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Protein

Non-structural maintenance of chromosomes element 1 homolog

Gene

NSMCE1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the SMC5-SMC6 complex, a complex involved in DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Has in vitro ubiquitin ligase activity in presence of NSMCE3. Is involved in positive regulation of response to DNA damage stimulus.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri188 – 23447NSE1-typeAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

Metal-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:6.3.2.-)
Short name:
Non-SMC element 1 homolog
Gene namesi
Name:NSMCE1
ORF Names:HSPC333, HSPC337
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:29897. NSMCE1.

Subcellular locationi

  • Nucleus 1 Publication
  • Chromosometelomere 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134943761.

Polymorphism and mutation databases

BioMutaiNSMCE1.
DMDMi209572785.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 266266Non-structural maintenance of chromosomes element 1 homologPRO_0000270944Add
BLAST

Post-translational modificationi

Ubiquitinated.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiQ8WV22.
MaxQBiQ8WV22.
PaxDbiQ8WV22.
PRIDEiQ8WV22.

PTM databases

iPTMnetiQ8WV22.
PhosphoSiteiQ8WV22.

Expressioni

Gene expression databases

BgeeiQ8WV22.
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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NDNL2Q96MG715EBI-2557372,EBI-2557356
SMC6Q96SB88EBI-2557372,EBI-605415

Protein-protein interaction databases

BioGridi128255. 18 interactions.
IntActiQ8WV22. 9 interactions.
MINTiMINT-4786791.
STRINGi9606.ENSP00000355077.

Structurei

Secondary structure

1
266
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 2412Combined sources
Beta strandi25 – 295Combined sources
Helixi30 – 4314Combined sources
Helixi53 – 6412Combined sources
Helixi65 – 673Combined sources
Beta strandi69 – 757Combined sources
Turni77 – 793Combined sources
Beta strandi82 – 9110Combined sources
Helixi95 – 984Combined sources
Helixi103 – 11816Combined sources
Beta strandi119 – 1224Combined sources
Helixi126 – 1305Combined sources
Helixi131 – 1333Combined sources
Beta strandi137 – 1393Combined sources
Helixi143 – 15513Combined sources
Beta strandi158 – 1625Combined sources
Beta strandi165 – 1684Combined sources
Helixi170 – 18314Combined sources
Turni185 – 1873Combined sources
Turni192 – 1943Combined sources
Beta strandi199 – 2035Combined sources
Beta strandi205 – 2073Combined sources
Helixi213 – 2197Combined sources
Turni220 – 2223Combined sources
Turni229 – 2313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CT0NMR-A181-241[»]
3NW0X-ray2.92A9-246[»]
ProteinModelPortaliQ8WV22.
SMRiQ8WV22. Positions 9-246.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WV22.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 102102Interaction with NSMCE3Add
BLAST

Sequence similaritiesi

Belongs to the NSE1 family.Curated
Contains 1 NSE1-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri188 – 23447NSE1-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG4718. Eukaryota.
ENOG4111RNS. LUCA.
GeneTreeiENSGT00390000009084.
HOGENOMiHOG000006778.
HOVERGENiHBG082058.
InParanoidiQ8WV22.
OMAiICNICHS.
PhylomeDBiQ8WV22.
TreeFamiTF314721.

Family and domain databases

InterProiIPR011513. Nse1.
IPR002219. PE/DAG-bd.
IPR001841. Znf_RING.
IPR014857. Znf_RING-like.
[Graphical view]
PANTHERiPTHR20973:SF0. PTHR20973:SF0. 1 hit.
PfamiPF07574. SMC_Nse1. 1 hit.
PF08746. zf-RING-like. 1 hit.
[Graphical view]

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 AAF29011.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence AAF29015.1 differs from that shown. Reason: Frameshift at position 147. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381T → R.
Corresponds to variant rs7195194 [ dbSNP | Ensembl ].
VAR_029822
Natural varianti47 – 471N → S.1 Publication
Corresponds to variant rs17856580 [ dbSNP | Ensembl ].
VAR_029823

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_006721023.2.
UniGeneiHs.284295.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

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_006721023.2.
UniGeneiHs.284295.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CT0NMR-A181-241[»]
3NW0X-ray2.92A9-246[»]
ProteinModelPortaliQ8WV22.
SMRiQ8WV22. Positions 9-246.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128255. 18 interactions.
IntActiQ8WV22. 9 interactions.
MINTiMINT-4786791.
STRINGi9606.ENSP00000355077.

PTM databases

iPTMnetiQ8WV22.
PhosphoSiteiQ8WV22.

Polymorphism and mutation databases

BioMutaiNSMCE1.
DMDMi209572785.

Proteomic databases

EPDiQ8WV22.
MaxQBiQ8WV22.
PaxDbiQ8WV22.
PRIDEiQ8WV22.

Protocols and materials databases

DNASUi197370.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi197370.
GeneCardsiNSMCE1.
H-InvDBHIX0012912.
HGNCiHGNC:29897. NSMCE1.
HPAiHPA041567.
HPA043091.
neXtProtiNX_Q8WV22.
PharmGKBiPA134943761.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4718. Eukaryota.
ENOG4111RNS. LUCA.
GeneTreeiENSGT00390000009084.
HOGENOMiHOG000006778.
HOVERGENiHBG082058.
InParanoidiQ8WV22.
OMAiICNICHS.
PhylomeDBiQ8WV22.
TreeFamiTF314721.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiNSMCE1. human.
EvolutionaryTraceiQ8WV22.
GenomeRNAii197370.
NextBioi89665.
PROiQ8WV22.

Gene expression databases

BgeeiQ8WV22.
CleanExiHS_NSMCE1.
ExpressionAtlasiQ8WV22. baseline and differential.
GenevisibleiQ8WV22. HS.

Family and domain databases

InterProiIPR011513. Nse1.
IPR002219. PE/DAG-bd.
IPR001841. Znf_RING.
IPR014857. Znf_RING-like.
[Graphical view]
PANTHERiPTHR20973:SF0. PTHR20973:SF0. 1 hit.
PfamiPF07574. SMC_Nse1. 1 hit.
PF08746. zf-RING-like. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Umbilical cord blood.
  2. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-266, VARIANT SER-47.
    Tissue: Pancreas.
  5. "Coordination of DNA damage responses via the Smc5/Smc6 complex."
    Harvey S.H., Sheedy D.M., Cuddihy A.R., O'Connell M.J.
    Mol. Cell. Biol. 24:662-674(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMC6.
  6. "Identification of the proteins, including MAGEG1, that make up the human SMC5-6 protein complex."
    Taylor E.M., Copsey A.C., Hudson J.J., Vidot S., Lehmann A.R.
    Mol. Cell. Biol. 28:1197-1206(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION, INTERACTION WITH SMC6; NSMCE2; NSMCE4A AND NSMCE3, IDENTIFICATION IN THE SMC5-SMC6 COMPLEX.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Interactions between the Nse3 and Nse4 components of the SMC5-6 complex identify evolutionarily conserved interactions between MAGE and EID Families."
    Hudson J.J., Bednarova K., Kozakova L., Liao C., Guerineau M., Colnaghi R., Vidot S., Marek J., Bathula S.R., Lehmann A.R., Palecek J.
    PLoS ONE 6:E17270-E17270(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NSMCE3.
  9. "Solution structure of the RING domain of the non-SMC element 1 protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 181-241, ZINC-BINDING.
  10. "MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases."
    Doyle J.M., Gao J., Wang J., Yang M., Potts P.R.
    Mol. Cell 39:963-974(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 9-246 IN COMPLEX WITH NSMCE3, FUNCTION.

Entry informationi

Entry nameiNSE1_HUMAN
AccessioniPrimary (citable) accession number: Q8WV22
Secondary accession number(s): D3DWF6, Q9P045, Q9P049
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: October 14, 2008
Last modified: April 13, 2016
This is version 127 of the entry and version 5 of the sequence. [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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.