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Protein

Non-structural maintenance of chromosomes element 1 homolog

Gene

NSMCE1

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

Functioni

RING-type zinc finger-containing E3 ubiquitin ligase that assembles with melanoma antigen protein (MAGE) to catalyze the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE stimulates and specifies ubiquitin ligase activity likely through recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme at the E3:substrate complex. Involved in maintenance of genome integrity, DNA damage response and DNA repair (PubMed:29225034, PubMed:20864041). NSMCE3/MAGEG1 and NSMCE1 ubiquitin ligase are components of SMC5-SMC6 complex and may positively regulate homologous recombination-mediated DNA repair (PubMed:18086888). MAGEF1-NSMCE1 ubiquitin ligase promotes proteasomal degradation of MMS19, a key component of the cytosolic iron-sulfur protein assembly (CIA) machinery. Down-regulation of MMS19 impairs the activity of several DNA repair and metabolism enzymes such as ERCC2/XPD, FANCJ, RTEL1 and POLD1 that require iron-sulfur clusters as cofactors (PubMed:29225034).3 Publications

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri191 – 232RING-type; atypicalPROSITE-ProRule annotationAdd BLAST42

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • protein dimerization activity Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processDNA damage, DNA recombination, DNA repair, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-3108214 SUMOylation of DNA damage response and repair proteins

Names & Taxonomyi

Protein namesi
Recommended name:
Non-structural maintenance of chromosomes element 1 homolog (EC:2.3.2.272 Publications)
Short name:
Non-SMC element 1 homolog
Gene namesi
Name:NSMCE1Imported
ORF Names:HSPC333, HSPC337
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

EuPathDBiHostDB:ENSG00000169189.16
HGNCiHGNC:29897 NSMCE1
MIMi617263 gene
neXtProtiNX_Q8WV22

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

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000169189
PharmGKBiPA134943761

Polymorphism and mutation databases

BioMutaiNSMCE1
DMDMi209572785

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002709441 – 266Non-structural maintenance of chromosomes element 1 homologAdd BLAST266

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei251PhosphoserineCombined sources1

Post-translational modificationi

Ubiquitinated.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8WV22
MaxQBiQ8WV22
PaxDbiQ8WV22
PeptideAtlasiQ8WV22
PRIDEiQ8WV22
ProteomicsDBi74738

PTM databases

iPTMnetiQ8WV22
PhosphoSitePlusiQ8WV22

Expressioni

Gene expression databases

BgeeiENSG00000169189
CleanExiHS_NSMCE1
ExpressionAtlasiQ8WV22 baseline and differential
GenevisibleiQ8WV22 HS

Organism-specific databases

HPAiHPA041567
HPA043091

Interactioni

Subunit structurei

Component of the SMC5-SMC6 complex which consists at least of SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NSMCE3. NSMCE1, NSMCE4A or EID3 and NSMCE3 probably form a subcomplex that bridges the head domains of the SMC5-SMC6 heterodimer (PubMed:18086888, PubMed:20864041). Interacts with NSMCE3 (PubMed:27427983). Interacts with MAGEF1 (PubMed:29225034).4 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein dimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi128255, 19 interactors
IntActiQ8WV22, 9 interactors
STRINGi9606.ENSP00000355077

Structurei

Secondary structure

1266
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 24Combined sources12
Beta strandi25 – 29Combined sources5
Helixi30 – 43Combined sources14
Helixi53 – 64Combined sources12
Helixi65 – 67Combined sources3
Beta strandi69 – 75Combined sources7
Turni77 – 79Combined sources3
Beta strandi82 – 91Combined sources10
Helixi95 – 98Combined sources4
Helixi103 – 118Combined sources16
Beta strandi119 – 122Combined sources4
Helixi126 – 130Combined sources5
Helixi131 – 133Combined sources3
Beta strandi137 – 139Combined sources3
Helixi143 – 155Combined sources13
Beta strandi158 – 162Combined sources5
Beta strandi165 – 168Combined sources4
Helixi170 – 183Combined sources14
Turni185 – 187Combined sources3
Beta strandi189 – 191Combined sources3
Turni192 – 194Combined sources3
Beta strandi197 – 200Combined sources4
Beta strandi205 – 207Combined sources3
Helixi213 – 219Combined sources7
Turni220 – 222Combined sources3
Turni229 – 231Combined sources3

3D structure databases

ProteinModelPortaliQ8WV22
SMRiQ8WV22
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WV22

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 102Interaction with NSMCE31 PublicationAdd BLAST102

Sequence similaritiesi

Belongs to the NSE1 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri191 – 232RING-type; atypicalPROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG4718 Eukaryota
ENOG4111RNS LUCA
GeneTreeiENSGT00390000009084
HOGENOMiHOG000006778
HOVERGENiHBG082058
InParanoidiQ8WV22
OMAiNKWLIEK
OrthoDBiEOG091G0JE5
PhylomeDBiQ8WV22
TreeFamiTF314721

Family and domain databases

CDDicd16493 RING-CH-C4HC3_NSE1, 1 hit
Gene3Di1.10.10.10, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR011513 Nse1
IPR002219 PE/DAG-bd
IPR036388 WH-like_DNA-bd_sf
IPR001841 Znf_RING
IPR014857 Znf_RING-like
IPR013083 Znf_RING/FYVE/PHD
PANTHERiPTHR20973 PTHR20973, 1 hit
PfamiView protein in Pfam
PF07574 SMC_Nse1, 1 hit
PF08746 zf-RING-like, 1 hit
PROSITEiView protein in PROSITE
PS50089 ZF_RING_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q8WV22-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQGSTRRMGV MTDVHRRFLQ LLMTHGVLEE WDVKRLQTHC YKVHDRNATV
60 70 80 90 100
DKLEDFINNI NSVLESLYIE IKRGVTEDDG RPIYALVNLA TTSISKMATD
110 120 130 140 150
FAENELDLFR KALELIIDSE TGFASSTNIL NLVDQLKGKK MRKKEAEQVL
160 170 180 190 200
QKFVQNKWLI EKEGEFTLHG RAILEMEQYI RETYPDAVKI CNICHSLLIQ
210 220 230 240 250
GQSCETCGIR MHLPCVAKYF QSNAEPRCPH CNDYWPHEIP KVFDPEKERE
260
SGVLKSNKKS LRSRQH
Length:266
Mass (Da):30,855
Last modified:October 14, 2008 - v5
Checksum:i58A3C2AF70FC8F39
GO

Sequence cautioni

The sequence AAF29011 differs from that shown. Reason: Frameshift at several positions.Curated
The sequence AAF29015 differs from that shown. Reason: Frameshift at position 147.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02982238T → R. Corresponds to variant dbSNP:rs7195194Ensembl.1
Natural variantiVAR_02982347N → S1 PublicationCorresponds to variant dbSNP:rs17856580Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF161451 mRNA Translation: AAF29011.1 Sequence problems.
AF161455 mRNA Translation: AAF29015.1 Sequence problems.
AC106739 Genomic DNA No translation available.
CH471145 Genomic DNA Translation: EAW55756.1
CH471145 Genomic DNA Translation: EAW55757.1
BC018938 mRNA Translation: AAH18938.4
CCDSiCCDS10628.2
RefSeqiNP_659547.2, NM_145080.3
XP_006721086.1, XM_006721023.3
UniGeneiHs.284295

Genome annotation databases

EnsembliENST00000361439; ENSP00000355077; ENSG00000169189
GeneIDi197370
KEGGihsa:197370
UCSCiuc002doi.2 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiNSE1_HUMAN
AccessioniPrimary (citable) accession number: Q8WV22
Secondary accession number(s): D3DWF6, Q9P045, Q9P049
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: October 14, 2008
Last modified: June 20, 2018
This is version 146 of the entry and version 5 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 16
    Human chromosome 16: 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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