Full text data of SERPINB12
SERPINB12
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Serpin B12
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Serpin B12
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96P63
ID SPB12_HUMAN Reviewed; 405 AA.
AC Q96P63;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=Serpin B12;
GN Name=SERPINB12;
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], AND CHARACTERIZATION.
RX PubMed=11604408; DOI=10.1074/jbc.M108879200;
RA Askew Y.S., Pak S.C., Luke C.J., Askew D.J., Cataltepe S., Mills D.R.,
RA Kato H., Lehoczky J., Dewar K., Birren B., Silverman G.A.;
RT "SERPINB12 is a novel member of the human ov-serpin family that is
RT widely expressed and inhibits trypsin-like serine proteinases.";
RL J. Biol. Chem. 276:49320-49330(2001).
CC -!- FUNCTION: Inhibits trypsin and plasmin, but not thrombin,
CC coagulation factor Xa, or urokinase-type plasminogen activator.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- TISSUE SPECIFICITY: Expressed in many tissues, including brain,
CC bone marrow, lymph node, heart, lung, liver, pancreas, testis,
CC ovary, and intestine.
CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
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DR EMBL; AF411191; AAL05571.1; -; mRNA.
DR RefSeq; NP_536722.1; NM_080474.1.
DR UniGene; Hs.348541; -.
DR ProteinModelPortal; Q96P63; -.
DR SMR; Q96P63; 2-405.
DR IntAct; Q96P63; 3.
DR STRING; 9606.ENSP00000269491; -.
DR MEROPS; I04.016; -.
DR PhosphoSite; Q96P63; -.
DR DMDM; 20140145; -.
DR PaxDb; Q96P63; -.
DR PRIDE; Q96P63; -.
DR Ensembl; ENST00000269491; ENSP00000269491; ENSG00000166634.
DR GeneID; 89777; -.
DR KEGG; hsa:89777; -.
DR UCSC; uc010xen.2; human.
DR CTD; 89777; -.
DR GeneCards; GC18P061196; -.
DR HGNC; HGNC:14220; SERPINB12.
DR HPA; CAB032802; -.
DR neXtProt; NX_Q96P63; -.
DR PharmGKB; PA37859; -.
DR eggNOG; COG4826; -.
DR HOGENOM; HOG000238519; -.
DR HOVERGEN; HBG005957; -.
DR KO; K13966; -.
DR OrthoDB; EOG7327PB; -.
DR PhylomeDB; Q96P63; -.
DR GenomeRNAi; 89777; -.
DR NextBio; 76255; -.
DR PRO; PR:Q96P63; -.
DR ArrayExpress; Q96P63; -.
DR Bgee; Q96P63; -.
DR CleanEx; HS_SERPINB12; -.
DR Genevestigator; Q96P63; -.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0019899; F:enzyme binding; NAS:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IMP:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; 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 Complete proteome; Cytoplasm; Polymorphism; Protease inhibitor;
KW Reference proteome; Serine protease inhibitor.
FT CHAIN 1 405 Serpin B12.
FT /FTId=PRO_0000094119.
FT SITE 370 371 Reactive bond (By similarity).
FT VARIANT 227 227 K -> E (in dbSNP:rs35582068).
FT /FTId=VAR_034513.
FT VARIANT 289 289 N -> T (in dbSNP:rs35352345).
FT /FTId=VAR_034514.
FT VARIANT 338 338 N -> S (in dbSNP:rs11664907).
FT /FTId=VAR_051952.
SQ SEQUENCE 405 AA; 46276 MW; FFE12D4C9B7F3DFA CRC64;
MDSLVTANTK FCFDLFQEIG KDDRHKNIFF SPLSLSAALG MVRLGARSDS AHQIDEVLHF
NEFSQNESKE PDPCLKSNKQ KAGSLNNESG LVSCYFGQLL SKLDRIKTDY TLSIANRLYG
EQEFPICQEY LDGVIQFYHT TIESVDFQKN PEKSRQEINF WVECQSQGKI KELFSKDAIN
AETVLVLVNA VYFKAKWETY FDHENTVDAP FCLNANENKS VKMMTQKGLY RIGFIEEVKA
QILEMRYTKG KLSMFVLLPS HSKDNLKGLE ELERKITYEK MVAWSSSENM SEESVVLSFP
RFTLEDSYDL NSILQDMGIT DIFDETRADL TGISPSPNLY LSKIIHKTFV EVDENGTQAA
AATGAVVSER SLRSWVEFNA NHPFLFFIRH NKTQTILFYG RVCSP
//
ID SPB12_HUMAN Reviewed; 405 AA.
AC Q96P63;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=Serpin B12;
GN Name=SERPINB12;
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], AND CHARACTERIZATION.
RX PubMed=11604408; DOI=10.1074/jbc.M108879200;
RA Askew Y.S., Pak S.C., Luke C.J., Askew D.J., Cataltepe S., Mills D.R.,
RA Kato H., Lehoczky J., Dewar K., Birren B., Silverman G.A.;
RT "SERPINB12 is a novel member of the human ov-serpin family that is
RT widely expressed and inhibits trypsin-like serine proteinases.";
RL J. Biol. Chem. 276:49320-49330(2001).
CC -!- FUNCTION: Inhibits trypsin and plasmin, but not thrombin,
CC coagulation factor Xa, or urokinase-type plasminogen activator.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- TISSUE SPECIFICITY: Expressed in many tissues, including brain,
CC bone marrow, lymph node, heart, lung, liver, pancreas, testis,
CC ovary, and intestine.
CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
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; AF411191; AAL05571.1; -; mRNA.
DR RefSeq; NP_536722.1; NM_080474.1.
DR UniGene; Hs.348541; -.
DR ProteinModelPortal; Q96P63; -.
DR SMR; Q96P63; 2-405.
DR IntAct; Q96P63; 3.
DR STRING; 9606.ENSP00000269491; -.
DR MEROPS; I04.016; -.
DR PhosphoSite; Q96P63; -.
DR DMDM; 20140145; -.
DR PaxDb; Q96P63; -.
DR PRIDE; Q96P63; -.
DR Ensembl; ENST00000269491; ENSP00000269491; ENSG00000166634.
DR GeneID; 89777; -.
DR KEGG; hsa:89777; -.
DR UCSC; uc010xen.2; human.
DR CTD; 89777; -.
DR GeneCards; GC18P061196; -.
DR HGNC; HGNC:14220; SERPINB12.
DR HPA; CAB032802; -.
DR neXtProt; NX_Q96P63; -.
DR PharmGKB; PA37859; -.
DR eggNOG; COG4826; -.
DR HOGENOM; HOG000238519; -.
DR HOVERGEN; HBG005957; -.
DR KO; K13966; -.
DR OrthoDB; EOG7327PB; -.
DR PhylomeDB; Q96P63; -.
DR GenomeRNAi; 89777; -.
DR NextBio; 76255; -.
DR PRO; PR:Q96P63; -.
DR ArrayExpress; Q96P63; -.
DR Bgee; Q96P63; -.
DR CleanEx; HS_SERPINB12; -.
DR Genevestigator; Q96P63; -.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0019899; F:enzyme binding; NAS:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IMP:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; 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 Complete proteome; Cytoplasm; Polymorphism; Protease inhibitor;
KW Reference proteome; Serine protease inhibitor.
FT CHAIN 1 405 Serpin B12.
FT /FTId=PRO_0000094119.
FT SITE 370 371 Reactive bond (By similarity).
FT VARIANT 227 227 K -> E (in dbSNP:rs35582068).
FT /FTId=VAR_034513.
FT VARIANT 289 289 N -> T (in dbSNP:rs35352345).
FT /FTId=VAR_034514.
FT VARIANT 338 338 N -> S (in dbSNP:rs11664907).
FT /FTId=VAR_051952.
SQ SEQUENCE 405 AA; 46276 MW; FFE12D4C9B7F3DFA CRC64;
MDSLVTANTK FCFDLFQEIG KDDRHKNIFF SPLSLSAALG MVRLGARSDS AHQIDEVLHF
NEFSQNESKE PDPCLKSNKQ KAGSLNNESG LVSCYFGQLL SKLDRIKTDY TLSIANRLYG
EQEFPICQEY LDGVIQFYHT TIESVDFQKN PEKSRQEINF WVECQSQGKI KELFSKDAIN
AETVLVLVNA VYFKAKWETY FDHENTVDAP FCLNANENKS VKMMTQKGLY RIGFIEEVKA
QILEMRYTKG KLSMFVLLPS HSKDNLKGLE ELERKITYEK MVAWSSSENM SEESVVLSFP
RFTLEDSYDL NSILQDMGIT DIFDETRADL TGISPSPNLY LSKIIHKTFV EVDENGTQAA
AATGAVVSER SLRSWVEFNA NHPFLFFIRH NKTQTILFYG RVCSP
//