical
18799573
TRIM5_HUMANTRIM5physical
16828831
TRIM5_HUMANTRIM5physical
18799578
TRIM5_HUMANTRIM5physical
17156811
GAG_HV1H2gagphysical
16809279
TRIM5_HUMANTRIM5physical
16254380
GAG_HV1H2gagphysical
17543365
TRIM5_HUMANTRIM5physical
17543365
TRIM5_HUMANTRIM5physical
16808955
GAG_HV1H2gagphysical
16808955
SQSTM_HUMANSQSTM1physical
20357094
NEMO_HUMANIKBKGphysical
21512573
M3K1_HUMANMAP3K1physical
21512573
M3K7_HUMANMAP3K7physical
21512573
TAB2_HUMANTAB2physical
21512573
TAB3_HUMANTAB3physical
21512573
UBC_HUMANUBCphysical
21512573
UB2D2_HUMANUBE2D2physical
18312418
TRIM5_HUMANTRIM5physical
22493164
TRI32_HUMANTRIM32physical
22493164
MKRN3_HUMANMKRN3physical
22493164
TRIM5_HUMANTRIM5physical
12878161
UB2D2_HUMANUBE2D2physical
12878161
UB2D3_HUMANUBE2D3physical
18799573
VIE1_HCMVMUL123physical
25412268
TRIM5_HUMANTRIM5physical
26212332
UBE2N_HUMANUBE2Nphysical
26212332
UB2D3_HUMANUBE2D3physical
26212332
SUMO1_HUMANSUMO1physical
25880753
CUED1_HUMANCUEDC1physical
28514442
SYYC_HUMANYARSphysical
28514442
CREB1_HUMANCREB1physical
28514442
LEG3_HUMANLGALS3physical
27693506
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 TRIM5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND MASSSPECTROMETRY.

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