Full text data of SPRR2B
SPRR2B
[Confidence: low (only semi-automatic identification from reviews)]
Small proline-rich protein 2B; SPR-2B
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Small proline-rich protein 2B; SPR-2B
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P35325
ID SPR2B_HUMAN Reviewed; 72 AA.
AC P35325; Q5T528;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1994, sequence version 1.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Small proline-rich protein 2B;
DE Short=SPR-2B;
GN Name=SPRR2B;
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 [GENOMIC DNA].
RC TISSUE=Skin;
RX PubMed=8325635; DOI=10.1006/geno.1993.1240;
RA Gibbs S., Fijneman R., Wiegant J., Geurts van Kessel A.,
RA van de Putte P., Backendorf C.;
RT "Molecular characterization and evolution of the SPRR family of
RT keratinocyte differentiation markers encoding small proline-rich
RT proteins.";
RL Genomics 16:630-637(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11279051; DOI=10.1074/jbc.M100336200;
RA Cabral A., Voskamp P., Cleton-Jansen A.-M., South A., Nizetic D.,
RA Backendorf C.;
RT "Structural organization and regulation of the small proline-rich
RT family of cornified envelope precursors suggest a role in adaptive
RT barrier function.";
RL J. Biol. Chem. 276:19231-19237(2001).
RN [3]
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).
CC -!- FUNCTION: Cross-linked envelope protein of keratinocytes. It is a
CC keratinocyte protein that first appears in the cell cytosol, but
CC ultimately becomes cross-linked to membrane proteins by
CC transglutaminase. All that results in the formation of an
CC insoluble envelope beneath the plasma membrane.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Suprabasal layers of squamous-differentiated
CC tissues such as epidermis, esophagus, tongue and trachea.
CC -!- DEVELOPMENTAL STAGE: Expressed during differentiation of squamous
CC cells.
CC -!- INDUCTION: By UV irradiation and carcinogenic agents. During
CC squamous differentiation of epidermal keratinocytes.
CC -!- SIMILARITY: Belongs to the cornifin (SPRR) family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L05188; AAA60576.1; -; Genomic_DNA.
DR EMBL; AF333952; AAK70940.1; -; Genomic_DNA.
DR EMBL; AL356867; CAI19808.1; -; Genomic_DNA.
DR PIR; I68511; I68511.
DR RefSeq; NP_001017418.1; NM_001017418.1.
DR UniGene; Hs.568239; -.
DR ProteinModelPortal; P35325; -.
DR IntAct; P35325; 4.
DR STRING; 9606.ENSP00000340703; -.
DR PhosphoSite; P35325; -.
DR DMDM; 464793; -.
DR PaxDb; P35325; -.
DR PRIDE; P35325; -.
DR DNASU; 6701; -.
DR Ensembl; ENST00000341611; ENSP00000340703; ENSG00000196805.
DR Ensembl; ENST00000368752; ENSP00000357741; ENSG00000196805.
DR Ensembl; ENST00000368755; ENSP00000357744; ENSG00000196805.
DR GeneID; 6701; -.
DR KEGG; hsa:6701; -.
DR UCSC; uc001fbg.3; human.
DR CTD; 6701; -.
DR GeneCards; GC01M153029; -.
DR HGNC; HGNC:11262; SPRR2B.
DR MIM; 182268; gene.
DR neXtProt; NX_P35325; -.
DR PharmGKB; PA36091; -.
DR OMA; PPPVCCE; -.
DR GenomeRNAi; 6701; -.
DR NextBio; 26129; -.
DR PRO; PR:P35325; -.
DR Bgee; P35325; -.
DR CleanEx; HS_SPRR2B; -.
DR Genevestigator; P35325; -.
DR GO; GO:0001533; C:cornified envelope; NAS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR GO; GO:0030216; P:keratinocyte differentiation; NAS:UniProtKB.
DR InterPro; IPR026075; SPRR/LCE.
DR PANTHER; PTHR23263; PTHR23263; 1.
PE 2: Evidence at transcript level;
KW Complete proteome; Cytoplasm; Keratinization; Polymorphism;
KW Reference proteome; Repeat.
FT CHAIN 1 72 Small proline-rich protein 2B.
FT /FTId=PRO_0000150009.
FT REPEAT 21 29 1.
FT REPEAT 30 38 2.
FT REPEAT 39 47 3.
FT REGION 21 47 3 X 9 AA tandem repeats of P-K-C-P-[EQ]-
FT P-C-P-P.
FT VARIANT 39 39 P -> S (in dbSNP:rs1048268).
FT /FTId=VAR_034518.
SQ SEQUENCE 72 AA; 7975 MW; 87B452D0F8B63448 CRC64;
MSYQQQQCKQ PCQPPPVCPT PKCPEPCPPP KCPEPCPPPK CPQPCPPQQC QQKYPPVTPS
PPCQPKYPPK SK
//
ID SPR2B_HUMAN Reviewed; 72 AA.
AC P35325; Q5T528;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1994, sequence version 1.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Small proline-rich protein 2B;
DE Short=SPR-2B;
GN Name=SPRR2B;
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 [GENOMIC DNA].
RC TISSUE=Skin;
RX PubMed=8325635; DOI=10.1006/geno.1993.1240;
RA Gibbs S., Fijneman R., Wiegant J., Geurts van Kessel A.,
RA van de Putte P., Backendorf C.;
RT "Molecular characterization and evolution of the SPRR family of
RT keratinocyte differentiation markers encoding small proline-rich
RT proteins.";
RL Genomics 16:630-637(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11279051; DOI=10.1074/jbc.M100336200;
RA Cabral A., Voskamp P., Cleton-Jansen A.-M., South A., Nizetic D.,
RA Backendorf C.;
RT "Structural organization and regulation of the small proline-rich
RT family of cornified envelope precursors suggest a role in adaptive
RT barrier function.";
RL J. Biol. Chem. 276:19231-19237(2001).
RN [3]
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).
CC -!- FUNCTION: Cross-linked envelope protein of keratinocytes. It is a
CC keratinocyte protein that first appears in the cell cytosol, but
CC ultimately becomes cross-linked to membrane proteins by
CC transglutaminase. All that results in the formation of an
CC insoluble envelope beneath the plasma membrane.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Suprabasal layers of squamous-differentiated
CC tissues such as epidermis, esophagus, tongue and trachea.
CC -!- DEVELOPMENTAL STAGE: Expressed during differentiation of squamous
CC cells.
CC -!- INDUCTION: By UV irradiation and carcinogenic agents. During
CC squamous differentiation of epidermal keratinocytes.
CC -!- SIMILARITY: Belongs to the cornifin (SPRR) family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L05188; AAA60576.1; -; Genomic_DNA.
DR EMBL; AF333952; AAK70940.1; -; Genomic_DNA.
DR EMBL; AL356867; CAI19808.1; -; Genomic_DNA.
DR PIR; I68511; I68511.
DR RefSeq; NP_001017418.1; NM_001017418.1.
DR UniGene; Hs.568239; -.
DR ProteinModelPortal; P35325; -.
DR IntAct; P35325; 4.
DR STRING; 9606.ENSP00000340703; -.
DR PhosphoSite; P35325; -.
DR DMDM; 464793; -.
DR PaxDb; P35325; -.
DR PRIDE; P35325; -.
DR DNASU; 6701; -.
DR Ensembl; ENST00000341611; ENSP00000340703; ENSG00000196805.
DR Ensembl; ENST00000368752; ENSP00000357741; ENSG00000196805.
DR Ensembl; ENST00000368755; ENSP00000357744; ENSG00000196805.
DR GeneID; 6701; -.
DR KEGG; hsa:6701; -.
DR UCSC; uc001fbg.3; human.
DR CTD; 6701; -.
DR GeneCards; GC01M153029; -.
DR HGNC; HGNC:11262; SPRR2B.
DR MIM; 182268; gene.
DR neXtProt; NX_P35325; -.
DR PharmGKB; PA36091; -.
DR OMA; PPPVCCE; -.
DR GenomeRNAi; 6701; -.
DR NextBio; 26129; -.
DR PRO; PR:P35325; -.
DR Bgee; P35325; -.
DR CleanEx; HS_SPRR2B; -.
DR Genevestigator; P35325; -.
DR GO; GO:0001533; C:cornified envelope; NAS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR GO; GO:0030216; P:keratinocyte differentiation; NAS:UniProtKB.
DR InterPro; IPR026075; SPRR/LCE.
DR PANTHER; PTHR23263; PTHR23263; 1.
PE 2: Evidence at transcript level;
KW Complete proteome; Cytoplasm; Keratinization; Polymorphism;
KW Reference proteome; Repeat.
FT CHAIN 1 72 Small proline-rich protein 2B.
FT /FTId=PRO_0000150009.
FT REPEAT 21 29 1.
FT REPEAT 30 38 2.
FT REPEAT 39 47 3.
FT REGION 21 47 3 X 9 AA tandem repeats of P-K-C-P-[EQ]-
FT P-C-P-P.
FT VARIANT 39 39 P -> S (in dbSNP:rs1048268).
FT /FTId=VAR_034518.
SQ SEQUENCE 72 AA; 7975 MW; 87B452D0F8B63448 CRC64;
MSYQQQQCKQ PCQPPPVCPT PKCPEPCPPP KCPEPCPPPK CPQPCPPQQC QQKYPPVTPS
PPCQPKYPPK SK
//
MIM
182268
*RECORD*
*FIELD* NO
182268
*FIELD* TI
*182268 SMALL PROLINE-RICH PROTEIN 2B; SPRR2B
*FIELD* TX
For background information on the SPRR gene family, see 182265.
read more
CLONING
Gibbs et al. (1993) concluded that there are 7 genes for the SPRR2
subfamily of small proline-rich proteins, including SPRR2B.
GENE FUNCTION
Using DNA microarray analysis, Zimmermann et al. (2005) identified
Sprr2a (182267) and Sprr2b as allergen-induced genes in a mouse model of
experimental asthma.
MAPPING
By analysis of human-rodent hybrid cell lines and FISH, Gibbs et al.
(1993) determined that all SPRR genes, including SPRR2B, are closely
linked within a 300-kb DNA segment on chromosome 1q21-q22.
*FIELD* RF
1. Gibbs, S.; Fijneman, R.; Wiegant, J.; Geurts van Kessel, A.; van
de Putte, P.; Backendorf, C.: Molecular characterization and evolution
of the SPRR family of keratinocyte differentiation markers encoding
small proline-rich proteins. Genomics 16: 630-637, 1993.
2. Zimmermann, N.; Doepker, M. P.; Witte, D. P.; Stringer, K. F.;
Fulkerson, P. C.; Pope, S. M.; Brandt, E. B.; Mishra, A.; King, N.
E.; Nikolaidis, N. M.; Wills-Karp, M.; Finkelman, F. D.; Rothenberg,
M. E.: Expression and regulation of small proline-rich protein 2
in allergic inflammation. Am. J. Respir. Cell Molec. Biol. 32: 428-435,
2005.
*FIELD* CN
Patricia A. Hartz - updated: 5/16/2007
*FIELD* CD
Victor A. McKusick: 6/18/1993
*FIELD* ED
mgross: 06/04/2007
mgross: 6/4/2007
terry: 5/16/2007
terry: 7/11/1994
carol: 6/18/1993
*RECORD*
*FIELD* NO
182268
*FIELD* TI
*182268 SMALL PROLINE-RICH PROTEIN 2B; SPRR2B
*FIELD* TX
For background information on the SPRR gene family, see 182265.
read more
CLONING
Gibbs et al. (1993) concluded that there are 7 genes for the SPRR2
subfamily of small proline-rich proteins, including SPRR2B.
GENE FUNCTION
Using DNA microarray analysis, Zimmermann et al. (2005) identified
Sprr2a (182267) and Sprr2b as allergen-induced genes in a mouse model of
experimental asthma.
MAPPING
By analysis of human-rodent hybrid cell lines and FISH, Gibbs et al.
(1993) determined that all SPRR genes, including SPRR2B, are closely
linked within a 300-kb DNA segment on chromosome 1q21-q22.
*FIELD* RF
1. Gibbs, S.; Fijneman, R.; Wiegant, J.; Geurts van Kessel, A.; van
de Putte, P.; Backendorf, C.: Molecular characterization and evolution
of the SPRR family of keratinocyte differentiation markers encoding
small proline-rich proteins. Genomics 16: 630-637, 1993.
2. Zimmermann, N.; Doepker, M. P.; Witte, D. P.; Stringer, K. F.;
Fulkerson, P. C.; Pope, S. M.; Brandt, E. B.; Mishra, A.; King, N.
E.; Nikolaidis, N. M.; Wills-Karp, M.; Finkelman, F. D.; Rothenberg,
M. E.: Expression and regulation of small proline-rich protein 2
in allergic inflammation. Am. J. Respir. Cell Molec. Biol. 32: 428-435,
2005.
*FIELD* CN
Patricia A. Hartz - updated: 5/16/2007
*FIELD* CD
Victor A. McKusick: 6/18/1993
*FIELD* ED
mgross: 06/04/2007
mgross: 6/4/2007
terry: 5/16/2007
terry: 7/11/1994
carol: 6/18/1993