Full text data of SELENBP1
SELENBP1
(SBP)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Selenium-binding protein 1 (56 kDa selenium-binding protein; SBP56; SP56)
Selenium-binding protein 1 (56 kDa selenium-binding protein; SBP56; SP56)
hRBCD
IPI00305719
IPI00305719 Similar to Selenium-binding protein 1 selenium binding soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00305719 Similar to Selenium-binding protein 1 selenium binding soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q13228
ID SBP1_HUMAN Reviewed; 472 AA.
AC Q13228; A6NML9; B2RDR3; B4DKP6; B4E1F3; Q49AQ8; Q96GX7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 29-MAY-2007, sequence version 2.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Selenium-binding protein 1;
DE AltName: Full=56 kDa selenium-binding protein;
DE Short=SBP56;
DE Short=SP56;
GN Name=SELENBP1; Synonyms=SBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=9027582;
RX DOI=10.1002/(SICI)1097-4644(199702)64:2<217::AID-JCB5>3.0.CO;2-#;
RA Chang P.W.G., Tsui S.K.W., Liew C., Lee C., Waye M.M.Y., Fung K.;
RT "Isolation, characterization, and chromosomal mapping of a novel cDNA
RT clone encoding human selenium binding protein.";
RL J. Cell. Biochem. 64:217-224(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Colon, Lung, and Synovial cell;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 255-276, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9679983;
RA Yang M., Sytkowski A.J.;
RT "Differential expression and androgen regulation of the human
RT selenium-binding protein gene hSP56 in prostate cancer cells.";
RL Cancer Res. 58:3150-3153(1998).
RN [9]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14991897; DOI=10.1002/path.1524;
RA Chen G., Wang H., Miller C.T., Thomas D.G., Gharib T.G., Misek D.E.,
RA Giordano T.J., Orringer M.B., Hanash S.M., Beer D.G.;
RT "Reduced selenium-binding protein 1 expression is associated with poor
RT outcome in lung adenocarcinomas.";
RL J. Pathol. 202:321-329(2004).
RN [10]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16223876; DOI=10.1073/pnas.0507666102;
RA Glatt S.J., Everall I.P., Kremen W.S., Corbeil J., Sasik R.,
RA Khanlou N., Han M., Liew C.-C., Tsuang M.T.;
RT "Comparative gene expression analysis of blood and brain provides
RT concurrent validation of SELENBP1 up-regulation in schizophrenia.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15533-15538(2005).
RN [11]
RP TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16380993; DOI=10.1002/ijc.21671;
RA Huang K.-C., Park D.C., Ng S.-K., Lee J.Y., Ni X., Ng W.-C.,
RA Bandera C.A., Welch W.R., Berkowitz R.S., Mok S.C., Ng S.-W.;
RT "Selenium binding protein 1 in ovarian cancer.";
RL Int. J. Cancer 118:2433-2440(2006).
RN [12]
RP TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16645984; DOI=10.1002/pmic.200500629;
RA Kim H., Kang H.J., You K.T., Kim S.H., Lee K.Y., Kim T.I., Kim C.,
RA Song S.Y., Kim H.-J., Lee C., Kim H.;
RT "Suppression of human selenium-binding protein 1 is a late event in
RT colorectal carcinogenesis and is associated with poor survival.";
RL Proteomics 6:3466-3476(2006).
RN [13]
RP INTERACTION WITH USP33.
RX PubMed=19118533; DOI=10.1016/j.bbrc.2008.12.110;
RA Jeong J.Y., Wang Y., Sytkowski A.J.;
RT "Human selenium binding protein-1 (hSP56) interacts with VDU1 in a
RT selenium-dependent manner.";
RL Biochem. Biophys. Res. Commun. 379:583-588(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Selenium-binding protein which may be involved in the
CC sensing of reactive xenobiotics in the cytoplasm. May be involved
CC in intra-Golgi protein transport (By similarity).
CC -!- SUBUNIT: Interacts with USP33.
CC -!- INTERACTION:
CC Q8TEY7-2:USP33; NbExp=5; IntAct=EBI-711619, EBI-719307;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Membrane;
CC Peripheral membrane protein (By similarity). Note=May associate
CC with Golgi membrane. May associate with the membrane of
CC autophagosomes (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q13228-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13228-2; Sequence=VSP_038440;
CC Name=3;
CC IsoId=Q13228-3; Sequence=VSP_045425;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, lung, colon,
CC prostate, kidney and pancreas. In brain, present both in neurons
CC and glia (at protein level). Down-regulated in lung
CC adenocarcinoma, colorectal carcinoma and ovarian cancer. Two-fold
CC up-regulated in brain and blood from schizophrenia patients.
CC -!- INDUCTION: Down-regulated by androgen in prostate cancer cells.
CC -!- PTM: Phosphorylated (Probable).
CC -!- PTM: The N-terminus is blocked (By similarity).
CC -!- SIMILARITY: Belongs to the selenium-binding protein family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG59258.1; Type=Miscellaneous discrepancy; Note=Intron retention;
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DR EMBL; U29091; AAB02395.1; -; mRNA.
DR EMBL; CR456852; CAG33133.1; -; mRNA.
DR EMBL; AK296661; BAG59258.1; ALT_SEQ; mRNA.
DR EMBL; AK303815; BAG64765.1; -; mRNA.
DR EMBL; AK315643; BAG38010.1; -; mRNA.
DR EMBL; AL391069; CAH70328.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53443.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53445.1; -; Genomic_DNA.
DR EMBL; BC009084; AAH09084.1; -; mRNA.
DR EMBL; BC032997; AAH32997.1; -; mRNA.
DR PIR; G01872; G01872.
DR RefSeq; NP_001245217.1; NM_001258288.1.
DR RefSeq; NP_001245218.1; NM_001258289.1.
DR RefSeq; NP_003935.2; NM_003944.3.
DR UniGene; Hs.632460; -.
DR ProteinModelPortal; Q13228; -.
DR IntAct; Q13228; 11.
DR MINT; MINT-5005535; -.
DR STRING; 9606.ENSP00000357861; -.
DR DMDM; 148840437; -.
DR REPRODUCTION-2DPAGE; IPI00012303; -.
DR REPRODUCTION-2DPAGE; Q13228; -.
DR UCD-2DPAGE; Q13228; -.
DR PaxDb; Q13228; -.
DR PRIDE; Q13228; -.
DR DNASU; 8991; -.
DR Ensembl; ENST00000368868; ENSP00000357861; ENSG00000143416.
DR Ensembl; ENST00000435071; ENSP00000408263; ENSG00000143416.
DR Ensembl; ENST00000447402; ENSP00000413960; ENSG00000143416.
DR GeneID; 8991; -.
DR KEGG; hsa:8991; -.
DR UCSC; uc010pcz.3; human.
DR CTD; 8991; -.
DR GeneCards; GC01M151339; -.
DR HGNC; HGNC:10719; SELENBP1.
DR HPA; CAB008366; -.
DR HPA; HPA005741; -.
DR HPA; HPA011731; -.
DR MIM; 604188; gene.
DR neXtProt; NX_Q13228; -.
DR PharmGKB; PA35641; -.
DR eggNOG; NOG84363; -.
DR HOGENOM; HOG000263885; -.
DR HOVERGEN; HBG017779; -.
DR InParanoid; Q13228; -.
DR KO; K17285; -.
DR OMA; STEWGAP; -.
DR OrthoDB; EOG76DTS8; -.
DR PhylomeDB; Q13228; -.
DR ChiTaRS; SELENBP1; human.
DR GeneWiki; SELENBP1; -.
DR GenomeRNAi; 8991; -.
DR NextBio; 33715; -.
DR PRO; PR:Q13228; -.
DR ArrayExpress; Q13228; -.
DR Bgee; Q13228; -.
DR CleanEx; HS_SELENBP1; -.
DR Genevestigator; Q13228; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0008430; F:selenium binding; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR008826; Se-bd.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR PANTHER; PTHR23300; PTHR23300; 1.
DR Pfam; PF05694; SBP56; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Membrane; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Selenium; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 472 Selenium-binding protein 1.
FT /FTId=PRO_0000174633.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 467 467 Phosphoserine (By similarity).
FT VAR_SEQ 1 64 Missing (in isoform 2).
FT /FTId=VSP_038440.
FT VAR_SEQ 59 120 Missing (in isoform 3).
FT /FTId=VSP_045425.
FT CONFLICT 80 80 C -> Y (in Ref. 1; AAB02395).
FT CONFLICT 92 92 T -> N (in Ref. 1; AAB02395).
FT CONFLICT 114 116 RAP -> GPQ (in Ref. 1; AAB02395).
FT CONFLICT 135 135 F -> C (in Ref. 1; AAB02395).
FT CONFLICT 260 262 DAA -> SAT (in Ref. 1; AAB02395).
FT CONFLICT 270 273 LSST -> SAPN (in Ref. 1; AAB02395).
FT CONFLICT 278 278 Y -> C (in Ref. 3; BAG59258).
FT CONFLICT 280 282 NEG -> TRE (in Ref. 1; AAB02395).
FT CONFLICT 305 306 EM -> GV (in Ref. 1; AAB02395).
FT CONFLICT 410 410 D -> E (in Ref. 1; AAB02395).
FT CONFLICT 442 442 F -> C (in Ref. 1; AAB02395).
SQ SEQUENCE 472 AA; 52391 MW; 6DC68F9B45FEC1BC CRC64;
MATKCGNCGP GYSTPLEAMK GPREEIVYLP CIYRNTGTEA PDYLATVDVD PKSPQYCQVI
HRLPMPNLKD ELHHSGWNTC SSCFGDSTKS RTKLVLPSLI SSRIYVVDVG SEPRAPKLHK
VIEPKDIHAK CELAFLHTSH CLASGEVMIS SLGDVKGNGK GGFVLLDGET FEVKGTWERP
GGAAPLGYDF WYQPRHNVMI STEWAAPNVL RDGFNPADVE AGLYGSHLYV WDWQRHEIVQ
TLSLKDGLIP LEIRFLHNPD AAQGFVGCAL SSTIQRFYKN EGGTWSVEKV IQVPPKKVKG
WLLPEMPGLI TDILLSLDDR FLYFSNWLHG DLRQYDISDP QRPRLTGQLF LGGSIVKGGP
VQVLEDEELK SQPEPLVVKG KRVAGGPQMI QLSLDGKRLY ITTSLYSAWD KQFYPDLIRE
GSVMLQVDVD TVKGGLKLNP NFLVDFGKEP LGPALAHELR YPGGDCSSDI WI
//
ID SBP1_HUMAN Reviewed; 472 AA.
AC Q13228; A6NML9; B2RDR3; B4DKP6; B4E1F3; Q49AQ8; Q96GX7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 29-MAY-2007, sequence version 2.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Selenium-binding protein 1;
DE AltName: Full=56 kDa selenium-binding protein;
DE Short=SBP56;
DE Short=SP56;
GN Name=SELENBP1; Synonyms=SBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=9027582;
RX DOI=10.1002/(SICI)1097-4644(199702)64:2<217::AID-JCB5>3.0.CO;2-#;
RA Chang P.W.G., Tsui S.K.W., Liew C., Lee C., Waye M.M.Y., Fung K.;
RT "Isolation, characterization, and chromosomal mapping of a novel cDNA
RT clone encoding human selenium binding protein.";
RL J. Cell. Biochem. 64:217-224(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Colon, Lung, and Synovial cell;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 255-276, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9679983;
RA Yang M., Sytkowski A.J.;
RT "Differential expression and androgen regulation of the human
RT selenium-binding protein gene hSP56 in prostate cancer cells.";
RL Cancer Res. 58:3150-3153(1998).
RN [9]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14991897; DOI=10.1002/path.1524;
RA Chen G., Wang H., Miller C.T., Thomas D.G., Gharib T.G., Misek D.E.,
RA Giordano T.J., Orringer M.B., Hanash S.M., Beer D.G.;
RT "Reduced selenium-binding protein 1 expression is associated with poor
RT outcome in lung adenocarcinomas.";
RL J. Pathol. 202:321-329(2004).
RN [10]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16223876; DOI=10.1073/pnas.0507666102;
RA Glatt S.J., Everall I.P., Kremen W.S., Corbeil J., Sasik R.,
RA Khanlou N., Han M., Liew C.-C., Tsuang M.T.;
RT "Comparative gene expression analysis of blood and brain provides
RT concurrent validation of SELENBP1 up-regulation in schizophrenia.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15533-15538(2005).
RN [11]
RP TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16380993; DOI=10.1002/ijc.21671;
RA Huang K.-C., Park D.C., Ng S.-K., Lee J.Y., Ni X., Ng W.-C.,
RA Bandera C.A., Welch W.R., Berkowitz R.S., Mok S.C., Ng S.-W.;
RT "Selenium binding protein 1 in ovarian cancer.";
RL Int. J. Cancer 118:2433-2440(2006).
RN [12]
RP TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16645984; DOI=10.1002/pmic.200500629;
RA Kim H., Kang H.J., You K.T., Kim S.H., Lee K.Y., Kim T.I., Kim C.,
RA Song S.Y., Kim H.-J., Lee C., Kim H.;
RT "Suppression of human selenium-binding protein 1 is a late event in
RT colorectal carcinogenesis and is associated with poor survival.";
RL Proteomics 6:3466-3476(2006).
RN [13]
RP INTERACTION WITH USP33.
RX PubMed=19118533; DOI=10.1016/j.bbrc.2008.12.110;
RA Jeong J.Y., Wang Y., Sytkowski A.J.;
RT "Human selenium binding protein-1 (hSP56) interacts with VDU1 in a
RT selenium-dependent manner.";
RL Biochem. Biophys. Res. Commun. 379:583-588(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Selenium-binding protein which may be involved in the
CC sensing of reactive xenobiotics in the cytoplasm. May be involved
CC in intra-Golgi protein transport (By similarity).
CC -!- SUBUNIT: Interacts with USP33.
CC -!- INTERACTION:
CC Q8TEY7-2:USP33; NbExp=5; IntAct=EBI-711619, EBI-719307;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Membrane;
CC Peripheral membrane protein (By similarity). Note=May associate
CC with Golgi membrane. May associate with the membrane of
CC autophagosomes (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q13228-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13228-2; Sequence=VSP_038440;
CC Name=3;
CC IsoId=Q13228-3; Sequence=VSP_045425;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, lung, colon,
CC prostate, kidney and pancreas. In brain, present both in neurons
CC and glia (at protein level). Down-regulated in lung
CC adenocarcinoma, colorectal carcinoma and ovarian cancer. Two-fold
CC up-regulated in brain and blood from schizophrenia patients.
CC -!- INDUCTION: Down-regulated by androgen in prostate cancer cells.
CC -!- PTM: Phosphorylated (Probable).
CC -!- PTM: The N-terminus is blocked (By similarity).
CC -!- SIMILARITY: Belongs to the selenium-binding protein family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG59258.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC -----------------------------------------------------------------------
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DR EMBL; U29091; AAB02395.1; -; mRNA.
DR EMBL; CR456852; CAG33133.1; -; mRNA.
DR EMBL; AK296661; BAG59258.1; ALT_SEQ; mRNA.
DR EMBL; AK303815; BAG64765.1; -; mRNA.
DR EMBL; AK315643; BAG38010.1; -; mRNA.
DR EMBL; AL391069; CAH70328.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53443.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53445.1; -; Genomic_DNA.
DR EMBL; BC009084; AAH09084.1; -; mRNA.
DR EMBL; BC032997; AAH32997.1; -; mRNA.
DR PIR; G01872; G01872.
DR RefSeq; NP_001245217.1; NM_001258288.1.
DR RefSeq; NP_001245218.1; NM_001258289.1.
DR RefSeq; NP_003935.2; NM_003944.3.
DR UniGene; Hs.632460; -.
DR ProteinModelPortal; Q13228; -.
DR IntAct; Q13228; 11.
DR MINT; MINT-5005535; -.
DR STRING; 9606.ENSP00000357861; -.
DR DMDM; 148840437; -.
DR REPRODUCTION-2DPAGE; IPI00012303; -.
DR REPRODUCTION-2DPAGE; Q13228; -.
DR UCD-2DPAGE; Q13228; -.
DR PaxDb; Q13228; -.
DR PRIDE; Q13228; -.
DR DNASU; 8991; -.
DR Ensembl; ENST00000368868; ENSP00000357861; ENSG00000143416.
DR Ensembl; ENST00000435071; ENSP00000408263; ENSG00000143416.
DR Ensembl; ENST00000447402; ENSP00000413960; ENSG00000143416.
DR GeneID; 8991; -.
DR KEGG; hsa:8991; -.
DR UCSC; uc010pcz.3; human.
DR CTD; 8991; -.
DR GeneCards; GC01M151339; -.
DR HGNC; HGNC:10719; SELENBP1.
DR HPA; CAB008366; -.
DR HPA; HPA005741; -.
DR HPA; HPA011731; -.
DR MIM; 604188; gene.
DR neXtProt; NX_Q13228; -.
DR PharmGKB; PA35641; -.
DR eggNOG; NOG84363; -.
DR HOGENOM; HOG000263885; -.
DR HOVERGEN; HBG017779; -.
DR InParanoid; Q13228; -.
DR KO; K17285; -.
DR OMA; STEWGAP; -.
DR OrthoDB; EOG76DTS8; -.
DR PhylomeDB; Q13228; -.
DR ChiTaRS; SELENBP1; human.
DR GeneWiki; SELENBP1; -.
DR GenomeRNAi; 8991; -.
DR NextBio; 33715; -.
DR PRO; PR:Q13228; -.
DR ArrayExpress; Q13228; -.
DR Bgee; Q13228; -.
DR CleanEx; HS_SELENBP1; -.
DR Genevestigator; Q13228; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0008430; F:selenium binding; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR008826; Se-bd.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR PANTHER; PTHR23300; PTHR23300; 1.
DR Pfam; PF05694; SBP56; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Membrane; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Selenium; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 472 Selenium-binding protein 1.
FT /FTId=PRO_0000174633.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 467 467 Phosphoserine (By similarity).
FT VAR_SEQ 1 64 Missing (in isoform 2).
FT /FTId=VSP_038440.
FT VAR_SEQ 59 120 Missing (in isoform 3).
FT /FTId=VSP_045425.
FT CONFLICT 80 80 C -> Y (in Ref. 1; AAB02395).
FT CONFLICT 92 92 T -> N (in Ref. 1; AAB02395).
FT CONFLICT 114 116 RAP -> GPQ (in Ref. 1; AAB02395).
FT CONFLICT 135 135 F -> C (in Ref. 1; AAB02395).
FT CONFLICT 260 262 DAA -> SAT (in Ref. 1; AAB02395).
FT CONFLICT 270 273 LSST -> SAPN (in Ref. 1; AAB02395).
FT CONFLICT 278 278 Y -> C (in Ref. 3; BAG59258).
FT CONFLICT 280 282 NEG -> TRE (in Ref. 1; AAB02395).
FT CONFLICT 305 306 EM -> GV (in Ref. 1; AAB02395).
FT CONFLICT 410 410 D -> E (in Ref. 1; AAB02395).
FT CONFLICT 442 442 F -> C (in Ref. 1; AAB02395).
SQ SEQUENCE 472 AA; 52391 MW; 6DC68F9B45FEC1BC CRC64;
MATKCGNCGP GYSTPLEAMK GPREEIVYLP CIYRNTGTEA PDYLATVDVD PKSPQYCQVI
HRLPMPNLKD ELHHSGWNTC SSCFGDSTKS RTKLVLPSLI SSRIYVVDVG SEPRAPKLHK
VIEPKDIHAK CELAFLHTSH CLASGEVMIS SLGDVKGNGK GGFVLLDGET FEVKGTWERP
GGAAPLGYDF WYQPRHNVMI STEWAAPNVL RDGFNPADVE AGLYGSHLYV WDWQRHEIVQ
TLSLKDGLIP LEIRFLHNPD AAQGFVGCAL SSTIQRFYKN EGGTWSVEKV IQVPPKKVKG
WLLPEMPGLI TDILLSLDDR FLYFSNWLHG DLRQYDISDP QRPRLTGQLF LGGSIVKGGP
VQVLEDEELK SQPEPLVVKG KRVAGGPQMI QLSLDGKRLY ITTSLYSAWD KQFYPDLIRE
GSVMLQVDVD TVKGGLKLNP NFLVDFGKEP LGPALAHELR YPGGDCSSDI WI
//
MIM
604188
*RECORD*
*FIELD* NO
604188
*FIELD* TI
*604188 SELENIUM-BINDING PROTEIN 1; SELENBP1
;;SELENIUM-BINDING PROTEIN, 56-KD; SP56
read more*FIELD* TX
CLONING
Selenium is an essential nutrient that exhibits potent anticarcinogenic
properties, and deficiency of selenium may cause certain neurologic
diseases. It has been proposed that the effects of selenium in
preventing cancer and neurologic diseases may be mediated by
selenium-binding proteins. By sequencing randomly selected human fetal
heart cDNAs, followed by searching sequence databases for sequence
similarities, Chang et al. (1997) identified a cDNA that has sequence
similarity to the mouse 56-kD selenium-binding protein (Sp56) gene. The
deduced 472-amino acid human SP56 (SELENBP1) has 87.3% and 86.4% amino
acid identity to mouse Sp56 and the acetaminophen metabolite-binding
protein AP56, respectively. Northern blot analysis of mouse tissues
detected the highest Sp56 expression in liver, kidney, and lung (see
also Lanfear et al., 1993).
GENE FUNCTION
Okunuki et al. (2007) identified selenium-binding protein as a candidate
retinal autoantigen in patients with Behcet disease (109650). Because
anti-SELENBP1 antibody-positive patients showed more frequent ocular
inflammation than the antibody-negative patient group, Okunuki et al.
(2007) concluded that autoimmunity against this retinal antigen might
contribute to the pathogenesis of uveitis in BD patients.
MAPPING
By FISH, Chang et al. (1997) mapped the SELENBP1 gene to 1q21-q22.
*FIELD* RF
1. Chang, P. W. G.; Tsui, S. K. W.; Liew, C.; Lee, C.; Waye, M. M.
Y.; Fung, K.: Isolation, characterization, and chromosomal mapping
of a novel cDNA clone encoding human selenium binding protein. J.
Cell. Biochem. 64: 217-224, 1997.
2. Lanfear, J.; Fleming, J.; Walker, M.; Harrison, P.: Different
patterns of regulation of the genes encoding the closely related 56
kDa selenium- and acetaminophen-binding proteins in normal tissues
and during carcinogenesis. Carcinogenesis 14: 335-340, 1993.
3. Okunuki, Y.; Usui, Y.; Takeuchi, M.; Kezuka, T.; Hattori, T.; Masuko,
K.; Nakamura, H.; Yudoh, K.; Usui, M.; Nishioka, K.; Kato, T.: Proteomic
surveillance of autoimmunity in Behcet's disease with uveitis: selenium
binding protein is a novel autoantigen in Behcet's disease. Exp.
Eye Res. 84: 823-831, 2007.
*FIELD* CN
Jane Kelly - updated: 04/22/2008
*FIELD* CD
Patti M. Sherman: 9/24/1999
*FIELD* ED
carol: 04/22/2008
mgross: 9/29/1999
mgross: 9/27/1999
psherman: 9/26/1999
*RECORD*
*FIELD* NO
604188
*FIELD* TI
*604188 SELENIUM-BINDING PROTEIN 1; SELENBP1
;;SELENIUM-BINDING PROTEIN, 56-KD; SP56
read more*FIELD* TX
CLONING
Selenium is an essential nutrient that exhibits potent anticarcinogenic
properties, and deficiency of selenium may cause certain neurologic
diseases. It has been proposed that the effects of selenium in
preventing cancer and neurologic diseases may be mediated by
selenium-binding proteins. By sequencing randomly selected human fetal
heart cDNAs, followed by searching sequence databases for sequence
similarities, Chang et al. (1997) identified a cDNA that has sequence
similarity to the mouse 56-kD selenium-binding protein (Sp56) gene. The
deduced 472-amino acid human SP56 (SELENBP1) has 87.3% and 86.4% amino
acid identity to mouse Sp56 and the acetaminophen metabolite-binding
protein AP56, respectively. Northern blot analysis of mouse tissues
detected the highest Sp56 expression in liver, kidney, and lung (see
also Lanfear et al., 1993).
GENE FUNCTION
Okunuki et al. (2007) identified selenium-binding protein as a candidate
retinal autoantigen in patients with Behcet disease (109650). Because
anti-SELENBP1 antibody-positive patients showed more frequent ocular
inflammation than the antibody-negative patient group, Okunuki et al.
(2007) concluded that autoimmunity against this retinal antigen might
contribute to the pathogenesis of uveitis in BD patients.
MAPPING
By FISH, Chang et al. (1997) mapped the SELENBP1 gene to 1q21-q22.
*FIELD* RF
1. Chang, P. W. G.; Tsui, S. K. W.; Liew, C.; Lee, C.; Waye, M. M.
Y.; Fung, K.: Isolation, characterization, and chromosomal mapping
of a novel cDNA clone encoding human selenium binding protein. J.
Cell. Biochem. 64: 217-224, 1997.
2. Lanfear, J.; Fleming, J.; Walker, M.; Harrison, P.: Different
patterns of regulation of the genes encoding the closely related 56
kDa selenium- and acetaminophen-binding proteins in normal tissues
and during carcinogenesis. Carcinogenesis 14: 335-340, 1993.
3. Okunuki, Y.; Usui, Y.; Takeuchi, M.; Kezuka, T.; Hattori, T.; Masuko,
K.; Nakamura, H.; Yudoh, K.; Usui, M.; Nishioka, K.; Kato, T.: Proteomic
surveillance of autoimmunity in Behcet's disease with uveitis: selenium
binding protein is a novel autoantigen in Behcet's disease. Exp.
Eye Res. 84: 823-831, 2007.
*FIELD* CN
Jane Kelly - updated: 04/22/2008
*FIELD* CD
Patti M. Sherman: 9/24/1999
*FIELD* ED
carol: 04/22/2008
mgross: 9/29/1999
mgross: 9/27/1999
psherman: 9/26/1999