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26S proteasome complex subunit SEM1 (26S proteasome complex subunit DSS1) (Deleted in split hand/split foot protein 1) (Split hand/foot deleted protein 1) (Split hand/foot malformation type 1 protein)

 SEM1_HUMAN              Reviewed;          70 AA.
P60896; Q13437; Q61067;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 1.
22-NOV-2017, entry version 132.
RecName: Full=26S proteasome complex subunit SEM1;
AltName: Full=26S proteasome complex subunit DSS1;
AltName: Full=Deleted in split hand/split foot protein 1;
AltName: Full=Split hand/foot deleted protein 1;
AltName: Full=Split hand/foot malformation type 1 protein;
Name=SEM1 {ECO:0000312|HGNC:HGNC:10845};
Synonyms=C7orf76, DSS1, SHFDG1, SHFM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8733122; DOI=10.1093/hmg/5.5.571;
Crackower M.A., Scherer S.W., Rommens J.M., Hui C.-C., Poorkaj P.,
Soder S., Cobben J.M., Hudgins L., Evans J.P., Tsui L.-C.;
"Characterization of the split hand/split foot malformation locus
SHFM1 at 7q21.3-q22.1 and analysis of a candidate gene for its
expression during limb development.";
Hum. Mol. Genet. 5:571-579(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[4]
FUNCTION.
PubMed=1317798; DOI=10.1111/j.1432-1033.1992.tb16961.x;
Kanayama H.O., Tamura T., Ugai S., Kagawa S., Tanahashi N.,
Yoshimura T., Tanaka K., Ichihara A.;
"Demonstration that a human 26S proteolytic complex consists of a
proteasome and multiple associated protein components and hydrolyzes
ATP and ubiquitin-ligated proteins by closely linked mechanisms.";
Eur. J. Biochem. 206:567-578(1992).
[5]
INTERACTION WITH BRCA2.
PubMed=10373512; DOI=10.1128/MCB.19.7.4633;
Marston N.J., Richards W.J., Hughes D., Bertwistle D., Marshall C.J.,
Ashworth A.;
"Interaction between the product of the breast cancer susceptibility
gene BRCA2 and DSS1, a protein functionally conserved from yeast to
mammals.";
Mol. Cell. Biol. 19:4633-4642(1999).
[6]
FUNCTION.
PubMed=15117943; DOI=10.1074/jbc.M403165200;
Sone T., Saeki Y., Toh-e A., Yokosawa H.;
"Sem1p is a novel subunit of the 26S proteasome from Saccharomyces
cerevisiae.";
J. Biol. Chem. 279:28807-28816(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17323924; DOI=10.1021/bi061994u;
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human
26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[8]
INTERACTION WITH BRCA2.
PubMed=21719596; DOI=10.1182/blood-2010-12-324541;
Biswas K., Das R., Alter B.P., Kuznetsov S.G., Stauffer S.,
North S.L., Burkett S., Brody L.C., Meyer S., Byrd R.A., Sharan S.K.;
"A comprehensive functional characterization of BRCA2 variants
associated with Fanconi anemia using mouse ES cell-based assay.";
Blood 118:2430-2442(2011).
[9]
INTERACTION WITH TREX-2 COMPLEX.
PubMed=22307388; DOI=10.1093/nar/gks059;
Jani D., Lutz S., Hurt E., Laskey R.A., Stewart M.,
Wickramasinghe V.O.;
"Functional and structural characterization of the mammalian TREX-2
complex that links transcription with nuclear messenger RNA export.";
Nucleic Acids Res. 40:4562-4573(2012).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
FUNCTION.
PubMed=24896180; DOI=10.1038/nature13374;
Bhatia V., Barroso S.I., Garcia-Rubio M.L., Tumini E.,
Herrera-Moyano E., Aguilera A.;
"BRCA2 prevents R-loop accumulation and associates with TREX-2 mRNA
export factor PCID2.";
Nature 511:362-365(2014).
[12]
X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH BRCA2.
PubMed=12228710; DOI=10.1126/science.297.5588.1837;
Yang H., Jeffrey P.D., Miller J., Kinnucan E., Sun Y., Thoma N.H.,
Zheng N., Chen P.L., Lee W.H., Pavletich N.P.;
"BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-
ssDNA structure.";
Science 297:1837-1848(2002).
[13]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-389, AND
SUBUNIT.
PubMed=27428775; DOI=10.1038/nsmb.3273;
Huang X., Luan B., Wu J., Shi Y.;
"An atomic structure of the human 26S proteasome.";
Nat. Struct. Mol. Biol. 23:778-785(2016).
[14]
STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS) OF 1-389, AND
SUBUNIT.
PubMed=27342858; DOI=10.1073/pnas.1608050113;
Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
"Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
-!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
involved in the ATP-dependent degradation of ubiquitinated
proteins. This complex plays a key role in the maintenance of
protein homeostasis by removing misfolded or damaged proteins,
which could impair cellular functions, and by removing proteins
whose functions are no longer required. Therefore, the proteasome
participates in numerous cellular processes, including cell cycle
progression, apoptosis, or DNA damage repair (PubMed:15117943).
Component of the TREX-2 complex (transcription and export complex
2), composed of at least ENY2, GANP, PCID2, SEM1, and either
centrin CETN2 or CETN3 (PubMed:22307388). The TREX-2 complex
functions in docking export-competent ribonucleoprotein particles
(mRNPs) to the nuclear entrance of the nuclear pore complex
(nuclear basket). TREX-2 participates in mRNA export and accurate
chromatin positioning in the nucleus by tethering genes to the
nuclear periphery. Binds and stabilizes BRCA2 and is thus involved
in the control of R-loop-associated DNA damage and thus
transcription-associated genomic instability. R-loop accumulation
increases in SEM1-depleted cells. {ECO:0000269|PubMed:1317798,
ECO:0000269|PubMed:15117943, ECO:0000269|PubMed:22307388,
ECO:0000269|PubMed:24896180}.
-!- SUBUNIT: Component of the 19S proteasome regulatory particle
complex. The 26S proteasome consists of a 20S core particle (CP)
and two 19S regulatory subunits (RP). The regulatory particle is
made of a lid composed of 9 subunits including SEM1, a base
containing 6 ATPases and few additional components
(PubMed:27428775, PubMed:27342858). Belongs to the TREX-2 complex
(transcription and export complex 2), composed of at least ENY2,
GANP, PCID2, SEM1, and either centrin CETN2 or CETN3
(PubMed:22307388). Interacts with the C-terminal of BRCA2
(PubMed:10373512, PubMed:21719596). {ECO:0000269|PubMed:10373512,
ECO:0000269|PubMed:12228710, ECO:0000269|PubMed:21719596,
ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:27342858,
ECO:0000269|PubMed:27428775}.
-!- INTERACTION:
P51587:BRCA2; NbExp=10; IntAct=EBI-79819, EBI-79792;
Q5JVF3:PCID2; NbExp=4; IntAct=EBI-79819, EBI-1051701;
Q5JVF3-1:PCID2; NbExp=3; IntAct=EBI-79819, EBI-15970419;
O43242:PSMD3; NbExp=3; IntAct=EBI-79819, EBI-357622;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=2;
Name=1;
IsoId=P60896-1; Sequence=Displayed;
Name=2;
IsoId=Q6ZVN7-1; Sequence=External;
-!- TISSUE SPECIFICITY: Expressed in limb bud, craniofacial primordia
and skin.
-!- SIMILARITY: Belongs to the DSS1/SEM1 family. {ECO:0000305}.
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EMBL; U41515; AAA91179.1; -; mRNA.
EMBL; AC073230; AAQ93368.1; -; Genomic_DNA.
EMBL; BC032782; AAH32782.1; -; mRNA.
CCDS; CCDS5646.1; -. [P60896-1]
PIR; G02284; G02284.
RefSeq; NP_006295.1; NM_006304.1. [P60896-1]
UniGene; Hs.489201; -.
UniGene; Hs.729869; -.
UniGene; Hs.734935; -.
PDB; 1IYJ; X-ray; 3.40 A; A/C=1-70.
PDB; 1MIU; X-ray; 3.10 A; B=1-70.
PDB; 1MJE; X-ray; 3.50 A; B=1-70.
PDB; 3T5X; X-ray; 2.12 A; B=1-70.
PDB; 5GJQ; EM; 4.50 A; Y=1-70.
PDB; 5GJR; EM; 3.50 A; AB/Y=1-70.
PDB; 5L4K; EM; 4.50 A; Y=1-70.
PDB; 5LN3; EM; 6.80 A; Y=1-70.
PDB; 5M32; EM; 3.80 A; s=1-70.
PDB; 5T0C; EM; 3.80 A; Ae/Be=1-70.
PDB; 5T0G; EM; 4.40 A; e=1-70.
PDB; 5T0H; EM; 6.80 A; e=1-70.
PDB; 5T0I; EM; 8.00 A; e=1-70.
PDB; 5T0J; EM; 8.00 A; e=1-70.
PDB; 5VGZ; EM; 3.70 A; e=1-70.
PDB; 5VHF; EM; 5.70 A; e=1-70.
PDB; 5VHH; EM; 6.10 A; e=1-70.
PDB; 5VHI; EM; 6.80 A; e=1-70.
PDB; 5VHS; EM; 8.80 A; e=38-70.
PDBsum; 1IYJ; -.
PDBsum; 1MIU; -.
PDBsum; 1MJE; -.
PDBsum; 3T5X; -.
PDBsum; 5GJQ; -.
PDBsum; 5GJR; -.
PDBsum; 5L4K; -.
PDBsum; 5LN3; -.
PDBsum; 5M32; -.
PDBsum; 5T0C; -.
PDBsum; 5T0G; -.
PDBsum; 5T0H; -.
PDBsum; 5T0I; -.
PDBsum; 5T0J; -.
PDBsum; 5VGZ; -.
PDBsum; 5VHF; -.
PDBsum; 5VHH; -.
PDBsum; 5VHI; -.
PDBsum; 5VHS; -.
DisProt; DP00617; -.
ProteinModelPortal; P60896; -.
SMR; P60896; -.
BioGrid; 113692; 137.
CORUM; P60896; -.
DIP; DIP-31023N; -.
IntAct; P60896; 73.
MINT; MINT-3022106; -.
STRING; 9606.ENSP00000248566; -.
ChEMBL; CHEMBL2364701; -.
iPTMnet; P60896; -.
PhosphoSitePlus; P60896; -.
BioMuta; SHFM1; -.
PaxDb; P60896; -.
PeptideAtlas; P60896; -.
PRIDE; P60896; -.
TopDownProteomics; P60896-1; -. [P60896-1]
DNASU; 7979; -.
Ensembl; ENST00000248566; ENSP00000248566; ENSG00000127922. [P60896-1]
GeneID; 7979; -.
CTD; 7979; -.
DisGeNET; 7979; -.
EuPathDB; HostDB:ENSG00000127922.9; -.
GeneCards; SEM1; -.
HGNC; HGNC:10845; SEM1.
HPA; HPA072648; -.
MalaCards; SEM1; -.
MIM; 601285; gene.
neXtProt; NX_P60896; -.
OpenTargets; ENSG00000127922; -.
Orphanet; 2440; Split hand-split foot malformation.
PharmGKB; PA35749; -.
eggNOG; KOG4764; Eukaryota.
eggNOG; ENOG41126I3; LUCA.
GeneTree; ENSGT00390000002695; -.
HOVERGEN; HBG005536; -.
InParanoid; P60896; -.
OMA; EELSVWE; -.
PhylomeDB; P60896; -.
TreeFam; TF314699; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
ChiTaRS; SHFM1; human.
EvolutionaryTrace; P60896; -.
GeneWiki; SHFM1; -.
GenomeRNAi; 7979; -.
PRO; PR:P60896; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000127922; -.
CleanEx; HS_SHFM1; -.
ExpressionAtlas; P60896; baseline and differential.
Genevisible; P60896; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IEA:InterPro.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0006406; P:mRNA export from nucleus; IEA:InterPro.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043248; P:proteasome assembly; IEA:InterPro.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
InterPro; IPR007834; DSS1_SEM1.
PANTHER; PTHR16771; PTHR16771; 1.
Pfam; PF05160; DSS1_SEM1; 1.
SMART; SM01385; DSS1_SEM1; 1.
1: Evidence at protein level;
3D-structure; Alternative promoter usage; Complete proteome;
Polymorphism; Proteasome; Reference proteome.
CHAIN 1 70 26S proteasome complex subunit SEM1.
/FTId=PRO_0000122961.
COMPBIAS 14 21 Asp/Glu-rich (highly acidic).
COMPBIAS 31 35 Asp/Glu-rich (highly acidic).
COMPBIAS 40 51 Asp/Glu-rich (highly acidic).
VARIANT 17 17 D -> G (in dbSNP:rs1802882).
/FTId=VAR_012003.
HELIX 10 12 {ECO:0000244|PDB:1MIU}.
STRAND 21 23 {ECO:0000244|PDB:1MJE}.
HELIX 42 44 {ECO:0000244|PDB:3T5X}.
HELIX 51 62 {ECO:0000244|PDB:3T5X}.
SEQUENCE 70 AA; 8278 MW; 0E0F58D2F3D9F723 CRC64;
MSEKKQPVDL GLLEEDDEFE EFPAEDWAGL DEDEDAHVWE DNWDDDNVED DFSNQLRAEL
EKHGYKMETS


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GWB-4E7C20 Deleted In Split-hand_split-foot 1 Region (DSS1) (SHFM1) Rabbit anti-Human Polyclonal (aa57-70) Antibody
EIAAB32776 Homo sapiens,Human,LMP7,Low molecular mass protein 7,Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit b
10-288-22044F Proteasome subunit alpha type 1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 0.05 mg
18-003-44181 Proteasome subunit alpha type-1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 Pol 0.05 mg Aff Pur
10-288-22044F Proteasome subunit alpha type 1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 0.1 mg
15-288-22044A Proteasome subunit alpha type 1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 Pol 0.1 mg
15-288-22044A Proteasome subunit alpha type 1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 Pol 0.05 mg
18-003-44182 Proteasome subunit alpha type-1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 Pol 0.1 mg Protein A
EIAAB32772 Lmp7,Low molecular mass protein 7,Macropain subunit C13,Mc13,Mouse,Multicatalytic endopeptidase complex subunit C13,Mus musculus,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subu
15-288-22161 Hairy_enhancer-of-split related with YRPW motif 1 - Hairy and enhancer of split-related protein 1; HESR-1; Cardiovascular helix-loop-helix factor 2; HES-related repressor protein 2; HERP2 Polyclonal 0.05 mg
15-288-22161 Hairy_enhancer-of-split related with YRPW motif 1 - Hairy and enhancer of split-related protein 1; HESR-1; Cardiovascular helix-loop-helix factor 2; HES-related repressor protein 2; HERP2 Polyclonal 0.1 mg
18-003-42229 Hairy_enhancer-of-split related with YRPW motif 1 - Hairy and enhancer of split-related protein 1; HESR-1; Cardiovascular helix-loop-helix factor 2; HES-related repressor protein 2; HERP2 Polyclonal 0.1 mg Protein A
10-288-22161F Hairy_enhancer-of-split related with YRPW motif 1 - Hairy and enhancer of split-related protein 1; HESR-1; Cardiovascular helix-loop-helix factor 2; HES-related repressor protein 2; HERP2 0.1 mg
10-288-22161F Hairy_enhancer-of-split related with YRPW motif 1 - Hairy and enhancer of split-related protein 1; HESR-1; Cardiovascular helix-loop-helix factor 2; HES-related repressor protein 2; HERP2 0.05 mg
18-003-43922 Amino-terminal enhancer of split - Amino enhancer of split; GRG protein; Protein ESP1; Gp130-associated protein GAM Polyclonal 0.1 mg Protein A
EIAAB32703 30 kDa prosomal protein,HC2,Homo sapiens,Human,Macropain subunit C2,Multicatalytic endopeptidase complex subunit C2,NU,PROS30,PROS-30,Proteasome component C2,Proteasome nu chain,Proteasome subunit alp
EIAAB32740 Lmp10,Low molecular mass protein 10,Macropain subunit MECl-1,Mecl1,Mouse,Multicatalytic endopeptidase complex subunit MECl-1,Mus musculus,Proteasome MECl-1,Proteasome subunit beta type-10,Proteasome s
EIAAB32742 Homo sapiens,Human,LMP10,Low molecular mass protein 10,Macropain subunit MECl-1,MECL1,Multicatalytic endopeptidase complex subunit MECl-1,Proteasome MECl-1,Proteasome subunit beta type-10,Proteasome s
ABP-PAB-10530 Split hand_foot deleted gene 1 (Shfdg1) polyclonal antibody 100 ug
EIAAB32739 Lmp10,Low molecular mass protein 10,Macropain subunit MECl-1,Mecl1,Multicatalytic endopeptidase complex subunit MECl-1,Proteasome MECl-1,Proteasome subunit beta type-10,Proteasome subunit beta-2i,Psmb


 

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