RNF17_HUMAN
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 03-AUG-2022, entry version 169.
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};
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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; 7.
DR IntAct; Q9BXT8; 4.
DR MINT; Q9BXT8; -.
DR STRING; 9606.ENSP00000255324; -.
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; Q9BXT8; -.
DR PeptideAtlas; Q9BXT8; -.
DR PRIDE; 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; 75 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 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; FYVRYVA; -.
DR PhylomeDB; Q9BXT8; -.
DR PathwayCommons; Q9BXT8; -.
DR SignaLink; Q9BXT8; -.
DR BioGRID-ORCS; 56163; 10 hits in 1104 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 right testis and 112 other tissues.
DR ExpressionAtlas; Q9BXT8; baseline and differential.
DR Genevisible; Q9BXT8; HS.
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; cd04508; TUDOR; 4.
DR Gene3D; 2.40.50.90; -; 4.
DR InterPro; IPR039117; RNF17.
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; PTHR16442; 1.
DR Pfam; PF00567; TUDOR; 5.
DR SMART; SM00333; TUDOR; 4.
DR SUPFAM; SSF50199; SSF50199; 1.
DR PROSITE; PS50304; TUDOR; 4.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
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
