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Protein

26S proteasome complex subunit SEM1

Gene

SEM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Biological processi

Enzyme and pathway databases

ReactomeiR-HSA-1169091 Activation of NF-kappaB in B cells
R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-1236974 ER-Phagosome pathway
R-HSA-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-HSA-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-HSA-174113 SCF-beta-TrCP mediated degradation of Emi1
R-HSA-174154 APC/C:Cdc20 mediated degradation of Securin
R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-180534 Vpu mediated degradation of CD4
R-HSA-180585 Vif-mediated degradation of APOBEC3G
R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-195253 Degradation of beta-catenin by the destruction complex
R-HSA-202424 Downstream TCR signaling
R-HSA-211733 Regulation of activated PAK-2p34 by proteasome mediated degradation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-HSA-350562 Regulation of ornithine decarboxylase (ODC)
R-HSA-382556 ABC-family proteins mediated transport
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-4608870 Asymmetric localization of PCP proteins
R-HSA-4641257 Degradation of AXIN
R-HSA-4641258 Degradation of DVL
R-HSA-5358346 Hedgehog ligand biogenesis
R-HSA-5362768 Hh mutants that don't undergo autocatalytic processing are degraded by ERAD
R-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5610780 Degradation of GLI1 by the proteasome
R-HSA-5610783 Degradation of GLI2 by the proteasome
R-HSA-5610785 GLI3 is processed to GLI3R by the proteasome
R-HSA-5632684 Hedgehog 'on' state
R-HSA-5658442 Regulation of RAS by GAPs
R-HSA-5668541 TNFR2 non-canonical NF-kB pathway
R-HSA-5676590 NIK-->noncanonical NF-kB signaling
R-HSA-5678895 Defective CFTR causes cystic fibrosis
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-5689603 UCH proteinases
R-HSA-5689880 Ub-specific processing proteases
R-HSA-68827 CDT1 association with the CDC6:ORC:origin complex
R-HSA-68949 Orc1 removal from chromatin
R-HSA-69017 CDK-mediated phosphorylation and removal of Cdc6
R-HSA-69229 Ubiquitin-dependent degradation of Cyclin D1
R-HSA-69481 G2/M Checkpoints
R-HSA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8941858 Regulation of RUNX3 expression and activity
R-HSA-8948751 Regulation of PTEN stability and activity
R-HSA-8951664 Neddylation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-9020702 Interleukin-1 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome complex subunit SEM1
Alternative name(s):
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
Gene namesi
Name:SEM1Imported
Synonyms:C7orf76, DSS1, SHFDG1, SHFM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

EuPathDBiHostDB:ENSG00000127922.9
HGNCiHGNC:10845 SEM1
MIMi601285 gene
neXtProtiNX_P60896

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Proteasome

Pathology & Biotechi

Organism-specific databases

DisGeNETi7979
MalaCardsiSEM1
OpenTargetsiENSG00000127922
Orphaneti2440 Split hand-split foot malformation
PharmGKBiPA35749

Chemistry databases

ChEMBLiCHEMBL2364701

Polymorphism and mutation databases

BioMutaiSHFM1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001229611 – 7026S proteasome complex subunit SEM1Add BLAST70

Proteomic databases

PaxDbiP60896
PeptideAtlasiP60896
PRIDEiP60896
TopDownProteomicsiP60896

PTM databases

iPTMnetiP60896
PhosphoSitePlusiP60896

Expressioni

Tissue specificityi

Expressed in limb bud, craniofacial primordia and skin.

Gene expression databases

BgeeiENSG00000127922
CleanExiHS_SHFM1
ExpressionAtlasiP60896 baseline and differential
GenevisibleiP60896 HS

Organism-specific databases

HPAiHPA072648

Interactioni

Subunit structurei

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).6 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi113692, 137 interactors
CORUMiP60896
DIPiDIP-31023N
IntActiP60896, 73 interactors
MINTiP60896
STRINGi9606.ENSP00000248566

Structurei

Secondary structure

170
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 12Combined sources3
Beta strandi21 – 23Combined sources3
Helixi42 – 44Combined sources3
Helixi51 – 62Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IYJX-ray3.40A/C1-70[»]
1MIUX-ray3.10B1-70[»]
1MJEX-ray3.50B1-70[»]
3T5XX-ray2.12B1-70[»]
5GJQelectron microscopy4.50Y1-70[»]
5GJRelectron microscopy3.50AB/Y1-70[»]
5L4Kelectron microscopy4.50Y1-70[»]
5LN3electron microscopy6.80Y1-70[»]
5M32electron microscopy3.80s1-70[»]
5T0Celectron microscopy3.80Ae/Be1-70[»]
5T0Gelectron microscopy4.40e1-70[»]
5T0Helectron microscopy6.80e1-70[»]
5T0Ielectron microscopy8.00e1-70[»]
5T0Jelectron microscopy8.00e1-70[»]
5VGZelectron microscopy3.70e1-70[»]
5VHFelectron microscopy5.70e1-70[»]
5VHHelectron microscopy6.10e1-70[»]
5VHIelectron microscopy6.80e1-70[»]
5VHSelectron microscopy8.80e38-70[»]
DisProtiDP00617
ProteinModelPortaliP60896
SMRiP60896
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60896

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi14 – 21Asp/Glu-rich (highly acidic)8
Compositional biasi31 – 35Asp/Glu-rich (highly acidic)5
Compositional biasi40 – 51Asp/Glu-rich (highly acidic)Add BLAST12

Sequence similaritiesi

Belongs to the DSS1/SEM1 family.Curated

Phylogenomic databases

eggNOGiKOG4764 Eukaryota
ENOG41126I3 LUCA
GeneTreeiENSGT00390000002695
HOVERGENiHBG005536
InParanoidiP60896
OMAiEELSVWE
PhylomeDBiP60896
TreeFamiTF314699

Family and domain databases

InterProiView protein in InterPro
IPR007834 DSS1_SEM1
PANTHERiPTHR16771 PTHR16771, 1 hit
PfamiView protein in Pfam
PF05160 DSS1_SEM1, 1 hit
SMARTiView protein in SMART
SM01385 DSS1_SEM1, 1 hit

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative promoter usage. AlignAdd to basket

Isoform 1 (identifier: P60896-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSEKKQPVDL GLLEEDDEFE EFPAEDWAGL DEDEDAHVWE DNWDDDNVED
60 70
DFSNQLRAEL EKHGYKMETS
Length:70
Mass (Da):8,278
Last modified:April 13, 2004 - v1
Checksum:i0E0F58D2F3D9F723
GO
Isoform 2 (identifier: Q6ZVN7-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry Q6ZVN7.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:128
Mass (Da):14,085
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01200317D → G. Corresponds to variant dbSNP:rs1802882Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41515 mRNA Translation: AAA91179.1
AC073230 Genomic DNA Translation: AAQ93368.1
BC032782 mRNA Translation: AAH32782.1
CCDSiCCDS5646.1 [P60896-1]
PIRiG02284
RefSeqiNP_006295.1, NM_006304.1 [P60896-1]
UniGeneiHs.489201
Hs.729869
Hs.734935

Genome annotation databases

EnsembliENST00000248566; ENSP00000248566; ENSG00000127922 [P60896-1]
GeneIDi7979

Keywords - Coding sequence diversityi

Alternative promoter usage, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiSEM1_HUMAN
AccessioniPrimary (citable) accession number: P60896
Secondary accession number(s): Q13437, Q61067
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: May 23, 2018
This is version 134 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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