TRI39_HUMAN - dbPTM
TRI39_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI39_HUMAN
UniProt AC Q9HCM9
Protein Name E3 ubiquitin-protein ligase TRIM39
Gene Name TRIM39
Organism Homo sapiens (Human).
Sequence Length 518
Subcellular Localization Cytoplasm, cytosol . Mitochondrion . Found predominantly in the cytosol. Partial shift from the cytosol to the mitochondria when colocalized with MOAP1.
Protein Description E3 ubiquitin-protein ligase. May facilitate apoptosis by inhibiting APC/C-Cdh1-mediated poly-ubiquitination and subsequent proteasome-mediated degradation of the pro-apoptotic protein MOAP1..
Protein Sequence MAETSLLEAGASAASTAAALENLQVEASCSVCLEYLKEPVIIECGHNFCKACITRWWEDLERDFPCPVCRKTSRYRSLRPNRQLGSMVEIAKQLQAVKRKIRDESLCPQHHEALSLFCYEDQEAVCLICAISHTHRAHTVVPLDDATQEYKEKLQKCLEPLEQKLQEITRCKSSEEKKPGELKRLVESRRQQILREFEELHRRLDEEQQVLLSRLEEEEQDILQRLRENAAHLGDKRRDLAHLAAEVEGKCLQSGFEMLKDVKSTLEKNIPRKFGGSLSTICPRDHKALLGLVKEINRCEKVKTMEVTSVSIELEKNFSNFPRQYFALRKILKQLIADVTLDPETAHPNLVLSEDRKSVKFVETRLRDLPDTPRRFTFYPCVLATEGFTSGRHYWEVEVGDKTHWAVGVCRDSVSRKGELTPLPETGYWRVRLWNGDKYAATTTPFTPLHIKVKPKRVGIFLDYEAGTLSFYNVTDRSHIYTFTDTFTEKLWPLFYPGIRAGRKNAAPLTIRPPTDWE
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
92UbiquitinationGSMVEIAKQLQAVKR
HHHHHHHHHHHHHHH		58.1421890473
92 (in isoform 1)Ubiquitination-58.1421890473
92UbiquitinationGSMVEIAKQLQAVKR
HHHHHHHHHHHHHHH		58.1421890473
92 (in isoform 2)Ubiquitination-58.1421890473
92UbiquitinationGSMVEIAKQLQAVKR
HHHHHHHHHHHHHHH		58.1421890473
98AcetylationAKQLQAVKRKIRDES
HHHHHHHHHHHCCCC		51.497492131
147PhosphorylationVVPLDDATQEYKEKL
EEECCHHHHHHHHHH		29.0021214269
150PhosphorylationLDDATQEYKEKLQKC
CCHHHHHHHHHHHHH		18.0321214269
156UbiquitinationEYKEKLQKCLEPLEQ
HHHHHHHHHHHHHHH		51.75-
277PhosphorylationIPRKFGGSLSTICPR
CCHHHCCCHHHCCCC		21.37-
279PhosphorylationRKFGGSLSTICPRDH
HHHCCCHHHCCCCCH		19.88-
280PhosphorylationKFGGSLSTICPRDHK
HHCCCHHHCCCCCHH		31.71-
304PhosphorylationNRCEKVKTMEVTSVS
HCCCCCEEEEEEEEE		22.8828060719
308PhosphorylationKVKTMEVTSVSIELE
CCEEEEEEEEEEEEH		15.3128060719
309PhosphorylationVKTMEVTSVSIELEK
CEEEEEEEEEEEEHH		21.0228060719
311PhosphorylationTMEVTSVSIELEKNF
EEEEEEEEEEEHHHC		15.3121815630
385PhosphorylationFYPCVLATEGFTSGR
CCEEEEECCCCCCCC		32.26-
422 (in isoform 2)Ubiquitination-59.5521890473
422UbiquitinationSRKGELTPLPETGYW
CCCCCEECCCCCCEE		59.5521890473
439PhosphorylationRLWNGDKYAATTTPF
EEECCCCCEEECCCC		13.2516094384
452 (in isoform 1)Ubiquitination-33.2021890473
452UbiquitinationPFTPLHIKVKPKRVG
CCCCEEEEECCCEEE		33.2021890473
452UbiquitinationPFTPLHIKVKPKRVG
CCCCEEEEECCCEEE		33.2021890473
468PhosphorylationFLDYEAGTLSFYNVT
EEEEECCEEEEEECC		26.6922461510
472PhosphorylationEAGTLSFYNVTDRSH
ECCEEEEEECCCCCC		12.8322461510
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 TRI39_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI39_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 TRI39_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI39_HUMANTRIM39physical
16189514
UBTD1_HUMANUBTD1physical
16189514
PLCD4_HUMANPLCD4physical
16189514
MOAP1_HUMANMOAP1physical
19100260
TRI39_HUMANTRIM39physical
22529100
UB2D1_HUMANUBE2D1physical
22529100
UBE2N_HUMANUBE2Nphysical
22493164
UB2D1_HUMANUBE2D1physical
22493164
UB2D2_HUMANUBE2D2physical
22493164
UB2E1_HUMANUBE2E1physical
22493164
UBC_HUMANUBCphysical
22493164
A4_HUMANAPPphysical
21832049
CBX5_HUMANCBX5physical
23077635
CBX1_HUMANCBX1physical
23077635
CBX3_HUMANCBX3physical
23077635
P53_HUMANTP53physical
23213260
CDN1A_HUMANCDKN1Aphysical
23213251
TRI39_HUMANTRIM39physical
22493164
KDM1A_HUMANKDM1Aphysical
23455924
TRI39_HUMANTRIM39physical
25416956
LXN_HUMANLXNphysical
25416956
UBTD1_HUMANUBTD1physical
25416956
UBXN6_HUMANUBXN6physical
25416956
LNX1_HUMANLNX1physical
25416956
UBTD2_HUMANUBTD2physical
25416956
TTC32_HUMANTTC32physical
25416956
ZKSC4_HUMANZKSCAN4physical
25416956
SMCO3_HUMANSMCO3physical
25416956
TRI39_HUMANTRIM39physical
21516116
PSMD9_HUMANPSMD9physical
21516116
UB2D1_HUMANUBE2D1physical
21516116
UB2E2_HUMANUBE2E2physical
21516116
PRPF3_HUMANPRPF3physical
21516116
CATIN_HUMANCACTINphysical
26363554
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 TRI39_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, AND MASSSPECTROMETRY.

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