ASZ1_HUMAN
ID ASZ1_HUMAN Reviewed; 475 AA.
AC Q8WWH4; A0AV27; A4D0V0; B7ZM20;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1;
DE AltName: Full=Ankyrin-like protein 1;
DE AltName: Full=Germ cell-specific ankyrin, SAM and basic leucine zipper domain-containing protein;
GN Name=ASZ1 {ECO:0000312|HGNC:HGNC:1350};
GN Synonyms=ALP1, ANKL1, C7orf7, GASZ {ECO:0000312|EMBL:AAL68815.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Ovary {ECO:0000269|PubMed:12040005}, and
RC Testis {ECO:0000269|PubMed:12040005};
RX PubMed=12040005; DOI=10.1210/mend.16.6.0864;
RA Yan W., Rajkovic A., Viveiros M.M., Burns K.H., Eppig J.J., Matzuk M.M.;
RT "Identification of Gasz, an evolutionarily conserved gene expressed
RT exclusively in germ cells and encoding a protein with four ankyrin repeats,
RT a sterile-alpha motif, and a basic leucine zipper.";
RL Mol. Endocrinol. 16:1168-1184(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Plays a central role during spermatogenesis by repressing
CC transposable elements and preventing their mobilization, which is
CC essential for the germline integrity. Acts via the piRNA metabolic
CC process, which mediates the repression of transposable elements during
CC meiosis by forming complexes composed of piRNAs and Piwi proteins and
CC governs the methylation and subsequent repression of transposons. Its
CC association with pi-bodies suggests a participation in the primary
CC piRNAs metabolic process. Required prior to the pachytene stage to
CC facilitate the production of multiple types of piRNAs, including those
CC associated with repeats involved in the regulation of retrotransposons.
CC May act by mediating protein-protein interactions during germ cell
CC maturation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DDX4, PIWIL1, RANBP9 and TDRD1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8WWH4; O15155: BET1; NbExp=3; IntAct=EBI-12239061, EBI-749204;
CC Q8WWH4; Q9H1M4: DEFB127; NbExp=3; IntAct=EBI-12239061, EBI-10305240;
CC Q8WWH4; Q9UBY5: LPAR3; NbExp=3; IntAct=EBI-12239061, EBI-12033434;
CC Q8WWH4; Q8N912: NRAC; NbExp=3; IntAct=EBI-12239061, EBI-12051377;
CC Q8WWH4; P78382: SLC35A1; NbExp=3; IntAct=EBI-12239061, EBI-12870360;
CC Q8WWH4; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-12239061, EBI-12188413;
CC Q8WWH4; A2RU14: TMEM218; NbExp=3; IntAct=EBI-12239061, EBI-10173151;
CC Q8WWH4; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-12239061, EBI-12111910;
CC Q8WWH4; O14798: TNFRSF10C; NbExp=3; IntAct=EBI-12239061, EBI-717441;
CC Q8WWH4; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-12239061, EBI-12195249;
CC Q8WWH4; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=4; IntAct=EBI-12239061, EBI-25492395;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Component of the
CC meiotic nuage, also named P granule, a germ-cell-specific organelle
CC required to repress transposon activity during meiosis. Specifically
CC localizes to pi-bodies, a subset of the nuage which contains primary
CC piRNAs (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WWH4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WWH4-2; Sequence=VSP_056918;
CC -!- TISSUE SPECIFICITY: Expressed exclusively in the testis and ovary and
CC at higher levels in the adult testis compared with the adult ovary.
CC {ECO:0000269|PubMed:12040005}.
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DR EMBL; AF461259; AAL68815.1; -; mRNA.
DR EMBL; AK093445; BAC04167.1; -; mRNA.
DR EMBL; CH236947; EAL24354.1; -; Genomic_DNA.
DR EMBL; BC126186; AAI26187.1; -; mRNA.
DR EMBL; BC126188; AAI26189.1; -; mRNA.
DR EMBL; BC144212; AAI44213.1; -; mRNA.
DR CCDS; CCDS5772.1; -. [Q8WWH4-1]
DR RefSeq; NP_001288750.1; NM_001301821.1. [Q8WWH4-2]
DR RefSeq; NP_001288751.1; NM_001301822.1.
DR RefSeq; NP_570124.1; NM_130768.2. [Q8WWH4-1]
DR AlphaFoldDB; Q8WWH4; -.
DR SMR; Q8WWH4; -.
DR BioGRID; 126466; 12.
DR IntAct; Q8WWH4; 11.
DR STRING; 9606.ENSP00000284629; -.
DR iPTMnet; Q8WWH4; -.
DR PhosphoSitePlus; Q8WWH4; -.
DR BioMuta; ASZ1; -.
DR DMDM; 34921898; -.
DR EPD; Q8WWH4; -.
DR MassIVE; Q8WWH4; -.
DR PaxDb; Q8WWH4; -.
DR PeptideAtlas; Q8WWH4; -.
DR PRIDE; Q8WWH4; -.
DR ProteomicsDB; 74886; -. [Q8WWH4-1]
DR Antibodypedia; 17481; 154 antibodies from 25 providers.
DR DNASU; 136991; -.
DR Ensembl; ENST00000284629.7; ENSP00000284629.2; ENSG00000154438.8. [Q8WWH4-1]
DR GeneID; 136991; -.
DR KEGG; hsa:136991; -.
DR MANE-Select; ENST00000284629.7; ENSP00000284629.2; NM_130768.3; NP_570124.1.
DR UCSC; uc003vjb.2; human. [Q8WWH4-1]
DR CTD; 136991; -.
DR DisGeNET; 136991; -.
DR GeneCards; ASZ1; -.
DR HGNC; HGNC:1350; ASZ1.
DR HPA; ENSG00000154438; Tissue enriched (testis).
DR MIM; 605797; gene.
DR neXtProt; NX_Q8WWH4; -.
DR OpenTargets; ENSG00000154438; -.
DR PharmGKB; PA25950; -.
DR VEuPathDB; HostDB:ENSG00000154438; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00880000138051; -.
DR HOGENOM; CLU_053259_0_0_1; -.
DR InParanoid; Q8WWH4; -.
DR OMA; RHLLTMK; -.
DR OrthoDB; 1428188at2759; -.
DR PhylomeDB; Q8WWH4; -.
DR TreeFam; TF352216; -.
DR PathwayCommons; Q8WWH4; -.
DR Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR SignaLink; Q8WWH4; -.
DR BioGRID-ORCS; 136991; 8 hits in 1066 CRISPR screens.
DR ChiTaRS; ASZ1; human.
DR GeneWiki; ASZ1; -.
DR GenomeRNAi; 136991; -.
DR Pharos; Q8WWH4; Tbio.
DR PRO; PR:Q8WWH4; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8WWH4; protein.
DR Bgee; ENSG00000154438; Expressed in right testis and 65 other tissues.
DR ExpressionAtlas; Q8WWH4; baseline and differential.
DR Genevisible; Q8WWH4; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0071546; C:pi-body; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0007140; P:male meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR CDD; cd09521; SAM_ASZ1; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR042650; Asz1_SAM.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cytoplasm; Developmental protein;
KW Differentiation; Meiosis; Phosphoprotein; Reference proteome; Repeat;
KW RNA-mediated gene silencing; Spermatogenesis.
FT CHAIN 1..475
FT /note="Ankyrin repeat, SAM and basic leucine zipper domain-
FT containing protein 1"
FT /id="PRO_0000066969"
FT REPEAT 45..74
FT /note="ANK 1"
FT /evidence="ECO:0000305"
FT REPEAT 78..107
FT /note="ANK 2"
FT /evidence="ECO:0000305"
FT REPEAT 110..144
FT /note="ANK 3"
FT /evidence="ECO:0000305"
FT REPEAT 148..177
FT /note="ANK 4"
FT /evidence="ECO:0000305"
FT REPEAT 181..210
FT /note="ANK 5"
FT /evidence="ECO:0000305"
FT REPEAT 214..243
FT /note="ANK 6"
FT /evidence="ECO:0000305"
FT DOMAIN 272..334
FT /note="SAM"
FT /evidence="ECO:0000305"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD46"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD46"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD46"
FT VAR_SEQ 388..396
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056918"
FT VARIANT 216
FT /note="K -> T (in dbSNP:rs1029396)"
FT /id="VAR_024175"
SQ SEQUENCE 475 AA; 53458 MW; 71B317BC07080434 CRC64;
MAASALRGLP VAGGGESSES EDDGWEIGYL DRTSQKLKRL LPIEEKKEKF KKAMTIGDVS
LVQELLDSGI SVDSNFQYGW TPLMYAASVA NAELVRVLLD RGANASFEKD KQSILITACS
AHGSEEQILK CVELLLSRNA DPNVACRRLM TPIMYAARDG HTQVVALLVA HGAEVNTQDE
NGYTALTWAA RQGHKNIVLK LLELGANKML QTKDGKMPSE IAKRNKHHEI FNLLSFTLNP
LEGKLQQLTK EDTICKILTT DSDREKDHIF SSYTAFGDLE VFLHGLGLEH MTDLLKERDI
TLRHLLTMRE DEFTKNGITS KDQQKILAAL KELQVEEIQF GELSEETKLE ISGDEFLNFL
LKLNKQCGHL ITAVQNVITE LPVNSQKITL EWASPQNFTS VCEELVNNVE DLSEKVCKLK
DLIQKLQNER ENDPTHIQLR EEVSTWNSRI LKRTAITICG FGFLLFICKL TFQRK
