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Protein

E3 ubiquitin-protein ligase Zswim2

Gene

Zswim2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri54 – 8734SWIM-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri147 – 19953RING-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri229 – 27850ZZ-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri344 – 38643RING-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • protein self-association Source: UniProtKB
  • ubiquitin protein ligase activity Source: MGI
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • positive regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
  • protein polyubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase Zswim2 (EC:6.3.2.-)
Alternative name(s):
MEKK1-related protein X
Short name:
MEX
ZZ-type zinc finger-containing protein 2
Zinc finger SWIM domain-containing protein 2
Gene namesi
Name:Zswim2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1919111. Zswim2.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi66 – 661C → S: Abogates ubiquitination activity and the ability to promote DR4- and Fas-induced apoptosis. 1 Publication
Mutagenesisi168 – 1681C → S: Abogates ubiquitination activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 631631E3 ubiquitin-protein ligase Zswim2PRO_0000223098Add
BLAST

Post-translational modificationi

Polyubiquitinated. Polyubiquitination is followed by degradation via the proteasome.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ9D9X6.
PRIDEiQ9D9X6.

PTM databases

PhosphoSiteiQ9D9X6.

Expressioni

Tissue specificityi

Expressed only in testis.1 Publication

Gene expression databases

BgeeiQ9D9X6.
CleanExiMM_ZSWIM2.
ExpressionAtlasiQ9D9X6. baseline and differential.
GenevisibleiQ9D9X6. MM.

Interactioni

Subunit structurei

Dimer. Interacts with UBE2D1.1 Publication

GO - Molecular functioni

  • protein self-association Source: UniProtKB

Protein-protein interaction databases

BioGridi214986. 3 interactions.
STRINGi10090.ENSMUSP00000044913.

Structurei

3D structure databases

ProteinModelPortaliQ9D9X6.
SMRiQ9D9X6. Positions 139-204, 209-291, 338-392.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni139 – 348210UBE2D1-bindingAdd
BLAST

Domaini

The SWIM-type zinc finger is required for ubiquitination activity.1 Publication

Sequence similaritiesi

Contains 2 RING-type zinc fingers.PROSITE-ProRule annotation
Contains 1 SWIM-type zinc finger.PROSITE-ProRule annotation
Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri54 – 8734SWIM-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri147 – 19953RING-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri229 – 27850ZZ-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri344 – 38643RING-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00390000006826.
HOGENOMiHOG000065782.
HOVERGENiHBG060888.
InParanoidiQ9D9X6.
KOiK15716.
OMAiCRFGCGN.
OrthoDBiEOG769ZKK.
PhylomeDBiQ9D9X6.
TreeFamiTF333237.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR007527. Znf_SWIM.
IPR000433. Znf_ZZ.
[Graphical view]
PfamiPF04434. SWIM. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 2 hits.
PS50966. ZF_SWIM. 1 hit.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D9X6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRGGCKASE KRRHLSESLS WQQDQALSSS IYLLRQIGPT GFLLKEEEPE
60 70 80 90 100
KGDFRVLLGN PHECSCPTFL KRGELCKHIC WVLLKKFKLP RNHESAFQLG
110 120 130 140 150
LTEGEINDLL RGIHQVQAPQ LRASDETAQV EEDGYLKQKD INAGDICPIC
160 170 180 190 200
QEVLLEKKLP VTFCRFGCGN NVHIKCMRIL ANYQDTGSDS SVLRCPLCRE
210 220 230 240 250
EFAPLKVILE EFKNSNKLIT ISEKERLDKH LGIPCNNCNQ LPIEGRCYKC
260 270 280 290 300
TECVEYHLCQ ECFDSCCHSS HAFASREKRN QRWRSVEKRS EVMKYLNTEN
310 320 330 340 350
EGEAKPGCFQ EKQGQFYTPK HVVKSLPLLM ITKKSKLLAP GYQCRLCLKS
360 370 380 390 400
FSFGQYTRLL PCTHKFHRKC IDNWLLHKCN SCPIDRQVIY NPLIWKGIAT
410 420 430 440 450
DGQAHQLASS KDIACLSKQQ EPKLFIPGTG LVLKGKRMGV LPSIPQYNSK
460 470 480 490 500
VLTTLQNPSD NYQNITMDDL CSVKLDNSNS RKLVFGYKIS KQFPTYLKNP
510 520 530 540 550
TTGQTPSQTF LPSLPHKNII CLTGRESPHI YEKDHIGQSQ KTSRGYEHIN
560 570 580 590 600
YNTRKSLGSR LRQHKRSSAL SSEDLNLTIN LGTTKLSLSK RQNNSMGKVR
610 620 630
QKLGHPPRRP AYPPLQTQNA ALSLIMQGIQ L
Length:631
Mass (Da):71,793
Last modified:June 1, 2001 - v1
Checksum:i4DBD3CCD323F8A8E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK006367 mRNA. Translation: BAB24549.1.
CCDSiCCDS16183.1.
RefSeqiNP_082240.1. NM_027964.2.
UniGeneiMm.116957.

Genome annotation databases

EnsembliENSMUST00000038223; ENSMUSP00000044913; ENSMUSG00000034552.
GeneIDi71861.
KEGGimmu:71861.
UCSCiuc008kif.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK006367 mRNA. Translation: BAB24549.1.
CCDSiCCDS16183.1.
RefSeqiNP_082240.1. NM_027964.2.
UniGeneiMm.116957.

3D structure databases

ProteinModelPortaliQ9D9X6.
SMRiQ9D9X6. Positions 139-204, 209-291, 338-392.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi214986. 3 interactions.
STRINGi10090.ENSMUSP00000044913.

PTM databases

PhosphoSiteiQ9D9X6.

Proteomic databases

PaxDbiQ9D9X6.
PRIDEiQ9D9X6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038223; ENSMUSP00000044913; ENSMUSG00000034552.
GeneIDi71861.
KEGGimmu:71861.
UCSCiuc008kif.1. mouse.

Organism-specific databases

CTDi151112.
MGIiMGI:1919111. Zswim2.

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00390000006826.
HOGENOMiHOG000065782.
HOVERGENiHBG060888.
InParanoidiQ9D9X6.
KOiK15716.
OMAiCRFGCGN.
OrthoDBiEOG769ZKK.
PhylomeDBiQ9D9X6.
TreeFamiTF333237.

Miscellaneous databases

NextBioi334752.
PROiQ9D9X6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D9X6.
CleanExiMM_ZSWIM2.
ExpressionAtlasiQ9D9X6. baseline and differential.
GenevisibleiQ9D9X6. MM.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR007527. Znf_SWIM.
IPR000433. Znf_ZZ.
[Graphical view]
PfamiPF04434. SWIM. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 2 hits.
PS50966. ZF_SWIM. 1 hit.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  2. "MEX is a testis-specific E3 ubiquitin ligase that promotes death receptor-induced apoptosis."
    Nishito Y., Hasegawa M., Inohara N., Nunez G.
    Biochem. J. 396:411-417(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, FUNCTION, UBIQUITINATION, SUBUNIT, DOMAIN, INTERACTION WITH UBE2D1, MUTAGENESIS OF CYS-66 AND CYS-168.

Entry informationi

Entry nameiZSWM2_MOUSE
AccessioniPrimary (citable) accession number: Q9D9X6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: June 1, 2001
Last modified: March 16, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.