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Protein

Selenoprotein P

Gene

SEPP1

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

Functioni

Might be responsible for some of the extracellular antioxidant defense properties of selenium or might be involved in the transport of selenium. May supply selenium to tissues such as brain and testis.

GO - Molecular functioni

  • selenium binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Selenium

Names & Taxonomyi

Protein namesi
Recommended name:
Selenoprotein P
Short name:
SeP
Gene namesi
Name:SEPP1
Synonyms:SELP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:10751. SEPP1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35672.

Polymorphism and mutation databases

BioMutaiSEPP1.
DMDMi172046864.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Add
BLAST
Chaini20 – 381362Selenoprotein PPRO_0000022313Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...)Sequence analysis
Glycosylationi83 – 831N-linked (GlcNAc...) (complex)3 Publications
Glycosylationi119 – 1191N-linked (GlcNAc...)2 Publications
Glycosylationi128 – 1281N-linked (GlcNAc...)1 Publication
Glycosylationi174 – 1741N-linked (GlcNAc...)By similarity
Modified residuei266 – 2661PhosphoserineCombined sources
Glycosylationi338 – 3381N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Phosphorylation sites are present in the extracellular medium.

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP49908.
PRIDEiP49908.

PTM databases

iPTMnetiP49908.
PhosphoSiteiP49908.

Expressioni

Tissue specificityi

Made in the liver and heart and secreted into the plasma. It is also found in the kidney.

Gene expression databases

BgeeiP49908.
CleanExiHS_SELP.
HS_SEPP1.
ExpressionAtlasiP49908. baseline and differential.
GenevisibleiP49908. HS.

Organism-specific databases

HPAiHPA036287.

Interactioni

Protein-protein interaction databases

BioGridi112313. 4 interactions.
IntActiP49908. 15 interactions.
MINTiMINT-6768876.
STRINGi9606.ENSP00000420939.

Structurei

3D structure databases

ProteinModelPortaliP49908.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi244 – 2496Poly-His

Sequence similaritiesi

Belongs to the selenoprotein P family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IXIQ. Eukaryota.
ENOG4111JK7. LUCA.
GeneTreeiENSGT00510000049326.
HOVERGENiHBG108473.
InParanoidiP49908.
OMAiSAITXQC.
OrthoDBiEOG7RFTJ0.
PhylomeDBiP49908.
TreeFamiTF333425.

Family and domain databases

InterProiIPR007671. Selenoprotein-P_N.
IPR007672. SelP_C.
[Graphical view]
PfamiPF04593. SelP_C. 1 hit.
PF04592. SelP_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P49908-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWRSLGLALA LCLLPSGGTE SQDQSSLCKQ PPAWSIRDQD PMLNSNGSVT
60 70 80 90 100
VVALLQASUY LCILQASKLE DLRVKLKKEG YSNISYIVVN HQGISSRLKY
110 120 130 140 150
THLKNKVSEH IPVYQQEENQ TDVWTLLNGS KDDFLIYDRC GRLVYHLGLP
160 170 180 190 200
FSFLTFPYVE EAIKIAYCEK KCGNCSLTTL KDEDFCKRVS LATVDKTVET
210 220 230 240 250
PSPHYHHEHH HNHGHQHLGS SELSENQQPG APNAPTHPAP PGLHHHHKHK
260 270 280 290 300
GQHRQGHPEN RDMPASEDLQ DLQKKLCRKR CINQLLCKLP TDSELAPRSU
310 320 330 340 350
CCHCRHLIFE KTGSAITUQC KENLPSLCSU QGLRAEENIT ESCQURLPPA
360 370 380
AUQISQQLIP TEASASURUK NQAKKUEUPS N
Length:381
Mass (Da):43,174
Last modified:February 26, 2008 - v3
Checksum:i00872B8030840B02
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 652LQ → IE in CAA77836 (PubMed:8421687).Curated
Sequence conflicti187 – 1871K → E in AAH15875 (PubMed:15489334).Curated
Sequence conflicti347 – 3471L → F in AAH46152 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121P → S.1 Publication
Corresponds to variant rs28919895 [ dbSNP | Ensembl ].
VAR_023256
Natural varianti234 – 2341A → T.2 Publications
Corresponds to variant rs3877899 [ dbSNP | Ensembl ].
VAR_023257
Natural varianti278 – 2781R → Q.1 Publication
Corresponds to variant rs28919923 [ dbSNP | Ensembl ].
VAR_023258
Natural varianti314 – 3141S → P.1 Publication
Corresponds to variant rs28919925 [ dbSNP | Ensembl ].
VAR_023259
Natural varianti368 – 3681R → C.1 Publication
Corresponds to variant rs28919926 [ dbSNP | Ensembl ].
VAR_023260

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei59 – 591Selenocysteine
Non-standard residuei300 – 3001Selenocysteine
Non-standard residuei318 – 3181Selenocysteine
Non-standard residuei330 – 3301Selenocysteine
Non-standard residuei345 – 3451Selenocysteine
Non-standard residuei352 – 3521Selenocysteine
Non-standard residuei367 – 3671Selenocysteine
Non-standard residuei369 – 3691Selenocysteine
Non-standard residuei376 – 3761Selenocysteine
Non-standard residuei378 – 3781Selenocysteine

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11793 mRNA. Translation: CAA77836.2.
DQ022288 Genomic DNA. Translation: AAY26400.1.
AC008945 Genomic DNA. No translation available.
BC005244 mRNA. No translation available.
BC015875 mRNA. Translation: AAH15875.1.
BC040075 mRNA. Translation: AAH40075.1.
BC046152 mRNA. Translation: AAH46152.1.
BC058919 mRNA. Translation: AAH58919.1.
CCDSiCCDS43311.1.
PIRiA47327.
RefSeqiNP_001078955.1. NM_001085486.1.
NP_005401.3. NM_005410.2.
UniGeneiHs.275775.
Hs.745017.

Genome annotation databases

EnsembliENST00000506577; ENSP00000425915; ENSG00000250722.
ENST00000511224; ENSP00000427671; ENSG00000250722.
ENST00000514985; ENSP00000420939; ENSG00000250722.
GeneIDi6414.
KEGGihsa:6414.
UCSCiuc011cpt.3. human.

Keywords - Coding sequence diversityi

Polymorphism, Selenocysteine

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11793 mRNA. Translation: CAA77836.2.
DQ022288 Genomic DNA. Translation: AAY26400.1.
AC008945 Genomic DNA. No translation available.
BC005244 mRNA. No translation available.
BC015875 mRNA. Translation: AAH15875.1.
BC040075 mRNA. Translation: AAH40075.1.
BC046152 mRNA. Translation: AAH46152.1.
BC058919 mRNA. Translation: AAH58919.1.
CCDSiCCDS43311.1.
PIRiA47327.
RefSeqiNP_001078955.1. NM_001085486.1.
NP_005401.3. NM_005410.2.
UniGeneiHs.275775.
Hs.745017.

3D structure databases

ProteinModelPortaliP49908.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112313. 4 interactions.
IntActiP49908. 15 interactions.
MINTiMINT-6768876.
STRINGi9606.ENSP00000420939.

PTM databases

iPTMnetiP49908.
PhosphoSiteiP49908.

Polymorphism and mutation databases

BioMutaiSEPP1.
DMDMi172046864.

Proteomic databases

PaxDbiP49908.
PRIDEiP49908.

Protocols and materials databases

DNASUi6414.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000506577; ENSP00000425915; ENSG00000250722.
ENST00000511224; ENSP00000427671; ENSG00000250722.
ENST00000514985; ENSP00000420939; ENSG00000250722.
GeneIDi6414.
KEGGihsa:6414.
UCSCiuc011cpt.3. human.

Organism-specific databases

CTDi6414.
GeneCardsiSEPP1.
H-InvDBHIX0004838.
HGNCiHGNC:10751. SEPP1.
HPAiHPA036287.
MIMi601484. gene.
neXtProtiNX_P49908.
PharmGKBiPA35672.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IXIQ. Eukaryota.
ENOG4111JK7. LUCA.
GeneTreeiENSGT00510000049326.
HOVERGENiHBG108473.
InParanoidiP49908.
OMAiSAITXQC.
OrthoDBiEOG7RFTJ0.
PhylomeDBiP49908.
TreeFamiTF333425.

Miscellaneous databases

GeneWikiiSEPP1.
GenomeRNAii6414.
NextBioi24910.
PROiP49908.
SOURCEiSearch...

Gene expression databases

BgeeiP49908.
CleanExiHS_SELP.
HS_SEPP1.
ExpressionAtlasiP49908. baseline and differential.
GenevisibleiP49908. HS.

Family and domain databases

InterProiIPR007671. Selenoprotein-P_N.
IPR007672. SelP_C.
[Graphical view]
PfamiPF04593. SelP_C. 1 hit.
PF04592. SelP_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Conserved nucleotide sequences in the open reading frame and 3' untranslated region of selenoprotein P mRNA."
    Hill K.E., Lloyd R.S., Burk R.F.
    Proc. Natl. Acad. Sci. U.S.A. 90:537-541(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart and Liver.
  2. Hill K.E.
    Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 59; 300; 318; 330; 345; 352; 367; 369; 376 AND 378.
  3. NIEHS SNPs program
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-112; THR-234; GLN-278; PRO-314 AND CYS-368.
  4. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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], VARIANT THR-234.
    Tissue: Bone marrow, Brain, Liver and PNS.
  6. "Purification of selenoprotein P from human plasma."
    Aakesson B., Bellew T., Burk R.F.
    Biochim. Biophys. Acta 1204:243-249(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  7. "A novel method for the purification of selenoprotein P from human plasma."
    Mostert V., Lombeck I., Abel J.
    Arch. Biochem. Biophys. 357:326-330(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "Selenoprotein P: properties, functions, and regulation."
    Mostert V.
    Arch. Biochem. Biophys. 376:433-438(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  9. "Selenoprotein P. A selenium-rich extracellular glycoprotein."
    Burk R.F., Hill K.E.
    J. Nutr. 124:1891-1897(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  10. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-119 AND ASN-128.
    Tissue: Plasma.
  11. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83 AND ASN-119.
    Tissue: Liver.
  12. Cited for: GLYCOSYLATION AT ASN-83.
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSEPP1_HUMAN
AccessioniPrimary (citable) accession number: P49908
Secondary accession number(s): Q6PD59
, Q6PI43, Q6PI87, Q6PJF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 26, 2008
Last modified: March 16, 2016
This is version 134 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. 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.