P05120 (PAI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SERPINB2
Synonyms:	PAI2, PLANH2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	415 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Inhibits urokinase-type plasminogen activator. The monocyte derived PAI-2 is distinct from the endothelial cell-derived PAI-1.
Subunit structure	Interacts with PSMB1. Ref.9
Subcellular location	Cytoplasm. Secreted › extracellular space.
Post-translational modification	The signal sequence is not cleaved.
Sequence similarities	Belongs to the serpin family. Ov-serpin subfamily.

Ontologies

Keywords
Biological process	Plasminogen activation
Cellular component	Cytoplasm Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Traceable author statement. Source: Reactome fibrinolysis Traceable author statement. Source: Reactome negative regulation of apoptotic process Traceable author statement PubMed 7499264. Source: ProtInc regulation of proteolysis Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Traceable author statement. Source: Reactome extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Traceable author statement. Source: Reactome
Molecular_function	serine-type endopeptidase inhibitor activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 415

415

Plasminogen activator inhibitor 2

PRO_0000223296

Signal peptide

1 – ?

Not cleaved

Sites

Site

380 – 381

2

Reactive bond

Amino acid modifications

Glycosylation

75

1

N-linked (GlcNAc...) Potential

Glycosylation

115

1

N-linked (GlcNAc...) Potential

Glycosylation

339

1

N-linked (GlcNAc...) Potential

Disulfide bond

5 ↔ 405

Natural variations

Natural variant

120

1

N → D. Ref.12
Corresponds to variant rs6098 [ dbSNP | Ensembl ].

VAR_011743

Natural variant

229

1

R → H. Ref.12
Corresponds to variant rs6100 [ dbSNP | Ensembl ].

VAR_014173

Natural variant

374

1

G → A.
Corresponds to variant rs34066931 [ dbSNP | Ensembl ].

VAR_051946

Natural variant

404

1

N → K. Ref.12
Corresponds to variant rs6103 [ dbSNP | Ensembl ].

VAR_011744

Natural variant

413

1

S → C. Ref.12
Corresponds to variant rs6104 [ dbSNP | Ensembl ].

VAR_011745

Experimental info

Sequence conflict

170

1

N → Y in AAH12609. Ref.7

Secondary structure

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415

Helix Strand Turn

Details...

Helix

4 – 22

19

Beta strand

23 – 26

4

Beta strand

28 – 30

3

Helix

32 – 44

13

Helix

48 – 57

10

Turn

58 – 63

6

Helix

100 – 102

3

Helix

103 – 114

12

Beta strand

123 – 132

10

Helix

139 – 149

11

Beta strand

154 – 156

3

Helix

158 – 176

19

Turn

177 – 179

3

Beta strand

196 – 204

9

Beta strand

208 – 210

3

Beta strand

220 – 225

6

Beta strand

228 – 232

5

Beta strand

234 – 246

13

Turn

247 – 250

4

Beta strand

251 – 258

8

Turn

259 – 261

3

Beta strand

262 – 271

10

Beta strand

274 – 278

5

Helix

280 – 285

6

Helix

288 – 294

7

Turn

297 – 299

3

Beta strand

300 – 310

11

Beta strand

312 – 319

8

Helix

321 – 326

6

Helix

331 – 333

3

Turn

335 – 337

3

Turn

341 – 343

3

Beta strand

353 – 362

10

Beta strand

387 – 389

3

Beta strand

394 – 400

7

Turn

401 – 404

4

Beta strand

405 – 412

8

Sequences

	Sequence		Length	Mass (Da)
	P05120 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 10DFAB5A4B1246FF	FASTA	415	46,596
	10 20 30 40 50 60 MEDLCVANTL FALNLFKHLA KASPTQNLFL SPWSISSTMA MVYMGSRGST EDQMAKVLQF 70 80 90 100 110 120 NEVGANAVTP MTPENFTSCG FMQQIQKGSY PDAILQAQAA DKIHSSFRSL SSAINASTGN 130 140 150 160 170 180 YLLESVNKLF GEKSASFREE YIRLCQKYYS SEPQAVDFLE CAEEARKKIN SWVKTQTKGK 190 200 210 220 230 240 IPNLLPEGSV DGDTRMVLVN AVYFKGKWKT PFEKKLNGLY PFRVNSAQRT PVQMMYLREK 250 260 270 280 290 300 LNIGYIEDLK AQILELPYAG DVSMFLLLPD EIADVSTGLE LLESEITYDK LNKWTSKDKM 310 320 330 340 350 360 AEDEVEVYIP QFKLEEHYEL RSILRSMGME DAFNKGRANF SGMSERNDLF LSEVFHQAMV 370 380 390 400 410 DVNEEGTEAA AGTGGVMTGR TGHGGPQFVA DHPFLFLIMH KITNCILFFG RFSSP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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]	"Characterization of single-nucleotide polymorphisms in coding regions of human genes." Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ASP-120; HIS-229; LYS-404 AND CYS-413.
[13]	Erratum Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 23:373-373(1999)
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00007117.

PIR

A32853.

RefSeq

NP_001137290.1. NM_001143818.1.
NP_002566.1. NM_002575.2.

UniGene

Hs.594481.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BY7	X-ray	2.00	A	1-415	[»]
1JRR	X-ray	1.60	A	1-415	[»]
			P	367-380	[»]
2ARQ	X-ray	1.85	A	1-415	[»]
			P	367-380	[»]
2ARR	X-ray	1.55	A	1-415	[»]
			P	367-380	[»]

ProteinModelPortal

P05120.

ModBase

Search...

Protein-protein interaction databases

IntAct

P05120. 1 interaction.

STRING

9606.ENSP00000299502.

Protein family/group databases

MEROPS

I04.007.

PTM databases

PhosphoSite

P05120.

Polymorphism databases

DMDM

1352712.

Proteomic databases

PaxDb

P05120.

PRIDE

P05120.

Protocols and materials databases

DNASU

5055.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000299502; ENSP00000299502; ENSG00000197632.
ENST00000457692; ENSP00000401645; ENSG00000197632.

GeneID

5055.

KEGG

hsa:5055.

UCSC

uc002ljo.3. human.

Organism-specific databases

CTD

5055.

GeneCards

GC18P061528.

H-InvDB

HIX0212740.

HGNC

HGNC:8584. SERPINB2.

HPA

HPA015480.

MIM

173390. gene.

neXtProt

NX_P05120.

PharmGKB

PA35500.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG4826.

HOGENOM

HOG000238519.

HOVERGEN

HBG005957.

InParanoid

P05120.

KO

K13963.

OMA

LFLIMHK.

OrthoDB

EOG4PC9S5.

PhylomeDB

P05120.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P05120.

Bgee

P05120.

CleanEx

HS_SERPINB2.

Genevestigator

P05120.

GermOnline

ENSG00000197632. Homo sapiens.

Family and domain databases

InterPro

IPR023795. Protease_inhib_I4_serpin_CS.
IPR015556. Protease_inhib_serine_PAI-2.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]

PANTHER

PTHR11461. PTHR11461. 1 hit.
PTHR11461:SF61. PTHR11461:SF61. 1 hit.

Pfam

PF00079. Serpin. 1 hit.
[Graphical view]

SMART

SM00093. SERPIN. 1 hit.
[Graphical view]

SUPFAM

SSF56574. Prot_inh_serpin. 1 hit.

PROSITE

PS00284. SERPIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SERPINB2. human.

DrugBank

DB00009. Alteplase.
DB00029. Anistreplase.
DB00015. Reteplase.
DB00031. Tenecteplase.
DB00013. Urokinase.

EvolutionaryTrace

P05120.

GenomeRNAi

5055.

NextBio

19484.

SOURCE

Search...

Entry information

Entry name

PAI2_HUMAN

Accession

Primary (citable) accession number: P05120
Secondary accession number(s): Q96E96

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 149 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.