Full text data of SERPINB1
SERPINB1
(ELANH2, MNEI, PI2)
[Confidence: low (only semi-automatic identification from reviews)]
Leukocyte elastase inhibitor; LEI (Monocyte/neutrophil elastase inhibitor; EI; M/NEI; Peptidase inhibitor 2; PI-2; Serpin B1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Leukocyte elastase inhibitor; LEI (Monocyte/neutrophil elastase inhibitor; EI; M/NEI; Peptidase inhibitor 2; PI-2; Serpin B1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P30740
ID ILEU_HUMAN Reviewed; 379 AA.
AC P30740; A8K5L2; Q53FB9; Q5W0E1; Q9UDF8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-APR-1993, sequence version 1.
DT 22-JAN-2014, entry version 135.
DE RecName: Full=Leukocyte elastase inhibitor;
DE Short=LEI;
DE AltName: Full=Monocyte/neutrophil elastase inhibitor;
DE Short=EI;
DE Short=M/NEI;
DE AltName: Full=Peptidase inhibitor 2;
DE Short=PI-2;
DE AltName: Full=Serpin B1;
GN Name=SERPINB1; Synonyms=ELANH2, MNEI, PI2;
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].
RX PubMed=1376927; DOI=10.1073/pnas.89.12.5635;
RA Remold-O'Donnell E., Chin J., Alberts M.;
RT "Sequence and molecular characterization of human monocyte/neutrophil
RT elastase inhibitor.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:5635-5639(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9630619; DOI=10.1016/S0378-1119(98)00189-9;
RA Zeng W., Silverman G.A., Remold-O'Donnell E.;
RT "Structure and sequence of human M/NEI (monocyte/neutrophil elastase
RT inhibitor), an Ov-serpin family gene.";
RL Gene 213:179-187(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
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 MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [8]
RP PROTEIN SEQUENCE OF 1-10, AND ACETYLATION AT MET-1.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP PROTEIN SEQUENCE OF 111-129; 216-244 AND 255-274.
RX PubMed=7578269; DOI=10.1016/0167-4889(95)00113-7;
RA Packard B.Z., Lee S.S., Remold-O'Donnell E., Komoriya A.;
RT "A serpin from human tumor cells with direct lymphoid immunomodulatory
RT activity: mitogenic stimulation of human tumor-infiltrating
RT lymphocytes.";
RL Biochim. Biophys. Acta 1269:41-50(1995).
RN [10]
RP PROTEIN SEQUENCE OF 178-185; 204-210 AND 364-371.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [11]
RP MASS SPECTROMETRY, FUNCTION, AND REACTIVE SITES.
RX PubMed=11747453; DOI=10.1021/bi0113925;
RA Cooley J., Takayama T.K., Shapiro S.D., Schechter N.M.,
RA Remold-O'Donnell E.;
RT "The serpin MNEI inhibits elastase-like and chymotrypsin-like serine
RT proteases through efficient reactions at two active sites.";
RL Biochemistry 40:15762-15770(2001).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137 AND LYS-177, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH GZMH,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=23269243; DOI=10.4049/jimmunol.1202542;
RA Wang L., Li Q., Wu L., Liu S., Zhang Y., Yang X., Zhu P., Zhang H.,
RA Zhang K., Lou J., Liu P., Tong L., Sun F., Fan Z.;
RT "Identification of SERPINB1 as a physiological inhibitor of human
RT granzyme H.";
RL J. Immunol. 190:1319-1330(2013).
CC -!- FUNCTION: Regulates the activity of the neutrophil proteases
CC elastase, cathepsin G, proteinase-3, chymase, chymotrypsin, and
CC kallikrein-3. Also functions as a potent intracellular inhibitor
CC of granzyme H.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasmic
CC granule.
CC -!- DOMAIN: Reactive bond 1 is specific for reaction with
CC chymotrypsin-like protease such as cathepsin G, chymotrypsin,
CC chymase or granzyme H, while reactive bond 2 is specific for
CC reaction with elastase-like protease such as neutrophil elastase,
CC proteinase-3, pancreatic elastase or PSA.
CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD97090.1; Type=Erroneous initiation;
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DR EMBL; M93056; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF053630; AAC31394.1; -; Genomic_DNA.
DR EMBL; AK291327; BAF84016.1; -; mRNA.
DR EMBL; BT006928; AAP35574.1; -; mRNA.
DR EMBL; AK223370; BAD97090.1; ALT_INIT; mRNA.
DR EMBL; AL139092; CAH73667.1; -; Genomic_DNA.
DR EMBL; BC009015; AAH09015.1; -; mRNA.
DR PIR; S27383; S27383.
DR RefSeq; NP_109591.1; NM_030666.3.
DR UniGene; Hs.381167; -.
DR PDB; 4GA7; X-ray; 2.90 A; A/B=1-379.
DR PDBsum; 4GA7; -.
DR ProteinModelPortal; P30740; -.
DR SMR; P30740; 1-379.
DR IntAct; P30740; 2.
DR MINT; MINT-4999893; -.
DR STRING; 9606.ENSP00000370115; -.
DR MEROPS; I04.006; -.
DR PhosphoSite; P30740; -.
DR DMDM; 266344; -.
DR OGP; P30740; -.
DR REPRODUCTION-2DPAGE; IPI00027444; -.
DR PaxDb; P30740; -.
DR PeptideAtlas; P30740; -.
DR PRIDE; P30740; -.
DR DNASU; 1992; -.
DR Ensembl; ENST00000380739; ENSP00000370115; ENSG00000021355.
DR GeneID; 1992; -.
DR KEGG; hsa:1992; -.
DR UCSC; uc003mub.4; human.
DR CTD; 1992; -.
DR GeneCards; GC06M002833; -.
DR HGNC; HGNC:3311; SERPINB1.
DR HPA; HPA018871; -.
DR MIM; 130135; gene.
DR neXtProt; NX_P30740; -.
DR PharmGKB; PA35046; -.
DR eggNOG; COG4826; -.
DR HOGENOM; HOG000238519; -.
DR HOVERGEN; HBG005957; -.
DR InParanoid; P30740; -.
DR KO; K13963; -.
DR OMA; TFHFNTV; -.
DR OrthoDB; EOG7327PB; -.
DR PhylomeDB; P30740; -.
DR ChiTaRS; SERPINB1; human.
DR GeneWiki; SERPINB1; -.
DR GenomeRNAi; 1992; -.
DR NextBio; 8055; -.
DR PMAP-CutDB; P30740; -.
DR PRO; PR:P30740; -.
DR ArrayExpress; P30740; -.
DR Bgee; P30740; -.
DR CleanEx; HS_SERPINB1; -.
DR Genevestigator; P30740; -.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; NAS:UniProtKB.
DR GO; GO:0030162; P:regulation of proteolysis; IBA:RefGenome.
DR InterPro; IPR023795; Serpin_CS.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Polymorphism; Protease inhibitor;
KW Reference proteome; Serine protease inhibitor.
FT CHAIN 1 379 Leukocyte elastase inhibitor.
FT /FTId=PRO_0000094101.
FT SITE 343 344 Reactive bond 1.
FT SITE 344 345 Reactive bond 2.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 137 137 N6-acetyllysine.
FT MOD_RES 177 177 N6-acetyllysine.
FT VARIANT 82 82 A -> V (in dbSNP:rs34825616).
FT /FTId=VAR_051945.
FT CONFLICT 137 137 K -> R (in Ref. 4; AAP35574).
FT CONFLICT 149 149 A -> V (in Ref. 3; BAF84016).
FT CONFLICT 264 264 L -> F (in Ref. 3; BAF84016).
FT CONFLICT 272 272 Missing (in Ref. 9; AA sequence).
FT CONFLICT 329 329 E -> K (in Ref. 3; BAF84016).
FT HELIX 3 22
FT STRAND 24 26
FT STRAND 28 30
FT HELIX 32 43
FT HELIX 48 57
FT HELIX 60 62
FT HELIX 66 77
FT STRAND 83 95
FT HELIX 102 111
FT STRAND 116 119
FT HELIX 121 139
FT TURN 140 142
FT STRAND 159 168
FT STRAND 171 173
FT TURN 177 179
FT STRAND 181 188
FT STRAND 191 209
FT TURN 210 213
FT STRAND 214 221
FT STRAND 224 235
FT STRAND 238 242
FT HELIX 244 249
FT HELIX 252 259
FT HELIX 261 263
FT STRAND 265 274
FT STRAND 276 283
FT HELIX 285 290
FT HELIX 295 297
FT TURN 299 301
FT TURN 305 307
FT STRAND 315 326
FT STRAND 345 347
FT STRAND 349 353
FT STRAND 358 364
FT TURN 365 368
FT STRAND 369 376
SQ SEQUENCE 379 AA; 42742 MW; BAAE08DFCBCD8CD3 CRC64;
MEQLSSANTR FALDLFLALS ENNPAGNIFI SPFSISSAMA MVFLGTRGNT AAQLSKTFHF
NTVEEVHSRF QSLNADINKR GASYILKLAN RLYGEKTYNF LPEFLVSTQK TYGADLASVD
FQHASEDARK TINQWVKGQT EGKIPELLAS GMVDNMTKLV LVNAIYFKGN WKDKFMKEAT
TNAPFRLNKK DRKTVKMMYQ KKKFAYGYIE DLKCRVLELP YQGEELSMVI LLPDDIEDES
TGLKKIEEQL TLEKLHEWTK PENLDFIEVN VSLPRFKLEE SYTLNSDLAR LGVQDLFNSS
KADLSGMSGA RDIFISKIVH KSFVEVNEEG TEAAAATAGI ATFCMLMPEE NFTADHPFLF
FIRHNSSGSI LFLGRFSSP
//
ID ILEU_HUMAN Reviewed; 379 AA.
AC P30740; A8K5L2; Q53FB9; Q5W0E1; Q9UDF8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-APR-1993, sequence version 1.
DT 22-JAN-2014, entry version 135.
DE RecName: Full=Leukocyte elastase inhibitor;
DE Short=LEI;
DE AltName: Full=Monocyte/neutrophil elastase inhibitor;
DE Short=EI;
DE Short=M/NEI;
DE AltName: Full=Peptidase inhibitor 2;
DE Short=PI-2;
DE AltName: Full=Serpin B1;
GN Name=SERPINB1; Synonyms=ELANH2, MNEI, PI2;
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].
RX PubMed=1376927; DOI=10.1073/pnas.89.12.5635;
RA Remold-O'Donnell E., Chin J., Alberts M.;
RT "Sequence and molecular characterization of human monocyte/neutrophil
RT elastase inhibitor.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:5635-5639(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9630619; DOI=10.1016/S0378-1119(98)00189-9;
RA Zeng W., Silverman G.A., Remold-O'Donnell E.;
RT "Structure and sequence of human M/NEI (monocyte/neutrophil elastase
RT inhibitor), an Ov-serpin family gene.";
RL Gene 213:179-187(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
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 MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [8]
RP PROTEIN SEQUENCE OF 1-10, AND ACETYLATION AT MET-1.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP PROTEIN SEQUENCE OF 111-129; 216-244 AND 255-274.
RX PubMed=7578269; DOI=10.1016/0167-4889(95)00113-7;
RA Packard B.Z., Lee S.S., Remold-O'Donnell E., Komoriya A.;
RT "A serpin from human tumor cells with direct lymphoid immunomodulatory
RT activity: mitogenic stimulation of human tumor-infiltrating
RT lymphocytes.";
RL Biochim. Biophys. Acta 1269:41-50(1995).
RN [10]
RP PROTEIN SEQUENCE OF 178-185; 204-210 AND 364-371.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [11]
RP MASS SPECTROMETRY, FUNCTION, AND REACTIVE SITES.
RX PubMed=11747453; DOI=10.1021/bi0113925;
RA Cooley J., Takayama T.K., Shapiro S.D., Schechter N.M.,
RA Remold-O'Donnell E.;
RT "The serpin MNEI inhibits elastase-like and chymotrypsin-like serine
RT proteases through efficient reactions at two active sites.";
RL Biochemistry 40:15762-15770(2001).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137 AND LYS-177, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH GZMH,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=23269243; DOI=10.4049/jimmunol.1202542;
RA Wang L., Li Q., Wu L., Liu S., Zhang Y., Yang X., Zhu P., Zhang H.,
RA Zhang K., Lou J., Liu P., Tong L., Sun F., Fan Z.;
RT "Identification of SERPINB1 as a physiological inhibitor of human
RT granzyme H.";
RL J. Immunol. 190:1319-1330(2013).
CC -!- FUNCTION: Regulates the activity of the neutrophil proteases
CC elastase, cathepsin G, proteinase-3, chymase, chymotrypsin, and
CC kallikrein-3. Also functions as a potent intracellular inhibitor
CC of granzyme H.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasmic
CC granule.
CC -!- DOMAIN: Reactive bond 1 is specific for reaction with
CC chymotrypsin-like protease such as cathepsin G, chymotrypsin,
CC chymase or granzyme H, while reactive bond 2 is specific for
CC reaction with elastase-like protease such as neutrophil elastase,
CC proteinase-3, pancreatic elastase or PSA.
CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD97090.1; Type=Erroneous initiation;
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DR EMBL; M93056; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF053630; AAC31394.1; -; Genomic_DNA.
DR EMBL; AK291327; BAF84016.1; -; mRNA.
DR EMBL; BT006928; AAP35574.1; -; mRNA.
DR EMBL; AK223370; BAD97090.1; ALT_INIT; mRNA.
DR EMBL; AL139092; CAH73667.1; -; Genomic_DNA.
DR EMBL; BC009015; AAH09015.1; -; mRNA.
DR PIR; S27383; S27383.
DR RefSeq; NP_109591.1; NM_030666.3.
DR UniGene; Hs.381167; -.
DR PDB; 4GA7; X-ray; 2.90 A; A/B=1-379.
DR PDBsum; 4GA7; -.
DR ProteinModelPortal; P30740; -.
DR SMR; P30740; 1-379.
DR IntAct; P30740; 2.
DR MINT; MINT-4999893; -.
DR STRING; 9606.ENSP00000370115; -.
DR MEROPS; I04.006; -.
DR PhosphoSite; P30740; -.
DR DMDM; 266344; -.
DR OGP; P30740; -.
DR REPRODUCTION-2DPAGE; IPI00027444; -.
DR PaxDb; P30740; -.
DR PeptideAtlas; P30740; -.
DR PRIDE; P30740; -.
DR DNASU; 1992; -.
DR Ensembl; ENST00000380739; ENSP00000370115; ENSG00000021355.
DR GeneID; 1992; -.
DR KEGG; hsa:1992; -.
DR UCSC; uc003mub.4; human.
DR CTD; 1992; -.
DR GeneCards; GC06M002833; -.
DR HGNC; HGNC:3311; SERPINB1.
DR HPA; HPA018871; -.
DR MIM; 130135; gene.
DR neXtProt; NX_P30740; -.
DR PharmGKB; PA35046; -.
DR eggNOG; COG4826; -.
DR HOGENOM; HOG000238519; -.
DR HOVERGEN; HBG005957; -.
DR InParanoid; P30740; -.
DR KO; K13963; -.
DR OMA; TFHFNTV; -.
DR OrthoDB; EOG7327PB; -.
DR PhylomeDB; P30740; -.
DR ChiTaRS; SERPINB1; human.
DR GeneWiki; SERPINB1; -.
DR GenomeRNAi; 1992; -.
DR NextBio; 8055; -.
DR PMAP-CutDB; P30740; -.
DR PRO; PR:P30740; -.
DR ArrayExpress; P30740; -.
DR Bgee; P30740; -.
DR CleanEx; HS_SERPINB1; -.
DR Genevestigator; P30740; -.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; NAS:UniProtKB.
DR GO; GO:0030162; P:regulation of proteolysis; IBA:RefGenome.
DR InterPro; IPR023795; Serpin_CS.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Polymorphism; Protease inhibitor;
KW Reference proteome; Serine protease inhibitor.
FT CHAIN 1 379 Leukocyte elastase inhibitor.
FT /FTId=PRO_0000094101.
FT SITE 343 344 Reactive bond 1.
FT SITE 344 345 Reactive bond 2.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 137 137 N6-acetyllysine.
FT MOD_RES 177 177 N6-acetyllysine.
FT VARIANT 82 82 A -> V (in dbSNP:rs34825616).
FT /FTId=VAR_051945.
FT CONFLICT 137 137 K -> R (in Ref. 4; AAP35574).
FT CONFLICT 149 149 A -> V (in Ref. 3; BAF84016).
FT CONFLICT 264 264 L -> F (in Ref. 3; BAF84016).
FT CONFLICT 272 272 Missing (in Ref. 9; AA sequence).
FT CONFLICT 329 329 E -> K (in Ref. 3; BAF84016).
FT HELIX 3 22
FT STRAND 24 26
FT STRAND 28 30
FT HELIX 32 43
FT HELIX 48 57
FT HELIX 60 62
FT HELIX 66 77
FT STRAND 83 95
FT HELIX 102 111
FT STRAND 116 119
FT HELIX 121 139
FT TURN 140 142
FT STRAND 159 168
FT STRAND 171 173
FT TURN 177 179
FT STRAND 181 188
FT STRAND 191 209
FT TURN 210 213
FT STRAND 214 221
FT STRAND 224 235
FT STRAND 238 242
FT HELIX 244 249
FT HELIX 252 259
FT HELIX 261 263
FT STRAND 265 274
FT STRAND 276 283
FT HELIX 285 290
FT HELIX 295 297
FT TURN 299 301
FT TURN 305 307
FT STRAND 315 326
FT STRAND 345 347
FT STRAND 349 353
FT STRAND 358 364
FT TURN 365 368
FT STRAND 369 376
SQ SEQUENCE 379 AA; 42742 MW; BAAE08DFCBCD8CD3 CRC64;
MEQLSSANTR FALDLFLALS ENNPAGNIFI SPFSISSAMA MVFLGTRGNT AAQLSKTFHF
NTVEEVHSRF QSLNADINKR GASYILKLAN RLYGEKTYNF LPEFLVSTQK TYGADLASVD
FQHASEDARK TINQWVKGQT EGKIPELLAS GMVDNMTKLV LVNAIYFKGN WKDKFMKEAT
TNAPFRLNKK DRKTVKMMYQ KKKFAYGYIE DLKCRVLELP YQGEELSMVI LLPDDIEDES
TGLKKIEEQL TLEKLHEWTK PENLDFIEVN VSLPRFKLEE SYTLNSDLAR LGVQDLFNSS
KADLSGMSGA RDIFISKIVH KSFVEVNEEG TEAAAATAGI ATFCMLMPEE NFTADHPFLF
FIRHNSSGSI LFLGRFSSP
//
MIM
130135
*RECORD*
*FIELD* NO
130135
*FIELD* TI
*130135 SERPIN PEPTIDASE INHIBITOR, CLADE B (OVALBUMIN), MEMBER 1; SERPINB1
;;PROTEASE INHIBITOR 2, MONOCYTE/NEUTROPHIL DERIVED; ELANH2;;
read moreELASTASE INHIBITOR, MONOCYTE/NEUTROPHIL; EI
*FIELD* TX
CLONING
Monocyte/neutrophil elastase inhibitor (EI) is a protein of
approximately 42,000 Mr with serpin-like functional properties.
Remold-O'Donnell et al. (1992) cloned EI cDNA and identified 3 EI mRNA
species of 1.5, 1.9, and 2.6 kb in monocyte-like cells and no
hybridizing mRNA in lymphoblastoid cells lacking detectable EI enzymatic
activity. The cDNA open reading frame encoded a 379-amino acid protein.
Its sequence established EI as a member of the serpin superfamily.
Sequence alignment indicated that the reactive center P1 residue is
cys-344, consistent with abrogation of elastase inhibitory activity by
iodoacetamide and making EI a naturally occurring cys-serpin.
MAPPING
In the course of studying 4 closely linked genes encoding members of the
ovalbumin family of serine proteinase inhibitors (Ov-serpins) located on
18q21.3, Schneider et al. (1995) investigated the mapping of elastase
inhibitor. They prepared PCR primer sets of the gene, and by using the
NIGMS monochromosomal somatic cell hybrid panel, showed that the EI gene
maps to chromosome 6.
By amplifying DNA of a somatic cell hybrid panel, Evans et al. (1995)
unambiguously localized ELANH2 to chromosome 6. With the use of a panel
of radiation and somatic cell hybrids specific for chromosome 6, they
refined the localization to the short arm telomeric of D6S89, F13A
(134570), and D6S202 at 6pter-p24.
*FIELD* RF
1. Evans, E.; Cooley, J.; Remold-O'Donnell, E.: Characterization
and chromosomal localization of ELANH2, the gene encoding human monocyte/neutrophil
elastase inhibitor. Genomics 28: 235-240, 1995.
2. Remold-O'Donnell, E.; Chin, J.; Alberts, M.: Sequence and molecular
characterization of human monocyte/neutrophil elastase inhibitor. Proc.
Nat. Acad. Sci. 89: 5635-5639, 1992.
3. Schneider, S. S.; Schick, C.; Fish, K. E.; Miller, E.; Pena, J.
C.; Treter, S. D.; Hui, S. M.; Silverman, G. A.: A serine proteinase
inhibitor locus at 18q21.3 contains a tandem duplication of the human
squamous cell carcinoma antigen gene. Proc. Nat. Acad. Sci. 92:
3147-3151, 1995.
*FIELD* CD
Victor A. McKusick: 7/7/1992
*FIELD* ED
carol: 08/03/2010
terry: 3/13/2002
terry: 5/22/1996
mark: 9/12/1995
carol: 2/1/1995
carol: 7/13/1992
carol: 7/7/1992
*RECORD*
*FIELD* NO
130135
*FIELD* TI
*130135 SERPIN PEPTIDASE INHIBITOR, CLADE B (OVALBUMIN), MEMBER 1; SERPINB1
;;PROTEASE INHIBITOR 2, MONOCYTE/NEUTROPHIL DERIVED; ELANH2;;
read moreELASTASE INHIBITOR, MONOCYTE/NEUTROPHIL; EI
*FIELD* TX
CLONING
Monocyte/neutrophil elastase inhibitor (EI) is a protein of
approximately 42,000 Mr with serpin-like functional properties.
Remold-O'Donnell et al. (1992) cloned EI cDNA and identified 3 EI mRNA
species of 1.5, 1.9, and 2.6 kb in monocyte-like cells and no
hybridizing mRNA in lymphoblastoid cells lacking detectable EI enzymatic
activity. The cDNA open reading frame encoded a 379-amino acid protein.
Its sequence established EI as a member of the serpin superfamily.
Sequence alignment indicated that the reactive center P1 residue is
cys-344, consistent with abrogation of elastase inhibitory activity by
iodoacetamide and making EI a naturally occurring cys-serpin.
MAPPING
In the course of studying 4 closely linked genes encoding members of the
ovalbumin family of serine proteinase inhibitors (Ov-serpins) located on
18q21.3, Schneider et al. (1995) investigated the mapping of elastase
inhibitor. They prepared PCR primer sets of the gene, and by using the
NIGMS monochromosomal somatic cell hybrid panel, showed that the EI gene
maps to chromosome 6.
By amplifying DNA of a somatic cell hybrid panel, Evans et al. (1995)
unambiguously localized ELANH2 to chromosome 6. With the use of a panel
of radiation and somatic cell hybrids specific for chromosome 6, they
refined the localization to the short arm telomeric of D6S89, F13A
(134570), and D6S202 at 6pter-p24.
*FIELD* RF
1. Evans, E.; Cooley, J.; Remold-O'Donnell, E.: Characterization
and chromosomal localization of ELANH2, the gene encoding human monocyte/neutrophil
elastase inhibitor. Genomics 28: 235-240, 1995.
2. Remold-O'Donnell, E.; Chin, J.; Alberts, M.: Sequence and molecular
characterization of human monocyte/neutrophil elastase inhibitor. Proc.
Nat. Acad. Sci. 89: 5635-5639, 1992.
3. Schneider, S. S.; Schick, C.; Fish, K. E.; Miller, E.; Pena, J.
C.; Treter, S. D.; Hui, S. M.; Silverman, G. A.: A serine proteinase
inhibitor locus at 18q21.3 contains a tandem duplication of the human
squamous cell carcinoma antigen gene. Proc. Nat. Acad. Sci. 92:
3147-3151, 1995.
*FIELD* CD
Victor A. McKusick: 7/7/1992
*FIELD* ED
carol: 08/03/2010
terry: 3/13/2002
terry: 5/22/1996
mark: 9/12/1995
carol: 2/1/1995
carol: 7/13/1992
carol: 7/7/1992