TRI37_HUMAN - dbPTM
TRI37_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI37_HUMAN
UniProt AC O94972
Protein Name E3 ubiquitin-protein ligase TRIM37 {ECO:0000305}
Gene Name TRIM37 {ECO:0000312|HGNC:HGNC:7523}
Organism Homo sapiens (Human).
Sequence Length 964
Subcellular Localization Cytoplasm, perinuclear region . Peroxisome . Found in vesicles of the peroxisome. Aggregates as aggresomes, a perinuclear region where certain misfolded or aggregated proteins are sequestered for proteasomal degradation.
Protein Description E3 ubiquitin-protein ligase required to prevent centriole reduplication. [PubMed: 15885686]
Protein Sequence MDEQSVESIAEVFRCFICMEKLRDARLCPHCSKLCCFSCIRRWLTEQRAQCPHCRAPLQLRELVNCRWAEEVTQQLDTLQLCSLTKHEENEKDKCENHHEKLSVFCWTCKKCICHQCALWGGMHGGHTFKPLAEIYEQHVTKVNEEVAKLRRRLMELISLVQEVERNVEAVRNAKDERVREIRNAVEMMIARLDTQLKNKLITLMGQKTSLTQETELLESLLQEVEHQLRSCSKSELISKSSEILMMFQQVHRKPMASFVTTPVPPDFTSELVPSYDSATFVLENFSTLRQRADPVYSPPLQVSGLCWRLKVYPDGNGVVRGYYLSVFLELSAGLPETSKYEYRVEMVHQSCNDPTKNIIREFASDFEVGECWGYNRFFRLDLLANEGYLNPQNDTVILRFQVRSPTFFQKSRDQHWYITQLEAAQTSYIQQINNLKERLTIELSRTQKSRDLSPPDNHLSPQNDDALETRAKKSACSDMLLEGGPTTASVREAKEDEEDEEKIQNEDYHHELSDGDLDLDLVYEDEVNQLDGSSSSASSTATSNTEENDIDEETMSGENDVEYNNMELEEGELMEDAAAAGPAGSSHGYVGSSSRISRRTHLCSAATSSLLDIDPLILIHLLDLKDRSSIENLWGLQPRPPASLLQPTASYSRKDKDQRKQQAMWRVPSDLKMLKRLKTQMAEVRCMKTDVKNTLSEIKSSSAASGDMQTSLFSADQAALAACGTENSGRLQDLGMELLAKSSVANCYIRNSTNKKSNSPKPARSSVAGSLSLRRAVDPGENSRSKGDCQTLSEGSPGSSQSGSRHSSPRALIHGSIGDILPKTEDRQCKALDSDAVVVAVFSGLPAVEKRRKMVTLGANAKGGHLEGLQMTDLENNSETGELQPVLPEGASAAPEEGMSSDSDIECDTENEEQEEHTSVGGFHDSFMVMTQPPDEDTHSSFPDGEQIGPEDLSFNTDENSGR
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
1Acetylation-------MDEQSVES
-------CCHHHHHH		13.2822814378
32PhosphorylationARLCPHCSKLCCFSC
CCCCCCCHHHHHHHH		26.15-
38PhosphorylationCSKLCCFSCIRRWLT
CHHHHHHHHHHHHHH		8.50-
52UbiquitinationTEQRAQCPHCRAPLQ
HHHHHCCCCCCCCHH		19.9632015554
80UbiquitinationTQQLDTLQLCSLTKH
HHHCHHHHHHHCCCC		42.3833845483
86UbiquitinationLQLCSLTKHEENEKD
HHHHHCCCCCHHCHH		55.0732015554
112UbiquitinationFCWTCKKCICHQCAL
HHHHCCHHHHHHHHH		2.1633845483
166UbiquitinationSLVQEVERNVEAVRN
HHHHHHHHHHHHHHC		58.6427667366
195O-linked_GlycosylationMMIARLDTQLKNKLI
HHHHHHHHHHHHHHH		40.1529351928
195PhosphorylationMMIARLDTQLKNKLI
HHHHHHHHHHHHHHH		40.15-
200UbiquitinationLDTQLKNKLITLMGQ
HHHHHHHHHHHHHCC		39.41-
200UbiquitinationLDTQLKNKLITLMGQ
HHHHHHHHHHHHHCC		39.4133845483
203PhosphorylationQLKNKLITLMGQKTS
HHHHHHHHHHCCCCC		22.56-
234UbiquitinationHQLRSCSKSELISKS
HHHHHCCHHHHHHHH		52.8833845483
257UbiquitinationQVHRKPMASFVTTPV
HHHCCCCCCEECCCC		14.3527667366
258PhosphorylationVHRKPMASFVTTPVP
HHCCCCCCEECCCCC		17.63-
261PhosphorylationKPMASFVTTPVPPDF
CCCCCEECCCCCCCC		24.30-
262PhosphorylationPMASFVTTPVPPDFT
CCCCEECCCCCCCCC		19.58-
289UbiquitinationVLENFSTLRQRADPV
EECCHHHHHHHCCCC		4.2127667366
313PhosphorylationLCWRLKVYPDGNGVV
EEEEEEEECCCCCEE		8.26-
360UbiquitinationNDPTKNIIREFASDF
CCHHHHHHHHHHHCC		4.8927667366
377UbiquitinationGECWGYNRFFRLDLL
CCCCCCCCCHHHHHH		24.48-
377UbiquitinationGECWGYNRFFRLDLL
CCCCCCCCCHHHHHH		24.4827667366
394UbiquitinationEGYLNPQNDTVILRF
CCCCCCCCCEEEEEE		48.4527667366
411UbiquitinationRSPTFFQKSRDQHWY
CCCCCCCCCCCCCEE		42.1527667366
434UbiquitinationTSYIQQINNLKERLT
HHHHHHHHCHHHHHE		43.3633845483
440UbiquitinationINNLKERLTIELSRT
HHCHHHHHEEEECCC		6.24-
444UbiquitinationKERLTIELSRTQKSR
HHHHEEEECCCCCCC		3.5722817900
448UbiquitinationTIELSRTQKSRDLSP
EEEECCCCCCCCCCC		40.3922817900
450PhosphorylationELSRTQKSRDLSPPD
EECCCCCCCCCCCCC		22.6223403867
454PhosphorylationTQKSRDLSPPDNHLS
CCCCCCCCCCCCCCC		38.3823401153
461PhosphorylationSPPDNHLSPQNDDAL
CCCCCCCCCCCHHHH		19.5230266825
470PhosphorylationQNDDALETRAKKSAC
CCHHHHHHHHHHHHH		36.4623403867
474UbiquitinationALETRAKKSACSDML
HHHHHHHHHHHHHHH		42.15-
497UbiquitinationSVREAKEDEEDEEKI
HHHHHHCCHHHHHHH		64.9732015554
525UbiquitinationLDLDLVYEDEVNQLD
CCEEEEEECCCCCCC		39.9733845483
535UbiquitinationVNQLDGSSSSASSTA
CCCCCCCCCCCCCCC		33.5622817900
539UbiquitinationDGSSSSASSTATSNT
CCCCCCCCCCCCCCC		30.1232015554
551UbiquitinationSNTEENDIDEETMSG
CCCCCCCCCCCHHCC		12.3829967540
557UbiquitinationDIDEETMSGENDVEY
CCCCCHHCCCCCCEE		50.8332015554
567UbiquitinationNDVEYNNMELEEGEL
CCCEECCEEECCCCH		5.7522817900
571UbiquitinationYNNMELEEGELMEDA
ECCEEECCCCHHHHH		71.2732015554
571 (in isoform 2)Ubiquitination-71.2721906983
578UbiquitinationEGELMEDAAAAGPAG
CCCHHHHHHHHCCCC		5.9129967540
579UbiquitinationGELMEDAAAAGPAGS
CCHHHHHHHHCCCCC		15.3422817900
588UbiquitinationAGPAGSSHGYVGSSS
HCCCCCCCCCCCCCC		33.0432015554
620UbiquitinationDIDPLILIHLLDLKD
CCCHHHHHHHCCCCC		1.3832015554
627UbiquitinationIHLLDLKDRSSIENL
HHHCCCCCCHHHHHH		64.0929967540
638UbiquitinationIENLWGLQPRPPASL
HHHHHCCCCCCCHHH		28.1922817900
639UbiquitinationENLWGLQPRPPASLL
HHHHCCCCCCCHHHC		56.65-
639UbiquitinationENLWGLQPRPPASLL
HHHHCCCCCCCHHHC		56.6529967540
642UbiquitinationWGLQPRPPASLLQPT
HCCCCCCCHHHCCCC		35.4422817900
645UbiquitinationQPRPPASLLQPTASY
CCCCCHHHCCCCCCC		5.8232015554
655UbiquitinationPTASYSRKDKDQRKQ
CCCCCCCCCHHHHHH		64.2922817900
659UbiquitinationYSRKDKDQRKQQAMW
CCCCCHHHHHHHHHH		61.2821906983
659UbiquitinationYSRKDKDQRKQQAMW
CCCCCHHHHHHHHHH		61.2832015554
661UbiquitinationRKDKDQRKQQAMWRV
CCCHHHHHHHHHHHC		40.9229967540
662UbiquitinationKDKDQRKQQAMWRVP
CCHHHHHHHHHHHCC		38.1533845483
665UbiquitinationDQRKQQAMWRVPSDL
HHHHHHHHHHCCHHH		1.7229967540
666UbiquitinationQRKQQAMWRVPSDLK
HHHHHHHHHCCHHHH		10.9229967540
670PhosphorylationQAMWRVPSDLKMLKR
HHHHHCCHHHHHHHH		53.3624719451
670UbiquitinationQAMWRVPSDLKMLKR
HHHHHCCHHHHHHHH		53.3622817900
672UbiquitinationMWRVPSDLKMLKRLK
HHHCCHHHHHHHHHH		4.0522817900
673UbiquitinationWRVPSDLKMLKRLKT
HHCCHHHHHHHHHHH		47.3729967540
676UbiquitinationPSDLKMLKRLKTQMA
CHHHHHHHHHHHHHH		52.7922817900
679UbiquitinationLKMLKRLKTQMAEVR
HHHHHHHHHHHHHHH		40.5232015554
689UbiquitinationMAEVRCMKTDVKNTL
HHHHHHHHHCHHHHH		45.2422817900
693UbiquitinationRCMKTDVKNTLSEIK
HHHHHCHHHHHHHHH		47.2021906983
693UbiquitinationRCMKTDVKNTLSEIK
HHHHHCHHHHHHHHH		47.2021906983
693 (in isoform 1)Ubiquitination-47.2021906983
700UbiquitinationKNTLSEIKSSSAASG
HHHHHHHHHCCCCCC		39.9929967540
702UbiquitinationTLSEIKSSSAASGDM
HHHHHHHCCCCCCCC		20.9922817900
702 (in isoform 2)Ubiquitination-20.9921906983
708UbiquitinationSSSAASGDMQTSLFS
HCCCCCCCCHHHCCC		24.42-
708UbiquitinationSSSAASGDMQTSLFS
HCCCCCCCCHHHCCC		24.4232015554
725UbiquitinationQAALAACGTENSGRL
HHHHHHCCCCCCCHH		31.1932015554
742UbiquitinationLGMELLAKSSVANCY
HHHHHHHHHHHHCEE		43.1432015554
743PhosphorylationGMELLAKSSVANCYI
HHHHHHHHHHHCEEE		25.1621406692
744PhosphorylationMELLAKSSVANCYIR
HHHHHHHHHHCEEEE		25.2521406692
749PhosphorylationKSSVANCYIRNSTNK
HHHHHCEEEECCCCC		11.6121406692
753UbiquitinationANCYIRNSTNKKSNS
HCEEEECCCCCCCCC		24.41-
753PhosphorylationANCYIRNSTNKKSNS
HCEEEECCCCCCCCC		24.4121406692
753UbiquitinationANCYIRNSTNKKSNS
HCEEEECCCCCCCCC		24.4129967540
754PhosphorylationNCYIRNSTNKKSNSP
CEEEECCCCCCCCCC		55.3921406692
766PhosphorylationNSPKPARSSVAGSLS
CCCCCCCHHHHHHHH		31.13-
767PhosphorylationSPKPARSSVAGSLSL
CCCCCCHHHHHHHHH		15.5028555341
771PhosphorylationARSSVAGSLSLRRAV
CCHHHHHHHHHHCCC		12.6822167270
773PhosphorylationSSVAGSLSLRRAVDP
HHHHHHHHHHCCCCC		22.8722167270
773UbiquitinationSSVAGSLSLRRAVDP
HHHHHHHHHHCCCCC		22.8722817900
784PhosphorylationAVDPGENSRSKGDCQ
CCCCCCCCCCCCCCC		33.36-
787UbiquitinationPGENSRSKGDCQTLS
CCCCCCCCCCCCCCC		58.6229967540
790UbiquitinationNSRSKGDCQTLSEGS
CCCCCCCCCCCCCCC		4.5421906983
790UbiquitinationNSRSKGDCQTLSEGS
CCCCCCCCCCCCCCC		4.5422817900
794PhosphorylationKGDCQTLSEGSPGSS
CCCCCCCCCCCCCCC		43.2128985074
797PhosphorylationCQTLSEGSPGSSQSG
CCCCCCCCCCCCCCC		23.2630576142
800PhosphorylationLSEGSPGSSQSGSRH
CCCCCCCCCCCCCCC		28.7028985074
801PhosphorylationSEGSPGSSQSGSRHS
CCCCCCCCCCCCCCC		33.9924719451
803PhosphorylationGSPGSSQSGSRHSSP
CCCCCCCCCCCCCCC		40.4628348404
805PhosphorylationPGSSQSGSRHSSPRA
CCCCCCCCCCCCCCH		31.8725849741
807UbiquitinationSSQSGSRHSSPRALI
CCCCCCCCCCCCHHH		34.0322817900
817PhosphorylationPRALIHGSIGDILPK
CCHHHCCCHHHHCCC		14.8324247654
820UbiquitinationLIHGSIGDILPKTED
HHCCCHHHHCCCCCC		37.27-
824UbiquitinationSIGDILPKTEDRQCK
CHHHHCCCCCCHHCC		62.1921906983
824UbiquitinationSIGDILPKTEDRQCK
CHHHHCCCCCCHHCC		62.1922817900
824 (in isoform 1)Ubiquitination-62.1921906983
825PhosphorylationIGDILPKTEDRQCKA
HHHHCCCCCCHHCCC		40.9728555341
844PhosphorylationAVVVAVFSGLPAVEK
CEEEEEECCCCHHHH		32.59-
854UbiquitinationPAVEKRRKMVTLGAN
CHHHHHHCCEEECCC		41.58-
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 ligaseTRIM37O94972
PMID:15885686
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI37_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 TRI37_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
F124B_HUMANFAM124Bphysical
16189514
MAGBI_HUMANMAGEB18physical
16189514
ELOA2_HUMANTCEB3Bphysical
16189514
APEX2_HUMANAPEX2physical
16189514
FXR2_HUMANFXR2physical
16189514
F107A_HUMANFAM107Aphysical
16189514
RIBC2_HUMANRIBC2physical
16189514
RHPN1_HUMANRHPN1physical
16189514
ZN655_HUMANZNF655physical
16189514
DLGP5_HUMANDLGAP5physical
16189514
PNKP_HUMANPNKPphysical
16189514
PRC1_HUMANPRC1physical
16189514
K0408_HUMANKIAA0408physical
16189514
ZN417_HUMANZNF417physical
16189514
MCM10_HUMANMCM10physical
16189514
MCRS1_HUMANMCRS1physical
16189514
NUD18_HUMANNUDT18physical
16189514
TOPK_HUMANPBKphysical
16189514
TRAF1_HUMANTRAF1physical
11279055
TRAF2_HUMANTRAF2physical
11279055
TRAF3_HUMANTRAF3physical
11279055
TRAF4_HUMANTRAF4physical
11279055
TRAF5_HUMANTRAF5physical
11279055
TRAF6_HUMANTRAF6physical
11279055
TRI37_HUMANTRIM37physical
11279055
UB2D1_HUMANUBE2D1physical
21143188
UB2D2_HUMANUBE2D2physical
21143188
UB2D3_HUMANUBE2D3physical
21143188
UB2E1_HUMANUBE2E1physical
21143188
UB2E2_HUMANUBE2E2physical
21143188
UB2E3_HUMANUBE2E3physical
21143188
RL9_HUMANRPL9physical
25416956
MCRS1_HUMANMCRS1physical
25416956
KAT5_HUMANKAT5physical
25416956
F107A_HUMANFAM107Aphysical
25416956
FA50B_HUMANFAM50Bphysical
25416956
RASD1_HUMANRASD1physical
25416956
UBS3A_HUMANUBASH3Aphysical
25416956
KIF9_HUMANKIF9physical
25416956
SCNM1_HUMANSCNM1physical
25416956
ZN329_HUMANZNF329physical
25416956
F161A_HUMANFAM161Aphysical
25416956
ADIP_HUMANSSX2IPphysical
25416956
C19L2_HUMANCWF19L2physical
25416956
ZN417_HUMANZNF417physical
25416956
ZMAT2_HUMANZMAT2physical
25416956
CD20B_HUMANCDC20Bphysical
25416956
H2A2C_HUMANHIST2H2ACphysical
25470042
EZH2_HUMANEZH2physical
25470042
SUZ12_HUMANSUZ12physical
25470042
BMI1_HUMANBMI1physical
25470042
H31T_HUMANHIST3H3physical
25470042
CTNB1_HUMANCTNNB1physical
26395261
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
253250Mulibrey nanism (MUL)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRI37_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-771 AND SER-773, ANDMASS SPECTROMETRY.

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