PLAU

Functionⁱ

Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.

Catalytic activityⁱ

Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.

Activity regulationⁱ

Inhibited by SERPINA5.2 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	224	Charge relay system	1
Active siteⁱ	275	Charge relay system	1
Active siteⁱ	376	Charge relay system	1

GO - Molecular functionⁱ

serine-type endopeptidase activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

blood coagulation Source: UniProtKB-KW
chemotaxis
Source: ProtInc
Traceable author statementⁱ
- 10749881
fibrinolysis
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
neutrophil degranulation Source: Reactome
plasminogen activation
Source: AgBase
Inferred from direct assayⁱ
- 25978044
positive regulation of cell migration
Source: MGI
Inferred from direct assayⁱ
- 25168896
proteolysis
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
regulation of cell adhesion mediated by integrin
Source: BHF-UCL
Inferred from direct assayⁱ
- 8837777
regulation of cell proliferation Source: Ensembl
regulation of signaling receptor activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 8837777
regulation of smooth muscle cell-matrix adhesion
Source: BHF-UCL
Inferred from direct assayⁱ
- 8837777
regulation of smooth muscle cell migration
Source: BHF-UCL
Inferred from direct assayⁱ
- 8837777
regulation of wound healing
Source: BHF-UCL
Inferred by curatorⁱ
- 8837777
response to hypoxia Source: Ensembl
signal transduction
Source: ProtInc
Traceable author statementⁱ
- 10749881
smooth muscle cell migration Source: Ensembl

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Protease, Serine protease
Biological process	Blood coagulation, Fibrinolysis, Hemostasis, Plasminogen activation

Enzyme and pathway databases

BRENDAⁱ	3.4.21.73 2681
Reactomeⁱ	R-HSA-6798695 Neutrophil degranulation R-HSA-75205 Dissolution of Fibrin Clot
SABIO-RKⁱ	P00749
SIGNORⁱ	P00749

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	S01.231

MEROPSⁱ

S01.231

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Urokinase-type plasminogen activator (EC:3.4.21.73) Short name: U-plasminogen activator Short name: uPA Cleaved into the following 3 chains: Urokinase-type plasminogen activator long chain A Urokinase-type plasminogen activator short chain A Urokinase-type plasminogen activator chain B
Gene namesⁱ	Name:PLAU
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 10

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000122861.15
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9052 PLAU
MIMⁱ	191840 gene
neXtProtⁱ	NX_P00749

Keywords - Cellular componentⁱ

Secreted

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Quebec platelet disorder (QPD)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal dominant bleeding disorder due to a gain-of-function defect in fibrinolysis. Although affected individuals do not exhibit systemic fibrinolysis, they show delayed onset bleeding after challenge, such as surgery. The hallmark of the disorder is markedly increased PLAU levels within platelets, which causes intraplatelet plasmin generation and secondary degradation of alpha-granule proteins.

Pharmaceutical useⁱ

Available under the name Abbokinase (Abbott). Used in Pulmonary Embolism (PE) to initiate fibrinolysis. Clinically used for therapy of thrombolytic disorders.

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	158	S → E: Abolishes phosphorylation, proadhesive function and ability to induce chemotactic response; when associated with E-323. 1 Publication		1
Mutagenesisⁱ	323	S → E: Abolishes phosphorylation, proadhesive function and ability to induce chemotactic response; when associated with E-158. 1 Publication		1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5328
MalaCards human disease database More...MalaCardsⁱ	PLAU
MIMⁱ	601709 phenotype
Orphanetⁱ	220436 Quebec platelet disorder
PharmGKBⁱ	PA33382

Chemistry databases

ChEMBLⁱ	CHEMBL3286
Drug and drug target database More...DrugBankⁱ	DB07122 1-[4-(2-oxo-2-phenylethyl)phenyl]guanidine DB01905 2-(2-Hydroxy-5-Methoxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine DB06854 2-(2-HYDROXY-BIPHENYL)-1H-BENZOIMIDAZOLE-5-CARBOXAMIDINE DB02193 2-(2-Hydroxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine DB03729 2-Amino-5-Hydroxy-Benzimidazole DB03136 4-Iodobenzo[B]Thiophene-2-Carboxamidine DB01977 6-(N-Phenylcarbamyl)-2-Naphthalenecarboxamidine DB07076 6-[(Z)-AMINO(IMINO)METHYL]-N-[3-(CYCLOPENTYLOXY)PHENYL]-2-NAPHTHAMIDE DB03082 6-[(Z)-Amino(Imino)Methyl]-N-[4-(Aminomethyl)Phenyl]-4-(Pyrimidin-2-Ylamino)-2-Naphthamide DB02398 6-[N-(4-(Aminomethyl)Phenyl)Carbamyl]-2-Naphthalenecarboxamidine DB03865 6-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-Carboxamidine DB06855 6-FLUORO-2-(2-HYDROXY-3-ISOBUTOXY-PHENYL)-1H-BENZOIMIDAZOLE-5-CARBOXAMIDINE DB06856 6-FLUORO-2-[2-HYDROXY-3-(2-METHYL-CYCLOHEXYLOXY)-PHENYL]-1H-INDOLE-5-CARBOXAMIDINE DB03046 7-Methoxy-8-[1-(Methylsulfonyl)-1h-Pyrazol-4-Yl]Naphthalene-2-Carboximidamide DB04059 8-(Pyrimidin-2-Ylamino)Naphthalene-2-Carboximidamide DB00594 Amiloride DB03127 Benzamidine DB02526 CRA_10655 DB03159 CRA_8696 DB03782 N-(1-Adamantyl)-N'-(4-Guanidinobenzyl)Urea DB06857 N-(4-CARBAMIMIDOYL-3-CHORO-PHENYL)-2-HYDROXY-3-IODO-5-METHYL-BENZAMIDE DB05254 Plasmin DB03476 Trans-6-(2-Phenylcyclopropyl)-Naphthalene-2-Carboxamidine DB00013 Urokinase
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2393

Polymorphism and mutation databases

BioMutaⁱ	PLAU
DMDMⁱ	254763341

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
Signal peptideⁱ	1 – 20	2 PublicationsAdd BLAST	20
ChainⁱPRO_0000028318	21 – 431	Urokinase-type plasminogen activatorAdd BLAST	411
ChainⁱPRO_0000028319	21 – 177	Urokinase-type plasminogen activator long chain AAdd BLAST	157
ChainⁱPRO_0000028320	156 – 177	Urokinase-type plasminogen activator short chain AAdd BLAST	22
ChainⁱPRO_0000028321	179 – 431	Urokinase-type plasminogen activator chain BAdd BLAST	253

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Disulfide bondⁱ	31 ↔ 39
Disulfide bondⁱ	33 ↔ 51
Glycosylationⁱ	38	O-linked (Fuc) threonine1 Publication	1
Disulfide bondⁱ	53 ↔ 62
Disulfide bondⁱ	70 ↔ 151
Disulfide bondⁱ	91 ↔ 133
Disulfide bondⁱ	122 ↔ 146
Modified residueⁱ	158	Phosphoserine1 Publication	1
Disulfide bondⁱ	168 ↔ 299	Interchain (between A and B chains)
Disulfide bondⁱ	209 ↔ 225
Disulfide bondⁱ	217 ↔ 288
Disulfide bondⁱ	313 ↔ 382
GlycosylationⁱCAR_000026	322	N-linked (GlcNAc...) asparagine	1
Modified residueⁱ	323	Phosphoserine1 Publication	1
Disulfide bondⁱ	345 ↔ 361
Disulfide bondⁱ	372 ↔ 400

Post-translational modificationⁱ

Phosphorylation of Ser-158 and Ser-323 abolishes proadhesive ability but does not interfere with receptor binding.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	177 – 178	Cleavage; during zymogen activation		2

Keywords - PTMⁱ

Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

EPDⁱ	P00749
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P00749
PaxDbⁱ	P00749
PeptideAtlas More...PeptideAtlasⁱ	P00749
PRIDEⁱ	P00749
ProteomicsDBⁱ	51279 51280 [P00749-2]

PTM databases

GlyConnectⁱ	519 612
iPTMnetⁱ	P00749
PhosphoSitePlusⁱ	P00749
UniCarbKBⁱ	P00749

Miscellaneous databases

PMAP-CutDBⁱ	P00749

PMAP-CutDBⁱ

P00749

Expressionⁱ

Tissue specificityⁱ

Expressed in the prostate gland and prostate cancers.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000122861 Expressed in 181 organ(s), highest expression level in epithelium of bronchus
CleanExⁱ	HS_PLAU
ExpressionAtlasⁱ	P00749 baseline and differential
Genevisibleⁱ	P00749 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA008719

HPAⁱ

HPA008719

Interactionⁱ

Subunit structureⁱ

Found in high and low molecular mass forms. Each consists of two chains, A and B. The high molecular mass form contains a long chain A which is cleaved to yield a short chain A. Forms heterodimer with SERPINA5. Binds LRP1B; binding is followed by internalization and degradation. Interacts with MRC2. Interacts with PLAUR.3 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
PLAUR	Q03405-1	2	EBI-3905042,EBI-15695188

With

Entry

#Exp.

IntAct

Notes

PLAUR

Q03405-1

2

EBI-3905042,EBI-15695188

Protein-protein interaction databases

BioGridⁱ	111344, 21 interactors
ComplexPortalⁱ	CPX-483 uPA-PAI-1 complex CPX-487 uPA-uPAR complex CPX-501 uPA-uPAR-vitronectin complex
Database of interacting proteins More...DIPⁱ	DIP-46387N
ELMⁱ	P00749
IntActⁱ	P00749, 9 interactors
Molecular INTeraction database More...MINTⁱ	P00749
STRINGⁱ	9606.ENSP00000361850

Chemistry databases

BindingDBⁱ

P00749

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	34 – 36	Combined sources	3
Beta strandⁱ	38 – 41	Combined sources	4
Turnⁱ	43 – 47	Combined sources	5
Beta strandⁱ	49 – 52	Combined sources	4
Beta strandⁱ	57 – 59	Combined sources	3
Beta strandⁱ	64 – 67	Combined sources	4
Beta strandⁱ	70 – 72	Combined sources	3
Beta strandⁱ	73 – 77	Combined sources	5
Beta strandⁱ	86 – 89	Combined sources	4
Beta strandⁱ	94 – 96	Combined sources	3
Helixⁱ	99 – 101	Combined sources	3
Beta strandⁱ	102 – 104	Combined sources	3
Beta strandⁱ	106 – 108	Combined sources	3
Helixⁱ	111 – 114	Combined sources	4
Beta strandⁱ	117 – 119	Combined sources	3
Beta strandⁱ	128 – 130	Combined sources	3
Beta strandⁱ	132 – 137	Combined sources	6
Beta strandⁱ	140 – 147	Combined sources	8
Helixⁱ	162 – 165	Combined sources	4
Beta strandⁱ	180 – 184	Combined sources	5
Helixⁱ	187 – 189	Combined sources	3
Beta strandⁱ	193 – 199	Combined sources	7
Beta strandⁱ	201 – 203	Combined sources	3
Beta strandⁱ	205 – 215	Combined sources	11
Beta strandⁱ	218 – 221	Combined sources	4
Helixⁱ	223 – 225	Combined sources	3
Turnⁱ	226 – 228	Combined sources	3
Helixⁱ	232 – 234	Combined sources	3
Beta strandⁱ	235 – 240	Combined sources	6
Beta strandⁱ	243 – 246	Combined sources	4
Beta strandⁱ	252 – 261	Combined sources	10
Beta strandⁱ	268 – 271	Combined sources	4
Beta strandⁱ	272 – 274	Combined sources	3
Beta strandⁱ	277 – 282	Combined sources	6
Beta strandⁱ	293 – 295	Combined sources	3
Beta strandⁱ	312 – 318	Combined sources	7
Beta strandⁱ	329 – 331	Combined sources	3
Beta strandⁱ	333 – 340	Combined sources	8
Helixⁱ	342 – 345	Combined sources	4
Turnⁱ	348 – 351	Combined sources	4
Helixⁱ	352 – 354	Combined sources	3
Turnⁱ	356 – 358	Combined sources	3
Beta strandⁱ	359 – 363	Combined sources	5
Beta strandⁱ	365 – 367	Combined sources	3
Beta strandⁱ	379 – 384	Combined sources	6
Beta strandⁱ	387 – 396	Combined sources	10
Beta strandⁱ	398 – 402	Combined sources	5
Beta strandⁱ	407 – 411	Combined sources	5
Helixⁱ	412 – 414	Combined sources	3
Helixⁱ	416 – 422	Combined sources	7

Show more details

3D structure databases

ProteinModelPortalⁱ	P00749
SMRⁱ	P00749
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P00749

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	27 – 63	EGF-likePROSITE-ProRule annotationAdd BLAST	37
Domainⁱ	70 – 151	KringlePROSITE-ProRule annotationAdd BLAST	82
Domainⁱ	179 – 424	Peptidase S1PROSITE-ProRule annotationAdd BLAST	246

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	34 – 57	Binds urokinase plasminogen activator surface receptorBy similarityAdd BLAST		24
Regionⁱ	152 – 177	Connecting peptideAdd BLAST		26

Sequence similaritiesⁱ

Belongs to the peptidase S1 family.PROSITE-ProRule annotation

Keywords - Domainⁱ

EGF-like domain, Kringle, Signal

Phylogenomic databases

eggNOGⁱ	ENOG410IGFI Eukaryota COG5640 LUCA
HOVERGENⁱ	HBG008633
InParanoidⁱ	P00749
KEGG Orthology (KO) More...KOⁱ	K01348
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0AH5
PhylomeDBⁱ	P00749
TreeFamⁱ	TF329901

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00108 KR, 1 hit cd00190 Tryp_SPc, 1 hit
Gene3Dⁱ	2.40.20.10, 1 hit
InterProⁱ	View protein in InterPro IPR013032 EGF-like_CS IPR000742 EGF-like_dom IPR000001 Kringle IPR013806 Kringle-like IPR018056 Kringle_CS IPR038178 Kringle_sf IPR009003 Peptidase_S1_PA IPR001314 Peptidase_S1A IPR001254 Trypsin_dom IPR018114 TRYPSIN_HIS IPR033116 TRYPSIN_SER IPR034814 Urokinase
PANTHERⁱ	PTHR24264:SF38 PTHR24264:SF38, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00051 Kringle, 1 hit PF00089 Trypsin, 1 hit
PRINTSⁱ	PR00722 CHYMOTRYPSIN
SMARTⁱ	View protein in SMART SM00130 KR, 1 hit SM00020 Tryp_SPc, 1 hit
SUPFAMⁱ	SSF50494 SSF50494, 1 hit SSF57440 SSF57440, 1 hit
PROSITEⁱ	View protein in PROSITE PS00022 EGF_1, 1 hit PS50026 EGF_3, 1 hit PS00021 KRINGLE_1, 1 hit PS50070 KRINGLE_2, 1 hit PS50240 TRYPSIN_DOM, 1 hit PS00134 TRYPSIN_HIS, 1 hit PS00135 TRYPSIN_SER, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

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

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P00749-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRALLARLLL CVLVVSDSKG SNELHQVPSN CDCLNGGTCV SNKYFSNIHW 
        60         70         80         90        100
CNCPKKFGGQ HCEIDKSKTC YEGNGHFYRG KASTDTMGRP CLPWNSATVL 
       110        120        130        140        150
QQTYHAHRSD ALQLGLGKHN YCRNPDNRRR PWCYVQVGLK PLVQECMVHD 
       160        170        180        190        200
CADGKKPSSP PEELKFQCGQ KTLRPRFKII GGEFTTIENQ PWFAAIYRRH 
       210        220        230        240        250
RGGSVTYVCG GSLISPCWVI SATHCFIDYP KKEDYIVYLG RSRLNSNTQG 
       260        270        280        290        300
EMKFEVENLI LHKDYSADTL AHHNDIALLK IRSKEGRCAQ PSRTIQTICL 
       310        320        330        340        350
PSMYNDPQFG TSCEITGFGK ENSTDYLYPE QLKMTVVKLI SHRECQQPHY 
       360        370        380        390        400
YGSEVTTKML CAADPQWKTD SCQGDSGGPL VCSLQGRMTL TGIVSWGRGC 
       410        420        430 
ALKDKPGVYT RVSHFLPWIR SHTKEENGLA L

Length:431

Mass (Da):48,507

Last modified:July 28, 2009 - v2

Checksum:ⁱ62C72400BC23115F

GO

Isoform 2 (identifier: P00749-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-29: MRALLARLLLCVLVVSDSKGSNELHQVPS → MVFHLRTRYEQA

« Hide

        10         20         30         40         50
MVFHLRTRYE QANCDCLNGG TCVSNKYFSN IHWCNCPKKF GGQHCEIDKS 
        60         70         80         90        100
KTCYEGNGHF YRGKASTDTM GRPCLPWNSA TVLQQTYHAH RSDALQLGLG 
       110        120        130        140        150
KHNYCRNPDN RRRPWCYVQV GLKPLVQECM VHDCADGKKP SSPPEELKFQ 
       160        170        180        190        200
CGQKTLRPRF KIIGGEFTTI ENQPWFAAIY RRHRGGSVTY VCGGSLISPC 
       210        220        230        240        250
WVISATHCFI DYPKKEDYIV YLGRSRLNSN TQGEMKFEVE NLILHKDYSA 
       260        270        280        290        300
DTLAHHNDIA LLKIRSKEGR CAQPSRTIQT ICLPSMYNDP QFGTSCEITG 
       310        320        330        340        350
FGKENSTDYL YPEQLKMTVV KLISHRECQQ PHYYGSEVTT KMLCAADPQW 
       360        370        380        390        400
KTDSCQGDSG GPLVCSLQGR MTLTGIVSWG RGCALKDKPG VYTRVSHFLP 
       410 
WIRSHTKEEN GLAL

Show »

Length:414

Mass (Da):46,908

Checksum:ⁱFB35DBE360D7E1CC

GO

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

E7ET40	E7ET40_HUMAN	Urokinase-type plasminogen activato... Urokinase-type plasminogen activator	PLAU	414	Annotation score:
S4R3G7	S4R3G7_HUMAN	Urokinase-type plasminogen activato... Urokinase-type plasminogen activator	PLAU	106	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	150	D → G in BAG60754 (PubMed:14702039).Curated	1
Sequence conflictⁱ	151	C → W in CAA26535 (PubMed:3888571).Curated	1
Sequence conflictⁱ	386	G → C in CAA26535 (PubMed:3888571).Curated	1
Sequence conflictⁱ	430	A → V in CAA26535 (PubMed:3888571).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_038730	15	V → L1 PublicationCorresponds to variant dbSNP:rs2227580EnsemblClinVar.	1
Natural variantⁱVAR_006722	141	P → L6 PublicationsCorresponds to variant dbSNP:rs2227564Ensembl.	1
Natural variantⁱVAR_013102	214	I → M2 Publications	1
Natural variantⁱVAR_038731	231	K → Q1 PublicationCorresponds to variant dbSNP:rs2227567EnsemblClinVar.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_038368	1 – 29	MRALL…HQVPS → MVFHLRTRYEQA in isoform 2. 1 PublicationAdd BLAST		29

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M15476 mRNA Translation: AAA61253.1 X02760 mRNA Translation: CAA26535.1 D00244 mRNA Translation: BAA00175.1 K03226 mRNA Translation: AAC97138.1 X02419 Genomic DNA Translation: CAA26268.1 AF377330 Genomic DNA Translation: AAK53822.1 BT007391 mRNA Translation: AAP36055.1 AK298560 mRNA Translation: BAG60754.1 AL596247 Genomic DNA No translation available. CH471083 Genomic DNA Translation: EAW54544.1 BC013575 mRNA Translation: AAH13575.1 D11143 mRNA Translation: BAA01919.1 K02286 Genomic DNA Translation: AAA61252.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS44442.1 [P00749-2] CCDS7339.1 [P00749-1]
PIRⁱ	A00931 UKHU
NCBI Reference Sequences More...RefSeqⁱ	NP_001138503.1, NM_001145031.2 [P00749-2] NP_001306120.1, NM_001319191.1 NP_002649.1, NM_002658.4 [P00749-1]
UniGeneⁱ	Hs.77274

Genome annotation databases

Ensemblⁱ	ENST00000372764; ENSP00000361850; ENSG00000122861 ENST00000496777; ENSP00000431795; ENSG00000122861
GeneIDⁱ	5328
KEGGⁱ	hsa:5328
UCSC genome browser More...UCSCⁱ	uc001jwa.4 human [P00749-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P00749	Plasminogen activator, urokinase, isoform CRA_a		HUMAN		431	UniRef100_P00749
Urokinase plasminogen activator (Fragment)		HUMAN		411
PLAU protein (Fragment)		HUMAN		17
Urokinase-type plasminogen activator (Fragment)		HUMAN		106
UPI00024CE88C		HUMAN		345
+5

Protein	Similar proteins		Species	Score	Length	Source
P00749	Urokinase-type plasminogen activator		PONAB		431	UniRef90_P00749
Plasminogen activator, urokinase, isoform CRA_a		HUMAN		431
Plasminogen activator, urokinase		GORGO		431
Plasminogen activator, urokinase		PANTR		431
Uncharacterized protein		PANPA		431
+31
P00749-2	Urokinase-type plasminogen activator		HUMAN		414	UniRef90_P00749-2
PLAU isoform 2		PANTR		414
Uncharacterized protein		PANPA		414
Uncharacterized protein		NOMLE		414
Plasminogen activator, urokinase		GORGO		414
+2

Protein	Similar proteins		Species	Score	Length	Source
P00749	Urokinase-type plasminogen activator		PONAB		431	UniRef50_P00749
Urokinase-type plasminogen activator		PAPCY		433
Plasminogen activator, urokinase, isoform CRA_a		HUMAN		431
Plasminogen activator, urokinase		PANTR		431
Uncharacterized protein		PANPA		431
+92

Cross-referencesⁱ

Web resourcesⁱ

Wikipedia

Urokinase entry

SeattleSNPs

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M15476 mRNA Translation: AAA61253.1 X02760 mRNA Translation: CAA26535.1 D00244 mRNA Translation: BAA00175.1 K03226 mRNA Translation: AAC97138.1 X02419 Genomic DNA Translation: CAA26268.1 AF377330 Genomic DNA Translation: AAK53822.1 BT007391 mRNA Translation: AAP36055.1 AK298560 mRNA Translation: BAG60754.1 AL596247 Genomic DNA No translation available. CH471083 Genomic DNA Translation: EAW54544.1 BC013575 mRNA Translation: AAH13575.1 D11143 mRNA Translation: BAA01919.1 K02286 Genomic DNA Translation: AAA61252.1
CCDSⁱ	CCDS44442.1 [P00749-2] CCDS7339.1 [P00749-1]
PIRⁱ	A00931 UKHU
RefSeqⁱ	NP_001138503.1, NM_001145031.2 [P00749-2] NP_001306120.1, NM_001319191.1 NP_002649.1, NM_002658.4 [P00749-1]
UniGeneⁱ	Hs.77274

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1C5W	X-ray	1.94	A	156-178	[»]
				B	179-431	[»]
	1C5X	X-ray	1.75	A	156-178	[»]
				B	179-431	[»]
	1C5Y	X-ray	1.65	A	156-178	[»]
				B	179-431	[»]
	1C5Z	X-ray	1.85	A	156-178	[»]
				B	179-431	[»]
	1EJN	X-ray	1.80	A	179-431	[»]
	1F5K	X-ray	1.80	U	179-431	[»]
	1F5L	X-ray	2.10	A	179-431	[»]
	1F92	X-ray	2.60	A	179-431	[»]
	1FV9	X-ray	3.00	A	179-423	[»]
	1GI7	X-ray	1.79	A	156-178	[»]
				B	179-423	[»]
	1GI8	X-ray	1.75	A	156-178	[»]
				B	179-423	[»]
	1GI9	X-ray	1.80	A	156-178	[»]
				B	179-423	[»]
	1GJ7	X-ray	1.50	A	156-178	[»]
				B	179-431	[»]
	1GJ8	X-ray	1.64	A	156-178	[»]
				B	179-431	[»]
	1GJ9	X-ray	1.80	A	156-178	[»]
				B	179-431	[»]
	1GJA	X-ray	1.56	A	156-178	[»]
				B	179-431	[»]
	1GJB	X-ray	1.90	A	156-178	[»]
				B	179-431	[»]
	1GJC	X-ray	1.73	A	156-178	[»]
				B	179-431	[»]
	1GJD	X-ray	1.75	A	156-178	[»]
				B	179-431	[»]
	1KDU	NMR	-	A	69-153	[»]
	1LMW	X-ray	2.50	A/C	156-178	[»]
				B/D	179-431	[»]
	1O3P	X-ray	1.81	A	156-178	[»]
				B	179-431	[»]
	1O5A	X-ray	1.68	A	156-178	[»]
				B	179-431	[»]
	1O5B	X-ray	1.85	A	156-178	[»]
				B	179-431	[»]
	1O5C	X-ray	1.63	A	156-178	[»]
				B	179-431	[»]
	1OWD	X-ray	2.32	A	179-423	[»]
	1OWE	X-ray	1.60	A	179-423	[»]
	1OWH	X-ray	1.61	A	179-423	[»]
	1OWI	X-ray	2.93	A	179-423	[»]
	1OWJ	X-ray	3.10	A	179-423	[»]
	1OWK	X-ray	2.80	A	179-423	[»]
	1SC8	X-ray	2.40	U	164-425	[»]
	1SQA	X-ray	2.00	A	179-423	[»]
	1SQO	X-ray	1.84	A	179-423	[»]
	1SQT	X-ray	1.90	A	179-423	[»]
	1U6Q	X-ray	2.02	A	179-423	[»]
	1URK	NMR	-	A	26-155	[»]
	1VJ9	X-ray	2.40	U	164-425	[»]
	1VJA	X-ray	2.00	U	164-425	[»]
	1W0Z	X-ray	1.90	U	179-425	[»]
	1W10	X-ray	2.00	U	179-425	[»]
	1W11	X-ray	2.00	U	179-425	[»]
	1W12	X-ray	2.40	U	179-425	[»]
	1W13	X-ray	2.00	U	179-425	[»]
1W14	X-ray	2.20	U	179-425	[»]
2FD6	X-ray	1.90	A	31-152	[»]
2I9A	X-ray	1.90	A/B/C/D	21-163	[»]
2I9B	X-ray	2.80	A/B/C/D	21-163	[»]
2NWN	X-ray	2.15	A	179-431	[»]
2O8T	X-ray	1.45	A	179-431	[»]
2O8U	X-ray	1.70	A	179-431	[»]
2O8W	X-ray	1.86	A	179-431	[»]
2R2W	X-ray	2.01	U	179-431	[»]
2VIN	X-ray	1.90	A	179-431	[»]
2VIO	X-ray	1.80	A	179-431	[»]
2VIP	X-ray	1.72	A	179-431	[»]
2VIQ	X-ray	2.00	A	179-431	[»]
2VIV	X-ray	1.72	A	179-431	[»]
2VIW	X-ray	2.05	A	179-431	[»]
2VNT	X-ray	2.20	A/B/C/D/E/F	156-431	[»]
3BT1	X-ray	2.80	A	21-153	[»]
3BT2	X-ray	2.50	A	21-153	[»]
3IG6	X-ray	1.83	A/C	156-178	[»]
			B/D	179-431	[»]
3KGP	X-ray	2.35	A	179-431	[»]
3KHV	X-ray	2.35	A	179-431	[»]
3KID	X-ray	2.71	U	179-431	[»]
3M61	X-ray	1.68	U	179-431	[»]
3MHW	X-ray	1.45	U	179-425	[»]
3MWI	X-ray	2.03	U	179-424	[»]
3OX7	X-ray	1.58	U	179-431	[»]
3OY5	X-ray	2.31	U	179-431	[»]
3OY6	X-ray	2.31	U	179-431	[»]
3PB1	X-ray	2.30	E	179-431	[»]
3QN7	X-ray	1.90	A	179-431	[»]
3U73	X-ray	3.19	A	21-152	[»]
4DVA	X-ray	1.94	U	179-424	[»]
4DW2	X-ray	2.97	U	179-424	[»]
4FU7	X-ray	2.00	A	179-424	[»]
4FU8	X-ray	2.20	A	179-424	[»]
4FU9	X-ray	1.60	A	179-424	[»]
4FUB	X-ray	1.90	A	179-424	[»]
4FUC	X-ray	1.72	A	179-424	[»]
4FUD	X-ray	2.00	A	179-424	[»]
4FUE	X-ray	2.00	A	179-424	[»]
4FUF	X-ray	2.00	A	179-424	[»]
4FUG	X-ray	1.80	A	179-424	[»]
4FUH	X-ray	1.60	A	179-424	[»]
4FUI	X-ray	2.00	A	179-424	[»]
4FUJ	X-ray	2.05	A	179-424	[»]
4GLY	X-ray	1.52	A	179-423	[»]
4H42	X-ray	2.01	U	179-426	[»]
4JK5	X-ray	1.55	A	179-423	[»]
4JK6	X-ray	2.20	A	179-423	[»]
4JNI	X-ray	1.17	U	179-425	[»]
4JNL	X-ray	2.00	U	179-425	[»]
4K24	X-ray	4.50	A	21-153	[»]
4MNV	X-ray	1.80	A	179-423	[»]
4MNW	X-ray	1.49	A	179-423	[»]
4MNX	X-ray	1.85	A	179-423	[»]
4MNY	X-ray	1.70	A/B	179-423	[»]
4OS1	X-ray	2.20	A	179-423	[»]
4OS2	X-ray	1.79	A	179-423	[»]
4OS4	X-ray	2.00	A	179-423	[»]
4OS5	X-ray	2.26	A	179-423	[»]
4OS6	X-ray	1.75	A	179-423	[»]
4OS7	X-ray	2.00	A	179-423	[»]
4X0W	X-ray	2.10	U	179-425	[»]
4X1N	X-ray	1.80	U	179-425	[»]
4X1P	X-ray	1.60	U	179-425	[»]
4X1Q	X-ray	2.28	U	179-425	[»]
4X1R	X-ray	2.10	U	179-425	[»]
4X1S	X-ray	1.90	U	179-425	[»]
4XSK	X-ray	1.50	U	179-424	[»]
4ZHL	X-ray	2.06	U	179-425	[»]
4ZHM	X-ray	1.90	U	179-425	[»]
4ZKN	X-ray	1.36	U	179-425	[»]
4ZKO	X-ray	1.29	U	179-425	[»]
4ZKR	X-ray	1.36	U	179-425	[»]
4ZKS	X-ray	1.85	U	179-425	[»]
5HGG	X-ray	1.97	A/B	179-424	[»]
5WXF	X-ray	1.46	U	179-431	[»]
5WXO	X-ray	1.64	U	179-431	[»]
5WXP	X-ray	1.75	U	179-431	[»]
5WXQ	X-ray	1.79	U	179-431	[»]
5WXR	X-ray	1.75	U	179-431	[»]
5WXS	X-ray	2.30	U	179-431	[»]
5WXT	X-ray	2.10	U	179-431	[»]
5XG4	X-ray	3.00	U	179-424	[»]
ProteinModelPortalⁱ	P00749
SMRⁱ	P00749
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	111344, 21 interactors
ComplexPortalⁱ	CPX-483 uPA-PAI-1 complex CPX-487 uPA-uPAR complex CPX-501 uPA-uPAR-vitronectin complex
DIPⁱ	DIP-46387N
ELMⁱ	P00749
IntActⁱ	P00749, 9 interactors
MINTⁱ	P00749
STRINGⁱ	9606.ENSP00000361850

Chemistry databases

BindingDBⁱ	P00749
ChEMBLⁱ	CHEMBL3286
DrugBankⁱ	DB07122 1-[4-(2-oxo-2-phenylethyl)phenyl]guanidine DB01905 2-(2-Hydroxy-5-Methoxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine DB06854 2-(2-HYDROXY-BIPHENYL)-1H-BENZOIMIDAZOLE-5-CARBOXAMIDINE DB02193 2-(2-Hydroxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine DB03729 2-Amino-5-Hydroxy-Benzimidazole DB03136 4-Iodobenzo[B]Thiophene-2-Carboxamidine DB01977 6-(N-Phenylcarbamyl)-2-Naphthalenecarboxamidine DB07076 6-[(Z)-AMINO(IMINO)METHYL]-N-[3-(CYCLOPENTYLOXY)PHENYL]-2-NAPHTHAMIDE DB03082 6-[(Z)-Amino(Imino)Methyl]-N-[4-(Aminomethyl)Phenyl]-4-(Pyrimidin-2-Ylamino)-2-Naphthamide DB02398 6-[N-(4-(Aminomethyl)Phenyl)Carbamyl]-2-Naphthalenecarboxamidine DB03865 6-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-Carboxamidine DB06855 6-FLUORO-2-(2-HYDROXY-3-ISOBUTOXY-PHENYL)-1H-BENZOIMIDAZOLE-5-CARBOXAMIDINE DB06856 6-FLUORO-2-[2-HYDROXY-3-(2-METHYL-CYCLOHEXYLOXY)-PHENYL]-1H-INDOLE-5-CARBOXAMIDINE DB03046 7-Methoxy-8-[1-(Methylsulfonyl)-1h-Pyrazol-4-Yl]Naphthalene-2-Carboximidamide DB04059 8-(Pyrimidin-2-Ylamino)Naphthalene-2-Carboximidamide DB00594 Amiloride DB03127 Benzamidine DB02526 CRA_10655 DB03159 CRA_8696 DB03782 N-(1-Adamantyl)-N'-(4-Guanidinobenzyl)Urea DB06857 N-(4-CARBAMIMIDOYL-3-CHORO-PHENYL)-2-HYDROXY-3-IODO-5-METHYL-BENZAMIDE DB05254 Plasmin DB03476 Trans-6-(2-Phenylcyclopropyl)-Naphthalene-2-Carboxamidine DB00013 Urokinase
GuidetoPHARMACOLOGYⁱ	2393

Protein family/group databases

MEROPSⁱ	S01.231

MEROPSⁱ

S01.231

PTM databases

GlyConnectⁱ	519 612
iPTMnetⁱ	P00749
PhosphoSitePlusⁱ	P00749
UniCarbKBⁱ	P00749

Polymorphism and mutation databases

BioMutaⁱ	PLAU
DMDMⁱ	254763341

Proteomic databases

EPDⁱ	P00749
MaxQBⁱ	P00749
PaxDbⁱ	P00749
PeptideAtlasⁱ	P00749
PRIDEⁱ	P00749
ProteomicsDBⁱ	51279 51280 [P00749-2]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	5328
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000372764; ENSP00000361850; ENSG00000122861 ENST00000496777; ENSP00000431795; ENSG00000122861
GeneIDⁱ	5328
KEGGⁱ	hsa:5328
UCSCⁱ	uc001jwa.4 human [P00749-1]

Organism-specific databases

CTDⁱ	5328
DisGeNETⁱ	5328
EuPathDBⁱ	HostDB:ENSG00000122861.15
GeneCardsⁱ	PLAU
HGNCⁱ	HGNC:9052 PLAU
HPAⁱ	HPA008719
MalaCardsⁱ	PLAU
MIMⁱ	191840 gene 601709 phenotype
neXtProtⁱ	NX_P00749
Orphanetⁱ	220436 Quebec platelet disorder
PharmGKBⁱ	PA33382
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG410IGFI Eukaryota COG5640 LUCA
HOVERGENⁱ	HBG008633
InParanoidⁱ	P00749
KOⁱ	K01348
OrthoDBⁱ	EOG091G0AH5
PhylomeDBⁱ	P00749
TreeFamⁱ	TF329901

Enzyme and pathway databases

BRENDAⁱ	3.4.21.73 2681
Reactomeⁱ	R-HSA-6798695 Neutrophil degranulation R-HSA-75205 Dissolution of Fibrin Clot
SABIO-RKⁱ	P00749
SIGNORⁱ	P00749

Miscellaneous databases

EvolutionaryTraceⁱ	P00749
GeneWikiⁱ	PLAU
GenomeRNAiⁱ	5328
PMAP-CutDBⁱ	P00749
Protein Ontology More...PROⁱ	PR:P00749
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000122861 Expressed in 181 organ(s), highest expression level in epithelium of bronchus
CleanExⁱ	HS_PLAU
ExpressionAtlasⁱ	P00749 baseline and differential
Genevisibleⁱ	P00749 HS

Family and domain databases

CDDⁱ	cd00108 KR, 1 hit cd00190 Tryp_SPc, 1 hit
Gene3Dⁱ	2.40.20.10, 1 hit
InterProⁱ	View protein in InterPro IPR013032 EGF-like_CS IPR000742 EGF-like_dom IPR000001 Kringle IPR013806 Kringle-like IPR018056 Kringle_CS IPR038178 Kringle_sf IPR009003 Peptidase_S1_PA IPR001314 Peptidase_S1A IPR001254 Trypsin_dom IPR018114 TRYPSIN_HIS IPR033116 TRYPSIN_SER IPR034814 Urokinase
PANTHERⁱ	PTHR24264:SF38 PTHR24264:SF38, 1 hit
Pfamⁱ	View protein in Pfam PF00051 Kringle, 1 hit PF00089 Trypsin, 1 hit
PRINTSⁱ	PR00722 CHYMOTRYPSIN
SMARTⁱ	View protein in SMART SM00130 KR, 1 hit SM00020 Tryp_SPc, 1 hit
SUPFAMⁱ	SSF50494 SSF50494, 1 hit SSF57440 SSF57440, 1 hit
PROSITEⁱ	View protein in PROSITE PS00022 EGF_1, 1 hit PS50026 EGF_3, 1 hit PS00021 KRINGLE_1, 1 hit PS50070 KRINGLE_2, 1 hit PS50240 TRYPSIN_DOM, 1 hit PS00134 TRYPSIN_HIS, 1 hit PS00135 TRYPSIN_SER, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	UROK_HUMAN
Accessionⁱ	P00749Primary (citable) accession number: P00749 Secondary accession number(s): B4DPZ2 , Q15844, Q16618, Q53XS3, Q5SWW9, Q969W6
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	July 28, 2009
	Last modified:	November 7, 2018
	This is version 235 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

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

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Peptidase families
Classification of peptidase families and list of entries
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 10
Human chromosome 10: entries, gene names and cross-references to MIM

UniProtKB

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UniProtKB - P00749 (UROK_HUMAN)

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Urokinase-type plasminogen activator

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<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

Sites

<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

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<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

Organism-specific databases

<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

Extracellular region or secreted

Plasma Membrane

Other locations

Keywords - Cellular componenti

<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

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<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

Amino acid modifications

Sites

Keywords - PTMi

Proteomic databases

PTM databases

Miscellaneous databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<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

Protein-protein interaction databases

Chemistry databases

<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

Secondary structure

3D structure databases

Miscellaneous databases

<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

Region

<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

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ