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E3 ubiquitin-protein ligase ZSWIM2 (EC 2.3.2.27) (MEKK1-related protein X) (MEX) (RING-type E3 ubiquitin transferase ZSWIM2) (ZZ-type zinc finger-containing protein 2) (Zinc finger SWIM domain-containing protein 2)

 ZSWM2_HUMAN             Reviewed;         633 AA.
Q8NEG5; B3KXV6; Q53SI3; Q57ZY3;
16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 2.
28-FEB-2018, entry version 127.
RecName: Full=E3 ubiquitin-protein ligase ZSWIM2;
EC=2.3.2.27;
AltName: Full=MEKK1-related protein X;
Short=MEX;
AltName: Full=RING-type E3 ubiquitin transferase ZSWIM2;
AltName: Full=ZZ-type zinc finger-containing protein 2;
AltName: Full=Zinc finger SWIM domain-containing protein 2;
Name=ZSWIM2; Synonyms=ZZZ2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
STRUCTURE BY NMR OF 208-292.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the ZZ domain of zinc finger SWIM domain
containing protein 2.";
Submitted (FEB-2009) to the PDB data bank.
-!- FUNCTION: E3 ubiquitin-protein ligase involved in the regulation
of Fas-, DR3- and DR4-mediated apoptosis. Functions in conjunction
with the UBE2D1, UBE2D3 and UBE2E1 E2 ubiquitin-conjugating
enzymes. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- SUBUNIT: Dimer. Interacts with UBE2D1. {ECO:0000250}.
-!- DOMAIN: The SWIM-type zinc finger is reqiered for ubiquitination
activity. {ECO:0000250}.
-!- PTM: Polyubiquitinated. Polyubiquitination is followed by
degradation via the proteasome (By similarity). {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; AK128006; BAG54618.1; -; mRNA.
EMBL; AC018735; AAY14907.1; -; Genomic_DNA.
EMBL; AC103914; AAX82016.1; -; Genomic_DNA.
EMBL; CH471058; EAX10929.1; -; Genomic_DNA.
EMBL; BC031094; AAH31094.1; -; mRNA.
CCDS; CCDS33348.1; -.
RefSeq; NP_872327.2; NM_182521.2.
UniGene; Hs.375054; -.
PDB; 2DIP; NMR; -; A=208-292.
PDBsum; 2DIP; -.
ProteinModelPortal; Q8NEG5; -.
SMR; Q8NEG5; -.
BioGrid; 127342; 8.
IntAct; Q8NEG5; 2.
STRING; 9606.ENSP00000295131; -.
iPTMnet; Q8NEG5; -.
PhosphoSitePlus; Q8NEG5; -.
BioMuta; ZSWIM2; -.
DMDM; 313104068; -.
PaxDb; Q8NEG5; -.
PeptideAtlas; Q8NEG5; -.
PRIDE; Q8NEG5; -.
DNASU; 151112; -.
Ensembl; ENST00000295131; ENSP00000295131; ENSG00000163012.
GeneID; 151112; -.
KEGG; hsa:151112; -.
UCSC; uc002upu.2; human.
CTD; 151112; -.
DisGeNET; 151112; -.
EuPathDB; HostDB:ENSG00000163012.3; -.
GeneCards; ZSWIM2; -.
HGNC; HGNC:30990; ZSWIM2.
neXtProt; NX_Q8NEG5; -.
OpenTargets; ENSG00000163012; -.
PharmGKB; PA134900131; -.
eggNOG; KOG0800; Eukaryota.
eggNOG; ENOG41121N2; LUCA.
GeneTree; ENSGT00390000006826; -.
HOGENOM; HOG000065782; -.
HOVERGEN; HBG060888; -.
InParanoid; Q8NEG5; -.
KO; K15716; -.
OMA; CRFGCGN; -.
OrthoDB; EOG091G0F9U; -.
PhylomeDB; Q8NEG5; -.
TreeFam; TF333237; -.
EvolutionaryTrace; Q8NEG5; -.
GenomeRNAi; 151112; -.
PRO; PR:Q8NEG5; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000163012; -.
CleanEx; HS_ZSWIM2; -.
ExpressionAtlas; Q8NEG5; baseline and differential.
Genevisible; Q8NEG5; HS.
GO; GO:0043621; F:protein self-association; IEA:Ensembl.
GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
Gene3D; 3.30.40.10; -; 2.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR007527; Znf_SWIM.
InterPro; IPR000433; Znf_ZZ.
Pfam; PF04434; SWIM; 1.
Pfam; PF13639; zf-RING_2; 1.
Pfam; PF00569; ZZ; 1.
SMART; SM00184; RING; 2.
PROSITE; PS50089; ZF_RING_2; 2.
PROSITE; PS50966; ZF_SWIM; 1.
PROSITE; PS01357; ZF_ZZ_1; 1.
PROSITE; PS50135; ZF_ZZ_2; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Metal-binding;
Reference proteome; Repeat; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 633 E3 ubiquitin-protein ligase ZSWIM2.
/FTId=PRO_0000223097.
ZN_FING 54 87 SWIM-type. {ECO:0000255|PROSITE-
ProRule:PRU00325}.
ZN_FING 147 198 RING-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 228 277 ZZ-type. {ECO:0000255|PROSITE-
ProRule:PRU00228}.
ZN_FING 344 388 RING-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
CONFLICT 88 88 K -> E (in Ref. 4; AAH31094).
{ECO:0000305}.
CONFLICT 265 265 C -> Y (in Ref. 4; AAH31094).
{ECO:0000305}.
CONFLICT 302 302 I -> T (in Ref. 4; AAH31094).
{ECO:0000305}.
CONFLICT 385 385 D -> G (in Ref. 4; AAH31094).
{ECO:0000305}.
CONFLICT 486 486 D -> E (in Ref. 4; AAH31094).
{ECO:0000305}.
CONFLICT 537 537 F -> Y (in Ref. 4; AAH31094).
{ECO:0000305}.
CONFLICT 544 544 M -> V (in Ref. 4; AAH31094).
{ECO:0000305}.
STRAND 235 237 {ECO:0000244|PDB:2DIP}.
STRAND 246 254 {ECO:0000244|PDB:2DIP}.
STRAND 256 258 {ECO:0000244|PDB:2DIP}.
HELIX 259 263 {ECO:0000244|PDB:2DIP}.
HELIX 267 269 {ECO:0000244|PDB:2DIP}.
STRAND 272 274 {ECO:0000244|PDB:2DIP}.
STRAND 277 279 {ECO:0000244|PDB:2DIP}.
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


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