TRI41_HUMAN - dbPTM
TRI41_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI41_HUMAN
UniProt AC Q8WV44
Protein Name E3 ubiquitin-protein ligase TRIM41
Gene Name TRIM41
Organism Homo sapiens (Human).
Sequence Length 630
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C..
Protein Sequence MAAVAMTPNPVQTLQEEAVCAICLDYFTDPVSIGCGHNFCRVCVTQLWGGEDEEDRDELDREEEEEDGEEEEVEAVGAGAGWDTPMRDEDYEGDMEEEVEEEEEGVFWTSGMSRSSWDNMDYVWEEEDEEEDLDYYLGDMEEEDLRGEDEEDEEEVLEEVEEEDLDPVTPLPPPPAPRRCFTCPQCRKSFPRRSFRPNLQLANMVQVIRQMHPTPGRGSRVTDQGICPKHQEALKLFCEVDEEAICVVCRESRSHKQHSVVPLEEVVQEYKAKLQGHVEPLRKHLEAVQKMKAKEERRVTELKSQMKSELAAVASEFGRLTRFLAEEQAGLERRLREMHEAQLGRAGAAASRLAEQAAQLSRLLAEAQERSQQGGLRLLQDIKETFNRCEEVQLQPPEVWSPDPCQPHSHDFLTDAIVRKMSRMFCQAARVDLTLDPDTAHPALMLSPDRRGVRLAERRQEVADHPKRFSADCCVLGAQGFRSGRHYWEVEVGGRRGWAVGAARESTHHKEKVGPGGSSVGSGDASSSRHHHRRRRLHLPQQPLLQREVWCVGTNGKRYQAQSSTEQTLLSPSEKPRRFGVYLDYEAGRLGFYNAETLAHVHTFSAAFLGERVFPFFRVLSKGTRIKLCP
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
84PhosphorylationGAGAGWDTPMRDEDY
CCCCCCCCCCCCCCC		16.6924275569
115PhosphorylationWTSGMSRSSWDNMDY
ECCCCCCCHHCCCCC		28.5924275569
116PhosphorylationTSGMSRSSWDNMDYV
CCCCCCCHHCCCCCC		37.0224275569
155 (in isoform 3)Ubiquitination-50.8121906983
194PhosphorylationRKSFPRRSFRPNLQL
HHHCCCCCCCCCHHH		27.2128555341
214PhosphorylationVIRQMHPTPGRGSRV
HHHHHCCCCCCCCCC		24.5622210691
219PhosphorylationHPTPGRGSRVTDQGI
CCCCCCCCCCCCCCC		23.40-
229UbiquitinationTDQGICPKHQEALKL
CCCCCCCCHHHHHHH		54.21-
235UbiquitinationPKHQEALKLFCEVDE
CCHHHHHHHHEECCC		46.71-
256SumoylationCRESRSHKQHSVVPL
EECCCCCCCCCEECH		51.4525218447
256UbiquitinationCRESRSHKQHSVVPL
EECCCCCCCCCEECH		51.4529967540
256SumoylationCRESRSHKQHSVVPL
EECCCCCCCCCEECH		51.45-
271UbiquitinationEEVVQEYKAKLQGHV
HHHHHHHHHHHCCCC		37.99-
273SumoylationVVQEYKAKLQGHVEP
HHHHHHHHHCCCCHH		36.87-
273UbiquitinationVVQEYKAKLQGHVEP
HHHHHHHHHCCCCHH		36.8729967540
273SumoylationVVQEYKAKLQGHVEP
HHHHHHHHHCCCCHH		36.87-
283UbiquitinationGHVEPLRKHLEAVQK
CCCHHHHHHHHHHHH		61.2929967540
290UbiquitinationKHLEAVQKMKAKEER
HHHHHHHHHHHHHHH		35.4529967540
303SuccinylationERRVTELKSQMKSEL
HHHHHHHHHHHHHHH		32.2023954790
303UbiquitinationERRVTELKSQMKSEL
HHHHHHHHHHHHHHH		32.2022817900
307 (in isoform 4)Ubiquitination-32.8921906983
307 (in isoform 2)Ubiquitination-32.8921906983
307 (in isoform 1)Ubiquitination-32.8921906983
307UbiquitinationTELKSQMKSELAAVA
HHHHHHHHHHHHHHH		32.8922817900
308PhosphorylationELKSQMKSELAAVAS
HHHHHHHHHHHHHHH		32.2822210691
315PhosphorylationSELAAVASEFGRLTR
HHHHHHHHHHHHHHH		27.1922210691
321PhosphorylationASEFGRLTRFLAEEQ
HHHHHHHHHHHHHHH		20.2922210691
383UbiquitinationLRLLQDIKETFNRCE
HHHHHHHHHHHHCCC		60.0221906983
383 (in isoform 2)Ubiquitination-60.0221906983
383 (in isoform 1)Ubiquitination-60.0221906983
401PhosphorylationLQPPEVWSPDPCQPH
CCCCCCCCCCCCCCC		25.3025159151
434PhosphorylationQAARVDLTLDPDTAH
HHHCCCCEECCCCCC		25.3428450419
439PhosphorylationDLTLDPDTAHPALML
CCEECCCCCCCHHHC		32.0522617229
447PhosphorylationAHPALMLSPDRRGVR
CCCHHHCCCCHHCCH		15.7022617229
512UbiquitinationESTHHKEKVGPGGSS
CCCCCCCCCCCCCCC		58.2422505724
518PhosphorylationEKVGPGGSSVGSGDA
CCCCCCCCCCCCCCC		27.97-
519PhosphorylationKVGPGGSSVGSGDAS
CCCCCCCCCCCCCCC		33.50-
522PhosphorylationPGGSSVGSGDASSSR
CCCCCCCCCCCCCCC		31.2021815630
526PhosphorylationSVGSGDASSSRHHHR
CCCCCCCCCCCCHHH		33.3221815630
528PhosphorylationGSGDASSSRHHHRRR
CCCCCCCCCCHHHCH		32.8921815630
557SumoylationWCVGTNGKRYQAQSS
EEEECCCCEEEECCC		50.42-
557SumoylationWCVGTNGKRYQAQSS
EEEECCCCEEEECCC		50.42-
557UbiquitinationWCVGTNGKRYQAQSS
EEEECCCCEEEECCC		50.42-
563PhosphorylationGKRYQAQSSTEQTLL
CCEEEECCCCCCCCC		42.0930108239
564PhosphorylationKRYQAQSSTEQTLLS
CEEEECCCCCCCCCC		24.7130108239
565PhosphorylationRYQAQSSTEQTLLSP
EEEECCCCCCCCCCC		37.0430108239
568PhosphorylationAQSSTEQTLLSPSEK
ECCCCCCCCCCCCCC		24.3530108239
571PhosphorylationSTEQTLLSPSEKPRR
CCCCCCCCCCCCCCE		29.5025849741
573PhosphorylationEQTLLSPSEKPRRFG
CCCCCCCCCCCCEEE		55.6830108239
575UbiquitinationTLLSPSEKPRRFGVY
CCCCCCCCCCEEEEE		48.4322817900
575 (in isoform 1)Ubiquitination-48.4321906983
582PhosphorylationKPRRFGVYLDYEAGR
CCCEEEEEEEECCCC		8.3420860994
585PhosphorylationRFGVYLDYEAGRLGF
EEEEEEEECCCCEEE		12.7020860994
621PhosphorylationFPFFRVLSKGTRIKL
HHHHHHCCCCCCEEE		26.6130622161
624PhosphorylationFRVLSKGTRIKLCP-
HHHCCCCCCEEECC-		32.7230622161
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 TRI41_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI41_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 TRI41_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZBT8A_HUMANZBTB8Aphysical
16189514
KPCA_HUMANPRKCAphysical
17893151
KPCB_HUMANPRKCBphysical
17893151
KPCZ_HUMANPRKCZphysical
17893151
KPCD_HUMANPRKCDphysical
17893151
TRI41_HUMANTRIM41physical
17893151
UB2D2_HUMANUBE2D2physical
17893151
A4_HUMANAPPphysical
21832049
TRI52_HUMANTRIM52physical
22493164
TRIM4_HUMANTRIM4physical
22493164
TRI41_HUMANTRIM41physical
22493164
TRI41_HUMANTRIM41physical
25416956
ZN670_HUMANZNF670physical
25416956
F10C1_HUMANFRA10AC1physical
25416956
ZN417_HUMANZNF417physical
25416956
ZN564_HUMANZNF564physical
25416956
F124A_HUMANFAM124Aphysical
25416956
ZBT38_HUMANZBTB38physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
GLCI1_HUMANGLCCI1physical
28514442
APBA2_HUMANAPBA2physical
28514442
ANKH1_HUMANANKHD1physical
28514442
PASK_HUMANPASKphysical
28514442
TRBP2_HUMANTARBP2physical
28514442
DICER_HUMANDICER1physical
28514442
ANR17_HUMANANKRD17physical
28514442
K0232_HUMANKIAA0232physical
28514442
GGPPS_HUMANGGPS1physical
28514442
DCA16_HUMANDCAF16physical
28514442
RRF2M_HUMANGFM2physical
28514442
ERBIN_HUMANERBB2IPphysical
28514442
PSMG4_HUMANPSMG4physical
28514442
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 TRI41_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447, AND MASSSPECTROMETRY.

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