ASZ1_HUMAN - dbPTM
ASZ1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASZ1_HUMAN
UniProt AC Q8WWH4
Protein Name Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1
Gene Name ASZ1 {ECO:0000312|HGNC:HGNC:1350}
Organism Homo sapiens (Human).
Sequence Length 475
Subcellular Localization Cytoplasm. Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Specifically localizes to pi-bodies, a subset of the nuage which contains primary piRNAs (By simil
Protein Description Plays a central role during spermatogenesis by repressing 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. Its association with pi-bodies suggests a participation in the primary piRNAs metabolic process. Required prior to the pachytene stage to facilitate the production of multiple types of piRNAs, including those associated with repeats involved in the regulation of retrotransposons. May act by mediating protein-protein interactions during germ cell maturation (By similarity)..
Protein Sequence MAASALRGLPVAGGGESSESEDDGWEIGYLDRTSQKLKRLLPIEEKKEKFKKAMTIGDVSLVQELLDSGISVDSNFQYGWTPLMYAASVANAELVRVLLDRGANASFEKDKQSILITACSAHGSEEQILKCVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKMLQTKDGKMPSEIAKRNKHHEIFNLLSFTLNPLEGKLQQLTKEDTICKILTTDSDREKDHIFSSYTAFGDLEVFLHGLGLEHMTDLLKERDITLRHLLTMREDEFTKNGITSKDQQKILAALKELQVEEIQFGELSEETKLEISGDEFLNFLLKLNKQCGHLITAVQNVITELPVNSQKITLEWASPQNFTSVCEELVNNVEDLSEKVCKLKDLIQKLQNERENDPTHIQLREEVSTWNSRILKRTAITICGFGFLLFICKLTFQRK
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
17PhosphorylationPVAGGGESSESEDDG
CCCCCCCCCCCCCCC
42.55-
18PhosphorylationVAGGGESSESEDDGW
CCCCCCCCCCCCCCC
40.62-
20PhosphorylationGGGESSESEDDGWEI
CCCCCCCCCCCCCCC
48.55-
151PhosphorylationVACRRLMTPIMYAAR
HHHHHHHCHHHHHHC
17.7925690035
155PhosphorylationRLMTPIMYAARDGHT
HHHCHHHHHHCCCCH
9.6025690035
216AcetylationMLQTKDGKMPSEIAK
HCCCCCCCCHHHHHH
58.747685219
372PhosphorylationKQCGHLITAVQNVIT
HHHCHHHHHHHHHHH
27.4324043423
379PhosphorylationTAVQNVITELPVNSQ
HHHHHHHHHCCCCCE
27.4724043423
385PhosphorylationITELPVNSQKITLEW
HHHCCCCCEEEEEEE
32.8424043423

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 ASZ1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASZ1_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 ASZ1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TS101_HUMANTSG101physical
21880841

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ASZ1_HUMAN

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Related Literatures of Post-Translational Modification

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