TRI36_HUMAN - dbPTM
TRI36_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI36_HUMAN
UniProt AC Q9NQ86
Protein Name E3 ubiquitin-protein ligase TRIM36
Gene Name TRIM36
Organism Homo sapiens (Human).
Sequence Length 728
Subcellular Localization Cytoplasm . Cytoplasmic vesicle, secretory vesicle, acrosome . Cytoplasm, cytoskeleton . Found in the acrosomal region of elongated spermatids and mature sperm.
Protein Description E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins. Involved in chromosome segregation and cell cycle regulation. [PubMed: 28087737 May play a role in the acrosome reaction and fertilization.]
Protein Sequence MSESGEMSEFGYIMELIAKGKVTIKNIERELICPACKELFTHPLILPCQHSICHKCVKELLLTLDDSFNDVGSDNSNQSSPRLRLPSPSMDKIDRINRPGWKRNSLTPRTTVFPCPGCEHDVDLGERGINGLFRNFTLETIVERYRQAARAATAIMCDLCKPPPQESTKSCMDCSASYCNECFKIHHPWGTIKAQHEYVGPTTNFRPKILMCPEHETERINMYCELCRRPVCHLCKLGGNHANHRVTTMSSAYKTLKEKLSKDIDYLIGKESQVKSQISELNLLMKETECNGERAKEEAITHFEKLFEVLEERKSSVLKAIDSSKKLRLDKFQTQMEEYQGLLENNGLVGYAQEVLKETDQSCFVQTAKQLHLRIQKATESLKSFRPAAQTSFEDYVVNTSKQTELLGELSFFSSGIDVPEINEEQSKVYNNALINWHHPEKDKADSYVLEYRKINRDDEMSWNEIEVCGTSKIIQDLENSSTYAFRVRAYKGSICSPCSRELILHTPPAPVFSFLFDEKCGYNNEHLLLNLKRDRVESRAGFNLLLAAERIQVGYYTSLDYIIGDTGITKGKHFWAFRVEPYSYLVKVGVASSDKLQEWLRSPRDAVSPRYEQDSGHDSGSEDACFDSSQPFTLVTIGMQKFFIPKSPTSSNEPENRVLPMPTSIGIFLDCDKGKVDFYDMDQMKCLYERQVDCSHTLYPAFALMGSGGIQLEEPITAKYLEYQEDM
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
2Phosphorylation------MSESGEMSE
------CCCCCCCCH		40.2325002506
4Phosphorylation----MSESGEMSEFG
----CCCCCCCCHHH		32.5225002506
6 (in isoform 4)Phosphorylation-49.1427732954
8PhosphorylationMSESGEMSEFGYIME
CCCCCCCCHHHHHHH		26.0225002506
8 (in isoform 4)Phosphorylation-26.0225159151
11 (in isoform 4)Phosphorylation-13.6527732954
12PhosphorylationGEMSEFGYIMELIAK
CCCCHHHHHHHHHHC		11.4725002506
23 (in isoform 3)Phosphorylation-29.71-
48 (in isoform 2)Phosphorylation-5.22-
48PhosphorylationTHPLILPCQHSICHK
CCCCCCCCCHHHHHH		5.22-
50PhosphorylationPLILPCQHSICHKCV
CCCCCCCHHHHHHHH		26.33-
50 (in isoform 2)Phosphorylation-26.33-
54 (in isoform 2)Phosphorylation-25.53-
54PhosphorylationPCQHSICHKCVKELL
CCCHHHHHHHHHHHH		25.53-
60PhosphorylationCHKCVKELLLTLDDS
HHHHHHHHHHCCCCC		3.83-
60 (in isoform 2)Phosphorylation-3.83-
73PhosphorylationDSFNDVGSDNSNQSS
CCCCCCCCCCCCCCC		33.2028348404
76PhosphorylationNDVGSDNSNQSSPRL
CCCCCCCCCCCCCCC		41.0328348404
79PhosphorylationGSDNSNQSSPRLRLP
CCCCCCCCCCCCCCC		46.7028348404
80PhosphorylationSDNSNQSSPRLRLPS
CCCCCCCCCCCCCCC		12.3228348404
87PhosphorylationSPRLRLPSPSMDKID
CCCCCCCCCCHHHHH		33.9125159151
89PhosphorylationRLRLPSPSMDKIDRI
CCCCCCCCHHHHHCC		43.9028450419
105PhosphorylationRPGWKRNSLTPRTTV
CCCCCCCCCCCCEEE		37.3426670566
107PhosphorylationGWKRNSLTPRTTVFP
CCCCCCCCCCEEEEE		15.5628102081
137PhosphorylationNGLFRNFTLETIVER
CHHHCCCCHHHHHHH		27.5123403867
140PhosphorylationFRNFTLETIVERYRQ
HCCCCHHHHHHHHHH		33.1723403867
145PhosphorylationLETIVERYRQAARAA
HHHHHHHHHHHHHHH		8.1228851738
170PhosphorylationPPQESTKSCMDCSAS
CCCCCCCHHHHCCHH		18.1124114839
175PhosphorylationTKSCMDCSASYCNEC
CCHHHHCCHHHHCCH		18.9124114839
177PhosphorylationSCMDCSASYCNECFK
HHHHCCHHHHCCHHH		17.5824114839
178PhosphorylationCMDCSASYCNECFKI
HHHCCHHHHCCHHHC		10.0624114839
236AcetylationRPVCHLCKLGGNHAN
CCCHHHHHCCCCCCC		57.4318528631
253PhosphorylationVTTMSSAYKTLKEKL
HHHHHHHHHHHHHHH		13.37-
254AcetylationTTMSSAYKTLKEKLS
HHHHHHHHHHHHHHH		47.2818528639
276PhosphorylationGKESQVKSQISELNL
CCHHHHHHHHHHHHH		33.6129083192
279PhosphorylationSQVKSQISELNLLMK
HHHHHHHHHHHHHHH		28.5228122231
383UbiquitinationQKATESLKSFRPAAQ
HHHHHHHHHHCCCHH		57.75-
384PhosphorylationKATESLKSFRPAAQT
HHHHHHHHHCCCHHC		31.6124719451
391PhosphorylationSFRPAAQTSFEDYVV
HHCCCHHCCHHHHEE		30.5628348404
392PhosphorylationFRPAAQTSFEDYVVN
HCCCHHCCHHHHEEE		17.9829802988
396PhosphorylationAQTSFEDYVVNTSKQ
HHCCHHHHEEECHHH		10.0927642862
462PhosphorylationINRDDEMSWNEIEVC
CCCCCCCCHHHEEEC		25.3827499020
482PhosphorylationIQDLENSSTYAFRVR
HHHHCCCCCEEEEEE		36.7025003641
483PhosphorylationQDLENSSTYAFRVRA
HHHCCCCCEEEEEEE		20.7725003641
484PhosphorylationDLENSSTYAFRVRAY
HHCCCCCEEEEEEEC		12.9925003641
494PhosphorylationRVRAYKGSICSPCSR
EEEECCCCCCCCCCC		19.1028348404
497PhosphorylationAYKGSICSPCSRELI
ECCCCCCCCCCCCHH		27.5428985074
583PhosphorylationWAFRVEPYSYLVKVG
EEEEEECCEEEEEEE		9.1030206219
584PhosphorylationAFRVEPYSYLVKVGV
EEEEECCEEEEEEEE		23.7830206219
585PhosphorylationFRVEPYSYLVKVGVA
EEEECCEEEEEEEEC		15.0730206219
603PhosphorylationKLQEWLRSPRDAVSP
HHHHHHHCCHHHCCC		23.3225002506
609PhosphorylationRSPRDAVSPRYEQDS
HCCHHHCCCCCCCCC		12.8424719451
612PhosphorylationRDAVSPRYEQDSGHD
HHHCCCCCCCCCCCC		22.7130624053
616PhosphorylationSPRYEQDSGHDSGSE
CCCCCCCCCCCCCCC		37.4130624053
620PhosphorylationEQDSGHDSGSEDACF
CCCCCCCCCCCCCCC		38.2526657352
622PhosphorylationDSGHDSGSEDACFDS
CCCCCCCCCCCCCCC		35.9326657352
629PhosphorylationSEDACFDSSQPFTLV
CCCCCCCCCCCEEEE		15.6027080861
630PhosphorylationEDACFDSSQPFTLVT
CCCCCCCCCCEEEEE		43.6627080861
634PhosphorylationFDSSQPFTLVTIGMQ
CCCCCCEEEEEEECE		27.3127080861
648PhosphorylationQKFFIPKSPTSSNEP
EEEECCCCCCCCCCC		28.2325850435
650PhosphorylationFFIPKSPTSSNEPEN
EECCCCCCCCCCCCC		52.4523312004
651PhosphorylationFIPKSPTSSNEPENR
ECCCCCCCCCCCCCC		34.2523312004
652PhosphorylationIPKSPTSSNEPENRV
CCCCCCCCCCCCCCC		47.9228102081
724PhosphorylationITAKYLEYQEDM---
CCHHHHHHHCCC---		18.0127642862
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 TRI36_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI36_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 TRI36_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_HUMANUBCphysical
19232519
CENPH_HUMANCENPHphysical
19232519
UB2D2_HUMANUBE2D2physical
19232519
TRI36_HUMANTRIM36physical
25416956
T3JAM_HUMANTRAF3IP3physical
25416956
ZN587_HUMANZNF587physical
25416956
ZN417_HUMANZNF417physical
25416956
ZMAT2_HUMANZMAT2physical
25416956
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRI36_HUMAN

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Related Literatures of Post-Translational Modification

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