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Protein

Selenoprotein M

Gene

SELM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May function as a thiol-disulfide oxidoreductase that participates in disulfide bond formation.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei45 – 451NucleophileBy similarity
Active sitei48 – 481NucleophileBy similarity

Names & Taxonomyi

Protein namesi
Recommended name:
Selenoprotein M
Short name:
SelM
Gene namesi
Name:SELM
Synonyms:SEPM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus

Pathology & Biotechi

Polymorphism and mutation databases

BioMutaiSELM.
DMDMi189034058.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 145122Selenoprotein MPRO_0000022298Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki45 ↔ 48Cysteinyl-selenocysteine (Cys-Sec)Sequence analysis

Proteomic databases

EPDiQ8WWX9.
MaxQBiQ8WWX9.
PaxDbiQ8WWX9.
PeptideAtlasiQ8WWX9.
PRIDEiQ8WWX9.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Organism-specific databases

HPAiCAB008667.
HPA019601.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MTUS2Q5JR593EBI-10277687,EBI-742948
NOTCH2NLQ7Z3S93EBI-10277687,EBI-945833

Protein-protein interaction databases

BioGridi126635. 4 interactions.
IntActiQ8WWX9. 2 interactions.
STRINGi9606.ENSP00000383155.

Structurei

3D structure databases

ProteinModelPortaliQ8WWX9.
SMRiQ8WWX9. Positions 25-145.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the selenoprotein M/SEP15 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IZY6. Eukaryota.
ENOG4112CA8. LUCA.
GeneTreeiENSGT00390000001255.
HOGENOMiHOG000168390.
HOVERGENiHBG108468.
InParanoidiQ8WWX9.
OMAiWAPAKPP.
PhylomeDBiQ8WWX9.

Family and domain databases

InterProiIPR014912. Sep15_SelM.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF08806. Sep15_SelM. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8WWX9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLLLPPLAL LLLLAALVAP ATAATAYRPD WNRLSGLTRA RVETCGGUQL
60 70 80 90 100
NRLKEVKAFV TQDIPFYHNL VMKHLPGADP ELVLLGRRYE ELERIPLSEM
110 120 130 140
TREEINALVQ ELGFYRKAAP DAQVPPEYVW APAKPPEETS DHADL
Length:145
Mass (Da):16,232
Last modified:February 26, 2008 - v3
Checksum:i556A41B02EF694BE
GO

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei48 – 481Selenocysteine

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY043487 mRNA. Translation: AAK95397.1.
AC005005 Genomic DNA. No translation available.
BC013421 mRNA. Translation: AAH13421.1.
BC030236 mRNA. Translation: AAH30236.1.
BC068004 mRNA. Translation: AAH68004.1.
CCDSiCCDS43003.1.
RefSeqiNP_536355.1. NM_080430.2.
UniGeneiHs.55940.

Genome annotation databases

GeneIDi140606.
KEGGihsa:140606.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY043487 mRNA. Translation: AAK95397.1.
AC005005 Genomic DNA. No translation available.
BC013421 mRNA. Translation: AAH13421.1.
BC030236 mRNA. Translation: AAH30236.1.
BC068004 mRNA. Translation: AAH68004.1.
CCDSiCCDS43003.1.
RefSeqiNP_536355.1. NM_080430.2.
UniGeneiHs.55940.

3D structure databases

ProteinModelPortaliQ8WWX9.
SMRiQ8WWX9. Positions 25-145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126635. 4 interactions.
IntActiQ8WWX9. 2 interactions.
STRINGi9606.ENSP00000383155.

Polymorphism and mutation databases

BioMutaiSELM.
DMDMi189034058.

Proteomic databases

EPDiQ8WWX9.
MaxQBiQ8WWX9.
PaxDbiQ8WWX9.
PeptideAtlasiQ8WWX9.
PRIDEiQ8WWX9.

Protocols and materials databases

DNASUi140606.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi140606.
KEGGihsa:140606.

Organism-specific databases

CTDi140606.
GeneCardsiSELM.
H-InvDBHIX0041150.
HPAiCAB008667.
HPA019601.
MIMi610918. gene.
neXtProtiNX_Q8WWX9.

Phylogenomic databases

eggNOGiENOG410IZY6. Eukaryota.
ENOG4112CA8. LUCA.
GeneTreeiENSGT00390000001255.
HOGENOMiHOG000168390.
HOVERGENiHBG108468.
InParanoidiQ8WWX9.
OMAiWAPAKPP.
PhylomeDBiQ8WWX9.

Miscellaneous databases

GenomeRNAii140606.
PROiQ8WWX9.
SOURCEiSearch...

Family and domain databases

InterProiIPR014912. Sep15_SelM.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF08806. Sep15_SelM. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian selenoprotein in which selenocysteine (Sec) incorporation is supported by a new form of Sec insertion sequence element."
    Korotkov K.V., Novoselov S.V., Hatfield D.L., Gladyshev V.N.
    Mol. Cell. Biol. 22:1402-1411(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Brain and Lung.

Entry informationi

Entry nameiSELM_HUMAN
AccessioniPrimary (citable) accession number: Q8WWX9
Secondary accession number(s): A8MPZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: February 26, 2008
Last modified: July 6, 2016
This is version 109 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.