TDRD5_HUMAN - dbPTM
TDRD5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TDRD5_HUMAN
UniProt AC Q8NAT2
Protein Name Tudor domain-containing protein 5
Gene Name TDRD5
Organism Homo sapiens (Human).
Sequence Length 981
Subcellular Localization Cytoplasm. Localizes to chromatoid body (CB) and pi-body (also called intermitochondrial cementin), 2 cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis..
Protein Description Required during spermiogenesis to participate in the repression transposable elements and prevent their mobilization, which is essential for the germline integrity. Probably acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Required for chromatoid body (CB) assembly (By similarity)..
Protein Sequence MSEQERIQECLRKEIRSLLISTKDGLSPQELEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVRVCPGAGGTVILKAIPDESTKGIASLVAKQRSSHKLRNSMHKGRPSIYSGPRSHRRVPYRGRVAPILPAVVKSELKDLLALSPVLLSDFEKAFAKRFGRSFQYMQYGFLSMFEVLNAASDVISVEQTRAGSLLMLKKSVTEEKPRGCPAGKIFTQPFRMKQGSYSTGFPVAKPCFSQPTSNMEPPKQIMSMEKTSKLNVVETSRLNHTEKLNQLENTFKSVIAQIGPGGTISSELKHKIKFVVSKFPEGLFISKLLGEYEVIFKEQLSPKKLGFLNVTELVGALSDILHVEFRKGHQDLLVFDADKKPLPPVQSDKKIEAKACVSSPPRNSLSTAAVKETVWNCPSKKQKEPQQKICKKPNLVVKPLQLQVETNKSELNLAMANHDIPPDAVPNKKLCRLPPLDTSSLIGVFVEYIISPSQFYIRIYSRDSSELLEDMMIEMRRCYSNQLVSDRYVMPECFIQPGHLCCVRISEDKWWYRVIIHRVLEKQEVEVFYPDFGNIGIVQKSSLRFLKCCYTKLPAQAIPCSLAWVRPVEEHWTSKAILQFQKLCGLKPLVGVVDEYVDGILNIFLCDTSSNEDVYFHHVLRTEGHAIVCRENISSKGFSELNPLALYTTSSGGPEDIVLTELGYPSQQHYFNEDRKISPQSKESELRILDEIPTGMPCLESVTIGDDIWDENWLPLQAKMGKGGDAASHLFTASLGGKNQYSSCKEMPQKDWCFSTPKDTWDDSWQPSGLVNGTKVEVHKPEVLGAQEKNTGTNRTQKQLDINGSSDSSTLPKLEEFCTSLTQSEQSADGSQSEPNNSQTQPKQIQLSTAAPCSTTAVDDSAEKPSGSVESSPEILKNEDFSSSRAITLYKDKRQESVDQLSLILSYECQISQKLYIPRSTATAALGAAARLATSRSLLHWYPSVKRMEA
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
21PhosphorylationEIRSLLISTKDGLSP
HHHHHHHHCCCCCCH
29.4024719451
110PhosphorylationSMHKGRPSIYSGPRS
CHHCCCCCCCCCCCC
32.5622210691
112PhosphorylationHKGRPSIYSGPRSHR
HCCCCCCCCCCCCCC
16.3522210691
117PhosphorylationSIYSGPRSHRRVPYR
CCCCCCCCCCCCCCC
25.2022210691
195PhosphorylationVEQTRAGSLLMLKKS
EEHHHCCCEEEEEEC
19.8317081983
440PhosphorylationLQVETNKSELNLAMA
EEEECCHHHHHHHHH
49.7622210691
469PhosphorylationCRLPPLDTSSLIGVF
CCCCCCCHHHHHHHH
28.0924043423
470PhosphorylationRLPPLDTSSLIGVFV
CCCCCCHHHHHHHHH
23.8624043423
471PhosphorylationLPPLDTSSLIGVFVE
CCCCCHHHHHHHHHH
26.5424043423
479PhosphorylationLIGVFVEYIISPSQF
HHHHHHHHCCCHHHE
9.7624043423
482PhosphorylationVFVEYIISPSQFYIR
HHHHHCCCHHHEEEE
14.6724043423
484PhosphorylationVEYIISPSQFYIRIY
HHHCCCHHHEEEEEE
26.5724043423
487PhosphorylationIISPSQFYIRIYSRD
CCCHHHEEEEEEECC
5.0124043423
492PhosphorylationQFYIRIYSRDSSELL
HEEEEEEECCHHHHH
27.5224719451
495PhosphorylationIRIYSRDSSELLEDM
EEEEECCHHHHHHHH
25.30-
510PhosphorylationMIEMRRCYSNQLVSD
HHHHHHHHCCCCCCC
14.62-
511PhosphorylationIEMRRCYSNQLVSDR
HHHHHHHCCCCCCCC
23.02-
516PhosphorylationCYSNQLVSDRYVMPE
HHCCCCCCCCCCCCH
25.59-
709PhosphorylationFNEDRKISPQSKESE
CCCCCCCCCCCHHHH
21.6624719451
734 (in isoform 1)Phosphorylation-28.64-
736 (in isoform 1)Phosphorylation-19.71-
747 (in isoform 1)Phosphorylation-7.87-
754 (in isoform 1)Phosphorylation-33.22-
822PhosphorylationLGAQEKNTGTNRTQK
CCCEECCCCCCCCEE
57.3529116813
824PhosphorylationAQEKNTGTNRTQKQL
CEECCCCCCCCEEEE
21.3529116813
827PhosphorylationKNTGTNRTQKQLDIN
CCCCCCCCEEEEECC
42.03-
892PhosphorylationSTTAVDDSAEKPSGS
CCCCCCCCCCCCCCC
33.59-
913PhosphorylationILKNEDFSSSRAITL
HHHCCCCCCCCCEEE
39.4624719451
919PhosphorylationFSSSRAITLYKDKRQ
CCCCCCEEEECCCCC
24.0524719451

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 TDRD5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TDRD5_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 TDRD5_HUMAN !!

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

Oops, there are no PPI records of TDRD5_HUMAN !!

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 TDRD5_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-195, AND MASSSPECTROMETRY.

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