ZSWM2_HUMAN
ID ZSWM2_HUMAN Reviewed; 633 AA.
AC Q8NEG5; B3KXV6; Q53SI3; Q57ZY3;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=E3 ubiquitin-protein ligase ZSWIM2;
DE EC=2.3.2.27;
DE AltName: Full=MEKK1-related protein X;
DE Short=MEX;
DE AltName: Full=RING-type E3 ubiquitin transferase ZSWIM2;
DE AltName: Full=ZZ-type zinc finger-containing protein 2;
DE AltName: Full=Zinc finger SWIM domain-containing protein 2;
GN Name=ZSWIM2; Synonyms=ZZZ2;
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 [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP STRUCTURE BY NMR OF 208-292.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ZZ domain of zinc finger SWIM domain containing
RT protein 2.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in the regulation of
CC Fas-, DR3- and DR4-mediated apoptosis. Functions in conjunction with
CC the UBE2D1, UBE2D3 and UBE2E1 E2 ubiquitin-conjugating enzymes.
CC {ECO:0000250}.
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;
CC -!- SUBUNIT: Dimer. Interacts with UBE2D1. {ECO:0000250}.
CC -!- DOMAIN: The SWIM-type zinc finger is required for ubiquitination
CC activity. {ECO:0000250}.
CC -!- PTM: Polyubiquitinated. Polyubiquitination is followed by degradation
CC via the proteasome (By similarity). {ECO:0000250}.
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DR EMBL; AK128006; BAG54618.1; -; mRNA.
DR EMBL; AC018735; AAY14907.1; -; Genomic_DNA.
DR EMBL; AC103914; AAX82016.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX10929.1; -; Genomic_DNA.
DR EMBL; BC031094; AAH31094.1; -; mRNA.
DR CCDS; CCDS33348.1; -.
DR RefSeq; NP_872327.2; NM_182521.2.
DR PDB; 2DIP; NMR; -; A=208-292.
DR PDBsum; 2DIP; -.
DR AlphaFoldDB; Q8NEG5; -.
DR SMR; Q8NEG5; -.
DR BioGRID; 127342; 11.
DR IntAct; Q8NEG5; 8.
DR STRING; 9606.ENSP00000295131; -.
DR iPTMnet; Q8NEG5; -.
DR PhosphoSitePlus; Q8NEG5; -.
DR BioMuta; ZSWIM2; -.
DR DMDM; 313104068; -.
DR jPOST; Q8NEG5; -.
DR PaxDb; Q8NEG5; -.
DR PeptideAtlas; Q8NEG5; -.
DR PRIDE; Q8NEG5; -.
DR ProteomicsDB; 73164; -.
DR Antibodypedia; 34014; 101 antibodies from 18 providers.
DR DNASU; 151112; -.
DR Ensembl; ENST00000295131.3; ENSP00000295131.2; ENSG00000163012.4.
DR GeneID; 151112; -.
DR KEGG; hsa:151112; -.
DR MANE-Select; ENST00000295131.3; ENSP00000295131.2; NM_182521.3; NP_872327.2.
DR UCSC; uc002upu.2; human.
DR CTD; 151112; -.
DR DisGeNET; 151112; -.
DR GeneCards; ZSWIM2; -.
DR HGNC; HGNC:30990; ZSWIM2.
DR HPA; ENSG00000163012; Tissue enriched (testis).
DR neXtProt; NX_Q8NEG5; -.
DR OpenTargets; ENSG00000163012; -.
DR PharmGKB; PA134900131; -.
DR VEuPathDB; HostDB:ENSG00000163012; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00390000006826; -.
DR HOGENOM; CLU_029121_0_0_1; -.
DR InParanoid; Q8NEG5; -.
DR OMA; KISQHFP; -.
DR OrthoDB; 797346at2759; -.
DR PhylomeDB; Q8NEG5; -.
DR TreeFam; TF333237; -.
DR PathwayCommons; Q8NEG5; -.
DR SignaLink; Q8NEG5; -.
DR BioGRID-ORCS; 151112; 11 hits in 1105 CRISPR screens.
DR EvolutionaryTrace; Q8NEG5; -.
DR GenomeRNAi; 151112; -.
DR Pharos; Q8NEG5; Tbio.
DR PRO; PR:Q8NEG5; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8NEG5; protein.
DR Bgee; ENSG00000163012; Expressed in left testis and 52 other tissues.
DR ExpressionAtlas; Q8NEG5; baseline and differential.
DR Genevisible; Q8NEG5; HS.
DR GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR007527; Znf_SWIM.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR InterPro; IPR039903; Zswim2.
DR PANTHER; PTHR21540; PTHR21540; 1.
DR Pfam; PF04434; SWIM; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00184; RING; 2.
DR PROSITE; PS50089; ZF_RING_2; 2.
DR PROSITE; PS50966; ZF_SWIM; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Metal-binding; Reference proteome; Repeat;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..633
FT /note="E3 ubiquitin-protein ligase ZSWIM2"
FT /id="PRO_0000223097"
FT ZN_FING 54..87
FT /note="SWIM-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00325"
FT ZN_FING 147..198
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 229..280
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 344..388
FT /note="RING-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT CONFLICT 88
FT /note="K -> E (in Ref. 4; AAH31094)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="C -> Y (in Ref. 4; AAH31094)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="I -> T (in Ref. 4; AAH31094)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="D -> G (in Ref. 4; AAH31094)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="D -> E (in Ref. 4; AAH31094)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="F -> Y (in Ref. 4; AAH31094)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="M -> V (in Ref. 4; AAH31094)"
FT /evidence="ECO:0000305"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:2DIP"
FT STRAND 246..254
FT /evidence="ECO:0007829|PDB:2DIP"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:2DIP"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:2DIP"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:2DIP"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:2DIP"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:2DIP"
SQ SEQUENCE 633 AA; 72732 MW; FB5B74E5E7FA625C CRC64;
MLRRGYKASE RRRHLSERLS WHQDQALSSS IYLLREMGPT GFLLREEEPE YMDFRVFLGN
PHVCNCSTFP KGGELCKHIC WVLLKKFKLP RNHESALQLG LGEREISDLL RGIHRVQTPQ
PGTNDENEHV EEDGYIKQKE IDSEDICSIC QELLLEKKLP VTFCRFGCGN SIHIKCMKIL
ANYQSTSNTS MLKCPLCRKE FAPLKLILEE FKNSSKLVAA AEKERLDKHL GIPCNNCKQF
PIEGKCYKCT ECIEYHLCQE CFDSCCHLSH TFTFREKRNQ KWRSLEKRAD EVVKYIDTKN
EIEEKMSHFQ EKQGQVYTPK HIVRSLPLQL ITKNSKLLAP GYQCLLCLKA FHLGQHTRLL
PCTHKFHRKC IDNWLFHKCN SCPIDGQVIY NPLTWKNSAV NGQAHQSVSN RDIIHLSKQK
EPDLFIPGTG LVLKQNRLGI LPSIPQCNFD ELNTPQSPKD AYENTTIDNL CSIKLDNSNS
KKLTYDYKIS QHFPRYLQDL PTVSFGKIPS QTLLPPIVHK NIVCPTAMES PCISGKFHTS
LSRMTKGCKC NNHNLKKTPA TKIREDNKRS TLLPEDFNLI VNWSTAKLSL SKRYSNCMGE
ITRKCSHLSR QPVSHSVNTK STELSLIIEG VQL
