SEM1_HUMAN
ID SEM1_HUMAN Reviewed; 70 AA.
AC P60896; Q13437; Q61067;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=26S proteasome complex subunit SEM1;
DE AltName: Full=26S proteasome complex subunit DSS1;
DE AltName: Full=Deleted in split hand/split foot protein 1;
DE AltName: Full=Split hand/foot deleted protein 1;
DE AltName: Full=Split hand/foot malformation type 1 protein;
GN Name=SEM1 {ECO:0000312|HGNC:HGNC:10845};
GN Synonyms=C7orf76, DSS1, SHFDG1, SHFM1;
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 [MRNA].
RX PubMed=8733122; DOI=10.1093/hmg/5.5.571;
RA Crackower M.A., Scherer S.W., Rommens J.M., Hui C.-C., Poorkaj P.,
RA Soder S., Cobben J.M., Hudgins L., Evans J.P., Tsui L.-C.;
RT "Characterization of the split hand/split foot malformation locus SHFM1 at
RT 7q21.3-q22.1 and analysis of a candidate gene for its expression during
RT limb development.";
RL Hum. Mol. Genet. 5:571-579(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP FUNCTION.
RX PubMed=1317798; DOI=10.1111/j.1432-1033.1992.tb16961.x;
RA Kanayama H.O., Tamura T., Ugai S., Kagawa S., Tanahashi N., Yoshimura T.,
RA Tanaka K., Ichihara A.;
RT "Demonstration that a human 26S proteolytic complex consists of a
RT proteasome and multiple associated protein components and hydrolyzes ATP
RT and ubiquitin-ligated proteins by closely linked mechanisms.";
RL Eur. J. Biochem. 206:567-578(1992).
RN [5]
RP INTERACTION WITH BRCA2.
RX PubMed=10373512; DOI=10.1128/mcb.19.7.4633;
RA Marston N.J., Richards W.J., Hughes D., Bertwistle D., Marshall C.J.,
RA Ashworth A.;
RT "Interaction between the product of the breast cancer susceptibility gene
RT BRCA2 and DSS1, a protein functionally conserved from yeast to mammals.";
RL Mol. Cell. Biol. 19:4633-4642(1999).
RN [6]
RP FUNCTION.
RX PubMed=15117943; DOI=10.1074/jbc.m403165200;
RA Sone T., Saeki Y., Toh-e A., Yokosawa H.;
RT "Sem1p is a novel subunit of the 26S proteasome from Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 279:28807-28816(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human 26S
RT proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [8]
RP INTERACTION WITH BRCA2.
RX PubMed=21719596; DOI=10.1182/blood-2010-12-324541;
RA Biswas K., Das R., Alter B.P., Kuznetsov S.G., Stauffer S., North S.L.,
RA Burkett S., Brody L.C., Meyer S., Byrd R.A., Sharan S.K.;
RT "A comprehensive functional characterization of BRCA2 variants associated
RT with Fanconi anemia using mouse ES cell-based assay.";
RL Blood 118:2430-2442(2011).
RN [9]
RP INTERACTION WITH TREX-2 COMPLEX.
RX PubMed=22307388; DOI=10.1093/nar/gks059;
RA Jani D., Lutz S., Hurt E., Laskey R.A., Stewart M., Wickramasinghe V.O.;
RT "Functional and structural characterization of the mammalian TREX-2 complex
RT that links transcription with nuclear messenger RNA export.";
RL Nucleic Acids Res. 40:4562-4573(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP FUNCTION.
RX PubMed=24896180; DOI=10.1038/nature13374;
RA Bhatia V., Barroso S.I., Garcia-Rubio M.L., Tumini E., Herrera-Moyano E.,
RA Aguilera A.;
RT "BRCA2 prevents R-loop accumulation and associates with TREX-2 mRNA export
RT factor PCID2.";
RL Nature 511:362-365(2014).
RN [12]
RP IDENTIFICATION IN THE HR COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=26833090; DOI=10.1016/j.molcel.2015.12.026;
RA Trego K.S., Groesser T., Davalos A.R., Parplys A.C., Zhao W., Nelson M.R.,
RA Hlaing A., Shih B., Rydberg B., Pluth J.M., Tsai M.S., Hoeijmakers J.H.J.,
RA Sung P., Wiese C., Campisi J., Cooper P.K.;
RT "Non-catalytic Roles for XPG with BRCA1 and BRCA2 in Homologous
RT Recombination and Genome Stability.";
RL Mol. Cell 61:535-546(2016).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH BRCA2.
RX PubMed=12228710; DOI=10.1126/science.297.5588.1837;
RA Yang H., Jeffrey P.D., Miller J., Kinnucan E., Sun Y., Thoma N.H.,
RA Zheng N., Chen P.L., Lee W.H., Pavletich N.P.;
RT "BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA
RT structure.";
RL Science 297:1837-1848(2002).
RN [14]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-389, AND SUBUNIT.
RX PubMed=27428775; DOI=10.1038/nsmb.3273;
RA Huang X., Luan B., Wu J., Shi Y.;
RT "An atomic structure of the human 26S proteasome.";
RL Nat. Struct. Mol. Biol. 23:778-785(2016).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS) OF 1-389, AND SUBUNIT.
RX PubMed=27342858; DOI=10.1073/pnas.1608050113;
RA Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
RA Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
RT "Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
CC -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC This complex plays a key role in the maintenance of protein homeostasis
CC by removing misfolded or damaged proteins, which could impair cellular
CC functions, and by removing proteins whose functions are no longer
CC required. Therefore, the proteasome participates in numerous cellular
CC processes, including cell cycle progression, apoptosis, or DNA damage
CC repair (PubMed:15117943). Component of the TREX-2 complex
CC (transcription and export complex 2), composed of at least ENY2, GANP,
CC PCID2, SEM1, and either centrin CETN2 or CETN3 (PubMed:22307388). The
CC TREX-2 complex functions in docking export-competent ribonucleoprotein
CC particles (mRNPs) to the nuclear entrance of the nuclear pore complex
CC (nuclear basket). TREX-2 participates in mRNA export and accurate
CC chromatin positioning in the nucleus by tethering genes to the nuclear
CC periphery. Binds and stabilizes BRCA2 and is thus involved in the
CC control of R-loop-associated DNA damage and thus transcription-
CC associated genomic instability. R-loop accumulation increases in SEM1-
CC depleted cells. {ECO:0000269|PubMed:1317798,
CC ECO:0000269|PubMed:15117943, ECO:0000269|PubMed:22307388,
CC ECO:0000269|PubMed:24896180}.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC regulatory subunits (RP). The regulatory particle is made of a lid
CC composed of 9 subunits including SEM1, a base containing 6 ATPases and
CC few additional components (PubMed:27428775, PubMed:27342858). Belongs
CC to the TREX-2 complex (transcription and export complex 2), composed of
CC at least ENY2, GANP, PCID2, SEM1, and either centrin CETN2 or CETN3
CC (PubMed:22307388). Component of the homologous recombination repair
CC (HR) complex composed of ERCC5/XPG, BRCA2, PALB2, DSS1 and RAD51
CC (PubMed:26833090). Interacts with the C-terminal of BRCA2
CC (PubMed:10373512, PubMed:21719596). {ECO:0000269|PubMed:10373512,
CC ECO:0000269|PubMed:12228710, ECO:0000269|PubMed:21719596,
CC ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:26833090,
CC ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775}.
CC -!- INTERACTION:
CC P60896; P51587: BRCA2; NbExp=10; IntAct=EBI-79819, EBI-79792;
CC P60896; Q01658: DR1; NbExp=3; IntAct=EBI-79819, EBI-750300;
CC P60896; P35637: FUS; NbExp=3; IntAct=EBI-79819, EBI-400434;
CC P60896; P28799: GRN; NbExp=3; IntAct=EBI-79819, EBI-747754;
CC P60896; Q00403: GTF2B; NbExp=3; IntAct=EBI-79819, EBI-389564;
CC P60896; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-79819, EBI-1054873;
CC P60896; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-79819, EBI-1055254;
CC P60896; Q5S007: LRRK2; NbExp=3; IntAct=EBI-79819, EBI-5323863;
CC P60896; P35240-4: NF2; NbExp=3; IntAct=EBI-79819, EBI-1014514;
CC P60896; Q5JVF3: PCID2; NbExp=3; IntAct=EBI-79819, EBI-1051701;
CC P60896; Q5JVF3-1: PCID2; NbExp=3; IntAct=EBI-79819, EBI-15970419;
CC P60896; O43242: PSMD3; NbExp=3; IntAct=EBI-79819, EBI-357622;
CC P60896; P00441: SOD1; NbExp=3; IntAct=EBI-79819, EBI-990792;
CC P60896; Q6NUL7: SPTLC1; NbExp=3; IntAct=EBI-79819, EBI-25912847;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26833090}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1;
CC IsoId=P60896-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZVN7-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Expressed in limb bud, craniofacial primordia and
CC skin.
CC -!- SIMILARITY: Belongs to the DSS1/SEM1 family. {ECO:0000305}.
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DR EMBL; U41515; AAA91179.1; -; mRNA.
DR EMBL; AC073230; AAQ93368.1; -; Genomic_DNA.
DR EMBL; BC032782; AAH32782.1; -; mRNA.
DR CCDS; CCDS5646.1; -. [P60896-1]
DR PIR; G02284; G02284.
DR RefSeq; NP_006295.1; NM_006304.1. [P60896-1]
DR PDB; 1IYJ; X-ray; 3.40 A; A/C=1-70.
DR PDB; 1MIU; X-ray; 3.10 A; B=1-70.
DR PDB; 1MJE; X-ray; 3.50 A; B=1-70.
DR PDB; 3T5X; X-ray; 2.12 A; B=1-70.
DR PDB; 5GJQ; EM; 4.50 A; Y=1-70.
DR PDB; 5GJR; EM; 3.50 A; AB/Y=1-70.
DR PDB; 5L4K; EM; 4.50 A; Y=1-70.
DR PDB; 5LN3; EM; 6.80 A; Y=1-70.
DR PDB; 5M32; EM; 3.80 A; s=1-70.
DR PDB; 5T0C; EM; 3.80 A; Ae/Be=1-70.
DR PDB; 5T0G; EM; 4.40 A; e=1-70.
DR PDB; 5T0H; EM; 6.80 A; e=1-70.
DR PDB; 5T0I; EM; 8.00 A; e=1-70.
DR PDB; 5T0J; EM; 8.00 A; e=1-70.
DR PDB; 5VFR; EM; 4.90 A; e=1-70.
DR PDB; 5VFT; EM; 7.00 A; e=1-70.
DR PDB; 5VGZ; EM; 3.70 A; e=1-70.
DR PDB; 5VHF; EM; 5.70 A; e=1-70.
DR PDB; 5VHH; EM; 6.10 A; e=1-70.
DR PDB; 5VHI; EM; 6.80 A; e=1-70.
DR PDB; 5VHS; EM; 8.80 A; e=38-70.
DR PDB; 6MSB; EM; 3.00 A; e=1-70.
DR PDB; 6MSD; EM; 3.20 A; e=1-70.
DR PDB; 6MSG; EM; 3.50 A; e=1-70.
DR PDB; 6MSH; EM; 3.60 A; e=1-70.
DR PDB; 6MSJ; EM; 3.30 A; e=1-70.
DR PDB; 6MSK; EM; 3.20 A; e=1-70.
DR PDB; 6WJD; EM; 4.80 A; e=1-70.
DR PDB; 6WJN; EM; 5.70 A; e=1-70.
DR PDBsum; 1IYJ; -.
DR PDBsum; 1MIU; -.
DR PDBsum; 1MJE; -.
DR PDBsum; 3T5X; -.
DR PDBsum; 5GJQ; -.
DR PDBsum; 5GJR; -.
DR PDBsum; 5L4K; -.
DR PDBsum; 5LN3; -.
DR PDBsum; 5M32; -.
DR PDBsum; 5T0C; -.
DR PDBsum; 5T0G; -.
DR PDBsum; 5T0H; -.
DR PDBsum; 5T0I; -.
DR PDBsum; 5T0J; -.
DR PDBsum; 5VFR; -.
DR PDBsum; 5VFT; -.
DR PDBsum; 5VGZ; -.
DR PDBsum; 5VHF; -.
DR PDBsum; 5VHH; -.
DR PDBsum; 5VHI; -.
DR PDBsum; 5VHS; -.
DR PDBsum; 6MSB; -.
DR PDBsum; 6MSD; -.
DR PDBsum; 6MSG; -.
DR PDBsum; 6MSH; -.
DR PDBsum; 6MSJ; -.
DR PDBsum; 6MSK; -.
DR PDBsum; 6WJD; -.
DR PDBsum; 6WJN; -.
DR AlphaFoldDB; P60896; -.
DR SMR; P60896; -.
DR BioGRID; 113692; 139.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; P60896; -.
DR DIP; DIP-31023N; -.
DR IntAct; P60896; 85.
DR MINT; P60896; -.
DR ChEMBL; CHEMBL2364701; -.
DR iPTMnet; P60896; -.
DR PhosphoSitePlus; P60896; -.
DR BioMuta; SEM1; -.
DR jPOST; P60896; -.
DR MassIVE; P60896; -.
DR PaxDb; P60896; -.
DR PeptideAtlas; P60896; -.
DR PRIDE; P60896; -.
DR ProteomicsDB; 57235; -.
DR Antibodypedia; 30181; 152 antibodies from 27 providers.
DR DNASU; 7979; -.
DR Ensembl; ENST00000248566.4; ENSP00000248566.2; ENSG00000127922.10. [P60896-1]
DR GeneID; 7979; -.
DR KEGG; hsa:7979; -.
DR MANE-Select; ENST00000248566.4; ENSP00000248566.2; NM_006304.2; NP_006295.1.
DR CTD; 7979; -.
DR DisGeNET; 7979; -.
DR GeneCards; SEM1; -.
DR HGNC; HGNC:10845; SEM1.
DR HPA; ENSG00000127922; Low tissue specificity.
DR MalaCards; SEM1; -.
DR MIM; 601285; gene.
DR neXtProt; NX_P60896; -.
DR OpenTargets; ENSG00000127922; -.
DR Orphanet; 2440; Isolated split hand-split foot malformation.
DR PharmGKB; PA35749; -.
DR VEuPathDB; HostDB:ENSG00000127922; -.
DR GeneTree; ENSGT00940000162732; -.
DR InParanoid; P60896; -.
DR OMA; TLWENNW; -.
DR PhylomeDB; P60896; -.
DR TreeFam; TF314699; -.
DR PathwayCommons; P60896; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
DR Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
DR Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9701192; Defective HDR through Homologous Recombination (HRR) due to BRCA1 loss-of-function.
DR Reactome; R-HSA-9704331; Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function.
DR Reactome; R-HSA-9704646; Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function.
DR Reactome; R-HSA-9709275; Impaired BRCA2 translocation to the nucleus.
DR Reactome; R-HSA-9709570; Impaired BRCA2 binding to RAD51.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-9763198; Impaired BRCA2 binding to SEM1 (DSS1).
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P60896; -.
DR SIGNOR; P60896; -.
DR BioGRID-ORCS; 7979; 665 hits in 1077 CRISPR screens.
DR ChiTaRS; SHFM1; human.
DR EvolutionaryTrace; P60896; -.
DR GeneWiki; SHFM1; -.
DR GenomeRNAi; 7979; -.
DR Pharos; P60896; Tbio.
DR PRO; PR:P60896; -.
DR Proteomes; UP000005640; Chromosome 7.
DR Bgee; ENSG00000127922; Expressed in calcaneal tendon and 202 other tissues.
DR ExpressionAtlas; P60896; baseline and differential.
DR Genevisible; P60896; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IEA:InterPro.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:InterPro.
DR GO; GO:0043248; P:proteasome assembly; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR DisProt; DP00617; -.
DR InterPro; IPR007834; DSS1_SEM1.
DR PANTHER; PTHR16771; PTHR16771; 1.
DR Pfam; PF05160; DSS1_SEM1; 1.
DR SMART; SM01385; DSS1_SEM1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Nucleus; Proteasome;
KW Reference proteome.
FT CHAIN 1..70
FT /note="26S proteasome complex subunit SEM1"
FT /id="PRO_0000122961"
FT VARIANT 17
FT /note="D -> G (in dbSNP:rs1802882)"
FT /id="VAR_012003"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1MIU"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1MJE"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:3T5X"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:3T5X"
SQ SEQUENCE 70 AA; 8278 MW; 0E0F58D2F3D9F723 CRC64;
MSEKKQPVDL GLLEEDDEFE EFPAEDWAGL DEDEDAHVWE DNWDDDNVED DFSNQLRAEL
EKHGYKMETS
