DZIP3_HUMAN
ID DZIP3_HUMAN Reviewed; 1208 AA.
AC Q86Y13; B3KN01; O75162; Q6P3R9; Q6PH82; Q86Y14; Q86Y15; Q86Y16; Q8IWI0;
AC Q96RS9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=E3 ubiquitin-protein ligase DZIP3;
DE EC=2.3.2.27 {ECO:0000269|PubMed:12538761};
DE AltName: Full=DAZ-interacting protein 3;
DE AltName: Full=RING-type E3 ubiquitin transferase DZIP3 {ECO:0000305};
DE AltName: Full=RNA-binding ubiquitin ligase of 138 kDa;
DE Short=hRUL138;
GN Name=DZIP3; Synonyms=KIAA0675;
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 (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, RNA-BINDING, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 662-LYS--LYS-666 AND CYS-1187.
RC TISSUE=Liver, and Uterus;
RX PubMed=12538761; DOI=10.1242/jcs.00261;
RA Kreft S.G., Nassal M.;
RT "hRUL138, a novel human RNA-binding RING-H2 ubiquitin-protein ligase.";
RL J. Cell Sci. 116:605-616(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin, and 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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 641-1208, AND INTERACTION WITH DAZ.
RX PubMed=12511597; DOI=10.1073/pnas.0234478100;
RA Moore F.L., Jaruzelska J., Fox M.S., Urano J., Firpo M.T., Turek P.J.,
RA Dorfman D.M., Reijo Pera R.A.;
RT "Human Pumilio-2 is expressed in embryonic stem cells and germ cells and
RT interacts with DAZ (Deleted in AZoospermia) and DAZ-like proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:538-543(2003).
CC -!- FUNCTION: E3 Ubiquitin ligase proteins mediate ubiquitination and
CC subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC form of a thioester and then directly transfers the ubiquitin to
CC targeted substrates. Able to specifically bind RNA.
CC {ECO:0000269|PubMed:12538761}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:12538761};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DAZ proteins. {ECO:0000269|PubMed:12511597}.
CC -!- INTERACTION:
CC Q86Y13; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-948630, EBI-541426;
CC Q86Y13; A7KAX9: ARHGAP32; NbExp=3; IntAct=EBI-948630, EBI-308663;
CC Q86Y13; P54253: ATXN1; NbExp=7; IntAct=EBI-948630, EBI-930964;
CC Q86Y13; O95429: BAG4; NbExp=3; IntAct=EBI-948630, EBI-2949658;
CC Q86Y13; Q96MT8: CEP63; NbExp=3; IntAct=EBI-948630, EBI-741977;
CC Q86Y13; Q96EF6: FBXO17; NbExp=3; IntAct=EBI-948630, EBI-2510157;
CC Q86Y13; Q6P1K8: GTF2H2C_2; NbExp=3; IntAct=EBI-948630, EBI-8469755;
CC Q86Y13; P52597: HNRNPF; NbExp=6; IntAct=EBI-948630, EBI-352986;
CC Q86Y13; P31943: HNRNPH1; NbExp=3; IntAct=EBI-948630, EBI-351590;
CC Q86Y13; Q9BUJ2: HNRNPUL1; NbExp=7; IntAct=EBI-948630, EBI-1018153;
CC Q86Y13; P31273: HOXC8; NbExp=3; IntAct=EBI-948630, EBI-1752118;
CC Q86Y13; P78337: PITX1; NbExp=3; IntAct=EBI-948630, EBI-748265;
CC Q86Y13; Q9BQ04: RBM4B; NbExp=4; IntAct=EBI-948630, EBI-715531;
CC Q86Y13; Q63HR2: TNS2; NbExp=3; IntAct=EBI-948630, EBI-949753;
CC Q86Y13; Q9H0E2: TOLLIP; NbExp=2; IntAct=EBI-948630, EBI-74615;
CC Q86Y13; Q96LR5: UBE2E2; NbExp=4; IntAct=EBI-948630, EBI-2129763;
CC Q86Y13; Q8TBK6: ZCCHC10; NbExp=6; IntAct=EBI-948630, EBI-597063;
CC Q86Y13; P17028: ZNF24; NbExp=5; IntAct=EBI-948630, EBI-707773;
CC Q86Y13; Q7L2R6: ZNF765; NbExp=3; IntAct=EBI-948630, EBI-9676069;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12538761}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86Y13-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q86Y13-2; Sequence=VSP_010971, VSP_010972;
CC -!- TISSUE SPECIFICITY: Widely expressed at low level. Highly expressed in
CC skeletal muscle, kidney and heart. Expressed at low level in placenta,
CC lung, brain, liver and pancreas. {ECO:0000269|PubMed:12538761}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39018.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH56674.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAK69484.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA31650.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY227651; AAO72967.1; -; mRNA.
DR EMBL; AY227652; AAO72968.1; -; mRNA.
DR EMBL; AY227653; AAO72969.1; -; Transcribed_RNA.
DR EMBL; AY227654; AAO72970.1; -; mRNA.
DR EMBL; AB014575; BAA31650.2; ALT_INIT; mRNA.
DR EMBL; AK023138; BAG51163.1; -; mRNA.
DR EMBL; BC039018; AAH39018.1; ALT_SEQ; mRNA.
DR EMBL; BC056674; AAH56674.1; ALT_SEQ; mRNA.
DR EMBL; BC063882; AAH63882.1; -; mRNA.
DR EMBL; AF279370; AAK69484.1; ALT_FRAME; mRNA.
DR CCDS; CCDS2952.1; -. [Q86Y13-1]
DR PIR; T00362; T00362.
DR RefSeq; NP_055463.1; NM_014648.3. [Q86Y13-1]
DR RefSeq; XP_005247971.1; XM_005247914.3. [Q86Y13-1]
DR RefSeq; XP_005247972.1; XM_005247915.3. [Q86Y13-1]
DR RefSeq; XP_005247973.1; XM_005247916.3. [Q86Y13-1]
DR RefSeq; XP_005247974.1; XM_005247917.3. [Q86Y13-1]
DR RefSeq; XP_005247975.1; XM_005247918.3. [Q86Y13-1]
DR RefSeq; XP_016863029.1; XM_017007540.1. [Q86Y13-1]
DR AlphaFoldDB; Q86Y13; -.
DR SMR; Q86Y13; -.
DR BioGRID; 115021; 127.
DR IntAct; Q86Y13; 52.
DR MINT; Q86Y13; -.
DR STRING; 9606.ENSP00000355028; -.
DR iPTMnet; Q86Y13; -.
DR PhosphoSitePlus; Q86Y13; -.
DR BioMuta; DZIP3; -.
DR DMDM; 50400482; -.
DR EPD; Q86Y13; -.
DR jPOST; Q86Y13; -.
DR MassIVE; Q86Y13; -.
DR MaxQB; Q86Y13; -.
DR PaxDb; Q86Y13; -.
DR PeptideAtlas; Q86Y13; -.
DR PRIDE; Q86Y13; -.
DR ProteomicsDB; 70350; -. [Q86Y13-1]
DR ProteomicsDB; 70351; -. [Q86Y13-2]
DR Antibodypedia; 32388; 165 antibodies from 21 providers.
DR DNASU; 9666; -.
DR Ensembl; ENST00000361582.8; ENSP00000355028.3; ENSG00000198919.13. [Q86Y13-1]
DR Ensembl; ENST00000463306.1; ENSP00000419981.1; ENSG00000198919.13. [Q86Y13-1]
DR Ensembl; ENST00000495008.5; ENSP00000418871.1; ENSG00000198919.13. [Q86Y13-2]
DR GeneID; 9666; -.
DR KEGG; hsa:9666; -.
DR MANE-Select; ENST00000361582.8; ENSP00000355028.3; NM_014648.4; NP_055463.1.
DR UCSC; uc003dxd.4; human. [Q86Y13-1]
DR CTD; 9666; -.
DR DisGeNET; 9666; -.
DR GeneCards; DZIP3; -.
DR HGNC; HGNC:30938; DZIP3.
DR HPA; ENSG00000198919; Low tissue specificity.
DR MIM; 608672; gene.
DR neXtProt; NX_Q86Y13; -.
DR OpenTargets; ENSG00000198919; -.
DR PharmGKB; PA162384137; -.
DR VEuPathDB; HostDB:ENSG00000198919; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000161692; -.
DR HOGENOM; CLU_007762_0_0_1; -.
DR InParanoid; Q86Y13; -.
DR OMA; GNDPSMM; -.
DR OrthoDB; 67312at2759; -.
DR PhylomeDB; Q86Y13; -.
DR TreeFam; TF333981; -.
DR PathwayCommons; Q86Y13; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q86Y13; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 9666; 11 hits in 1118 CRISPR screens.
DR ChiTaRS; DZIP3; human.
DR GenomeRNAi; 9666; -.
DR Pharos; Q86Y13; Tbio.
DR PRO; PR:Q86Y13; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q86Y13; protein.
DR Bgee; ENSG00000198919; Expressed in bronchial epithelial cell and 202 other tissues.
DR ExpressionAtlas; Q86Y13; baseline and differential.
DR Genevisible; Q86Y13; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019902; F:phosphatase binding; IDA:UniProtKB.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR033103; DZIP3.
DR InterPro; IPR041249; HEPN_DZIP3.
DR InterPro; IPR043866; TTC3/DZIP3_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15727:SF4; PTHR15727:SF4; 1.
DR Pfam; PF19179; DUF5861; 1.
DR Pfam; PF18738; HEPN_DZIP3; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Metal-binding;
KW Reference proteome; RNA-binding; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..1208
FT /note="E3 ubiquitin-protein ligase DZIP3"
FT /id="PRO_0000055898"
FT ZN_FING 1148..1188
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 10..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 14..43
FT /evidence="ECO:0000255"
FT COILED 647..676
FT /evidence="ECO:0000255"
FT COILED 792..853
FT /evidence="ECO:0000255"
FT COILED 904..939
FT /evidence="ECO:0000255"
FT COMPBIAS 10..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 302..303
FT /note="GE -> EF (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_010971"
FT VAR_SEQ 304..1208
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_010972"
FT MUTAGEN 662..666
FT /note="KKKTK->SGSTA: Strongly decreases RNA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:12538761"
FT MUTAGEN 1187
FT /note="C->S: Abolishes ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:12538761"
FT CONFLICT 368
FT /note="D -> G (in Ref. 4; AAH56674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1208 AA; 138604 MW; 76945A63AF85207E CRC64;
MDSLPDEFFV RHPAVEDQRK EETENKLEKS SGQLNKQEND IPTDLVPVNL LLEVKKLLNA
INTLPKGVVP HIKKFLQEDF SFQTMQREVA ANSQNGEEIV PALTLRFLIT QLEAALRNIQ
AGNYTAHQIN IGYYLTLLFL YGVALTERGK KEDYTEAENK FLVMKMMIQE NEICENFMSL
VYFGRGLLRC AQKRYNGGLL EFHKSLQEIG DKNDHWFDID PTEDEDLPTT FKDLLNNFIK
TTESNIMKQT ICSYLDCERS CEADILKNTS YKGFFQLMCS KSCCVYFHKI CWKKFKNLKY
PGENDQSFSG KKCLKEGCTG DMVRMLQCDV PGIVKILFEV VRKDEYITIE NLGASYRKLI
SLKITDTDIR PKISLKFNTK DEMPIFKLDY NYFYHLLHII IISGTDIVRQ IFDEAMPPPL
LKKELLIHKN VLESYYNHLW TNHPLGGSWH LLYPPNKELP QSKQFDLCLL LALIKHLNVF
PAPKKGWNME PPSSDISKSA DILRLCKYRD ILLSEILMNG LTESQFNSIW KKVSDILLRL
GMMQEDIDKV KENPIENISL DYHQLSVYLG IPVPEIIQRM LSCYQQGIAL QSITGSQRIE
IEELQNEEEE LSPPLMEYNI NVKSHPEIQF AEINKDGTSI PSESSTESLK DLQEVKSKQR
KKKKTKNKKN KDSKEDQVPY VVEKEEQLRK EQANPHSVSR LIKDDASDVQ EDSAMEDKFY
SLDELHILDM IEQGSAGKVT TDYGETEKER LARQRQLYKL HYQCEDFKRQ LRTVTFRWQE
NQMQIKKKDK IIASLNQQVA FGINKVSKLQ RQIHAKDNEI KNLKEQLSMK RSQWEMEKHN
LESTMKTYVS KLNAETSRAL TAEVYFLQCR RDFGLLHLEQ TEKECLNQLA RVTHMAASNL
ESLQLKAAVD SWNAIVADVR NKIAFLRTQY NEQINKVKQG FALSTLPPVQ LPPPPPSPEI
LMQQFLGRPL VKESFFRPIL TVPQMPAVCP GVVSATGQPR APLMTGIAWA LPAPVGDAVP
PSAGLRSDPS IMNWERITDR LKTAFPQQTR KELTDFLRKL KDAYGKSLSE LTFDEIVCKI
SQFIDPKKSQ SQGKSVSNVN CVSPSHSPSQ PDAAQPPKPA WRPLTSQGPA TWEGASNPDE
EEEEEEPCVI CHENLSPENL SVLPCAHKFH AQCIRPWLMQ QGTCPTCRLH VLLPEEFPGH
PSRQLPKI
