TROP_HUMAN - dbPTM
TROP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TROP_HUMAN
UniProt AC Q12816
Protein Name Trophinin
Gene Name TRO
Organism Homo sapiens (Human).
Sequence Length 1431
Subcellular Localization
Protein Description Could be involved with bystin and tastin in a cell adhesion molecule complex that mediates an initial attachment of the blastocyst to uterine epithelial cells at the time of the embryo implantation. Directly responsible for homophilic cell adhesion..
Protein Sequence MDRRNDYGYRVPLFQGPLPPPGSLGLPFPPDIQTETTEEDSVLLMHTLLAATKDSLAMDPPVVNRPKKSKTKKAPIKTITKAAPAAPPVPAANEIATNKPKITWQALNLPVITQISQALPTTEVTNTQASSVTAQPKKANKMKRVTAKAAQGSQSPTGHEGGTIQLKSPLQVLKLPVISQNIHAPIANESASSQALITSIKPKKASKAKKAANKAIASATEVSLAATATHTATTQGQITNETASIHTTAASIRTKKASKARKTIAKVINTDTEHIEALNVTDAATRQIEASVVAIRPKKSKGKKAASRGPNSVSEISEAPLATQIVTNQALAATLRVKRGSRARKAATKARATESQTPNADQGAQAKIASAQTNVSALETQVAAAVQALADDYLAQLSLEPTTRTRGKRNRKSKHLNGDERSGSNYRRIPWGRRPAPPRDVAILQERANKLVKYLLVKDQTKIPIKRSDMLRDVIQEYDEYFPEIIERASYTLEKMFRVNLKEIDKQSSLYILISTQESSAGILGTTKDTPKLGLLMVILSVIFMNGNKASEAVIWEVLRKLGLRPGVRHSLFGEVRKLITDEFVKQKYLEYKRVPNSRPPEYEFFWGLRSYHETSKMKVLKFACRVQKKDPKDWAVQYREAVEMEVQAAAVAVAEAEARAEARAQMGIGEEAVAGPWNWDDMDIDCLTREELGDDAQAWSRFSFEIEARAQENADASTNVNFSRGASTRAGFSDGASISFNGAPSSSGGFSGGPGITFGVAPSTSASFSNTASISFGGTLSTSSSFSSAASISFGCAHSTSTSFSSEASISFGGMPCTSASFSGGVSSSFSGPLSTSATFSGGASSGFGGTLSTTAGFSGVLSTSTSFGSAPTTSTVFSSALSTSTGFGGILSTSVCFGGSPSSSGSFGGTLSTSICFGGSPCTSTGFGGTLSTSVSFGGSSSTSANFGGTLSTSICFDGSPSTGAGFGGALNTSASFGSVLNTSTGFGGAMSTSADFGGTLSTSVCFGGSPGTSVSFGSALNTNAGYGGAVSTNTDFGGTLSTSVCFGGSPSTSAGFGGALNTNASFGCAVSTSASFSGAVSTSACFSGAPITNPGFGGAFSTSAGFGGALSTAADFGGTPSNSIGFGAAPSTSVSFGGAHGTSLCFGGAPSTSLCFGSASNTNLCFGGPPSTSACFSGATSPSFCDGPSTSTGFSFGNGLSTNAGFGGGLNTSAGFGGGLGTSAGFSGGLSTSSGFDGGLGTSAGFGGGPGTSTGFGGGLGTSAGFSGGLGTSAGFGGGLVTSDGFGGGLGTNASFGSTLGTSAGFSGGLSTSDGFGSRPNASFDRGLSTIIGFGSGSNTSTGFTGEPSTSTGFSSGPSSIVGFSGGPSTGVGFCSGPSTSGFSGGPSTGAGFGGGPNTGAGFGGGPSTSAGFGSGAASLGACGFSYG
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
56UbiquitinationLAATKDSLAMDPPVV
HHHCCHHHCCCCCCC
7.0221890473
56UbiquitinationLAATKDSLAMDPPVV
HHHCCHHHCCCCCCC
7.0221890473
78PhosphorylationTKKAPIKTITKAAPA
CCCCCCCEEECCCCC
34.30-
81UbiquitinationAPIKTITKAAPAAPP
CCCCEEECCCCCCCC
38.41-
99AcetylationANEIATNKPKITWQA
HHHHHCCCCCCCHHH
43.2520167786
146PhosphorylationANKMKRVTAKAAQGS
CCCCHHHHHHHHCCC
26.86-
153PhosphorylationTAKAAQGSQSPTGHE
HHHHHCCCCCCCCCC
18.5330266825
155PhosphorylationKAAQGSQSPTGHEGG
HHHCCCCCCCCCCCC
26.5730266825
157PhosphorylationAQGSQSPTGHEGGTI
HCCCCCCCCCCCCCE
57.3230266825
163PhosphorylationPTGHEGGTIQLKSPL
CCCCCCCCEEECCCC
19.1922199227
168PhosphorylationGGTIQLKSPLQVLKL
CCCEEECCCCEEEEC
39.1630266825
189UbiquitinationIHAPIANESASSQAL
CCCCCCCCCCCCHHH
38.36-
191UbiquitinationAPIANESASSQALIT
CCCCCCCCCCHHHHH
13.66-
196UbiquitinationESASSQALITSIKPK
CCCCCHHHHHHCCCC
3.21-
220UbiquitinationNKAIASATEVSLAAT
HHHHHHHHHHHHHHH
34.13-
220UbiquitinationNKAIASATEVSLAAT
HHHHHHHHHHHHHHH
34.1321890473
225UbiquitinationSATEVSLAATATHTA
HHHHHHHHHHCCCCC
8.68-
236UbiquitinationTHTATTQGQITNETA
CCCCCCCCCCCCCCC
20.83-
266UbiquitinationKARKTIAKVINTDTE
HHHHHHHHHHCCCHH
39.53-
298AcetylationSVVAIRPKKSKGKKA
EEEEEECCCCCCCCC
60.897303111
299AcetylationVVAIRPKKSKGKKAA
EEEEECCCCCCCCCH
61.157303121
301AcetylationAIRPKKSKGKKAASR
EEECCCCCCCCCHHC
81.357303131
301UbiquitinationAIRPKKSKGKKAASR
EEECCCCCCCCCHHC
81.35-
312PhosphorylationAASRGPNSVSEISEA
CHHCCCCCHHHHCCC
30.1022210691
323PhosphorylationISEAPLATQIVTNQA
HCCCCCCHHHHHHHH
26.8922210691
327PhosphorylationPLATQIVTNQALAAT
CCCHHHHHHHHHHHH
24.2022210691
334PhosphorylationTNQALAATLRVKRGS
HHHHHHHHHHHHHHH
14.97-
413PhosphorylationRGKRNRKSKHLNGDE
CCCCCCCCCCCCCCC
23.28-
422PhosphorylationHLNGDERSGSNYRRI
CCCCCCCCCCCCCCC
44.52-
424PhosphorylationNGDERSGSNYRRIPW
CCCCCCCCCCCCCCC
31.75-
426PhosphorylationDERSGSNYRRIPWGR
CCCCCCCCCCCCCCC
11.72-
453UbiquitinationERANKLVKYLLVKDQ
HHHHHHHHHHHCCCC
40.3921890473
453UbiquitinationERANKLVKYLLVKDQ
HHHHHHHHHHHCCCC
40.3921890473
458UbiquitinationLVKYLLVKDQTKIPI
HHHHHHCCCCCCCCC
44.05-
462UbiquitinationLLVKDQTKIPIKRSD
HHCCCCCCCCCCHHH
40.63-
466UbiquitinationDQTKIPIKRSDMLRD
CCCCCCCCHHHHHHH
40.26-
478PhosphorylationLRDVIQEYDEYFPEI
HHHHHHHHHHHHHHH
9.5629759185
481PhosphorylationVIQEYDEYFPEIIER
HHHHHHHHHHHHHHH
22.8729759185
495UbiquitinationRASYTLEKMFRVNLK
HHCHHHHHHHCCCHH
46.59-
502UbiquitinationKMFRVNLKEIDKQSS
HHHCCCHHHHCCCCC
47.63-
578UbiquitinationSLFGEVRKLITDEFV
HHHHHHHHHHCHHHH
49.79-
586UbiquitinationLITDEFVKQKYLEYK
HHCHHHHHHHHHHCC
46.52-
5862-HydroxyisobutyrylationLITDEFVKQKYLEYK
HHCHHHHHHHHHHCC
46.52-
588UbiquitinationTDEFVKQKYLEYKRV
CHHHHHHHHHHCCCC
46.19-
593UbiquitinationKQKYLEYKRVPNSRP
HHHHHHCCCCCCCCC
37.23-
617UbiquitinationRSYHETSKMKVLKFA
CCCCCCCHHHHHHHH
50.5921890473
622UbiquitinationTSKMKVLKFACRVQK
CCHHHHHHHHHHCCC
33.62-
633UbiquitinationRVQKKDPKDWAVQYR
HCCCCCHHHHHHHHH
75.84-
701PhosphorylationGDDAQAWSRFSFEIE
CCCHHHHHHHCEEEH
26.8529083192
1333PhosphorylationSFDRGLSTIIGFGSG
CCCCCCCEEEEECCC
22.96-
1339PhosphorylationSTIIGFGSGSNTSTG
CEEEEECCCCCCCCC
36.47-
1345PhosphorylationGSGSNTSTGFTGEPS
CCCCCCCCCCCCCCC
33.99-

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 TROP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TROP_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 TROP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KPCD_HUMANPRKCDphysical
21191175

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 TROP_HUMAN

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Related Literatures of Post-Translational Modification

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