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Protein

Plasminogen activator inhibitor 2

Gene

SERPINB2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits urokinase-type plasminogen activator. The monocyte derived PAI-2 is distinct from the endothelial cell-derived PAI-1.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei380 – 3812Reactive bond

GO - Molecular functioni

  1. serine-type endopeptidase inhibitor activity Source: GO_Central

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. fibrinolysis Source: Reactome
  3. negative regulation of apoptotic process Source: ProtInc
  4. negative regulation of endopeptidase activity Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Biological processi

Plasminogen activation

Enzyme and pathway databases

ReactomeiREACT_641. Dissolution of Fibrin Clot.

Protein family/group databases

MEROPSiI04.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Plasminogen activator inhibitor 2
Short name:
PAI-2
Alternative name(s):
Monocyte Arg-serpin
Placental plasminogen activator inhibitor
Serpin B2
Urokinase inhibitor
Gene namesi
Name:SERPINB2
Synonyms:PAI2, PLANH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:8584. SERPINB2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular region Source: Reactome
  3. extracellular space Source: GO_Central
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35500.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 415415Plasminogen activator inhibitor 2PRO_0000223296Add
BLAST
Signal peptidei1 – ?Not cleaved

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi5 ↔ 405
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi339 – 3391N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

The signal sequence is not cleaved.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP05120.
PaxDbiP05120.
PRIDEiP05120.

PTM databases

PhosphoSiteiP05120.

Expressioni

Gene expression databases

BgeeiP05120.
CleanExiHS_SERPINB2.
ExpressionAtlasiP05120. baseline and differential.
GenevestigatoriP05120.

Organism-specific databases

HPAiHPA015480.

Interactioni

Subunit structurei

Interacts with PSMB1.1 Publication

Protein-protein interaction databases

BioGridi111092. 13 interactions.
IntActiP05120. 1 interaction.
MINTiMINT-270968.
STRINGi9606.ENSP00000299502.

Structurei

Secondary structure

1
415
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2217Combined sources
Beta strandi24 – 263Combined sources
Beta strandi28 – 303Combined sources
Helixi32 – 4514Combined sources
Helixi48 – 5710Combined sources
Turni58 – 625Combined sources
Helixi100 – 1023Combined sources
Helixi103 – 11513Combined sources
Beta strandi122 – 13211Combined sources
Helixi139 – 14911Combined sources
Beta strandi154 – 1563Combined sources
Helixi158 – 17619Combined sources
Turni177 – 1793Combined sources
Beta strandi194 – 20512Combined sources
Beta strandi208 – 2103Combined sources
Beta strandi220 – 2256Combined sources
Beta strandi228 – 2325Combined sources
Beta strandi234 – 24613Combined sources
Helixi247 – 2493Combined sources
Beta strandi251 – 26919Combined sources
Beta strandi275 – 2784Combined sources
Helixi280 – 2856Combined sources
Helixi288 – 2958Combined sources
Turni297 – 2993Combined sources
Beta strandi301 – 31010Combined sources
Beta strandi312 – 3198Combined sources
Helixi321 – 3277Combined sources
Helixi331 – 3333Combined sources
Turni335 – 3373Combined sources
Turni341 – 3433Combined sources
Beta strandi349 – 36214Combined sources
Beta strandi368 – 37912Combined sources
Beta strandi387 – 3893Combined sources
Beta strandi394 – 4007Combined sources
Turni401 – 4044Combined sources
Beta strandi405 – 4128Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BY7X-ray2.00A1-415[»]
1JRRX-ray1.60A1-415[»]
P367-380[»]
2ARQX-ray1.85A1-415[»]
P367-380[»]
2ARRX-ray1.55A1-415[»]
P367-380[»]
ProteinModelPortaliP05120.
SMRiP05120. Positions 3-415.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05120.

Family & Domainsi

Sequence similaritiesi

Belongs to the serpin family. Ov-serpin subfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118789.
HOGENOMiHOG000238519.
HOVERGENiHBG005957.
InParanoidiP05120.
KOiK13963.
OMAiQIQKGTY.
PhylomeDBiP05120.
TreeFamiTF352619.

Family and domain databases

InterProiIPR015556. PAI-2.
IPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PTHR11461:SF61. PTHR11461:SF61. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 2 hits.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05120-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDLCVANTL FALNLFKHLA KASPTQNLFL SPWSISSTMA MVYMGSRGST
60 70 80 90 100
EDQMAKVLQF NEVGANAVTP MTPENFTSCG FMQQIQKGSY PDAILQAQAA
110 120 130 140 150
DKIHSSFRSL SSAINASTGN YLLESVNKLF GEKSASFREE YIRLCQKYYS
160 170 180 190 200
SEPQAVDFLE CAEEARKKIN SWVKTQTKGK IPNLLPEGSV DGDTRMVLVN
210 220 230 240 250
AVYFKGKWKT PFEKKLNGLY PFRVNSAQRT PVQMMYLREK LNIGYIEDLK
260 270 280 290 300
AQILELPYAG DVSMFLLLPD EIADVSTGLE LLESEITYDK LNKWTSKDKM
310 320 330 340 350
AEDEVEVYIP QFKLEEHYEL RSILRSMGME DAFNKGRANF SGMSERNDLF
360 370 380 390 400
LSEVFHQAMV DVNEEGTEAA AGTGGVMTGR TGHGGPQFVA DHPFLFLIMH
410
KITNCILFFG RFSSP
Length:415
Mass (Da):46,596
Last modified:February 1, 1996 - v2
Checksum:i10DFAB5A4B1246FF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701N → Y in AAH12609 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti120 – 1201N → D.1 Publication
Corresponds to variant rs6098 [ dbSNP | Ensembl ].
VAR_011743
Natural varianti229 – 2291R → H.1 Publication
Corresponds to variant rs6100 [ dbSNP | Ensembl ].
VAR_014173
Natural varianti374 – 3741G → A.
Corresponds to variant rs34066931 [ dbSNP | Ensembl ].
VAR_051946
Natural varianti404 – 4041N → K.1 Publication
Corresponds to variant rs6103 [ dbSNP | Ensembl ].
VAR_011744
Natural varianti413 – 4131S → C.1 Publication
Corresponds to variant rs6104 [ dbSNP | Ensembl ].
VAR_011745

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02685 mRNA. Translation: AAA36413.1.
M18082 mRNA. Translation: AAA60006.1.
Y00630 mRNA. Translation: CAA68666.1.
J03603 mRNA. Translation: AAA60004.1.
M24657
, M24651, M24652, M24653, M24654, M24655, M24656 Genomic DNA. Translation: AAA60348.1.
M31551
, M31547, M31548, M31549, M31550 Genomic DNA. Translation: AAA36797.1.
BC012609 mRNA. Translation: AAH12609.1.
CCDSiCCDS11989.1.
PIRiA32853.
RefSeqiNP_001137290.1. NM_001143818.1.
NP_002566.1. NM_002575.2.
UniGeneiHs.594481.

Genome annotation databases

EnsembliENST00000299502; ENSP00000299502; ENSG00000197632.
ENST00000457692; ENSP00000401645; ENSG00000197632.
GeneIDi5055.
KEGGihsa:5055.
UCSCiuc002ljo.3. human.

Polymorphism databases

DMDMi1352712.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02685 mRNA. Translation: AAA36413.1.
M18082 mRNA. Translation: AAA60006.1.
Y00630 mRNA. Translation: CAA68666.1.
J03603 mRNA. Translation: AAA60004.1.
M24657
, M24651, M24652, M24653, M24654, M24655, M24656 Genomic DNA. Translation: AAA60348.1.
M31551
, M31547, M31548, M31549, M31550 Genomic DNA. Translation: AAA36797.1.
BC012609 mRNA. Translation: AAH12609.1.
CCDSiCCDS11989.1.
PIRiA32853.
RefSeqiNP_001137290.1. NM_001143818.1.
NP_002566.1. NM_002575.2.
UniGeneiHs.594481.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BY7X-ray2.00A1-415[»]
1JRRX-ray1.60A1-415[»]
P367-380[»]
2ARQX-ray1.85A1-415[»]
P367-380[»]
2ARRX-ray1.55A1-415[»]
P367-380[»]
ProteinModelPortaliP05120.
SMRiP05120. Positions 3-415.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111092. 13 interactions.
IntActiP05120. 1 interaction.
MINTiMINT-270968.
STRINGi9606.ENSP00000299502.

Chemistry

DrugBankiDB00031. Tenecteplase.
DB00013. Urokinase.

Protein family/group databases

MEROPSiI04.007.

PTM databases

PhosphoSiteiP05120.

Polymorphism databases

DMDMi1352712.

Proteomic databases

MaxQBiP05120.
PaxDbiP05120.
PRIDEiP05120.

Protocols and materials databases

DNASUi5055.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000299502; ENSP00000299502; ENSG00000197632.
ENST00000457692; ENSP00000401645; ENSG00000197632.
GeneIDi5055.
KEGGihsa:5055.
UCSCiuc002ljo.3. human.

Organism-specific databases

CTDi5055.
GeneCardsiGC18P061528.
H-InvDBHIX0212740.
HGNCiHGNC:8584. SERPINB2.
HPAiHPA015480.
MIMi173390. gene.
neXtProtiNX_P05120.
PharmGKBiPA35500.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118789.
HOGENOMiHOG000238519.
HOVERGENiHBG005957.
InParanoidiP05120.
KOiK13963.
OMAiQIQKGTY.
PhylomeDBiP05120.
TreeFamiTF352619.

Enzyme and pathway databases

ReactomeiREACT_641. Dissolution of Fibrin Clot.

Miscellaneous databases

ChiTaRSiSERPINB2. human.
EvolutionaryTraceiP05120.
GeneWikiiPlasminogen_activator_inhibitor-2.
GenomeRNAii5055.
NextBioi19484.
PROiP05120.
SOURCEiSearch...

Gene expression databases

BgeeiP05120.
CleanExiHS_SERPINB2.
ExpressionAtlasiP05120. baseline and differential.
GenevestigatoriP05120.

Family and domain databases

InterProiIPR015556. PAI-2.
IPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PTHR11461:SF61. PTHR11461:SF61. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 2 hits.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and expression in Escherichia coli of a plasminogen activator inhibitor from human placenta."
    Ye R.D., Wun T.-Z., Sadler J.E.
    J. Biol. Chem. 262:3718-3725(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  2. "Plasminogen activator inhibitor 2: regulation of gene transcription during phorbol ester-mediated differentiation of U-937 human histiocytic lymphoma cells."
    Schleuning W.-D., Medcalf R.L., Hession C., Rothenbuhler R., Shaw A., Kruithof E.K.O.
    Mol. Cell. Biol. 7:4564-4567(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Human monocyte Arg-Serpin cDNA. Sequence, chromosomal assignment, and homology to plasminogen activator-inhibitor."
    Webb A.C., Collins K.L., Snyder S.F., Alexander S.J., Rosenwasser L.J., Eddy R.L., Shows T.B., Auron P.E.
    J. Exp. Med. 166:77-94(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Monocyte.
  4. "Cloning and expression of a cDNA coding for a human monocyte-derived plasminogen activator inhibitor."
    Antalis T.M., Clark M.A., Barnes T., Lehrbach P.R., Devine P.L., Schevzov G., Goss N.H., Stephens R.W., Tolstoshev P.
    Proc. Natl. Acad. Sci. U.S.A. 85:985-989(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Monocyte.
  5. "Structure of the gene for human plasminogen activator inhibitor-2. The nearest mammalian homologue of chicken ovalbumin."
    Ye R.D., Ahern S.M., le Beau M.M., Lebo R.V., Sadler J.E.
    J. Biol. Chem. 264:5495-5502(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "Chromosomal organization and localization of the human urokinase inhibitor gene: perfect structural conservation with ovalbumin."
    Samia J.A., Alexander S.J., Horton K.W., Auron P.E., Byers M.G., Shows T.B. Jr., Webb A.C.
    Genomics 6:159-167(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  8. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
    Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
    Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 12-17; 103-108 AND 314-321.
  9. "Interaction of plasminogen activator inhibitor-2 and proteasome subunit, beta type 1."
    Fan J., Zhang Y.Q., Li P., Hou M., Tan L., Wang X., Zhu Y.S.
    Acta Biochim. Biophys. Sin. 36:42-46(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSMB1.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "The crystal structure of plasminogen activator inhibitor 2 at 2.0-A resolution: implications for serpin function."
    Harrop S.J., Jankova L., Coles M., Jardine D., Whittaker J.S., Gould A.R., Meister A., King G.C., Mabbutt B.C., Curmi P.M.G.
    Structure 7:43-54(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  12. Cited for: VARIANTS ASP-120; HIS-229; LYS-404 AND CYS-413.

Entry informationi

Entry nameiPAI2_HUMAN
AccessioniPrimary (citable) accession number: P05120
Secondary accession number(s): Q96E96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: February 1, 1996
Last modified: March 4, 2015
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.