TDRD1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TDRD1_HUMAN
• UniProt AC: Q9BXT4
• Protein Name: Tudor domain-containing protein 1
• Gene Name: TDRD1
• Organism: Homo sapiens (Human).
• Sequence Length: 1180
• Subcellular Localization: Cytoplasm. Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Also present in chromatoid body (By similarity)..
• Protein Description: Plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for the germline integrity. 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 governs the methylation and subsequent repression of transposons. Required for the localization of Piwi proteins to the meiotic nuage. Involved in the piRNA metabolic process by ensuring the entry of correct transcripts into the normal piRNA pool and limiting the entry of cellular transcripts into the piRNA pathway. May act by allowing the recruitment of piRNA biogenesis or loading factors that ensure the correct entry of transcripts and piRNAs into Piwi proteins (By similarity)..
• Protein Sequence: MSVKSPFNVMSRNNLEAPPCKMTEPFNFEKNENKLPPHESLRSPGTLPNHPNFRLKSSENGNKKNNFLLCEQTKQYLASQEDNSVSSNPNGINGEVVGSKGDRKKLPAGNSVSPPSAESNSPPKEVNIKPGNNVRPAKSKKLNKLVENSLSISNPGLFTSLGPPLRSTTCHRCGLFGSLRCSQCKQTYYCSTACQRRDWSAHSIVCRPVQPNFHKLENKSSIETKDVEVNNKSDCPLGVTKEIAIWAERIMFSDLRSLQLKKTMEIKGTVTEFKHPGDFYVQLYSSEVLEYMNQLSASLKETYANVHEKDYIPVKGEVCIAKYTVDQTWNRAIIQNVDVQQKKAHVLYIDYGNEEIIPLNRIYHLNRNIDLFPPCAIKCFVANVIPAEGNWSSDCIKATKPLLMEQYCSIKIVDILEEEVVTFAVEVELPNSGKLLDHVLIEMGYGLKPSGQDSKKENADQSDPEDVGKMTTENNIVVDKSDLIPKVLTLNVGDEFCGVVAHIQTPEDFFCQQLQSGRKLAELQASLSKYCDQLPPRSDFYPAIGDICCAQFSEDDQWYRASVLAYASEESVLVGYVDYGNFEILSLMRLCPIIPKLLELPMQAIKCVLAGVKPSLGIWTPEAICLMKKLVQNKIITVKVVDKLENSSLVELIDKSETPHVSVSKVLLDAGFAVGEQSMVTDKPSDVKETSVPLGVEGKVNPLEWTWVELGVDQTVDVVVCVIYSPGEFYCHVLKEDALKKLNDLNKSLAEHCQQKLPNGFKAEIGQPCCAFFAGDGSWYRALVKEILPNGHVKVHFVDYGNIEEVTADELRMISSTFLNLPFQGIRCQLADIQSRNKHWSEEAITRFQMCVAGIKLQARVVEVTENGIGVELTDLSTCYPRIISDVLIDEHLVLKSASPHKDLPNDRLVNKHELQVHVQGLQATSSAEQWKTIELPVDKTIQANVLEIISPNLFYALPKGMPENQEKLCMLTAELLEYCNAPKSRPPYRPRIGDACCAKYTSDDFWYRAVVLGTSDTDVEVLYADYGNIETLPLCRVQPITSSHLALPFQIIRCSLEGLMELNGSSSQLIIMLLKNFMLNQNVMLSVKGITKNVHTVSVEKCSENGTVDVADKLVTFGLAKNITPQRQSALNTEKMYRMNCCCTELQKQVEKHEHILLFLLNNSTNQNKFIEMKKLLKS

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
2	Phosphorylation	------MSVKSPFNV ------CCCCCCCCC	49.94	24719451
5	Phosphorylation	---MSVKSPFNVMSR ---CCCCCCCCCCCC	32.35	24043423
11	Phosphorylation	KSPFNVMSRNNLEAP CCCCCCCCCCCCCCC	27.81	24043423
43	Phosphorylation	PPHESLRSPGTLPNH CCCCCCCCCCCCCCC	32.73	27251275
76	Phosphorylation	LCEQTKQYLASQEDN EEHHHHHHHHCCCCC	13.04	24043423
79	Phosphorylation	QTKQYLASQEDNSVS HHHHHHHCCCCCCCC	31.35	24043423
84	Phosphorylation	LASQEDNSVSSNPNG HHCCCCCCCCCCCCC	35.38	24043423
86	Phosphorylation	SQEDNSVSSNPNGIN CCCCCCCCCCCCCCC	24.99	24043423
87	Phosphorylation	QEDNSVSSNPNGING CCCCCCCCCCCCCCC	54.90	24043423
99	Phosphorylation	INGEVVGSKGDRKKL CCCEECCCCCCCCCC	23.12	24043423
111	Phosphorylation	KKLPAGNSVSPPSAE CCCCCCCCCCCCCCC	24.05	28102081
113	Phosphorylation	LPAGNSVSPPSAESN CCCCCCCCCCCCCCC	30.80	23312004
116	Phosphorylation	GNSVSPPSAESNSPP CCCCCCCCCCCCCCC	48.31	28102081
119	Phosphorylation	VSPPSAESNSPPKEV CCCCCCCCCCCCCCC	42.18	30177828
121	Phosphorylation	PPSAESNSPPKEVNI CCCCCCCCCCCCCCC	52.43	28102081
149	Phosphorylation	LNKLVENSLSISNPG HHHHHHHCCCCCCCC	15.24	-
151	Phosphorylation	KLVENSLSISNPGLF HHHHHCCCCCCCCHH	24.64	-
191	Phosphorylation	CKQTYYCSTACQRRD CCCEEEECHHHHCCC	11.70	-
192	Phosphorylation	KQTYYCSTACQRRDW CCEEEECHHHHCCCC	28.08	-
253	Phosphorylation	WAERIMFSDLRSLQL HHHHHHHHHHHHHCC	20.53	24719451
263	Phosphorylation	RSLQLKKTMEIKGTV HHHCCCEEEEEEEEE	20.60	-
392	Phosphorylation	IPAEGNWSSDCIKAT CCCCCCCCHHHHHHH	21.94	29978859
393	Phosphorylation	PAEGNWSSDCIKATK CCCCCCCHHHHHHHH	28.28	29978859
399	Phosphorylation	SSDCIKATKPLLMEQ CHHHHHHHHHHHHHH	28.35	29978859
407	Phosphorylation	KPLLMEQYCSIKIVD HHHHHHHHCEEEEEE	3.78	29978859
409	O-linked_Glycosylation	LLMEQYCSIKIVDIL HHHHHHCEEEEEECC	23.22	30379171
409	Phosphorylation	LLMEQYCSIKIVDIL HHHHHHCEEEEEECC	23.22	29978859
462	Phosphorylation	KKENADQSDPEDVGK CCCCCCCCCHHHHHH	56.53	30177828
526	Phosphorylation	KLAELQASLSKYCDQ HHHHHHHHHHHHHHC	21.88	27251275
528	Phosphorylation	AELQASLSKYCDQLP HHHHHHHHHHHHCCC	21.05	29743597
647	Phosphorylation	VVDKLENSSLVELID EEECCCCCCCEEEEC	18.70	24719451
648	Phosphorylation	VDKLENSSLVELIDK EECCCCCCCEEEECC	48.27	24719451
664	Phosphorylation	ETPHVSVSKVLLDAG CCCCEEHHHHHHHCC	15.00	24719451
691	Phosphorylation	PSDVKETSVPLGVEG CCCCCCCCCCCCCCC	23.87	-
1056	Phosphorylation	PFQIIRCSLEGLMEL CHHHEEECHHHHHHH	21.43	-
1087	Phosphorylation	LNQNVMLSVKGITKN CCCCEEEEECCCCCC	12.04	24719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TDRD1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TDRD1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TDRD1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of TDRD1_HUMAN !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.