TRI62_HUMAN - dbPTM
TRI62_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI62_HUMAN
UniProt AC Q9BVG3
Protein Name E3 ubiquitin-protein ligase TRIM62
Gene Name TRIM62
Organism Homo sapiens (Human).
Sequence Length 475
Subcellular Localization Cytoplasm .
Protein Description E3 ubiquitin ligase whose activity is dependent on E2 ubiquitin-conjugating enzyme UBE2D2..
Protein Sequence MACSLKDELLCSICLSIYQDPVSLGCEHYFCRRCITEHWVRQEAQGARDCPECRRTFAEPALAPSLKLANIVERYSSFPLDAILNARRAARPCQAHDKVKLFCLTDRALLCFFCDEPALHEQHQVTGIDDAFDELQRELKDQLQALQDSEREHTEALQLLKRQLAETKSSTKSLRTTIGEAFERLHRLLRERQKAMLEELEADTARTLTDIEQKVQRYSQQLRKVQEGAQILQERLAETDRHTFLAGVASLSERLKGKIHETNLTYEDFPTSKYTGPLQYTIWKSLFQDIHPVPAALTLDPGTAHQRLILSDDCTIVAYGNLHPQPLQDSPKRFDVEVSVLGSEAFSSGVHYWEVVVAEKTQWVIGLAHEAASRKGSIQIQPSRGFYCIVMHDGNQYSACTEPWTRLNVRDKLDKVGVFLDYDQGLLIFYNADDMSWLYTFREKFPGKLCSYFSPGQSHANGKNVQPLRINTVRI
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
40UbiquitinationRCITEHWVRQEAQGA
HHHHHHHHHHHHCCC		4.96-
40UbiquitinationRCITEHWVRQEAQGA
HHHHHHHHHHHHCCC		4.9622817900
65PhosphorylationAEPALAPSLKLANIV
CCCCCCHHHHHHHHH		32.3127251275
67UbiquitinationPALAPSLKLANIVER
CCCCHHHHHHHHHHH		50.3021906983
73UbiquitinationLKLANIVERYSSFPL
HHHHHHHHHHHCCCH		41.95-
75PhosphorylationLANIVERYSSFPLDA
HHHHHHHHHCCCHHH		8.6527642862
76PhosphorylationANIVERYSSFPLDAI
HHHHHHHHCCCHHHH		31.5524719451
93UbiquitinationARRAARPCQAHDKVK
HHHHHCCCCCCCCCE		4.6822817900
93UbiquitinationARRAARPCQAHDKVK
HHHHHCCCCCCCCCE		4.68-
100UbiquitinationCQAHDKVKLFCLTDR
CCCCCCCEEEEECCC		41.40-
103UbiquitinationHDKVKLFCLTDRALL
CCCCEEEEECCCCEE		6.0729967540
103UbiquitinationHDKVKLFCLTDRALL
CCCCEEEEECCCCEE		6.07-
135UbiquitinationIDDAFDELQRELKDQ
CHHHHHHHHHHHHHH		6.6522817900
137UbiquitinationDAFDELQRELKDQLQ
HHHHHHHHHHHHHHH		64.9322817900
137UbiquitinationDAFDELQRELKDQLQ
HHHHHHHHHHHHHHH		64.93-
140UbiquitinationDELQRELKDQLQALQ
HHHHHHHHHHHHHHH		38.3832142685
147UbiquitinationKDQLQALQDSEREHT
HHHHHHHHHHHHHHH		56.0221963094
152UbiquitinationALQDSEREHTEALQL
HHHHHHHHHHHHHHH		51.6229967540
152UbiquitinationALQDSEREHTEALQL
HHHHHHHHHHHHHHH		51.62-
154PhosphorylationQDSEREHTEALQLLK
HHHHHHHHHHHHHHH		20.4228450419
161UbiquitinationTEALQLLKRQLAETK
HHHHHHHHHHHHHCH		46.8421906983
167PhosphorylationLKRQLAETKSSTKSL
HHHHHHHCHHCCHHH		30.53-
169PhosphorylationRQLAETKSSTKSLRT
HHHHHCHHCCHHHHH		51.14-
173PhosphorylationETKSSTKSLRTTIGE
HCHHCCHHHHHHHHH		24.1526270265
176PhosphorylationSSTKSLRTTIGEAFE
HCCHHHHHHHHHHHH		28.2326270265
177PhosphorylationSTKSLRTTIGEAFER
CCHHHHHHHHHHHHH		22.1326270265
194UbiquitinationRLLRERQKAMLEELE
HHHHHHHHHHHHHHH		41.82-
214UbiquitinationTLTDIEQKVQRYSQQ
HHHHHHHHHHHHHHH		27.7821906983
224UbiquitinationRYSQQLRKVQEGAQI
HHHHHHHHHHHHHHH		57.7929967540
241UbiquitinationERLAETDRHTFLAGV
HHHHHCCHHHHHHHH		37.8622817900
243PhosphorylationLAETDRHTFLAGVAS
HHHCCHHHHHHHHHH		22.6522210691
254UbiquitinationGVASLSERLKGKIHE
HHHHHHHHHCCCCEE		38.02-
256UbiquitinationASLSERLKGKIHETN
HHHHHHHCCCCEECC		65.4622817900
258UbiquitinationLSERLKGKIHETNLT
HHHHHCCCCEECCCC		39.0222817900
266PhosphorylationIHETNLTYEDFPTSK
CEECCCCHHCCCCCC		19.3727642862
273UbiquitinationYEDFPTSKYTGPLQY
HHCCCCCCCCCCHHH		49.6729967540
283UbiquitinationGPLQYTIWKSLFQDI
CCHHHHHHHHHCCCC		4.0322817900
294UbiquitinationFQDIHPVPAALTLDP
CCCCCCCCCEEEECC		19.1022817900
319PhosphorylationDDCTIVAYGNLHPQP
CCCEEEEECCCCCCC		8.8227642862
325UbiquitinationAYGNLHPQPLQDSPK
EECCCCCCCCCCCCC		40.3622817900
327UbiquitinationGNLHPQPLQDSPKRF
CCCCCCCCCCCCCCC		8.1222817900
336UbiquitinationDSPKRFDVEVSVLGS
CCCCCCEEEEEEECC		7.8122817900
338UbiquitinationPKRFDVEVSVLGSEA
CCCCEEEEEEECCCH		4.8822817900
342UbiquitinationDVEVSVLGSEAFSSG
EEEEEEECCCHHCCC		22.68-
375UbiquitinationAHEAASRKGSIQIQP
HHHHHHCCCCEEEEC		55.29-
463UbiquitinationGQSHANGKNVQPLRI
CCCCCCCCCCCCCEE		54.47-
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 ligaseTRIM62Q9BVG3
PMID:23402750
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI62_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 TRI62_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMAD3_HUMANSMAD3physical
23838884
CARD9_HUMANCARD9physical
26488816
UB2D2_HUMANUBE2D2physical
26488816
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 TRI62_HUMAN

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Related Literatures of Post-Translational Modification

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