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Protein

Plasminogen

Gene

PLG

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

Functioni

Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells.1 Publication
Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo.1 Publication

Catalytic activityi

Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa; higher selectivity than trypsin. Converts fibrin into soluble products.1 Publication

Enzyme regulationi

Converted into plasmin by plasminogen activators, both plasminogen and its activator being bound to fibrin. Activated with catalytic amounts of streptokinase. Plasmin activity inhibited by SERPINE2.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei134Fibrin1
Binding sitei136Fibrin1
Binding sitei136Omega-aminocarboxylic acids1
Binding sitei158Omega-aminocarboxylic acids1
Binding sitei172Omega-aminocarboxylic acids1
Binding sitei432Omega-aminocarboxylic acids1
Binding sitei445Omega-aminocarboxylic acids1
Active sitei622Charge relay system1
Active sitei665Charge relay system1
Active sitei760Charge relay system1

GO - Molecular functioni

  • apolipoprotein binding Source: BHF-UCL
  • protein domain specific binding Source: UniProtKB
  • receptor binding Source: AgBase
  • serine-type endopeptidase activity Source: BHF-UCL
  • serine-type peptidase activity Source: AgBase

GO - Biological processi

  • blood coagulation Source: HGNC
  • cellular protein metabolic process Source: Reactome
  • extracellular matrix disassembly Source: BHF-UCL
  • fibrinolysis Source: Reactome
  • negative regulation of cell-cell adhesion mediated by cadherin Source: BHF-UCL
  • negative regulation of cell proliferation Source: ProtInc
  • negative regulation of cell-substrate adhesion Source: BHF-UCL
  • negative regulation of fibrinolysis Source: BHF-UCL
  • platelet degranulation Source: Reactome
  • positive regulation of fibrinolysis Source: BHF-UCL
  • tissue remodeling Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Fibrinolysis, Hemostasis, Tissue remodeling

Enzyme and pathway databases

BioCyciMetaCyc:HS04553-MONOMER.
ZFISH:HS04553-MONOMER.
BRENDAi3.4.21.7. 2681.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1592389. Activation of Matrix Metalloproteinases.
R-HSA-186797. Signaling by PDGF.
R-HSA-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
R-HSA-75205. Dissolution of Fibrin Clot.
SABIO-RKP00747.

Protein family/group databases

MEROPSiS01.233.

Names & Taxonomyi

Protein namesi
Gene namesi
Name:PLG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:9071. PLG.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • cell surface Source: BHF-UCL
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • extrinsic component of external side of plasma membrane Source: BHF-UCL
  • plasma membrane Source: Reactome
  • platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Plasminogen deficiency (PLGD)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by decreased serum plasminogen activity. Two forms of the disorder are distinguished: type 1 deficiency is additionally characterized by decreased plasminogen antigen levels and clinical symptoms, whereas type 2 deficiency, also known as dysplasminogenemia, is characterized by normal, or slightly reduced antigen levels, and absence of clinical manifestations. Plasminogen deficiency type 1 results in markedly impaired extracellular fibrinolysis and chronic mucosal pseudomembranous lesions due to subepithelial fibrin deposition and inflammation. The most common clinical manifestation of type 1 deficiency is ligneous conjunctivitis in which pseudomembranes formation on the palpebral surfaces of the eye progresses to white, yellow-white, or red thick masses with a wood-like consistency that replace the normal mucosa.
See also OMIM:217090
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01865738K → E in PLGD; common mutation. 1 PublicationCorresponds to variant rs73015965dbSNPEnsembl.1
Natural variantiVAR_018658147L → P in PLGD. 1 PublicationCorresponds to variant rs770198253dbSNPEnsembl.1
Natural variantiVAR_018659235R → H in PLGD; severe type 1 deficiency. 1 PublicationCorresponds to variant rs121918030dbSNPEnsembl.1
Natural variantiVAR_006627374V → F in PLGD; Nagoya-1. 1 PublicationCorresponds to variant rs121918028dbSNPEnsembl.1
Natural variantiVAR_018660532R → H in PLGD. 1 Publication1
Natural variantiVAR_006628591S → P in PLGD; may be associated with susceptibility to thrombosis. 1 PublicationCorresponds to variant rs121918029dbSNPEnsembl.1
Natural variantiVAR_006629620A → T in PLGD; type 2 plasminogen deficiency; decreased activity; Nagoya-2/Tochigi/Kagoshima; may be associated with susceptibility to thrombosis. 4 PublicationsCorresponds to variant rs121918027dbSNPEnsembl.1
Natural variantiVAR_006630751G → R in PLGD; Kanagawa-1; 50% activity. 1 PublicationCorresponds to variant rs121918033dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi741S → A: Proteolytically cleaved, but abolishes plasmin activity and cell detachment. 1 Publication1

Keywords - Diseasei

Disease mutation, Thrombophilia

Organism-specific databases

DisGeNETi5340.
MalaCardsiPLG.
MIMi217090. phenotype.
OpenTargetsiENSG00000122194.
Orphaneti722. Hypoplasminogenemia.
97231. Ligneous conjunctivitis.
PharmGKBiPA33405.

Chemistry databases

ChEMBLiCHEMBL1801.
DrugBankiDB00009. Alteplase.
DB00513. Aminocaproic Acid.
DB00029. Anistreplase.
DB06692. Aprotinin.
DB00015. Reteplase.
DB00086. Streptokinase.
DB00031. Tenecteplase.
DB00302. Tranexamic Acid.
DB00013. Urokinase.
GuidetoPHARMACOLOGYi2394.

Polymorphism and mutation databases

BioMutaiPLG.
DMDMi130316.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 192 PublicationsAdd BLAST19
ChainiPRO_000002805320 – 810PlasminogenAdd BLAST791
ChainiPRO_000002805420 – 580Plasmin heavy chain AAdd BLAST561
PeptideiPRO_000002805520 – 97Activation peptideAdd BLAST78
ChainiPRO_000002805779 – 466AngiostatinAdd BLAST388
ChainiPRO_000002805698 – 580Plasmin heavy chain A, short formAdd BLAST483
ChainiPRO_0000028058581 – 810Plasmin light chain BAdd BLAST230

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi49 ↔ 73
Disulfide bondi53 ↔ 61
Disulfide bondi103 ↔ 181
Disulfide bondi124 ↔ 164
Disulfide bondi152 ↔ 176
Disulfide bondi185 ↔ 262
Disulfide bondi188 ↔ 316
Disulfide bondi206 ↔ 245
Disulfide bondi234 ↔ 257
GlycosylationiCAR_000016268O-linked (GalNAc...)2 Publications1
Disulfide bondi275 ↔ 352
Disulfide bondi296 ↔ 335
GlycosylationiCAR_000017308N-linked (GlcNAc...)2 Publications1
Disulfide bondi324 ↔ 347
GlycosylationiCAR_000018365O-linked (GalNAc...)1 Publication1
Disulfide bondi377 ↔ 454
Disulfide bondi398 ↔ 437
Disulfide bondi426 ↔ 449
Disulfide bondi481 ↔ 560
Disulfide bondi502 ↔ 543
Disulfide bondi531 ↔ 555
Disulfide bondi567 ↔ 685Interchain (between A and B chains)
Disulfide bondi577 ↔ 585Interchain (between A and B chains)
Modified residuei597Phosphoserine1 Publication1
Disulfide bondi607 ↔ 623
Modified residuei688PhosphoserineCombined sources1
Disulfide bondi699 ↔ 766
Disulfide bondi729 ↔ 745
Disulfide bondi756 ↔ 784

Post-translational modificationi

N-linked glycan contains N-acetyllactosamine and sialic acid. O-linked glycans consist of Gal-GalNAc disaccharide modified with up to 2 sialic acid residues (microheterogeneity).3 Publications
In the presence of the inhibitor, the activation involves only cleavage after Arg-580, yielding two chains held together by two disulfide bonds. In the absence of the inhibitor, the activation involves additionally the removal of the activation peptide.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei78 – 79Cleavage; by stromelysin-12
Sitei466 – 467Cleavage; by stromelysin-192
Sitei580 – 581Cleavage; by plasminogen activator2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

EPDiP00747.
MaxQBiP00747.
PaxDbiP00747.
PeptideAtlasiP00747.
PRIDEiP00747.

2D gel databases

SWISS-2DPAGEP00747.

PTM databases

iPTMnetiP00747.
PhosphoSitePlusiP00747.
UniCarbKBiP00747.

Miscellaneous databases

PMAP-CutDBP00747.

Expressioni

Tissue specificityi

Present in plasma and many other extracellular fluids. It is synthesized in the liver.

Gene expression databases

BgeeiENSG00000122194.
CleanExiHS_PLG.
ExpressionAtlasiP00747. baseline and differential.
GenevisibleiP00747. HS.

Organism-specific databases

HPAiCAB000668.
CAB016678.
HPA021602.
HPA048823.

Interactioni

Subunit structurei

Interacts (both mature PLG and the angiostatin peptide) with CSPG4 and AMOT (PubMed:10889192, PubMed:16043488). Interacts (via the Kringle domains) with HRG; the interaction tethers PLG to the cell surface and enhances its activation (PubMed:9102401, PubMed:19712047). Interacts (via Kringle 4 domain) with ADA; the interaction stimulates PLG activation when in complex with DPP4 (PubMed:15016824). Angiostatin: Interacts with ATP5A1; the interaction inhibits most of the angiogenic effects of angiostatin (PubMed:10077593).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q6V4L12EBI-999394,EBI-984250From a different organism.
Q6V4L42EBI-999394,EBI-984286From a different organism.
Q6V4L52EBI-999394,EBI-984118From a different organism.
Q6V4L92EBI-999394,EBI-984197From a different organism.
APOHP027492EBI-999394,EBI-2114682
sakQ99SU77EBI-999394,EBI-7689378From a different organism.
skcP007792EBI-999394,EBI-1035089From a different organism.

GO - Molecular functioni

  • apolipoprotein binding Source: BHF-UCL
  • protein domain specific binding Source: UniProtKB
  • receptor binding Source: AgBase

Protein-protein interaction databases

BioGridi111356. 35 interactors.
IntActiP00747. 31 interactors.
STRINGi9606.ENSP00000308938.

Chemistry databases

BindingDBiP00747.

Structurei

Secondary structure

1810
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 33Combined sources9
Beta strandi36 – 42Combined sources7
Helixi46 – 55Combined sources10
Beta strandi57 – 59Combined sources3
Beta strandi63 – 67Combined sources5
Turni68 – 71Combined sources4
Beta strandi72 – 77Combined sources6
Turni80 – 82Combined sources3
Beta strandi85 – 96Combined sources12
Helixi97 – 99Combined sources3
Beta strandi102 – 104Combined sources3
Beta strandi105 – 110Combined sources6
Helixi113 – 115Combined sources3
Turni119 – 121Combined sources3
Beta strandi131 – 133Combined sources3
Turni139 – 141Combined sources3
Turni143 – 146Combined sources4
Beta strandi148 – 150Combined sources3
Beta strandi155 – 157Combined sources3
Beta strandi163 – 167Combined sources5
Beta strandi172 – 175Combined sources4
Beta strandi180 – 182Combined sources3
Beta strandi184 – 186Combined sources3
Beta strandi205 – 207Combined sources3
Beta strandi209 – 211Combined sources3
Beta strandi213 – 215Combined sources3
Turni221 – 223Combined sources3
Helixi225 – 227Combined sources3
Beta strandi237 – 239Combined sources3
Beta strandi244 – 248Combined sources5
Beta strandi253 – 256Combined sources4
Beta strandi273 – 276Combined sources4
Beta strandi281 – 283Combined sources3
Beta strandi291 – 293Combined sources3
Beta strandi295 – 297Combined sources3
Beta strandi303 – 305Combined sources3
Turni311 – 313Combined sources3
Helixi315 – 317Combined sources3
Beta strandi334 – 339Combined sources6
Beta strandi343 – 346Combined sources4
Beta strandi377 – 379Combined sources3
Beta strandi382 – 384Combined sources3
Beta strandi405 – 407Combined sources3
Turni413 – 415Combined sources3
Turni417 – 419Combined sources3
Beta strandi429 – 431Combined sources3
Beta strandi436 – 441Combined sources6
Beta strandi446 – 450Combined sources5
Beta strandi460 – 462Combined sources3
Beta strandi481 – 483Combined sources3
Beta strandi487 – 489Combined sources3
Beta strandi509 – 511Combined sources3
Beta strandi514 – 516Combined sources3
Turni518 – 520Combined sources3
Turni522 – 525Combined sources4
Beta strandi542 – 546Combined sources5
Beta strandi552 – 554Combined sources3
Beta strandi582 – 586Combined sources5
Beta strandi595 – 599Combined sources5
Beta strandi605 – 613Combined sources9
Beta strandi616 – 619Combined sources4
Helixi621 – 624Combined sources4
Helixi630 – 632Combined sources3
Beta strandi634 – 638Combined sources5
Beta strandi640 – 644Combined sources5
Beta strandi650 – 659Combined sources10
Turni661 – 663Combined sources3
Beta strandi667 – 673Combined sources7
Beta strandi698 – 703Combined sources6
Beta strandi708 – 710Combined sources3
Turni711 – 714Combined sources4
Beta strandi717 – 724Combined sources8
Helixi726 – 729Combined sources4
Turni732 – 737Combined sources6
Beta strandi743 – 747Combined sources5
Beta strandi749 – 751Combined sources3
Beta strandi752 – 754Combined sources3
Beta strandi763 – 767Combined sources5
Beta strandi769 – 778Combined sources10
Helixi780 – 782Combined sources3
Beta strandi791 – 795Combined sources5
Helixi796 – 798Combined sources3
Helixi800 – 808Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B2INMR-A181-263[»]
1BMLX-ray2.90A/B561-810[»]
1BUIX-ray2.65A/B561-810[»]
1CEAX-ray2.06A/B100-187[»]
1CEBX-ray2.07A/B100-187[»]
1DDJX-ray2.00A/B/C/D564-810[»]
1HPJNMR-A103-181[»]
1HPKNMR-A103-181[»]
1I5KX-ray2.70A/B184-262[»]
1KI0X-ray1.75A100-352[»]
1KRNX-ray1.67A374-461[»]
1L4DX-ray2.30A562-810[»]
1L4ZX-ray2.80A563-810[»]
1PK4X-ray1.90A376-454[»]
1PKRX-ray2.48A101-181[»]
1PMKX-ray2.25A/B374-461[»]
1QRZX-ray2.00A/B/C/D565-810[»]
1RJXX-ray2.30B564-810[»]
2DOHX-ray2.30X100-333[»]
2DOIX-ray3.10A/X100-333[»]
2KNFNMR-A480-562[»]
2L0SNMR-A272-354[»]
2PK4X-ray2.25A375-454[»]
3UIRX-ray2.78A/B564-810[»]
4A5TX-ray3.49S20-810[»]
4CIKX-ray1.78A101-181[»]
4DCBX-ray2.03F576-585[»]
4DURX-ray2.45A/B20-810[»]
4DUUX-ray5.20A20-810[»]
5HPGX-ray1.66A/B480-563[»]
DisProtiDP00191.
ProteinModelPortaliP00747.
SMRiP00747.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00747.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 98PANPROSITE-ProRule annotationAdd BLAST79
Domaini103 – 181Kringle 1PROSITE-ProRule annotationAdd BLAST79
Domaini184 – 262Kringle 2PROSITE-ProRule annotationAdd BLAST79
Domaini275 – 352Kringle 3PROSITE-ProRule annotationAdd BLAST78
Domaini377 – 454Kringle 4PROSITE-ProRule annotationAdd BLAST78
Domaini481 – 560Kringle 5PROSITE-ProRule annotationAdd BLAST80
Domaini581 – 808Peptidase S1PROSITE-ProRule annotationAdd BLAST228

Domaini

Kringle domains mediate interaction with CSPG4.1 Publication

Sequence similaritiesi

Belongs to the peptidase S1 family. Plasminogen subfamily.PROSITE-ProRule annotation
Contains 5 kringle domains.PROSITE-ProRule annotation
Contains 1 PAN domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Kringle, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IDXR. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000119133.
HOGENOMiHOG000112892.
HOVERGENiHBG004381.
InParanoidiP00747.
KOiK01315.
OMAiFPNKNLK.
OrthoDBiEOG091G0AH5.
PhylomeDBiP00747.
TreeFamiTF329901.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR003609. Pan_app.
IPR023317. Pept_S1A_plasmin.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00051. Kringle. 5 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001150. Plasmin. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00130. KR. 5 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 5 hits.
PROSITEiPS00021. KRINGLE_1. 5 hits.
PS50070. KRINGLE_2. 5 hits.
PS50948. PAN. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00747-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEHKEVVLLL LLFLKSGQGE PLDDYVNTQG ASLFSVTKKQ LGAGSIEECA
60 70 80 90 100
AKCEEDEEFT CRAFQYHSKE QQCVIMAENR KSSIIIRMRD VVLFEKKVYL
110 120 130 140 150
SECKTGNGKN YRGTMSKTKN GITCQKWSST SPHRPRFSPA THPSEGLEEN
160 170 180 190 200
YCRNPDNDPQ GPWCYTTDPE KRYDYCDILE CEEECMHCSG ENYDGKISKT
210 220 230 240 250
MSGLECQAWD SQSPHAHGYI PSKFPNKNLK KNYCRNPDRE LRPWCFTTDP
260 270 280 290 300
NKRWELCDIP RCTTPPPSSG PTYQCLKGTG ENYRGNVAVT VSGHTCQHWS
310 320 330 340 350
AQTPHTHNRT PENFPCKNLD ENYCRNPDGK RAPWCHTTNS QVRWEYCKIP
360 370 380 390 400
SCDSSPVSTE QLAPTAPPEL TPVVQDCYHG DGQSYRGTSS TTTTGKKCQS
410 420 430 440 450
WSSMTPHRHQ KTPENYPNAG LTMNYCRNPD ADKGPWCFTT DPSVRWEYCN
460 470 480 490 500
LKKCSGTEAS VVAPPPVVLL PDVETPSEED CMFGNGKGYR GKRATTVTGT
510 520 530 540 550
PCQDWAAQEP HRHSIFTPET NPRAGLEKNY CRNPDGDVGG PWCYTTNPRK
560 570 580 590 600
LYDYCDVPQC AAPSFDCGKP QVEPKKCPGR VVGGCVAHPH SWPWQVSLRT
610 620 630 640 650
RFGMHFCGGT LISPEWVLTA AHCLEKSPRP SSYKVILGAH QEVNLEPHVQ
660 670 680 690 700
EIEVSRLFLE PTRKDIALLK LSSPAVITDK VIPACLPSPN YVVADRTECF
710 720 730 740 750
ITGWGETQGT FGAGLLKEAQ LPVIENKVCN RYEFLNGRVQ STELCAGHLA
760 770 780 790 800
GGTDSCQGDS GGPLVCFEKD KYILQGVTSW GLGCARPNKP GVYVRVSRFV
810
TWIEGVMRNN
Length:810
Mass (Da):90,569
Last modified:July 1, 1989 - v2
Checksum:i8B31CB877CCB3AB6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti50A → AQ AA sequence (PubMed:122932).Curated1
Sequence conflicti72Q → E AA sequence (Ref. 7) Curated1
Sequence conflicti72Q → E AA sequence (PubMed:122932).Curated1
Sequence conflicti86Missing AA sequence (Ref. 7) Curated1
Sequence conflicti86Missing AA sequence (PubMed:122932).Curated1
Sequence conflicti361Q → E AA sequence (Ref. 7) Curated1
Sequence conflicti361Q → E AA sequence (Ref. 9) Curated1
Sequence conflicti701I → V in AAA36451 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01865738K → E in PLGD; common mutation. 1 PublicationCorresponds to variant rs73015965dbSNPEnsembl.1
Natural variantiVAR_01177946I → R.Corresponds to variant rs1049573dbSNPEnsembl.1
Natural variantiVAR_01628757E → K.1 PublicationCorresponds to variant rs4252070dbSNPEnsembl.1
Natural variantiVAR_016288133H → Q.1 PublicationCorresponds to variant rs4252186dbSNPEnsembl.1
Natural variantiVAR_033653134R → K.Corresponds to variant rs2817dbSNPEnsembl.1
Natural variantiVAR_018658147L → P in PLGD. 1 PublicationCorresponds to variant rs770198253dbSNPEnsembl.1
Natural variantiVAR_018659235R → H in PLGD; severe type 1 deficiency. 1 PublicationCorresponds to variant rs121918030dbSNPEnsembl.1
Natural variantiVAR_016289261R → H.1 PublicationCorresponds to variant rs4252187dbSNPEnsembl.1
Natural variantiVAR_006627374V → F in PLGD; Nagoya-1. 1 PublicationCorresponds to variant rs121918028dbSNPEnsembl.1
Natural variantiVAR_016290408R → W.1 PublicationCorresponds to variant rs4252119dbSNPEnsembl.1
Natural variantiVAR_011780453K → I.Corresponds to variant rs1804181dbSNPEnsembl.1
Natural variantiVAR_016291472D → N.4 PublicationsCorresponds to variant rs4252125dbSNPEnsembl.1
Natural variantiVAR_016292494A → V.1 PublicationCorresponds to variant rs4252128dbSNPEnsembl.1
Natural variantiVAR_016293523R → W.1 PublicationCorresponds to variant rs4252129dbSNPEnsembl.1
Natural variantiVAR_018660532R → H in PLGD. 1 Publication1
Natural variantiVAR_006628591S → P in PLGD; may be associated with susceptibility to thrombosis. 1 PublicationCorresponds to variant rs121918029dbSNPEnsembl.1
Natural variantiVAR_006629620A → T in PLGD; type 2 plasminogen deficiency; decreased activity; Nagoya-2/Tochigi/Kagoshima; may be associated with susceptibility to thrombosis. 4 PublicationsCorresponds to variant rs121918027dbSNPEnsembl.1
Natural variantiVAR_031213676V → D.1 PublicationCorresponds to variant rs17857492dbSNPEnsembl.1
Natural variantiVAR_006630751G → R in PLGD; Kanagawa-1; 50% activity. 1 PublicationCorresponds to variant rs121918033dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34276
, M33272, M33274, M33275, M33278, M33279, M33280, M33282, M33283, M33284, M33285, M33286, M33287, M33288, M33289, M33290, M34272, M34273, M34275 Genomic DNA. Translation: AAA60113.1.
X05199 mRNA. Translation: CAA28831.1.
M74220 mRNA. Translation: AAA36451.1.
AY192161 Genomic DNA. Translation: AAN85555.1.
AL109933 Genomic DNA. Translation: CAI22908.1.
BC060513 mRNA. Translation: AAH60513.1.
K02922 mRNA. Translation: AAA60124.1.
CCDSiCCDS5279.1.
PIRiA35229. PLHU.
RefSeqiNP_000292.1. NM_000301.3.
UniGeneiHs.143436.

Genome annotation databases

EnsembliENST00000308192; ENSP00000308938; ENSG00000122194.
GeneIDi5340.
KEGGihsa:5340.
UCSCiuc003qtm.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Plasmin entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34276
, M33272, M33274, M33275, M33278, M33279, M33280, M33282, M33283, M33284, M33285, M33286, M33287, M33288, M33289, M33290, M34272, M34273, M34275 Genomic DNA. Translation: AAA60113.1.
X05199 mRNA. Translation: CAA28831.1.
M74220 mRNA. Translation: AAA36451.1.
AY192161 Genomic DNA. Translation: AAN85555.1.
AL109933 Genomic DNA. Translation: CAI22908.1.
BC060513 mRNA. Translation: AAH60513.1.
K02922 mRNA. Translation: AAA60124.1.
CCDSiCCDS5279.1.
PIRiA35229. PLHU.
RefSeqiNP_000292.1. NM_000301.3.
UniGeneiHs.143436.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B2INMR-A181-263[»]
1BMLX-ray2.90A/B561-810[»]
1BUIX-ray2.65A/B561-810[»]
1CEAX-ray2.06A/B100-187[»]
1CEBX-ray2.07A/B100-187[»]
1DDJX-ray2.00A/B/C/D564-810[»]
1HPJNMR-A103-181[»]
1HPKNMR-A103-181[»]
1I5KX-ray2.70A/B184-262[»]
1KI0X-ray1.75A100-352[»]
1KRNX-ray1.67A374-461[»]
1L4DX-ray2.30A562-810[»]
1L4ZX-ray2.80A563-810[»]
1PK4X-ray1.90A376-454[»]
1PKRX-ray2.48A101-181[»]
1PMKX-ray2.25A/B374-461[»]
1QRZX-ray2.00A/B/C/D565-810[»]
1RJXX-ray2.30B564-810[»]
2DOHX-ray2.30X100-333[»]
2DOIX-ray3.10A/X100-333[»]
2KNFNMR-A480-562[»]
2L0SNMR-A272-354[»]
2PK4X-ray2.25A375-454[»]
3UIRX-ray2.78A/B564-810[»]
4A5TX-ray3.49S20-810[»]
4CIKX-ray1.78A101-181[»]
4DCBX-ray2.03F576-585[»]
4DURX-ray2.45A/B20-810[»]
4DUUX-ray5.20A20-810[»]
5HPGX-ray1.66A/B480-563[»]
DisProtiDP00191.
ProteinModelPortaliP00747.
SMRiP00747.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111356. 35 interactors.
IntActiP00747. 31 interactors.
STRINGi9606.ENSP00000308938.

Chemistry databases

BindingDBiP00747.
ChEMBLiCHEMBL1801.
DrugBankiDB00009. Alteplase.
DB00513. Aminocaproic Acid.
DB00029. Anistreplase.
DB06692. Aprotinin.
DB00015. Reteplase.
DB00086. Streptokinase.
DB00031. Tenecteplase.
DB00302. Tranexamic Acid.
DB00013. Urokinase.
GuidetoPHARMACOLOGYi2394.

Protein family/group databases

MEROPSiS01.233.

PTM databases

iPTMnetiP00747.
PhosphoSitePlusiP00747.
UniCarbKBiP00747.

Polymorphism and mutation databases

BioMutaiPLG.
DMDMi130316.

2D gel databases

SWISS-2DPAGEP00747.

Proteomic databases

EPDiP00747.
MaxQBiP00747.
PaxDbiP00747.
PeptideAtlasiP00747.
PRIDEiP00747.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308192; ENSP00000308938; ENSG00000122194.
GeneIDi5340.
KEGGihsa:5340.
UCSCiuc003qtm.5. human.

Organism-specific databases

CTDi5340.
DisGeNETi5340.
GeneCardsiPLG.
HGNCiHGNC:9071. PLG.
HPAiCAB000668.
CAB016678.
HPA021602.
HPA048823.
MalaCardsiPLG.
MIMi173350. gene.
217090. phenotype.
neXtProtiNX_P00747.
OpenTargetsiENSG00000122194.
Orphaneti722. Hypoplasminogenemia.
97231. Ligneous conjunctivitis.
PharmGKBiPA33405.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IDXR. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000119133.
HOGENOMiHOG000112892.
HOVERGENiHBG004381.
InParanoidiP00747.
KOiK01315.
OMAiFPNKNLK.
OrthoDBiEOG091G0AH5.
PhylomeDBiP00747.
TreeFamiTF329901.

Enzyme and pathway databases

BioCyciMetaCyc:HS04553-MONOMER.
ZFISH:HS04553-MONOMER.
BRENDAi3.4.21.7. 2681.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1592389. Activation of Matrix Metalloproteinases.
R-HSA-186797. Signaling by PDGF.
R-HSA-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
R-HSA-75205. Dissolution of Fibrin Clot.
SABIO-RKP00747.

Miscellaneous databases

ChiTaRSiPLG. human.
EvolutionaryTraceiP00747.
GeneWikiiPlasmin.
Plasminogen_activator.
GenomeRNAii5340.
PMAP-CutDBP00747.
PROiP00747.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000122194.
CleanExiHS_PLG.
ExpressionAtlasiP00747. baseline and differential.
GenevisibleiP00747. HS.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR003609. Pan_app.
IPR023317. Pept_S1A_plasmin.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00051. Kringle. 5 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001150. Plasmin. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00130. KR. 5 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 5 hits.
PROSITEiPS00021. KRINGLE_1. 5 hits.
PS50070. KRINGLE_2. 5 hits.
PS50948. PAN. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPLMN_HUMAN
AccessioniPrimary (citable) accession number: P00747
Secondary accession number(s): Q15146, Q5TEH4, Q6PA00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: November 2, 2016
This is version 217 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

Miscellaneous

Plasmin is inactivated by alpha-2-antiplasmin immediately after dissociation from the clot.

Keywords - Technical termi

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

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

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 one 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.