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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei134 – 1341Fibrin
Binding sitei136 – 1361Fibrin
Binding sitei136 – 1361Omega-aminocarboxylic acids
Binding sitei158 – 1581Omega-aminocarboxylic acids
Binding sitei172 – 1721Omega-aminocarboxylic acids
Binding sitei432 – 4321Omega-aminocarboxylic acids
Binding sitei445 – 4451Omega-aminocarboxylic acids
Active sitei622 – 6221Charge relay system
Active sitei665 – 6651Charge relay system
Active sitei760 – 7601Charge relay system

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.
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381K → E in PLGD; common mutation. 1 Publication
Corresponds to variant rs73015965 [ dbSNP | Ensembl ].
VAR_018657
Natural varianti147 – 1471L → P in PLGD. 1 Publication
VAR_018658
Natural varianti235 – 2351R → H in PLGD; severe type 1 deficiency. 1 Publication
Corresponds to variant rs121918030 [ dbSNP | Ensembl ].
VAR_018659
Natural varianti374 – 3741V → F in PLGD; Nagoya-1. 1 Publication
Corresponds to variant rs121918028 [ dbSNP | Ensembl ].
VAR_006627
Natural varianti532 – 5321R → H in PLGD. 1 Publication
VAR_018660
Natural varianti591 – 5911S → P in PLGD; may be associated with susceptibility to thrombosis. 1 Publication
Corresponds to variant rs121918029 [ dbSNP | Ensembl ].
VAR_006628
Natural varianti620 – 6201A → T in PLGD; type 2 plasminogen deficiency; decreased activity; Nagoya-2/Tochigi/Kagoshima; may be associated with susceptibility to thrombosis. 4 Publications
Corresponds to variant rs121918027 [ dbSNP | Ensembl ].
VAR_006629
Natural varianti751 – 7511G → R in PLGD; Kanagawa-1; 50% activity. 1 Publication
Corresponds to variant rs121918033 [ dbSNP | Ensembl ].
VAR_006630

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi741 – 7411S → A: Proteolytically cleaved, but abolishes plasmin activity and cell detachment. 1 Publication

Keywords - Diseasei

Disease mutation, Thrombophilia

Organism-specific databases

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

Chemistry

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19192 PublicationsAdd
BLAST
Chaini20 – 810791PlasminogenPRO_0000028053Add
BLAST
Chaini20 – 580561Plasmin heavy chain APRO_0000028054Add
BLAST
Peptidei20 – 9778Activation peptidePRO_0000028055Add
BLAST
Chaini79 – 466388AngiostatinPRO_0000028057Add
BLAST
Chaini98 – 580483Plasmin heavy chain A, short formPRO_0000028056Add
BLAST
Chaini581 – 810230Plasmin light chain BPRO_0000028058Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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
Glycosylationi268 – 2681O-linked (GalNAc...)2 PublicationsCAR_000016
Disulfide bondi275 ↔ 352
Disulfide bondi296 ↔ 335
Glycosylationi308 – 3081N-linked (GlcNAc...)2 PublicationsCAR_000017
Disulfide bondi324 ↔ 347
Glycosylationi365 – 3651O-linked (GalNAc...)1 PublicationCAR_000018
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 residuei597 – 5971Phosphoserine1 Publication
Disulfide bondi607 ↔ 623
Modified residuei688 – 6881PhosphoserineCombined sources
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)LengthDescriptionGraphical viewFeature identifierActions
Sitei78 – 792Cleavage; by stromelysin-1
Sitei466 – 4672Cleavage; by stromelysin-19
Sitei580 – 5812Cleavage; by plasminogen activator

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.
PhosphoSiteiP00747.
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. Interacts (via the Kringle domains) with HRG; the interaction tethers PLG to the cell surface and enhances its activation (By similarity).By similarity

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 interactions.
IntActiP00747. 31 interactions.
STRINGi9606.ENSP00000308938.

Chemistry

BindingDBiP00747.

Structurei

Secondary structure

1
810
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 339Combined sources
Beta strandi36 – 427Combined sources
Helixi46 – 5510Combined sources
Beta strandi57 – 593Combined sources
Beta strandi63 – 675Combined sources
Turni68 – 714Combined sources
Beta strandi72 – 776Combined sources
Turni80 – 823Combined sources
Beta strandi85 – 9612Combined sources
Helixi97 – 993Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi105 – 1106Combined sources
Helixi113 – 1153Combined sources
Turni119 – 1213Combined sources
Beta strandi131 – 1333Combined sources
Turni139 – 1413Combined sources
Turni143 – 1464Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi163 – 1675Combined sources
Beta strandi172 – 1754Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi184 – 1863Combined sources
Beta strandi205 – 2073Combined sources
Beta strandi209 – 2113Combined sources
Beta strandi213 – 2153Combined sources
Turni221 – 2233Combined sources
Helixi225 – 2273Combined sources
Beta strandi237 – 2393Combined sources
Beta strandi244 – 2485Combined sources
Beta strandi253 – 2564Combined sources
Beta strandi273 – 2764Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi291 – 2933Combined sources
Beta strandi295 – 2973Combined sources
Beta strandi303 – 3053Combined sources
Turni311 – 3133Combined sources
Helixi315 – 3173Combined sources
Beta strandi334 – 3396Combined sources
Beta strandi343 – 3464Combined sources
Beta strandi377 – 3793Combined sources
Beta strandi382 – 3843Combined sources
Beta strandi405 – 4073Combined sources
Turni413 – 4153Combined sources
Turni417 – 4193Combined sources
Beta strandi429 – 4313Combined sources
Beta strandi436 – 4416Combined sources
Beta strandi446 – 4505Combined sources
Beta strandi460 – 4623Combined sources
Beta strandi481 – 4833Combined sources
Beta strandi487 – 4893Combined sources
Beta strandi509 – 5113Combined sources
Beta strandi514 – 5163Combined sources
Turni518 – 5203Combined sources
Turni522 – 5254Combined sources
Beta strandi542 – 5465Combined sources
Beta strandi552 – 5543Combined sources
Beta strandi582 – 5865Combined sources
Beta strandi595 – 5995Combined sources
Beta strandi605 – 6139Combined sources
Beta strandi616 – 6194Combined sources
Helixi621 – 6244Combined sources
Helixi630 – 6323Combined sources
Beta strandi634 – 6385Combined sources
Beta strandi640 – 6445Combined sources
Beta strandi650 – 65910Combined sources
Turni661 – 6633Combined sources
Beta strandi667 – 6737Combined sources
Beta strandi698 – 7036Combined sources
Beta strandi708 – 7103Combined sources
Turni711 – 7144Combined sources
Beta strandi717 – 7248Combined sources
Helixi726 – 7294Combined sources
Turni732 – 7376Combined sources
Beta strandi743 – 7475Combined sources
Beta strandi749 – 7513Combined sources
Beta strandi752 – 7543Combined sources
Beta strandi763 – 7675Combined sources
Beta strandi769 – 77810Combined sources
Helixi780 – 7823Combined sources
Beta strandi791 – 7955Combined sources
Helixi796 – 7983Combined sources
Helixi800 – 8089Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 20-810.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00747.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 9879PANPROSITE-ProRule annotationAdd
BLAST
Domaini103 – 18179Kringle 1PROSITE-ProRule annotationAdd
BLAST
Domaini184 – 26279Kringle 2PROSITE-ProRule annotationAdd
BLAST
Domaini275 – 35278Kringle 3PROSITE-ProRule annotationAdd
BLAST
Domaini377 – 45478Kringle 4PROSITE-ProRule annotationAdd
BLAST
Domaini481 – 56080Kringle 5PROSITE-ProRule annotationAdd
BLAST
Domaini581 – 808228Peptidase S1PROSITE-ProRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501A → AQ AA sequence (PubMed:122932).Curated
Sequence conflicti72 – 721Q → E AA sequence (Ref. 7) Curated
Sequence conflicti72 – 721Q → E AA sequence (PubMed:122932).Curated
Sequence conflicti86 – 861Missing AA sequence (Ref. 7) Curated
Sequence conflicti86 – 861Missing AA sequence (PubMed:122932).Curated
Sequence conflicti361 – 3611Q → E AA sequence (Ref. 7) Curated
Sequence conflicti361 – 3611Q → E AA sequence (Ref. 9) Curated
Sequence conflicti701 – 7011I → V in AAA36451 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381K → E in PLGD; common mutation. 1 Publication
Corresponds to variant rs73015965 [ dbSNP | Ensembl ].
VAR_018657
Natural varianti46 – 461I → R.
Corresponds to variant rs1049573 [ dbSNP | Ensembl ].
VAR_011779
Natural varianti57 – 571E → K.1 Publication
Corresponds to variant rs4252070 [ dbSNP | Ensembl ].
VAR_016287
Natural varianti133 – 1331H → Q.1 Publication
Corresponds to variant rs4252186 [ dbSNP | Ensembl ].
VAR_016288
Natural varianti134 – 1341R → K.
Corresponds to variant rs2817 [ dbSNP | Ensembl ].
VAR_033653
Natural varianti147 – 1471L → P in PLGD. 1 Publication
VAR_018658
Natural varianti235 – 2351R → H in PLGD; severe type 1 deficiency. 1 Publication
Corresponds to variant rs121918030 [ dbSNP | Ensembl ].
VAR_018659
Natural varianti261 – 2611R → H.1 Publication
Corresponds to variant rs4252187 [ dbSNP | Ensembl ].
VAR_016289
Natural varianti374 – 3741V → F in PLGD; Nagoya-1. 1 Publication
Corresponds to variant rs121918028 [ dbSNP | Ensembl ].
VAR_006627
Natural varianti408 – 4081R → W.1 Publication
Corresponds to variant rs4252119 [ dbSNP | Ensembl ].
VAR_016290
Natural varianti453 – 4531K → I.
Corresponds to variant rs1804181 [ dbSNP | Ensembl ].
VAR_011780
Natural varianti472 – 4721D → N.4 Publications
Corresponds to variant rs4252125 [ dbSNP | Ensembl ].
VAR_016291
Natural varianti494 – 4941A → V.1 Publication
Corresponds to variant rs4252128 [ dbSNP | Ensembl ].
VAR_016292
Natural varianti523 – 5231R → W.1 Publication
Corresponds to variant rs4252129 [ dbSNP | Ensembl ].
VAR_016293
Natural varianti532 – 5321R → H in PLGD. 1 Publication
VAR_018660
Natural varianti591 – 5911S → P in PLGD; may be associated with susceptibility to thrombosis. 1 Publication
Corresponds to variant rs121918029 [ dbSNP | Ensembl ].
VAR_006628
Natural varianti620 – 6201A → T in PLGD; type 2 plasminogen deficiency; decreased activity; Nagoya-2/Tochigi/Kagoshima; may be associated with susceptibility to thrombosis. 4 Publications
Corresponds to variant rs121918027 [ dbSNP | Ensembl ].
VAR_006629
Natural varianti676 – 6761V → D.1 Publication
Corresponds to variant rs17857492 [ dbSNP | Ensembl ].
VAR_031213
Natural varianti751 – 7511G → R in PLGD; Kanagawa-1; 50% activity. 1 Publication
Corresponds to variant rs121918033 [ dbSNP | Ensembl ].
VAR_006630

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
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. Positions 20-810.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111356. 35 interactions.
IntActiP00747. 31 interactions.
STRINGi9606.ENSP00000308938.

Chemistry

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.
PhosphoSiteiP00747.
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.
GeneCardsiPLG.
HGNCiHGNC:9071. PLG.
HPAiCAB000668.
CAB016678.
HPA021602.
HPA048823.
MalaCardsiPLG.
MIMi173350. gene.
217090. phenotype.
neXtProtiNX_P00747.
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.
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: September 7, 2016
This is version 215 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.