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Protein

Plasminogen

Gene

PLG

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 (By similarity).By similarity

Miscellaneous

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher selectivity than trypsin. Converts fibrin into soluble products. EC:3.4.21.7

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Converted into plasmin by plasminogen activators, both plasminogen and its activator being bound to fibrin. Cannot be activated with streptokinase.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei624Charge relay system1
Active sitei667Charge relay system1
Active sitei762Charge relay system1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • protein domain specific binding Source: AgBase
  • serine-type endopeptidase activity Source: GO_Central
  • signaling receptor binding Source: AgBase

GO - Biological processi

  • blood coagulation Source: UniProtKB-KW
  • fibrinolysis Source: UniProtKB-KW
  • response to heat Source: AgBase
  • tissue remodeling Source: UniProtKB-KW

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processBlood coagulation, Fibrinolysis, Hemostasis, Tissue remodeling

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P06868

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S01.233

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Plasminogen (EC:3.4.21.7)
Cleaved into the following 4 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PLG
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2957

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 261 PublicationAdd BLAST26
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002803927 – 812PlasminogenAdd BLAST786
ChainiPRO_000002804027 – 583Plasmin heavy chain AAdd BLAST557
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_000002804127 – 104Activation peptideBy similarityAdd BLAST78
ChainiPRO_0000028042105 – 583Plasmin heavy chain A, short formBy similarityAdd BLAST479
ChainiPRO_0000028043584 – 812Plasmin light chain BAdd BLAST229

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi56 ↔ 80By similarity
Disulfide bondi60 ↔ 68By similarity
Disulfide bondi110 ↔ 188By similarity
Disulfide bondi131 ↔ 171By similarity
Disulfide bondi159 ↔ 183By similarity
Disulfide bondi192 ↔ 269By similarity
Disulfide bondi195 ↔ 323By similarity
Disulfide bondi213 ↔ 252By similarity
Disulfide bondi241 ↔ 264By similarity
Disulfide bondi282 ↔ 359By similarity
Disulfide bondi303 ↔ 342By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>GlycosylationiCAR_000014315N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi331 ↔ 354By similarity
GlycosylationiCAR_000015365O-linked (GalNAc...) serine2 Publications1
Disulfide bondi384 ↔ 461By similarity
Disulfide bondi405 ↔ 444By similarity
Disulfide bondi433 ↔ 456By similarity
Disulfide bondi485 ↔ 564By similarity
Disulfide bondi506 ↔ 547By similarity
Disulfide bondi535 ↔ 559By similarity
Disulfide bondi570 ↔ 687Interchain (between A and B chains)By similarity
Disulfide bondi580 ↔ 588Interchain (between A and B chains)By similarity
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei600PhosphoserineBy similarity1
Disulfide bondi609 ↔ 625By similarity
Disulfide bondi701 ↔ 768By similarity
Disulfide bondi731 ↔ 747By similarity
Disulfide bondi758 ↔ 786By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-linked glycan contains N-acetyllactosamine and sialic acid. O-linked glycans consist of Gal-GalNAc disaccharide which is modified with up to 2 sialic acid residues (microheterogeneity).2 Publications
In the presence of the inhibitor, the activation involves only cleavage after Arg-583, 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 (By similarity).By similarity

Keywords - PTMi

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

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P06868

PeptideAtlas

More...
PeptideAtlasi
P06868

PRoteomics IDEntifications database

More...
PRIDEi
P06868

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
500

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P06868

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with CSPG4 and AMOT. Interacts (via the Kringle domains) with HRG; the interaction tethers PLG to the cell surface and enhances its activation. Interacts (via Kringle 4 domain) with ADA; the interaction stimulates PLG activation when in complex with DPP4. Angiostatin: Interacts with ATP5F1A; the interaction inhibits most of the angiogenic effects of angiostatin.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000001674

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P06868

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P06868

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P06868

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini29 – 105PANPROSITE-ProRule annotationAdd BLAST77
Domaini110 – 188Kringle 1PROSITE-ProRule annotationAdd BLAST79
Domaini192 – 269Kringle 2PROSITE-ProRule annotationAdd BLAST78
Domaini282 – 359Kringle 3PROSITE-ProRule annotationAdd BLAST78
Domaini384 – 461Kringle 4PROSITE-ProRule annotationAdd BLAST78
Domaini485 – 564Kringle 5PROSITE-ProRule annotationAdd BLAST80
Domaini584 – 810Peptidase S1PROSITE-ProRule annotationAdd BLAST227

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Kringle domains mediate interaction with CSPG4.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase S1 family. Plasminogen subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Kringle, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IDXR Eukaryota
COG5640 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000112892

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG004381

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P06868

KEGG Orthology (KO)

More...
KOi
K01315

Database of Orthologous Groups

More...
OrthoDBi
164039at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00108 KR, 5 hits
cd00190 Tryp_SPc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.20.10, 4 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000001 Kringle
IPR013806 Kringle-like
IPR018056 Kringle_CS
IPR038178 Kringle_sf
IPR003609 Pan_app
IPR023317 Pept_S1A_plasmin
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00051 Kringle, 5 hits
PF00024 PAN_1, 1 hit
PF00089 Trypsin, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001150 Plasmin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00722 CHYMOTRYPSIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00130 KR, 5 hits
SM00473 PAN_AP, 1 hit
SM00020 Tryp_SPc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50494 SSF50494, 1 hit
SSF57440 SSF57440, 5 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P06868-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLPASPKMEH KAVVFLLLLF LKSGLGDLLD DYVNTQGASL LSLSRKNLAG
60 70 80 90 100
RSVEDCAAKC EEETDFVCRA FQYHSKEQQC VVMAENSKNT PVFRMRDVIL
110 120 130 140 150
YEKRIYLLEC KTGNGQTYRG TTAETKSGVT CQKWSATSPH VPKFSPEKFP
160 170 180 190 200
LAGLEENYCR NPDNDENGPW CYTTDPDKRY DYCDIPECED KCMHCSGENY
210 220 230 240 250
EGKIAKTMSG RDCQAWDSQS PHAHGYIPSK FPNKNLKMNY CRNPDGEPRP
260 270 280 290 300
WCFTTDPQKR WEFCDIPRCT TPPPSSGPKY QCLKGTGKNY GGTVAVTESG
310 320 330 340 350
HTCQRWSEQT PHKHNRTPEN FPCKNLEENY CRNPNGEKAP WCYTTNSEVR
360 370 380 390 400
WEYCTIPSCE SSPLSTERMD VPVPPEQTPV PQDCYHGNGQ SYRGTSSTTI
410 420 430 440 450
TGRKCQSWSS MTPHRHLKTP ENYPNAGLTM NYCRNPDADK SPWCYTTDPR
460 470 480 490 500
VRWEFCNLKK CSETPEQVPA APQAPGVENP PEADCMIGTG KSYRGKKATT
510 520 530 540 550
VAGVPCQEWA AQEPHQHSIF TPETNPQSGL ERNYCRNPDG DVNGPWCYTM
560 570 580 590 600
NPRKPFDYCD VPQCESSFDC GKPKVEPKKC SGRIVGGCVS KPHSWPWQVS
610 620 630 640 650
LRRSSRHFCG GTLISPKWVL TAAHCLDNIL ALSFYKVILG AHNEKVREQS
660 670 680 690 700
VQEIPVSRLF REPSQADIAL LKLSRPAIIT KEVIPACLPP PNYMVAARTE
710 720 730 740 750
CYITGWGETQ GTFGEGLLKE AHLPVIENKV CNRNEYLDGR VKPTELCAGH
760 770 780 790 800
LIGGTDSCQG DSGGPLVCFE KDKYILQGVT SWGLGCARPN KPGVYVRVSP
810
YVPWIEETMR RN
Length:812
Mass (Da):91,216
Last modified:November 1, 1997 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i38A6AA691E220946
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti335N → D AA sequence (PubMed:3846532).Curated1
Sequence conflicti516Q → H AA sequence (PubMed:3846532).Curated1
Sequence conflicti555P → L AA sequence (PubMed:3846532).Curated1
Sequence conflicti744T → R in AAA30714 (PubMed:6148961).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X79402 mRNA Translation: CAA55939.1
K02935 mRNA Translation: AAA30714.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S45046 PLBO

NCBI Reference Sequences

More...
RefSeqi
NP_776376.1, NM_173951.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Bt.306

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
280897

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:280897

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79402 mRNA Translation: CAA55939.1
K02935 mRNA Translation: AAA30714.1
PIRiS45046 PLBO
RefSeqiNP_776376.1, NM_173951.2
UniGeneiBt.306

3D structure databases

ProteinModelPortaliP06868
SMRiP06868
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000001674

Chemistry databases

BindingDBiP06868
ChEMBLiCHEMBL2957

Protein family/group databases

MEROPSiS01.233

PTM databases

GlyConnecti500
UniCarbKBiP06868

Proteomic databases

PaxDbiP06868
PeptideAtlasiP06868
PRIDEiP06868

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi280897
KEGGibta:280897

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5340

Phylogenomic databases

eggNOGiENOG410IDXR Eukaryota
COG5640 LUCA
HOGENOMiHOG000112892
HOVERGENiHBG004381
InParanoidiP06868
KOiK01315
OrthoDBi164039at2759

Enzyme and pathway databases

SABIO-RKiP06868

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P06868

Family and domain databases

CDDicd00108 KR, 5 hits
cd00190 Tryp_SPc, 1 hit
Gene3Di2.40.20.10, 4 hits
InterProiView protein in InterPro
IPR000001 Kringle
IPR013806 Kringle-like
IPR018056 Kringle_CS
IPR038178 Kringle_sf
IPR003609 Pan_app
IPR023317 Pept_S1A_plasmin
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF00051 Kringle, 5 hits
PF00024 PAN_1, 1 hit
PF00089 Trypsin, 1 hit
PIRSFiPIRSF001150 Plasmin, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
SMARTiView protein in SMART
SM00130 KR, 5 hits
SM00473 PAN_AP, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF57440 SSF57440, 5 hits
PROSITEiView protein in PROSITE
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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPLMN_BOVIN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P06868
Secondary accession number(s): Q28162
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1997
Last modified: January 16, 2019
This is version 160 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
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