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Q13228 (SBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Selenium-binding protein 1
Alternative name(s):
56 kDa selenium-binding protein
Short name=SBP56
Short name=SP56
Gene names
Name:SELENBP1
Synonyms:SBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length472 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Selenium-binding protein which may be involved in the sensing of reactive xenobiotics in the cytoplasm. May be involved in intra-Golgi protein transport By similarity.

Subunit structure

Interacts with USP33. Ref.13

Subcellular location

Nucleus. Cytoplasmcytosol. Membrane; Peripheral membrane protein By similarity. Note: May associate with Golgi membrane. May associate with the membrane of autophagosomes By similarity. Ref.9 Ref.10

Tissue specificity

Highly expressed in liver, lung, colon, prostate, kidney and pancreas. In brain, present both in neurons and glia (at protein level). Down-regulated in lung adenocarcinoma, colorectal carcinoma and ovarian cancer. Two-fold up-regulated in brain and blood from schizophrenia patients. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Induction

Down-regulated by androgen in prostate cancer cells. Ref.8

Post-translational modification

Phosphorylated Probable. Ref.9

The N-terminus is blocked By similarity.

Sequence similarities

Belongs to the selenium-binding protein family.

Sequence caution

The sequence BAG59258.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   LigandSelenium
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processprotein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionselenium binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

USP33Q8TEY7-25EBI-711619,EBI-719307

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13228-1)

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.
Isoform 2 (identifier: Q13228-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-64: Missing.
Isoform 3 (identifier: Q13228-3)

The sequence of this isoform differs from the canonical sequence as follows:
     59-120: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 472471Selenium-binding protein 1
PRO_0000174633

Amino acid modifications

Modified residue21N-acetylalanine Ref.15
Modified residue4671Phosphoserine By similarity

Natural variations

Alternative sequence1 – 6464Missing in isoform 2.
VSP_038440
Alternative sequence59 – 12062Missing in isoform 3.
VSP_045425

Experimental info

Sequence conflict801C → Y in AAB02395. Ref.1
Sequence conflict921T → N in AAB02395. Ref.1
Sequence conflict114 – 1163RAP → GPQ in AAB02395. Ref.1
Sequence conflict1351F → C in AAB02395. Ref.1
Sequence conflict260 – 2623DAA → SAT in AAB02395. Ref.1
Sequence conflict270 – 2734LSST → SAPN in AAB02395. Ref.1
Sequence conflict2781Y → C in BAG59258. Ref.3
Sequence conflict280 – 2823NEG → TRE in AAB02395. Ref.1
Sequence conflict305 – 3062EM → GV in AAB02395. Ref.1
Sequence conflict4101D → E in AAB02395. Ref.1
Sequence conflict4421F → C in AAB02395. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 29, 2007. Version 2.
Checksum: 6DC68F9B45FEC1BC

FASTA47252,391
        10         20         30         40         50         60 
MATKCGNCGP GYSTPLEAMK GPREEIVYLP CIYRNTGTEA PDYLATVDVD PKSPQYCQVI 

        70         80         90        100        110        120 
HRLPMPNLKD ELHHSGWNTC SSCFGDSTKS RTKLVLPSLI SSRIYVVDVG SEPRAPKLHK 

       130        140        150        160        170        180 
VIEPKDIHAK CELAFLHTSH CLASGEVMIS SLGDVKGNGK GGFVLLDGET FEVKGTWERP 

       190        200        210        220        230        240 
GGAAPLGYDF WYQPRHNVMI STEWAAPNVL RDGFNPADVE AGLYGSHLYV WDWQRHEIVQ 

       250        260        270        280        290        300 
TLSLKDGLIP LEIRFLHNPD AAQGFVGCAL SSTIQRFYKN EGGTWSVEKV IQVPPKKVKG 

       310        320        330        340        350        360 
WLLPEMPGLI TDILLSLDDR FLYFSNWLHG DLRQYDISDP QRPRLTGQLF LGGSIVKGGP 

       370        380        390        400        410        420 
VQVLEDEELK SQPEPLVVKG KRVAGGPQMI QLSLDGKRLY ITTSLYSAWD KQFYPDLIRE 

       430        440        450        460        470 
GSVMLQVDVD TVKGGLKLNP NFLVDFGKEP LGPALAHELR YPGGDCSSDI WI 

« Hide

Isoform 2 [UniParc].

Checksum: 7765636B7CE8ACA7
Show »

FASTA40845,349
Isoform 3 [UniParc].

Checksum: 966714583DDE49F3
Show »

FASTA41045,469

References

« Hide 'large scale' references
[1]"Isolation, characterization, and chromosomal mapping of a novel cDNA clone encoding human selenium binding protein."
Chang P.W.G., Tsui S.K.W., Liew C., Lee C., Waye M.M.Y., Fung K.
J. Cell. Biochem. 64:217-224(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Heart.
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: Colon, Lung and Synovial cell.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORMS 1 AND 2).
Tissue: Colon and Testis.
[7]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 255-276, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[8]"Differential expression and androgen regulation of the human selenium-binding protein gene hSP56 in prostate cancer cells."
Yang M., Sytkowski A.J.
Cancer Res. 58:3150-3153(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[9]"Reduced selenium-binding protein 1 expression is associated with poor outcome in lung adenocarcinomas."
Chen G., Wang H., Miller C.T., Thomas D.G., Gharib T.G., Misek D.E., Giordano T.J., Orringer M.B., Hanash S.M., Beer D.G.
J. Pathol. 202:321-329(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Comparative gene expression analysis of blood and brain provides concurrent validation of SELENBP1 up-regulation in schizophrenia."
Glatt S.J., Everall I.P., Kremen W.S., Corbeil J., Sasik R., Khanlou N., Han M., Liew C.-C., Tsuang M.T.
Proc. Natl. Acad. Sci. U.S.A. 102:15533-15538(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[11]"Selenium binding protein 1 in ovarian cancer."
Huang K.-C., Park D.C., Ng S.-K., Lee J.Y., Ni X., Ng W.-C., Bandera C.A., Welch W.R., Berkowitz R.S., Mok S.C., Ng S.-W.
Int. J. Cancer 118:2433-2440(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"Suppression of human selenium-binding protein 1 is a late event in colorectal carcinogenesis and is associated with poor survival."
Kim H., Kang H.J., You K.T., Kim S.H., Lee K.Y., Kim T.I., Kim C., Song S.Y., Kim H.-J., Lee C., Kim H.
Proteomics 6:3466-3476(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
[13]"Human selenium binding protein-1 (hSP56) interacts with VDU1 in a selenium-dependent manner."
Jeong J.Y., Wang Y., Sytkowski A.J.
Biochem. Biophys. Res. Commun. 379:583-588(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH USP33.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U29091 mRNA. Translation: AAB02395.1.
CR456852 mRNA. Translation: CAG33133.1.
AK296661 mRNA. Translation: BAG59258.1. Sequence problems.
AK303815 mRNA. Translation: BAG64765.1.
AK315643 mRNA. Translation: BAG38010.1.
AL391069 Genomic DNA. Translation: CAH70328.1.
CH471121 Genomic DNA. Translation: EAW53443.1.
CH471121 Genomic DNA. Translation: EAW53445.1.
BC009084 mRNA. Translation: AAH09084.1.
BC032997 mRNA. Translation: AAH32997.1.
PIRG01872.
RefSeqNP_001245217.1. NM_001258288.1.
NP_001245218.1. NM_001258289.1.
NP_003935.2. NM_003944.3.
UniGeneHs.632460.

3D structure databases

ProteinModelPortalQ13228.
SMRQ13228. Positions 10-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114472. 26 interactions.
IntActQ13228. 11 interactions.
MINTMINT-5005535.
STRING9606.ENSP00000357861.

Polymorphism databases

DMDM148840437.

2D gel databases

REPRODUCTION-2DPAGEIPI00012303.
Q13228.
UCD-2DPAGEQ13228.

Proteomic databases

PaxDbQ13228.
PRIDEQ13228.

Protocols and materials databases

DNASU8991.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368868; ENSP00000357861; ENSG00000143416. [Q13228-1]
ENST00000435071; ENSP00000408263; ENSG00000143416. [Q13228-2]
ENST00000447402; ENSP00000413960; ENSG00000143416. [Q13228-3]
GeneID8991.
KEGGhsa:8991.
UCSCuc001exx.4. human. [Q13228-1]

Organism-specific databases

CTD8991.
GeneCardsGC01M151339.
HGNCHGNC:10719. SELENBP1.
HPACAB008366.
HPA005741.
HPA011731.
MIM604188. gene.
neXtProtNX_Q13228.
PharmGKBPA35641.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG84363.
HOGENOMHOG000263885.
HOVERGENHBG017779.
InParanoidQ13228.
KOK17285.
OMASTEWGAP.
OrthoDBEOG76DTS8.
PhylomeDBQ13228.
TreeFamTF315241.

Gene expression databases

ArrayExpressQ13228.
BgeeQ13228.
CleanExHS_SELENBP1.
GenevestigatorQ13228.

Family and domain databases

Gene3D2.130.10.10. 2 hits.
InterProIPR008826. Se-bd.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PANTHERPTHR23300. PTHR23300. 1 hit.
PfamPF05694. SBP56. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSELENBP1. human.
GeneWikiSELENBP1.
GenomeRNAi8991.
NextBio33715.
PROQ13228.
SOURCESearch...

Entry information

Entry nameSBP1_HUMAN
AccessionPrimary (citable) accession number: Q13228
Secondary accession number(s): A6NML9 expand/collapse secondary AC list , B2RDR3, B4DKP6, B4E1F3, Q49AQ8, Q96GX7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 29, 2007
Last modified: April 16, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM