ID RNF17_HUMAN Reviewed; 1623 AA. AC Q9BXT8; Q5T2J9; Q6P1W3; Q9BXT7; Q9NUY9; DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 3. DT 24-JAN-2024, entry version 177. DE RecName: Full=RING finger protein 17; DE AltName: Full=Tudor domain-containing protein 4; GN Name=RNF17; Synonyms=TDRD4; 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] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Testis; RX PubMed=11279525; DOI=10.1038/86927; RA Wang P.J., McCarrey J.R., Yang F., Page D.C.; RT "An abundance of X-linked genes expressed in spermatogonia."; RL Nat. Genet. 27:422-426(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 765-1623 (ISOFORM 5), AND VARIANT RP LYS-1380. RC TISSUE=Testis; 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). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 914-1623 (ISOFORM 4), AND VARIANT RP LYS-1380. RC TISSUE=Placenta; 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 [5] RP STRUCTURE BY NMR OF 949-1026. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the tudor domain of tudor domain-containing protein RT 4."; RL Submitted (OCT-2007) to the PDB data bank. CC -!- FUNCTION: Seems to be involved in regulation of transcriptional CC activity of MYC. In vitro, inhibits DNA-binding activity of Mad-MAX CC heterodimers. Can recruit Mad transcriptional repressors (MXD1, MXD3, CC MXD4 and MXI1) to the cytoplasm. May be involved in spermiogenesis (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with MXD1, MXD3, MXD4, MXI1 and PIWIL1. Self- CC associates (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. CC Note=Predominantly found in the cytoplasm. Component of a nuage in male CC germ cells (an electron-dense spherical cytoplasmic body present in CC late pachytene and diplotene spermatocytes and in elonging spermatids) CC (By similarity). {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q9BXT8-3; Sequence=Displayed; CC Name=2; CC IsoId=Q9BXT8-1; Sequence=VSP_033073, VSP_033074; CC Name=3; CC IsoId=Q9BXT8-2; Sequence=VSP_005753, VSP_005754; CC Name=4; CC IsoId=Q9BXT8-4; Sequence=VSP_033076; CC Name=5; CC IsoId=Q9BXT8-5; Sequence=VSP_033075; CC -!- TISSUE SPECIFICITY: Testis specific. CC -!- SEQUENCE CAUTION: CC Sequence=AAH64847.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAA91972.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF285602; AAK31981.1; -; mRNA. DR EMBL; AF285603; AAK31982.1; -; mRNA. DR EMBL; AL354798; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL391560; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC064847; AAH64847.1; ALT_INIT; mRNA. DR EMBL; AK001907; BAA91972.1; ALT_INIT; mRNA. DR CCDS; CCDS9308.2; -. [Q9BXT8-3] DR RefSeq; NP_112567.2; NM_031277.2. [Q9BXT8-3] DR PDB; 2EQK; NMR; -; A=949-1026. DR PDBsum; 2EQK; -. DR AlphaFoldDB; Q9BXT8; -. DR SMR; Q9BXT8; -. DR BioGRID; 121096; 9. DR IntAct; Q9BXT8; 3. DR MINT; Q9BXT8; -. DR STRING; 9606.ENSP00000255324; -. DR GlyGen; Q9BXT8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BXT8; -. DR PhosphoSitePlus; Q9BXT8; -. DR BioMuta; RNF17; -. DR DMDM; 187608889; -. DR EPD; Q9BXT8; -. DR jPOST; Q9BXT8; -. DR MassIVE; Q9BXT8; -. DR MaxQB; Q9BXT8; -. DR PaxDb; 9606-ENSP00000255324; -. DR PeptideAtlas; Q9BXT8; -. DR ProteomicsDB; 79511; -. [Q9BXT8-3] DR ProteomicsDB; 79512; -. [Q9BXT8-1] DR ProteomicsDB; 79513; -. [Q9BXT8-2] DR ProteomicsDB; 79514; -. [Q9BXT8-4] DR ProteomicsDB; 79515; -. [Q9BXT8-5] DR Antibodypedia; 22496; 93 antibodies from 19 providers. DR DNASU; 56163; -. DR Ensembl; ENST00000255324.10; ENSP00000255324.5; ENSG00000132972.19. [Q9BXT8-3] DR Ensembl; ENST00000255325.6; ENSP00000255325.6; ENSG00000132972.19. [Q9BXT8-1] DR GeneID; 56163; -. DR KEGG; hsa:56163; -. DR MANE-Select; ENST00000255324.10; ENSP00000255324.5; NM_031277.3; NP_112567.2. DR UCSC; uc001upr.4; human. [Q9BXT8-3] DR AGR; HGNC:10060; -. DR CTD; 56163; -. DR DisGeNET; 56163; -. DR GeneCards; RNF17; -. DR HGNC; HGNC:10060; RNF17. DR HPA; ENSG00000132972; Tissue enriched (testis). DR MalaCards; RNF17; -. DR MIM; 605793; gene. DR neXtProt; NX_Q9BXT8; -. DR OpenTargets; ENSG00000132972; -. DR PharmGKB; PA34424; -. DR VEuPathDB; HostDB:ENSG00000132972; -. DR eggNOG; KOG2039; Eukaryota. DR eggNOG; KOG2279; Eukaryota. DR GeneTree; ENSGT00940000157559; -. DR HOGENOM; CLU_003202_1_0_1; -. DR InParanoid; Q9BXT8; -. DR OMA; TMQWSKK; -. DR OrthoDB; 3152325at2759; -. DR PhylomeDB; Q9BXT8; -. DR PathwayCommons; Q9BXT8; -. DR SignaLink; Q9BXT8; -. DR SIGNOR; Q9BXT8; -. DR BioGRID-ORCS; 56163; 13 hits in 1182 CRISPR screens. DR ChiTaRS; RNF17; human. DR EvolutionaryTrace; Q9BXT8; -. DR GenomeRNAi; 56163; -. DR Pharos; Q9BXT8; Tbio. DR PRO; PR:Q9BXT8; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q9BXT8; Protein. DR Bgee; ENSG00000132972; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 114 other cell types or tissues. DR ExpressionAtlas; Q9BXT8; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007286; P:spermatid development; IEA:Ensembl. DR CDD; cd20414; Tudor_TDRD4_rpt1; 1. DR CDD; cd20415; Tudor_TDRD4_rpt2; 1. DR CDD; cd20416; Tudor_TDRD4_rpt3; 1. DR CDD; cd20417; Tudor_TDRD4_rpt4; 1. DR CDD; cd20418; Tudor_TDRD4_rpt5; 1. DR Gene3D; 2.30.30.140; -; 5. DR Gene3D; 2.40.50.90; -; 4. DR InterPro; IPR039117; RNF17. DR InterPro; IPR047845; RNF17-like_TUDOR_rpt1. DR InterPro; IPR047847; RNF17-like_TUDOR_rpt2. DR InterPro; IPR047848; RNF17-like_TUDOR_rpt3. DR InterPro; IPR047849; RNF17-like_TUDOR_rpt4. DR InterPro; IPR047850; RNF17-like_TUDOR_rpt5. DR InterPro; IPR035437; SNase_OB-fold_sf. DR InterPro; IPR002999; Tudor. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR16442; RING FINGER PROTEIN 17; 1. DR PANTHER; PTHR16442:SF1; RING FINGER PROTEIN 17; 1. DR Pfam; PF00567; TUDOR; 5. DR SMART; SM00333; TUDOR; 4. DR SUPFAM; SSF57850; RING/U-box; 1. DR SUPFAM; SSF50199; Staphylococcal nuclease; 1. DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 5. DR PROSITE; PS50304; TUDOR; 4. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; Q9BXT8; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Developmental protein; Differentiation; Metal-binding; Nucleus; KW Reference proteome; Repeat; Spermatogenesis; Zinc; Zinc-finger. FT CHAIN 1..1623 FT /note="RING finger protein 17" FT /id="PRO_0000183165" FT DOMAIN 726..784 FT /note="Tudor 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211" FT DOMAIN 962..1021 FT /note="Tudor 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211" FT DOMAIN 1228..1285 FT /note="Tudor 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211" FT DOMAIN 1479..1539 FT /note="Tudor 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211" FT ZN_FING 32..75 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1438..1462 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 234 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99MV7" FT VAR_SEQ 414..449 FT /note="SSAELVFVSHVIDPCHFYIRKYSQIKDAKVLEKKVN -> TCGTDDLGETPR FT YPKKPLQKNSSVPFGSKADTVTTV (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11279525" FT /id="VSP_005753" FT VAR_SEQ 450..1623 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11279525" FT /id="VSP_005754" FT VAR_SEQ 651..653 FT /note="FKS -> DLI (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11279525" FT /id="VSP_033073" FT VAR_SEQ 654..1623 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11279525" FT /id="VSP_033074" FT VAR_SEQ 1320..1325 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_033075" FT VAR_SEQ 1326..1368 FT /note="ELPKNPWEKLSIHLYFDGMSLSYFMAYYKYCTSEHTEEMLKEK -> K (in FT isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_033076" FT VARIANT 346 FT /note="K -> N (in dbSNP:rs1451568)" FT /id="VAR_024613" FT VARIANT 467 FT /note="G -> S (in dbSNP:rs9581180)" FT /id="VAR_028132" FT VARIANT 501 FT /note="S -> G (in dbSNP:rs9507413)" FT /id="VAR_028133" FT VARIANT 573 FT /note="A -> P (in dbSNP:rs10161760)" FT /id="VAR_052098" FT VARIANT 667 FT /note="H -> R (in dbSNP:rs9511451)" FT /id="VAR_052099" FT VARIANT 1110 FT /note="N -> K (in dbSNP:rs3783082)" FT /id="VAR_052100" FT VARIANT 1380 FT /note="E -> K (in dbSNP:rs9507425)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_052101" FT CONFLICT 361 FT /note="P -> S (in Ref. 1; AAK31981)" FT /evidence="ECO:0000305" FT HELIX 949..955 FT /evidence="ECO:0007829|PDB:2EQK" FT STRAND 968..972 FT /evidence="ECO:0007829|PDB:2EQK" FT STRAND 974..976 FT /evidence="ECO:0007829|PDB:2EQK" FT STRAND 979..987 FT /evidence="ECO:0007829|PDB:2EQK" FT STRAND 989..996 FT /evidence="ECO:0007829|PDB:2EQK" FT TURN 998..1000 FT /evidence="ECO:0007829|PDB:2EQK" FT STRAND 1003..1007 FT /evidence="ECO:0007829|PDB:2EQK" FT TURN 1008..1010 FT /evidence="ECO:0007829|PDB:2EQK" FT STRAND 1011..1013 FT /evidence="ECO:0007829|PDB:2EQK" FT HELIX 1016..1019 FT /evidence="ECO:0007829|PDB:2EQK" SQ SEQUENCE 1623 AA; 184643 MW; 3E710E6DD706CDF9 CRC64; MAAEASKTGP SRSSYQRMGR KSQPWGAAEI QCTRCGRRVS RSSGHHCELQ CGHAFCELCL LMTEECTTII CPDCEVATAV NTRQRYYPMA GYIKEDSIME KLQPKTIKNC SQDFKKTADQ LTTGLERSAS TDKTLLNSSA VMLDTNTAEE IDEALNTAHH SFEQLSIAGK ALEHMQKQTI EERERVIEVV EKQFDQLLAF FDSRKKNLCE EFARTTDDYL SNLIKAKSYI EEKKNNLNAA MNIARALQLS PSLRTYCDLN QIIRTLQLTS DSELAQVSSP QLRNPPRLSV NCSEIICMFN NMGKIEFRDS TKCYPQENEI RQNVQKKYNN KKELSCYDTY PPLEKKKVDM SVLTSEAPPP PLQPETNDVH LEAKNFQPQK DVATASPKTI AVLPQMGSSP DVIIEEIIED NVESSAELVF VSHVIDPCHF YIRKYSQIKD AKVLEKKVNE FCNRSSHLDP SDILELGARI FVSSIKNGMW CRGTITELIP IEGRNTRKPC SPTRLFVHEV ALIQIFMVDF GNSEVLIVTG VVDTHVRPEH SAKQHIALND LCLVLRKSEP YTEGLLKDIQ PLAQPCSLKD IVPQNSNEGW EEEAKVEFLK MVNNKAVSMK VFREEDGVLI VDLQKPPPNK ISSDMPVSLR DALVFMELAK FKSQSLRSHF EKNTTLHYHP PILPKEMTDV SVTVCHINSP GDFYLQLIEG LDILFLLKTI EEFYKSEDGE NLEILCPVQD QACVAKFEDG IWYRAKVIGL PGHQEVEVKY VDFGNTAKIT IKDVRKIKDE FLNAPEKAIK CKLAYIEPYK RTMQWSKEAK EKFEEKAQDK FMTCSVIKIL EDNVLLVELF DSLGAPEMTT TSINDQLVKE GLASYEIGYI LKDNSQKHIE VWDPSPEEII SNEVHNLNPV SAKSLPNENF QSLYNKELPV HICNVISPEK IYVQWLLTEN LLNSLEEKMI AAYENSKWEP VKWENDMHCA VKIQDKNQWR RGQIIRMVTD TLVEVLLYDV GVELVVNVDC LRKLEENLKT MGRLSLECSL VDIRPAGGSD KWTATACDCL SLYLTGAVAT IILQVDSEEN NTTWPLPVKI FCRDEKGERV DVSKYLIKKG LALRERRINN LDNSHSLSEK SLEVPLEQED SVVTNCIKTN FDPDKKTADI ISEQKVSEFQ EKILEPRTTR GYKPPAIPNM NVFEATVSCV GDDGTIFVVP KLSEFELIKM TNEIQSNLKC LGLLEPYFWK KGEACAVRGS DTLWYRGKVM EVVGGAVRVQ YLDHGFTEKI PQCHLYPILL YPDIPQFCIP CQLHNTTPVG NVWQPDAIEV LQQLLSKRQV DIHIMELPKN PWEKLSIHLY FDGMSLSYFM AYYKYCTSEH TEEMLKEKPR SDHDKKYEEE QWEIRFEELL SAETDTPLLP PYLSSSLPSP GELYAVQVKH VVSPNEVYIC LDSIETSNQS NQHSDTDDSG VSGESESESL DEALQRVNKK VEALPPLTDF RTEMPCLAEY DDGLWYRAKI VAIKEFNPLS ILVQFVDYGS TAKLTLNRLC QIPSHLMRYP ARAIKVLLAG FKPPLRDLGE TRIPYCPKWS MEALWAMIDC LQGKQLYAVS MAPAPEQIVT LYDDEQHPVH MPLVEMGLAD KDE //