PIWIL1
entrez
9271
canonical
uniprot
Q96J94
canonical
ensembl
ENSG00000125207
resolver
ensembl
ENSG00000275051
resolver
ensp
ENSP00000245255
resolver
genesymbol
PIWIL1
resolver
genesymbol_syn
HIWI
resolver
hgnc
HGNC:9007
resolver
uniprot
A4F266
resolver
uniprot
O95404
resolver
uniprot
Q8NA60
resolver
uniprot
Q8TBY5
resolver
uniprot
Q96JD5
resolver
uniprot_entry
PIWL1_HUMAN
resolver
uniprot_sec
A4F266
resolver
uniprot_sec
O95404
resolver
uniprot_sec
Q8NA60
resolver
uniprot_sec
Q8TBY5
resolver
uniprot_sec
Q96JD5
resolver
amino_acid_sequence
MTGRARARARGRARGQETAQLVGSTASQQPGYIQPRPQPPPAEGELFGRGRQRGTAGGTAKSQGLQISAGFQELSLAERGGRRRDFHDLGVNTRQNLDHVKESKTGSSGIIVRLSTNHFRLTSRPQWALYQYHIDYNPLMEARRLRSALLFQHEDLIGKCHAFDGTILFLPKRLQQKVTEVFSKTRNGEDVRITITLTNELPPTSPTCLQFYNIIFRRLLKIMNLQQIGRNYYNPNDPIDIPSHRLVIWPGFTTSILQYENSIMLCTDVSHKVLRSETVLDFMFNFYHQTEEHKFQEQVSKELIGLVVLTKYNNKTYRVDDIDWDQNPKSTFKKADGSEVSFLEYYRKQYNQEITDLKQPVLVSQPKRRRGPGGTLPGPAMLIPELCYLTGLTDKMRNDFNVMKDLAVHTRLTPEQRQREVGRLIDYIHKNDNVQRELRDWGLSFDSNLLSFSGRILQTEKIHQGGKTFDYNPQFADWSKETRGAPLISVKPLDNWLLIYTRRNYEAANSLIQNLFKVTPAMGMQMRKAIMIEVDDRTEAYLRVLQQKVTADTQIVVCLLSSNRKDKYDAIKKYLCTDCPTPSQCVVARTLGKQQTVMAIATKIALQMNCKMGGELWRVDIPLKLVMIVGIDCYHDMTAGRRSIAGFVASINEGMTRWFSRCIFQDRGQELVDGLKVCLQAALRAWNSCNEYMPSRIIVYRDGVGDGQLKTLVNYEVPQFLDCLKSIGRGYNPRLTVIVVKKRVNTRFFAQSGGRLQNPLPGTVIDVEVTRPEWYDFFIVSQAVRSGSVSPTHYNVIYDNSGLKPDHIQRLTYKLCHIYYNWPGVIRVPAPCQYAHKLAFLVGQSIHREPNLSLSNRLYYL
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in PIWIL1 may be a cause of a disorder resulting in the absence of sperm (azoospermia) in the semen, leading to male infertility. Male sterility can be caused by defects in ubiquitination and degradation during late spermatogenesis. {ECO:0000269|PubMed:28552346}.
uniprot
proteins
ec_number
3.1.26.-
uniprot
proteins
function
FUNCTION: Endoribonuclease that plays a central role in postnatal germ cells 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. Directly binds methylated piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. Strongly prefers a uridine in the first position of their guide (g1U preference, also named 1U-bias). Not involved in the piRNA amplification loop, also named ping-pong amplification cycle. Acts as an endoribonuclease that cleaves transposon messenger RNAs. Besides their function in transposable elements repression, piRNAs are probably involved in other processes during meiosis such as translation regulation. Probable component of some RISC complex, which mediates RNA cleavage and translational silencing. Also plays a role in the formation of chromatoid bodies and is required for some miRNAs stability. Required to sequester RNF8 in the cytoplasm until late spermatogenesis; RNF8 being released upon ubiquitination and degradation of PIWIL1. {ECO:0000250|UniProtKB:Q9JMB7}.; FUNCTION: [Isoform 3]: May be a negative developmental regulator (PubMed:12037681, PubMed:16287078). {ECO:0000269|PubMed:12037681, ECO:0000269|PubMed:16287078}.
uniprot
proteins
mass_dalton
98603
uniprot
proteins
mutagenesis
MUTAGEN 379; /note="P->H: Impairs binding to 2'-O-methylated 3'-end of piRNAs; when associated with Y-381."; /evidence="ECO:0000269|PubMed:21193640"; MUTAGEN 381; /note="M->Y: Impairs binding to 2'-O-methylated 3'-end of piRNAs; when associated with H-379."; /evidence="ECO:0000269|PubMed:21193640
uniprot
proteins
post_translational_modification
PTM: Arginine methylation by PRMT5 is required for the interaction with Tudor domain-containing protein (TDRD1, TDRKH/TDRD2, RNF17/TDRD4, TDRD6, TDRD7 and TDRD9) and subsequent localization to the meiotic nuage, also named P granule. {ECO:0000250|UniProtKB:Q9JMB7}.; PTM: Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) in late spermatids, leading to its degradation (PubMed:28552346). Ubiquitination only takes place following piRNA-binding in adult testis (By similarity). Ubiquitination and degradation in late spermatogenesis by APC/C is probably required to release RNF8 from the cytoplasm and promote histone to protamine exchange by RNF8 (By similarity). {ECO:0000250|UniProtKB:Q9JMB7, ECO:0000305|PubMed:28552346}.
uniprot
proteins
protein_family
Argonaute family
uniprot
proteins
protein_family
Piwi subfamily
uniprot
proteins
pubmed
11154219
uniprot
proteins
pubmed
12037681
uniprot
proteins
pubmed
12906857
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14749716
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16287078
uniprot
proteins
pubmed
17544373
uniprot
proteins
pubmed
21193640
uniprot
proteins
pubmed
21465557
uniprot
proteins
pubmed
23436708
uniprot
proteins
pubmed
28552346
uniprot
proteins
sequence_length
861
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9JMB7}. Note=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. {ECO:0000250|UniProtKB:Q9JMB7}.
uniprot
proteins