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P00747

- PLMN_HUMAN

UniProt

P00747 - PLMN_HUMAN

Protein

Plasminogen

Gene

PLG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 194 (01 Oct 2014)
      Sequence version 2 (01 Jul 1989)
      Previous versions | rss
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    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
    Sitei78 – 792Cleavage; by stromelysin-1
    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
    Sitei466 – 4672Cleavage; by stromelysin-19
    Sitei580 – 5812Cleavage; by plasminogen activator
    Active sitei622 – 6221Charge relay system
    Active sitei665 – 6651Charge relay system
    Active sitei760 – 7601Charge relay system

    GO - Molecular functioni

    1. apolipoprotein binding Source: BHF-UCL
    2. protein binding Source: UniProtKB
    3. protein domain specific binding Source: UniProtKB
    4. serine-type endopeptidase activity Source: BHF-UCL
    5. serine-type peptidase activity Source: AgBase

    GO - Biological processi

    1. blood coagulation Source: HGNC
    2. cellular protein metabolic process Source: Reactome
    3. extracellular matrix disassembly Source: BHF-UCL
    4. extracellular matrix organization Source: Reactome
    5. fibrinolysis Source: Reactome
    6. labyrinthine layer blood vessel development Source: Ensembl
    7. mononuclear cell migration Source: Ensembl
    8. muscle cell cellular homeostasis Source: Ensembl
    9. myoblast differentiation Source: Ensembl
    10. negative regulation of cell-cell adhesion mediated by cadherin Source: BHF-UCL
    11. negative regulation of cell proliferation Source: ProtInc
    12. negative regulation of cell-substrate adhesion Source: BHF-UCL
    13. negative regulation of fibrinolysis Source: BHF-UCL
    14. platelet activation Source: Reactome
    15. platelet degranulation Source: Reactome
    16. positive regulation of fibrinolysis Source: BHF-UCL
    17. proteolysis involved in cellular protein catabolic process Source: Ensembl
    18. tissue regeneration Source: Ensembl
    19. tissue remodeling Source: UniProtKB-KW
    20. trophoblast giant cell differentiation Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Blood coagulation, Fibrinolysis, Hemostasis, Tissue remodeling

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04553-MONOMER.
    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
    REACT_16888. Signaling by PDGF.
    REACT_641. 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
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:9071. PLG.

    Subcellular locationi

    Secreted 2 Publications
    Note: Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin. Interaction with HRG tethers it to the cell surface.

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. cell surface Source: BHF-UCL
    3. extracellular region Source: Reactome
    4. extracellular space Source: BHF-UCL
    5. extracellular vesicular exosome Source: UniProt
    6. extrinsic component of external side of plasma membrane Source: BHF-UCL
    7. plasma membrane Source: Reactome
    8. platelet alpha granule lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Plasminogen deficiency (PLGD) [MIM:217090]: A 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.8 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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
    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
    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
    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

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

    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
    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

    Keywords - PTMi

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

    Proteomic databases

    MaxQBiP00747.
    PeptideAtlasiP00747.
    PRIDEiP00747.

    2D gel databases

    SWISS-2DPAGEP00747.

    PTM databases

    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

    ArrayExpressiP00747.
    BgeeiP00747.
    CleanExiHS_PLG.
    GenevestigatoriP00747.

    Organism-specific databases

    HPAiCAB000668.
    CAB016678.
    HPA021602.

    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.
    sakQ99SU77EBI-999394,EBI-7689378From a different organism.
    skcP007792EBI-999394,EBI-1035089From a different organism.

    Protein-protein interaction databases

    BioGridi111356. 34 interactions.
    IntActiP00747. 29 interactions.
    STRINGi9606.ENSP00000308938.

    Structurei

    Secondary structure

    1
    810
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi25 – 339
    Beta strandi36 – 427
    Helixi46 – 5510
    Beta strandi57 – 593
    Beta strandi63 – 675
    Turni68 – 714
    Beta strandi72 – 776
    Turni80 – 823
    Beta strandi85 – 9612
    Helixi97 – 993
    Beta strandi102 – 1043
    Beta strandi105 – 1106
    Helixi113 – 1153
    Turni119 – 1213
    Beta strandi131 – 1333
    Turni139 – 1413
    Helixi143 – 1453
    Beta strandi148 – 1503
    Beta strandi155 – 1573
    Beta strandi163 – 1675
    Beta strandi172 – 1754
    Beta strandi180 – 1823
    Beta strandi184 – 1863
    Beta strandi205 – 2073
    Beta strandi209 – 2113
    Beta strandi213 – 2153
    Turni221 – 2233
    Helixi225 – 2273
    Beta strandi237 – 2393
    Beta strandi244 – 2485
    Beta strandi253 – 2564
    Beta strandi273 – 2764
    Beta strandi281 – 2833
    Beta strandi291 – 2933
    Beta strandi295 – 2973
    Beta strandi303 – 3053
    Turni311 – 3133
    Helixi315 – 3173
    Beta strandi334 – 3396
    Beta strandi343 – 3464
    Beta strandi377 – 3793
    Beta strandi382 – 3843
    Beta strandi405 – 4073
    Turni413 – 4153
    Turni417 – 4193
    Beta strandi429 – 4313
    Beta strandi436 – 4416
    Beta strandi446 – 4505
    Beta strandi481 – 4833
    Beta strandi487 – 4893
    Beta strandi509 – 5113
    Beta strandi514 – 5163
    Turni518 – 5203
    Turni522 – 5254
    Beta strandi542 – 5465
    Beta strandi552 – 5543
    Beta strandi582 – 5865
    Beta strandi595 – 5995
    Beta strandi605 – 6139
    Beta strandi616 – 6194
    Helixi621 – 6244
    Helixi630 – 6323
    Beta strandi634 – 6385
    Beta strandi640 – 6445
    Beta strandi650 – 65910
    Turni661 – 6633
    Beta strandi667 – 6737
    Beta strandi698 – 7036
    Beta strandi708 – 7103
    Turni711 – 7144
    Beta strandi717 – 7248
    Helixi726 – 7294
    Turni732 – 7376
    Beta strandi743 – 7475
    Beta strandi749 – 7513
    Beta strandi752 – 7543
    Beta strandi763 – 7675
    Beta strandi769 – 77810
    Helixi780 – 7823
    Beta strandi791 – 7955
    Helixi796 – 7983
    Helixi800 – 8089

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    HOGENOMiHOG000112892.
    HOVERGENiHBG004381.
    InParanoidiP00747.
    KOiK01315.
    OMAiEGLEENY.
    OrthoDBiEOG75B84T.
    PhylomeDBiP00747.
    TreeFamiTF329901.

    Family and domain databases

    Gene3Di2.40.20.10. 5 hits.
    InterProiIPR000001. Kringle.
    IPR013806. Kringle-like.
    IPR018056. Kringle_CS.
    IPR003014. PAN-1_domain.
    IPR003609. Pan_app.
    IPR023317. Pept_S1A_plasmin.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [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

    MEHKEVVLLL LLFLKSGQGE PLDDYVNTQG ASLFSVTKKQ LGAGSIEECA    50
    AKCEEDEEFT CRAFQYHSKE QQCVIMAENR KSSIIIRMRD VVLFEKKVYL 100
    SECKTGNGKN YRGTMSKTKN GITCQKWSST SPHRPRFSPA THPSEGLEEN 150
    YCRNPDNDPQ GPWCYTTDPE KRYDYCDILE CEEECMHCSG ENYDGKISKT 200
    MSGLECQAWD SQSPHAHGYI PSKFPNKNLK KNYCRNPDRE LRPWCFTTDP 250
    NKRWELCDIP RCTTPPPSSG PTYQCLKGTG ENYRGNVAVT VSGHTCQHWS 300
    AQTPHTHNRT PENFPCKNLD ENYCRNPDGK RAPWCHTTNS QVRWEYCKIP 350
    SCDSSPVSTE QLAPTAPPEL TPVVQDCYHG DGQSYRGTSS TTTTGKKCQS 400
    WSSMTPHRHQ KTPENYPNAG LTMNYCRNPD ADKGPWCFTT DPSVRWEYCN 450
    LKKCSGTEAS VVAPPPVVLL PDVETPSEED CMFGNGKGYR GKRATTVTGT 500
    PCQDWAAQEP HRHSIFTPET NPRAGLEKNY CRNPDGDVGG PWCYTTNPRK 550
    LYDYCDVPQC AAPSFDCGKP QVEPKKCPGR VVGGCVAHPH SWPWQVSLRT 600
    RFGMHFCGGT LISPEWVLTA AHCLEKSPRP SSYKVILGAH QEVNLEPHVQ 650
    EIEVSRLFLE PTRKDIALLK LSSPAVITDK VIPACLPSPN YVVADRTECF 700
    ITGWGETQGT FGAGLLKEAQ LPVIENKVCN RYEFLNGRVQ STELCAGHLA 750
    GGTDSCQGDS GGPLVCFEKD KYILQGVTSW GLGCARPNKP GVYVRVSRFV 800
    TWIEGVMRNN 810
    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 1 PublicationCurated
    Sequence conflicti72 – 721Q → E AA sequence (PubMed:122932)Curated
    Sequence conflicti86 – 861Missing AA sequence 1 PublicationCurated
    Sequence conflicti86 – 861Missing AA sequence (PubMed:122932)Curated
    Sequence conflicti361 – 3611Q → E AA sequence 1 PublicationCurated
    Sequence conflicti361 – 3611Q → E AA sequence 1 PublicationCurated
    Sequence conflicti701 – 7011I → V in AAA36451. 1 PublicationCurated

    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
    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
    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
    VAR_006630

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.4. human.

    Polymorphism databases

    DMDMi130316.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Plasmin entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS5279.1.
    PIRi A35229. PLHU.
    RefSeqi NP_000292.1. NM_000301.3.
    UniGenei Hs.143436.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B2I NMR - A 181-263 [» ]
    1BML X-ray 2.90 A/B 561-810 [» ]
    1BUI X-ray 2.65 A/B 561-810 [» ]
    1CEA X-ray 2.06 A/B 100-187 [» ]
    1CEB X-ray 2.07 A/B 100-187 [» ]
    1DDJ X-ray 2.00 A/B/C/D 564-810 [» ]
    1HPJ NMR - A 103-181 [» ]
    1HPK NMR - A 103-181 [» ]
    1I5K X-ray 2.70 A/B 184-262 [» ]
    1KI0 X-ray 1.75 A 100-352 [» ]
    1KRN X-ray 1.67 A 374-461 [» ]
    1L4D X-ray 2.30 A 562-810 [» ]
    1L4Z X-ray 2.80 A 563-810 [» ]
    1PK4 X-ray 1.90 A 376-454 [» ]
    1PKR X-ray 2.48 A 101-181 [» ]
    1PMK X-ray 2.25 A/B 374-461 [» ]
    1QRZ X-ray 2.00 A/B/C/D 565-810 [» ]
    1RJX X-ray 2.30 B 564-810 [» ]
    2DOH X-ray 2.30 X 100-333 [» ]
    2DOI X-ray 3.10 A/X 100-333 [» ]
    2KNF NMR - A 480-562 [» ]
    2L0S NMR - A 272-354 [» ]
    2PK4 X-ray 2.25 A 375-454 [» ]
    3UIR X-ray 2.78 A/B 564-810 [» ]
    4A5T X-ray 3.49 S 20-810 [» ]
    4CIK X-ray 1.78 A 101-181 [» ]
    4DCB X-ray 2.03 F 576-585 [» ]
    4DUR X-ray 2.45 A/B 20-810 [» ]
    4DUU X-ray 5.20 A 20-810 [» ]
    5HPG X-ray 1.66 A/B 480-563 [» ]
    DisProti DP00191.
    ProteinModelPortali P00747.
    SMRi P00747. Positions 20-810.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111356. 34 interactions.
    IntActi P00747. 29 interactions.
    STRINGi 9606.ENSP00000308938.

    Chemistry

    BindingDBi P00747.
    ChEMBLi CHEMBL1801.
    DrugBanki DB00513. Aminocaproic Acid.
    DB00086. Streptokinase.
    DB00302. Tranexamic Acid.
    DB00013. Urokinase.
    GuidetoPHARMACOLOGYi 2394.

    Protein family/group databases

    MEROPSi S01.233.

    PTM databases

    PhosphoSitei P00747.
    UniCarbKBi P00747.

    Polymorphism databases

    DMDMi 130316.

    2D gel databases

    SWISS-2DPAGE P00747.

    Proteomic databases

    MaxQBi P00747.
    PeptideAtlasi P00747.
    PRIDEi P00747.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000308192 ; ENSP00000308938 ; ENSG00000122194 .
    GeneIDi 5340.
    KEGGi hsa:5340.
    UCSCi uc003qtm.4. human.

    Organism-specific databases

    CTDi 5340.
    GeneCardsi GC06P161123.
    HGNCi HGNC:9071. PLG.
    HPAi CAB000668.
    CAB016678.
    HPA021602.
    MIMi 173350. gene.
    217090. phenotype.
    neXtProti NX_P00747.
    Orphaneti 722. Hypoplasminogenemia.
    97231. Ligneous conjunctivitis.
    PharmGKBi PA33405.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000112892.
    HOVERGENi HBG004381.
    InParanoidi P00747.
    KOi K01315.
    OMAi EGLEENY.
    OrthoDBi EOG75B84T.
    PhylomeDBi P00747.
    TreeFami TF329901.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS04553-MONOMER.
    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
    REACT_16888. Signaling by PDGF.
    REACT_641. Dissolution of Fibrin Clot.
    SABIO-RK P00747.

    Miscellaneous databases

    EvolutionaryTracei P00747.
    GeneWikii Plasmin.
    Plasminogen_activator.
    GenomeRNAii 5340.
    NextBioi 20698.
    PMAP-CutDB P00747.
    PROi P00747.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00747.
    Bgeei P00747.
    CleanExi HS_PLG.
    Genevestigatori P00747.

    Family and domain databases

    Gene3Di 2.40.20.10. 5 hits.
    InterProi IPR000001. Kringle.
    IPR013806. Kringle-like.
    IPR018056. Kringle_CS.
    IPR003014. PAN-1_domain.
    IPR003609. Pan_app.
    IPR023317. Pept_S1A_plasmin.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00051. Kringle. 5 hits.
    PF00024. PAN_1. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001150. Plasmin. 1 hit.
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00130. KR. 5 hits.
    SM00473. PAN_AP. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF57440. SSF57440. 5 hits.
    PROSITEi PS00021. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the gene for human plasminogen, a key proenzyme in the fibrinolytic system."
      Petersen T.E., Martzen M.R., Ichinose A., Davie E.W.
      J. Biol. Chem. 265:6104-6111(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASN-472.
    2. "Molecular cloning and characterization of a full-length cDNA clone for human plasminogen."
      Forsgren M., Raden B., Israelsson M., Larsson K., Heden L.-O.
      FEBS Lett. 213:254-260(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Expression of recombinant human plasminogen and aglycoplasminogen in HeLa cells."
      Browne M.J., Chapman C.G., Dodd I., Carey J.E., Lawrence G.M.P., Mitchell D., Robinson J.H.
      Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    4. SeattleSNPs variation discovery resource
      Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-57; GLN-133; HIS-261; TRP-408; ASN-472; VAL-494 AND TRP-523.
    5. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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], VARIANT ASP-676.
      Tissue: Kidney.
    7. Sottrup-Jensen L., Petersen T.E., Magnusson S.
      Submitted (JUL-1977) to the PIR data bank
      Cited for: PROTEIN SEQUENCE OF 20-810, VARIANT ASN-472.
    8. "Structural relationship between 'glutamic acid' and 'lysine' forms of human plasminogen and their interaction with the NH2-terminal activation peptide as studied by affinity chromatography."
      Wiman B., Wallen P.
      Eur. J. Biochem. 50:489-494(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-100.
    9. "The primary structure of human plasminogen."
      Sottrup-Jensen L., Claeys H., Zajdel M., Petersen T.E., Magnusson S.
      (In) Davidson J.F., Rowan R.M., Samama M.M., Desnoyers P.C. (eds.); Progress in chemical fibrinolysis and thrombolysis, pp.3:191-209, Raven Press, New York (1978)
      Cited for: PROTEIN SEQUENCE OF 95-580; 581-626; 657-700 AND 732-810, VARIANT ASN-472.
    10. "Characterization of a complementary deoxyribonucleic acid coding for human and bovine plasminogen."
      Malinowski D.P., Sadler J.E., Davie E.W.
      Biochemistry 23:4243-4250(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 292-810.
    11. "Amino-acid sequence of the cyanogen-bromide fragment from human plasminogen that forms the linkage between the plasmin chains."
      Wiman B., Wallen P.
      Eur. J. Biochem. 58:539-547(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 483-604.
    12. "Primary structure of the B-chain of human plasmin."
      Wiman B.
      Eur. J. Biochem. 76:129-137(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 581-810.
    13. "The primary structure of human plasminogen. II. The histidine loop of human plasmin: light (B) chain active center histidine sequence."
      Robbins K.C., Bernabe P., Arzadon L., Summaria L.
      J. Biol. Chem. 248:1631-1633(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE.
    14. "Studies on the active center of human plasmin. Partial amino acid sequence of a peptide containing the active center serine residue."
      Groskopf W.R., Summaria L., Robbins K.C.
      J. Biol. Chem. 244:3590-3597(1969) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE.
    15. "Structure of the omega-aminocarboxylic acid-binding sites of human plasminogen. Arginine 70 and aspartic acid 56 are essential for binding of ligand by kringle 4."
      Trexler M., Vali Z., Patthy L.
      J. Biol. Chem. 257:7401-7406(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: OMEGA-AMINOCARBOXYLIC ACID-BINDING SITES.
    16. "The fibrin-binding site of human plasminogen. Arginines 32 and 34 are essential for fibrin affinity of the kringle 1 domain."
      Vali Z., Patthy L.
      J. Biol. Chem. 259:13690-13694(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: FIBRIN AND OMEGA-AMINOCARBOXYLIC ACID BINDING SITES.
    17. "Serine-578 is a major phosphorylation locus in human plasma plasminogen."
      Wang H., Prorok M., Bretthauer R.K., Castellino F.J.
      Biochemistry 36:8100-8106(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-597.
    18. "The N- and O-linked carbohydrate chains of human, bovine and porcine plasminogen. Species specificity in relation to sialylation and fucosylation patterns."
      Marti T., Schaller J., Rickli E.E., Schmid K., Kamerling J.P., Gerwig G.J., van Halbeek H., Vliegenthart J.F.G.
      Eur. J. Biochem. 173:57-63(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-268; ASN-308 AND THR-365, STRUCTURE OF CARBOHYDRATES.
    19. "Acceleration of plasminogen activation by tissue plasminogen activator on surface-bound histidine-proline-rich glycoprotein."
      Borza D.B., Morgan W.T.
      J. Biol. Chem. 272:5718-5726(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HRG.
    20. "Evidence for a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2."
      Pirie-Shepherd S.R., Stevens R.D., Andon N.L., Enghild J.J., Pizzo S.V.
      J. Biol. Chem. 272:7408-7411(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-268.
    21. "Angiostatin: a novel angiogenesis inhibitor that mediates the suppression of metastases by a Lewis lung carcinoma."
      O'Reilly M.S., Holmgren L., Shing Y., Chen C., Rosenthal R.A., Moses M., Lane W.S., Cao Y., Sage E.H., Folkman J.
      Cell 79:315-328(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF ANGIOSTATIN, PARTIAL PROTEIN SEQUENCE.
    22. "A recombinant human angiostatin protein inhibits experimental primary and metastatic cancer."
      Sim B.K., O'Reilly M.S., Liang H., Fortier A.H., He W., Madsen J.W., Lapcevich R., Nacy C.A.
      Cancer Res. 57:1329-1334(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF ANGIOSTATIN.
    23. "Generation of an angiostatin-like fragment from plasminogen by stromelysin-1 (MMP-3)."
      Lijnen H.R., Ugwu F., Bini A., Collen D.
      Biochemistry 37:4699-4702(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC CLEAVAGE.
    24. Cited for: INTERACTION WITH ATP5A1, SUBCELLULAR LOCATION.
    25. "Binding of the NG2 proteoglycan to kringle domains modulates the functional properties of angiostatin and plasmin(ogen)."
      Goretzki L., Lombardo C.R., Stallcup W.B.
      J. Biol. Chem. 275:28625-28633(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CSPG4, DOMAIN.
    26. "Protease nexin-1 inhibits plasminogen activation-induced apoptosis of adherent cells."
      Rossignol P., Ho-Tin-Noe B., Vranckx R., Bouton M.C., Meilhac O., Lijnen H.R., Guillin M.C., Michel J.B., Angles-Cano E.
      J. Biol. Chem. 279:10346-10356(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, ENZYME REGULATION, SUBCELLULAR LOCATION, FUNCTION OF PLASMIN, MUTAGENESIS OF SER-741.
    27. "Angiomotin regulates endothelial cell-cell junctions and cell motility."
      Bratt A., Birot O., Sinha I., Veitonmaeki N., Aase K., Ernkvist M., Holmgren L.
      J. Biol. Chem. 280:34859-34869(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AMOT.
    28. "Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
      Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
      Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-308.
      Tissue: Milk.
    29. "A unique proteolytic fragment of human fibrinogen containing the A alpha COOH-terminal domain of the native molecule."
      Kirschbaum N.E., Budzynski A.Z.
      J. Biol. Chem. 265:13669-13676(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    30. "Regulation of histidine-rich glycoprotein (HRG) function via plasmin-mediated proteolytic cleavage."
      Poon I.K., Olsson A.K., Hulett M.D., Parish C.R.
      Biochem. J. 424:27-37(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HRG.
    31. "Crystal and molecular structure of human plasminogen kringle 4 refined at 1.9-A resolution."
      Mulichak A.M., Tulinsky A., Ravichandran K.G.
      Biochemistry 30:10576-10588(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 374-461.
    32. "The refined structure of the epsilon-aminocaproic acid complex of human plasminogen kringle 4."
      Wu T.-P., Padmanabhan K., Tulinsky A., Mulichak A.M.
      Biochemistry 30:10589-10594(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 374-461.
    33. "The structure of recombinant plasminogen kringle 1 and the fibrin binding site."
      Wu T.-P., Padmanabhan K.P., Tulinsky A.
      Blood Coagul. Fibrinolysis 5:157-166(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 101-181.
    34. "Crystal structures of the recombinant kringle 1 domain of human plasminogen in complexes with the ligands epsilon-aminocaproic acid and trans-4-(aminomethyl)cyclohexane-1-carboxylic Acid."
      Mathews I.I., Vanderhoff-Hanaver P., Castellino F.J., Tulinsky A.
      Biochemistry 35:2567-2576(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 102-181.
    35. "Structure of human plasminogen kringle 4 at 1.68 Angstrom and 277 K. A possible structural role of disordered residues."
      Stec B., Yamano A., Whitlow M., Teeter M.M.
      Acta Crystallogr. D 53:169-178(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 376-454.
    36. "The ternary microplasmin-staphylokinase-microplasmin complex is a proteinase-cofactor-substrate complex in action."
      Parry M.A., Fernandez-Catalan C., Bergner A., Huber R., Hopfner K.P., Schlott B., Guehrs K.H., Bode W.
      Nat. Struct. Biol. 5:917-923(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 561-810, DISULFIDE BONDS.
    37. "Structure and ligand binding determinants of the recombinant kringle 5 domain of human plasminogen."
      Chang Y., Mochalkin I., McCance S.G., Cheng B., Tulinsky A., Castellino F.J.
      Biochemistry 37:3258-3271(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 480-563.
    38. "Human plasminogen catalytic domain undergoes an unusual conformational change upon activation."
      Wang X., Terzyan S., Tang J., Loy J.A., Lin X., Zhang X.C.
      J. Mol. Biol. 295:903-914(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 564-810, DISULFIDE BONDS.
    39. "Structure and binding determinants of the recombinant kringle-2 domain of human plasminogen to an internal peptide from a group A Streptococcal surface protein."
      Rios-Steiner J.L., Schenone M., Mochalkin I., Tulinsky A., Castellino F.J.
      J. Mol. Biol. 308:705-719(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 183-262.
    40. "The X-ray crystallographic structure of the angiogenesis inhibitor angiostatin."
      Abad M.C., Arni R.K., Grella D.K., Castellino F.J., Tulinsky A., Geiger J.H.
      J. Mol. Biol. 318:1009-1017(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 100-352, DISULFIDE BONDS.
    41. "Effects of deletion of streptokinase residues 48-59 on plasminogen activation."
      Wakeham N., Terzyan S., Zhai P., Loy J.A., Tang J., Zhang X.C.
      Protein Eng. 15:753-761(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 562-810.
    42. "Characterization of Lys-698-to-Met substitution in human plasminogen catalytic domain."
      Terzyan S., Wakeham N., Zhai P., Rodgers K., Zhang X.C.
      Proteins 56:277-284(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 564-810.
    43. "The structure of human microplasmin in complex with textilinin-1, an aprotinin-like inhibitor from the Australian brown snake."
      Millers E.K., Johnson L.A., Birrell G.W., Masci P.P., Lavin M.F., de Jersey J., Guddat L.W.
      PLoS ONE 8:E54104-E54104(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.78 ANGSTROMS) OF 564-810 IN COMPLEX WITH THE SNAKE VENOM PROTEASE INHIBITOR TEXTILININ-1, DISULFIDE BOND.
    44. "Solution structure of the kringle 4 domain from human plasminogen by 1H nuclear magnetic resonance spectroscopy and distance geometry."
      Atkinson R.A., Williams R.J.P.
      J. Mol. Biol. 212:541-552(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 374-461.
    45. "1H-NMR assignments and secondary structure of human plasminogen kringle 1."
      Rejante M.R., Llinas M.
      Eur. J. Biochem. 221:927-937(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 96-184.
    46. "Solution structure of the epsilon-aminohexanoic acid complex of human plasminogen kringle 1."
      Rejante M.R., Llinas M.
      Eur. J. Biochem. 221:939-949(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 96-184.
    47. "Recombinant gene expression and 1H NMR characteristics of the kringle (2 + 3) supermodule: spectroscopic/functional individuality of plasminogen kringle domains."
      Soehndel S., Hu C.-K., Marti D., Affolter M., Schaller J., Llinas M., Rickli E.E.
      Biochemistry 35:2357-2364(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 183-354.
    48. "Ligand preferences of kringle 2 and homologous domains of human plasminogen: canvassing weak, intermediate, and high-affinity binding sites by 1H-NMR."
      Marti D.N., Hu C.K., An S.S., von Haller P., Schaller J., Llinas M.
      Biochemistry 36:11591-11604(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 183-263.
    49. "Two types of abnormal genes for plasminogen in families with a predisposition for thrombosis."
      Ichinose A., Espling E.S., Takamatsu J., Saito H., Shinmyozu K., Maruyama I., Petersen T.E., Davie E.W.
      Proc. Natl. Acad. Sci. U.S.A. 88:115-119(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PLGD PHE-374 AND THR-620.
    50. Erratum
      Ichinose A., Espling E.S., Takamatsu J., Saito H., Shinmyozu K., Maruyama I., Petersen T.E., Davie E.W.
      Proc. Natl. Acad. Sci. U.S.A. 88:2067-2067(1991)
    51. "Congenital plasminogen deficiency caused by a Ser-572 to Pro mutation."
      Azuma H., Uno Y., Shigekiyo T., Saito S.
      Blood 82:475-480(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PLGD PRO-591.
    52. "Plasminogen Tochigi: inactive plasmin resulting from replacement of alanine-600 by threonine in the active site."
      Miyata T., Iwanaga S., Sakata Y., Aoki N.
      Proc. Natl. Acad. Sci. U.S.A. 79:6132-6136(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PLGD THR-620.
    53. "Plasminogens Tochigi II and Nagoya: two additional molecular defects with Ala-600-->Thr replacement found in plasmin light chain variants."
      Miyata T., Iwanaga S., Sakata Y., Aoki N., Takamatsu J., Kamiya T.
      J. Biochem. 96:277-287(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PLGD THR-620.
    54. "Plasminogen with type-I mutation is polymorphic in the Japanese population."
      Kikuchi S., Yamanouchi Y., Li L., Kobayashi K., Ijima H., Miyazaki R., Tsuchiya S., Hamaguchi H.
      Hum. Genet. 90:7-11(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PLGD THR-620.
    55. "Homozygous mutations in the plasminogen gene of two unrelated girls with ligneous conjunctivitis."
      Schuster V., Mingers A.-M., Seidenspinner S., Nuessgens Z., Pukrop T., Kreth H.W.
      Blood 90:958-966(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PLGD HIS-235.
    56. "Plasminogen Kanagawa-I, a novel missense mutation, is caused by the amino acid substitution G732R."
      Higuchi Y., Furihata K., Ueno I., Ishikawa S., Okumura N., Tozuka M., Sakurai N.
      Br. J. Haematol. 103:867-870(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PLGD ARG-751.
    57. "Compound-heterozygous mutations in the plasminogen gene predispose to the development of ligneous conjunctivitis."
      Schuster V., Seidenspinner S., Zeitler P., Escher C., Pleyer U., Bernauer W., Stiehm E.R., Isenberg S., Seregard S., Olsson T., Mingers A.-M., Schambeck C., Kreth H.W.
      Blood 93:3457-3466(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PLGD GLU-38; PRO-147 AND HIS-532.

    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: October 1, 2014
    This is version 194 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

    External Data

    Dasty 3