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Reviewed, UniProtKB/Swiss-Prot P40318 (SSM4_YEAST)

Last modified July 22, 2008. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    E3 ubiquitin-protein ligase Doa10
    EC=6.3.2.-
Gene names
Name: SSM4
Synonyms: DOA10
Ordered Locus Names: YIL030C
ORF Names: YI3299.01C, YI9905.18C
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length1319 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC6 and UBC7 E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of a broad range of substrates, inluding endoplasmic reticulum membrane proteins, soluble nuclear proteins and soluble cytoplasmic proteins. Part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Part of the ERAD-C complex which contains SSM4, UBC7, CUE1, CDC48, NPL4, UFD1 AND SEL1/UBX2. Interacts with SEL1/UBX2. Interacts with UBC6 and UBC7.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus inner membrane; Multi-pass membrane protein.

Domain

The RING-CH-type zinc finger domain is required for E3 ligase activity.

Sequence similarities

Contains 1 RING-CH-type zinc finger.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

P103561EBI-18208,EBI-22726
P255611EBI-18208,EBI-21696
P255761EBI-18208,EBI-21752
P256171EBI-18208,EBI-375711
P380811EBI-18208,EBI-21453
P387161EBI-18208,EBI-24682
P387581EBI-18208,EBI-24443
P408921EBI-18208,EBI-26263
P471371EBI-18208,EBI-25572
P531831EBI-18208,EBI-23747
P532651EBI-18208,EBI-23264
P540071EBI-18208,EBI-27168
Q044581EBI-18208,EBI-27205
Q075051EBI-18208,EBI-5951
Q086861EBI-18208,EBI-19264
Q089681EBI-18208,EBI-29375
Q107401EBI-18208,EBI-10175
AAT2P235421EBI-18208,EBI-2002
ABZ1P372541EBI-18208,EBI-12831
ADE12P802101EBI-18208,EBI-14267
ADE17P380091EBI-18208,EBI-14223
ADH2P003311EBI-18208,EBI-2222
AIP1P466801EBI-18208,EBI-2406
ALA1P408251EBI-18208,EBI-18648
AMD1P152741EBI-18208,EBI-2548
ARA2Q042121EBI-18208,EBI-28073
BNA5Q059791EBI-18208,EBI-10016
CDC48P256941EBI-18208,EBI-4308
CTF4Q014541EBI-18208,EBI-5209
CUE1P384281EBI-18208,EBI-27580
ENO2P009251EBI-18208,EBI-6475
ERR1Q120071EBI-18208,EBI-35679
FPP1P085241EBI-18208,EBI-7069
FSP2P530511EBI-18208,EBI-10464
GLN1P322881EBI-18208,EBI-7665
GND1P387201EBI-18208,EBI-1965
GPH1P067381EBI-18208,EBI-13389
GSF2Q046971EBI-18208,EBI-27807
GSP1P328351EBI-18208,EBI-7926
GUS1P466551EBI-18208,EBI-18665
HSP104P315391EBI-18208,EBI-8050
IDP3P539821EBI-18208,EBI-8892
IPP1P008171EBI-18208,EBI-9338
LAH1P333991EBI-18208,EBI-10046
LYS1P389981EBI-18208,EBI-10264
MAL32P381581EBI-18208,EBI-10326
MAM33P405131EBI-18208,EBI-10316
MET12P461511EBI-18208,EBI-11567
MLS1P309521EBI-18208,EBI-10428
MVP1P409591EBI-18208,EBI-11636
NOB1Q084441EBI-18208,EBI-29777
NPT1P396831EBI-18208,EBI-12218
OYE3P418161EBI-18208,EBI-12734
PAN5P387871EBI-18208,EBI-12913
PCK1P109631EBI-18208,EBI-13770
PDC5P164671EBI-18208,EBI-5696
PDI1P179671EBI-18208,EBI-13012
PFK2P168621EBI-18208,EBI-9435
PRO2P548851EBI-18208,EBI-13872
PTP1P250441EBI-18208,EBI-14183
PYC1P111541EBI-18208,EBI-14358
RNR1P215241EBI-18208,EBI-15234
RPL8AP170761EBI-18208,EBI-15431
SEC13Q044911EBI-18208,EBI-16529
SEL1Q042281EBI-18208,EBI-27730
SOL1P502781EBI-18208,EBI-17675
SSA2P105921EBI-18208,EBI-8603
STE6P128661EBI-18208,EBI-18383
STM1P390151EBI-18208,EBI-11238
STR3P531011EBI-18208,EBI-24097
TES1P419031EBI-18208,EBI-14154
THI80P352021EBI-18208,EBI-19195
THR4P161201EBI-18208,EBI-19259
TIF34P402171EBI-18208,EBI-8951
UBC6P332961EBI-18208,EBI-19745
UBC7Q021591EBI-18208,EBI-19749
UBP15P501011EBI-18208,EBI-19898
YPT6Q992601EBI-18208,EBI-29503

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 13191319E3 ubiquitin-protein ligase Doa10

Regions

Topological domain1 – 131131Cytoplasmic Potential
Transmembrane132 – 15221 Potential
Topological domain153 – 20351Extracellular Potential
Transmembrane204 – 22421 Potential
Topological domain225 – 468244Cytoplasmic Potential
Transmembrane469 – 48921 Potential
Topological domain490 – 4912Extracellular Potential
Transmembrane492 – 51221 Potential
Topological domain513 – 626114Cytoplasmic Potential
Transmembrane627 – 64721 Potential
Topological domain648 – 66013Extracellular Potential
Transmembrane661 – 68121 Potential
Topological domain682 – 73958Cytoplasmic Potential
Transmembrane740 – 76021 Potential
Topological domain761 – 965205Extracellular Potential
Transmembrane966 – 98621 Potential
Topological domain987 – 9882Cytoplasmic Potential
Transmembrane989 – 100921 Potential
Topological domain1010 – 101910Extracellular Potential
Transmembrane1020 – 104021 Potential
Topological domain1041 – 111373Cytoplasmic Potential
Transmembrane1114 – 113421 Potential
Topological domain1135 – 116834Extracellular Potential
Transmembrane1169 – 118921 Potential
Topological domain1190 – 121324Cytoplasmic Potential
Transmembrane1214 – 123421 Potential
Topological domain1235 – 127036Extracellular Potential
Transmembrane1271 – 129121 Potential
Topological domain1292 – 131928Cytoplasmic Potential
Zinc finger31 – 10070RING-CH-type
Compositional bias288 – 2914Poly-Ala
Compositional bias293 – 2964Poly-Asn
Compositional bias332 – 34110Asp/Gln/Ser-rich (acidic)
Compositional bias369 – 3746Poly-Gln

Amino acid modifications

Modified residue8971Phosphoserine

Experimental info

Sequence conflict2411L → F in CAA54133. Ref.1
Sequence conflict7431A → T in CAA54133. Ref.1
Sequence conflict10851N → D in CAA54133. Ref.1
Sequence conflict11861Y → F in CAA54133. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P40318-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 3EDFF7F9D90A0C8C

FASTA1,319151,455
        10         20         30         40         50         60 
MDVDSDVNVS RLRDELHKVA NEETDTATFN DDAPSGATCR ICRGEATEDN PLFHPCKCRG 

        70         80         90        100        110        120 
SIKYMHESCL LEWVASKNID ISKPGADVKC DICHYPIQFK TIYAENMPEK IPFSLLLSKS 

       130        140        150        160        170        180 
ILTFFEKARL ALTIGLAAVL YIIGVPLVWN MFGKLYTMML DGSSPYPGDF LKSLIYGYDQ 

       190        200        210        220        230        240 
SATPELTTRA IFYQLLQNHS FTSLQFIMIV ILHIALYFQY DMIVREDVFS KMVFHKIGPR 

       250        260        270        280        290        300 
LSPKDLKSRL KERFPMMDDR MVEYLAREMR AHDENRQEQG HDRLNMPAAA ADNNNNVINP 

       310        320        330        340        350        360 
RNDNVPPQDP NDHRNFENLR HVDELDHDEA TEEHENNDSD NSLPSGDDSS RILPGSSSDN 

       370        380        390        400        410        420 
EEDEEAEGQQ QQQQPEEEAD YRDHIEPNPI DMWANRRAQN EFDDLIAAQQ NAINRPNAPV 

       430        440        450        460        470        480 
FIPPPAQNRA GNVDQDEQDF GAAVGVPPAQ ANPDDQGQGP LVINLKLKLL NVIAYFIIAV 

       490        500        510        520        530        540 
VFTAIYLAIS YLFPTFIGFG LLKIYFGIFK VILRGLCHLY YLSGAHIAYN GLTKLVPKVD 

       550        560        570        580        590        600 
VAMSWISDHL IHDIIYLYNG YTENTMKHSI FIRALPALTT YLTSVSIVCA SSNLVSRGYG 

       610        620        630        640        650        660 
RENGMSNPTR RLIFQILFAL KCTFKVFTLF FIELAGFPIL AGVMLDFSLF CPILASNSRM 

       670        680        690        700        710        720 
LWVPSICAIW PPFSLFVYWT IGTLYMYWFA KYIGMIRKNI IRPGVLFFIR SPEDPNIKIL 

       730        740        750        760        770        780 
HDSLIHPMSI QLSRLCLSMF IYAIFIVLGF GFHTRIFFPF MLKSNLLSVP EAYKPTSIIS 

       790        800        810        820        830        840 
WKFNTILLTL YFTKRILESS SYVKPLLERY WKTIFKLCSR KLRLSSFILG KDTPTERGHI 

       850        860        870        880        890        900 
VYRNLFYKYI AAKNAEWSNQ ELFTKPKTLE QAEELFGQVR DVHAYFVPDG VLMRVPSSDI 

       910        920        930        940        950        960 
VSRNYVQTMF VPVTKDDKLL KPLDLERIKE RNKRAAGEFG YLDEQNTEYD QYYIVYVPPD 

       970        980        990       1000       1010       1020 
FRLRYMTLLG LVWLFASILM LGVTFISQAL INFVCSFGFL PVVKLLLGER NKVYVAWKEL 

      1030       1040       1050       1060       1070       1080 
SDISYSYLNI YYVCVGSVCL SKIAKDILHF TEGQNTLDEH AVDENEVEEV EHDIPERDIN 

      1090       1100       1110       1120       1130       1140 
NAPVNNINNV EEGQGIFMAI FNSIFDSMLV KYNLMVFIAI MIAVIRTMVS WVVLTDGILA 

      1150       1160       1170       1180       1190       1200 
CYNYLTIRVF GNSSYTIGNS KWFKYDESLL FVVWIISSMV NFGTGYKSLK LFFRNRNTSK 

      1210       1220       1230       1240       1250       1260 
LNFLKTMALE LFKQGFLHMV IYVLPIIILS LVFLRDVSTK QIIDISHGSR SFTLSLNESF 

      1270       1280       1290       1300       1310 
PTWTRMQDIY FGLLIALESF TFFFQATVLF IQWFKSTVQN VKDEVYTKGR ALENLPDES

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References

« Hide 'large scale' references
[1]"Inactivation of SSM4, a new Saccharomyces cerevisiae gene, suppresses mRNA instability due to RNA14 mutations."
Mandart E., Dufour M.-E., Lacroute F.
Mol. Gen. Genet. 245:323-333(1994) [PubMed: 7816042] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 28383 / FL100 / VTT C-80102.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed: 9169870] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]"A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation."
Swanson R., Locher M., Hochstrasser M.
Genes Dev. 15:2660-2674(2001) [PubMed: 11641273] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[4]"Ubx2 links the Cdc48 complex to ER-associated protein degradation."
Neuber O., Jarosch E., Volkwein C., Walter J., Sommer T.
Nat. Cell Biol. 7:993-998(2005) [PubMed: 16179953] [Abstract]
Cited for: INTERACTION WITH SEL1; UBC6 AND UBC7, IDENTIFICATION IN COMPLEX WITH SEL1 AND CDC48.
[5]"Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation."
Schuberth C., Buchberger A.
Nat. Cell Biol. 7:999-1006(2005) [PubMed: 16179952] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN COMPLEX WITH SEL1; CDC48 AND UFD1.
[6]"Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins."
Carvalho P., Goder V., Rapoport T.A.
Cell 126:361-373(2006) [PubMed: 16873066] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE ERAD-C COMPLEX WITH UBC7; CUE1; CDC48, NPL4 AND SEL1.
[7]"Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways."
Ravid T., Kreft S.G., Hochstrasser M.
EMBO J. 25:533-543(2006) [PubMed: 16437165] [Abstract]
Cited for: FUNCTION.
[8]"Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI)."
Kreft S.G., Wang L., Hochstrasser M.
J. Biol. Chem. 281:4646-4653(2006) [PubMed: 16373356] [Abstract]
Cited for: TOPOLOGY.
[9]"Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase."
Deng M., Hochstrasser M.
Nature 443:827-831(2006) [PubMed: 17051211] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION.
[10]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 0:0-0(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-897, MASS SPECTROMETRY.

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Cross-references

Sequence databases

X76715 Genomic DNA. Translation: CAA54133.1.
Z46881 Genomic DNA. Translation: CAA86961.1.
Z46861 Genomic DNA. Translation: CAA86921.1.
PIRS49951.
RefSeqNP_012234.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:7286N.
IntActP40318.

Proteomic databases

PeptideAtlasP40318.

Genome annotation databases

EnsemblYIL030C. Saccharomyces cerevisiae. [Contig view]
GeneID854781.
GenomeReviewsGene locus YIL030C in contig Z47047_GR.
KEGGsce:YIL030C.
NMPDRfig|4932.3.peg.1768.

Organism-specific databases

CYGDYIL030c.
SGDS000001292. SSM4.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP40318.

Gene expression databases

ArrayExpressP40318.
GermOnlineYIL030C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR011016. ZnF_var-RING.
[Graphical view]
Gene3DG3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.
PfamPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00744. RINGv. 1 hit.
[Graphical view]
PROSITEPS51292. ZF_RING_CH. 1 hit.
[Graphical view]
ProDomP40318.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

LinkHubP40318.
ProtoNetSearch...

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Entry information

Entry nameSSM4_YEAST
AccessionPrimary (citable) accession number: P40318
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 22, 2008
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)