BTBDI_HUMAN - dbPTM
BTBDI_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BTBDI_HUMAN
UniProt AC B2RXH4
Protein Name BTB/POZ domain-containing protein 18 {ECO:0000305}
Gene Name BTBD18 {ECO:0000312|HGNC:HGNC:37214}
Organism Homo sapiens (Human).
Sequence Length 712
Subcellular Localization Nucleus .
Protein Description Specifically required during spermatogenesis to promote expression of piRNA precursors. The piRNA metabolic process 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, which is essential for the germline integrity. Acts by facilitating transcription elongation at piRNA loci during pachytene..
Protein Sequence MCSPASPKILYRNPRFLRLAFLQLHHQQQSDVFCDVLLQAEGEAVPAHCCILSACSPFFTERLERERPAQGGKVVLELGGLKISTLRKLVDFLYTSEMEVSQEEAQDVLSAARQLRVSELESLQLEGGKLVKAPQGRRLNRECLQPTSAAPISARVVTPSHHPHTPLPTNQTPCPLGAIRLKSLGKEEGPQENNRQNADNLSGTLLLKRKARACPTPQEKNSSPSSHSQEPRENKNDTALDPTVLSPPSLYPSVDKHLLPRKIRLSRSKPSPGICTSKPSSILSGSSSVPATPGRRLWRQRSVNKETPEDKPKPGRASPLQSTPNPSGLGKTGGSRKRSPEVRAPNSDSAEEGQVGRVKLRKIVNGTCWEVVQETPLKNTQDSPQIPDPGGDFQEPSGTQPFSSNEQEMSPTRTELCQDSPMCTKLQDILVSASHSPDHPVVKSEFESSPELVEKEPMLAIDCREPYAFDTALLEQPCEAEEYRITSAAATSELEEILDFMLCGSDIEPPIGSLESPGAEGCRTPTYHLTETGKNWIEGEEWCLPDMELWPRELTELEKEPAGENRGPTELLSPLVMPSEVSEVLSVGGRWTPDLEITSSQPLDGQEDKLLHVSSLDTPQRSYGDLSPPCSNWVETGLEVSLTTDELLYPSPKAGKEVSGHSELLGSLPASSEEEEIDVVDWTAEGRLVPTTVPSVWPDPSSESETEVDILT
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
186UbiquitinationIRLKSLGKEEGPQEN
CCHHHCCCCCCCCCC
58.8630230243
202PhosphorylationRQNADNLSGTLLLKR
CCCCCCCCHHHHHHH
35.6722210691
204PhosphorylationNADNLSGTLLLKRKA
CCCCCCHHHHHHHHH
15.7422210691
246PhosphorylationALDPTVLSPPSLYPS
CCCCCCCCCHHHCCC
30.3524719451
253PhosphorylationSPPSLYPSVDKHLLP
CCHHHCCCCCHHHCC
29.4124719451
280PhosphorylationGICTSKPSSILSGSS
CCCCCCCCHHCCCCC
33.4728111955
281PhosphorylationICTSKPSSILSGSSS
CCCCCCCHHCCCCCC
35.7628111955
284PhosphorylationSKPSSILSGSSSVPA
CCCCHHCCCCCCCCC
34.6528111955
286PhosphorylationPSSILSGSSSVPATP
CCHHCCCCCCCCCCC
18.9628111955
287PhosphorylationSSILSGSSSVPATPG
CHHCCCCCCCCCCCC
38.5928111955
288PhosphorylationSILSGSSSVPATPGR
HHCCCCCCCCCCCCH
33.5428111955
292PhosphorylationGSSSVPATPGRRLWR
CCCCCCCCCCHHHHH
21.8728111955
335PhosphorylationGLGKTGGSRKRSPEV
CCCCCCCCCCCCCCC
35.6519664995
375PhosphorylationCWEVVQETPLKNTQD
CCEEHCCCCCCCCCC
19.4824275569
380PhosphorylationQETPLKNTQDSPQIP
CCCCCCCCCCCCCCC
31.9724275569
420PhosphorylationRTELCQDSPMCTKLQ
HHHHHCCCCCHHHHH
6.67-
486PhosphorylationEAEEYRITSAAATSE
CCCCCCCCCHHHCHH
11.87-
487PhosphorylationAEEYRITSAAATSEL
CCCCCCCCHHHCHHH
17.34-
671PhosphorylationLLGSLPASSEEEEID
HCCCCCCCCCCCCCC
36.02-
672PhosphorylationLGSLPASSEEEEIDV
CCCCCCCCCCCCCCE
51.65-

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 BTBDI_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BTBDI_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 BTBDI_HUMAN !!

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

Oops, there are no PPI records of BTBDI_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BTBDI_HUMAN

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Related Literatures of Post-Translational Modification

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