P03952 (KLKB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Plasma kallikrein
EC=3.4.21.34

Alternative name(s):
Fletcher factor
Kininogenin
Plasma prekallikrein

Cleaved into the following 2 chains:

1. Plasma kallikrein heavy chain
2. Plasma kallikrein light chain

Gene names

Name:	KLKB1
Synonyms:	KLK3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	638 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin.
Catalytic activity	Cleaves selectively Arg-|-Xaa and Lys-|-Xaa bonds, including Lys-|-Arg and Arg-|-Ser bonds in (human) kininogen to release bradykinin.
Enzyme regulation	Inhibited by SERPINA5. Ref.9
Subunit structure	Forms a heterodimer with SERPINA5. The zymogen is activated by factor XIIa, which cleaves the molecule into a light chain, which contains the active site, and a heavy chain, which associates with HMW kininogen. These chains are linked by one or more disulfide bonds.
Subcellular location	Secreted.
Involvement in disease	Prekallikrein deficiency (PKK deficiency) [MIM:612423]: This disorder is a blood coagulation defect. Note: The disease is caused by mutations affecting the gene represented in this entry.
Sequence similarities	Belongs to the peptidase S1 family. Plasma kallikrein subfamily. Contains 4 apple domains. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Biological process	Blood coagulation Fibrinolysis Hemostasis Inflammatory response
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Repeat Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Factor XII activation Traceable author statement PubMed 2510163. Source: BHF-UCL blood coagulation, intrinsic pathway Traceable author statement. Source: Reactome extracellular matrix disassembly Traceable author statement. Source: Reactome fibrinolysis Inferred from electronic annotation. Source: UniProtKB-KW plasminogen activation Inferred from direct assay PubMed 89876. Source: BHF-UCL positive regulation of fibrinolysis Inferred from direct assay PubMed 89876. Source: BHF-UCL proteolysis Traceable author statement PubMed 1993180. Source: ProtInc
Cellular_component	extracellular space Inferred from direct assay PubMed 89876. Source: BHF-UCL plasma membrane Traceable author statement. Source: Reactome
Molecular_function	serine-type endopeptidase activity Traceable author statement PubMed 1993180. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Chain

20 – 390

371

Plasma kallikrein heavy chain

PRO_0000028021

Chain

391 – 638

248

Plasma kallikrein light chain

PRO_0000028022

Regions

Domain

21 – 104

84

Apple 1

Domain

111 – 194

84

Apple 2

Domain

201 – 284

84

Apple 3

Domain

292 – 375

84

Apple 4

Domain

391 – 626

236

Peptidase S1

Sites

Active site

434

1

Charge relay system

Active site

483

1

Charge relay system

Active site

578

1

Charge relay system

Amino acid modifications

Glycosylation

127

1

N-linked (GlcNAc...) Ref.1 Ref.11

Glycosylation

308

1

N-linked (GlcNAc...) Ref.1 Ref.11 Ref.12

Glycosylation

396

1

N-linked (GlcNAc...) Ref.1 Ref.11 Ref.12

Glycosylation

453

1

N-linked (GlcNAc...) Ref.1 Ref.10 Ref.11 Ref.12

Glycosylation

494

1

N-linked (GlcNAc...) Ref.1 Ref.11 Ref.12

Disulfide bond

21 ↔ 104

Ref.8

Disulfide bond

47 ↔ 77

Ref.8

Disulfide bond

51 ↔ 57

Ref.8

Disulfide bond

111 ↔ 194

Ref.8

Disulfide bond

137 ↔ 166

Ref.8

Disulfide bond

141 ↔ 147

Ref.8

Disulfide bond

201 ↔ 284

Ref.8

Disulfide bond

227 ↔ 256

Ref.8

Disulfide bond

231 ↔ 237

Ref.8

Disulfide bond

292 ↔ 375

Ref.8

Disulfide bond

318 ↔ 347

Ref.8

Disulfide bond

322 ↔ 328

Ref.8

Disulfide bond

340 ↔ 345

Ref.8

Disulfide bond

383 ↔ 503

Ref.8

Disulfide bond

419 ↔ 435

Ref.8

Disulfide bond

517 ↔ 584

Ref.8

Disulfide bond

548 ↔ 563

Ref.8

Disulfide bond

574 ↔ 602

Ref.8

Natural variations

Natural variant

123

1

G → R in PKK deficiency; reduces the binding activity of Apple domain 2 to HMW kininogen. Ref.14

VAR_054907

Natural variant

143

1

N → S in PKK deficiency; reduces the binding activity of Apple domain 2 to HMW kininogen. Ref.2 Ref.4 Ref.14
Corresponds to variant rs3733402 [ dbSNP | Ensembl ].

VAR_013598

Natural variant

178

1

A → T. Ref.4
Corresponds to variant rs4253257 [ dbSNP | Ensembl ].

VAR_016280

Natural variant

202

1

H → Q. Ref.2 Ref.4
Corresponds to variant rs4253373 [ dbSNP | Ensembl ].

VAR_013599

Natural variant

208

1

H → P. Ref.2

VAR_013600

Natural variant

210

1

A → E.
Corresponds to variant rs2278542 [ dbSNP | Ensembl ].

VAR_020180

Natural variant

269

1

S → C. Ref.4
Corresponds to variant rs4253376 [ dbSNP | Ensembl ].

VAR_016281

Natural variant

311

1

F → V. Ref.4
Corresponds to variant rs4253377 [ dbSNP | Ensembl ].

VAR_016282

Natural variant

358

1

T → A. Ref.4
Corresponds to variant rs4253379 [ dbSNP | Ensembl ].

VAR_016283

Natural variant

381

1

S → A. Ref.4
Corresponds to variant rs4253301 [ dbSNP | Ensembl ].

VAR_016284

Natural variant

442

1

Q → P. Ref.4
Corresponds to variant rs4253316 [ dbSNP | Ensembl ].

VAR_016285

Natural variant

548

1

C → Y in PKK deficiency. Ref.13

VAR_054908

Natural variant

560

1

R → Q. Ref.4 Ref.7
Corresponds to variant rs4253325 [ dbSNP | Ensembl ].

VAR_016286

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

638

Helix Strand Turn

Details...

Beta strand

405 – 425

21

Beta strand

428 – 431

4

Helix

433 – 436

4

Helix

442 – 444

3

Beta strand

445 – 448

4

Helix

454 – 456

3

Beta strand

466 – 471

6

Beta strand

479 – 482

4

Beta strand

485 – 491

7

Helix

507 – 511

5

Beta strand

515 – 523

9

Beta strand

525 – 528

4

Beta strand

536 – 543

8

Helix

545 – 549

5

Beta strand

561 – 564

4

Beta strand

581 – 586

6

Beta strand

589 – 598

10

Beta strand

600 – 603

4

Beta strand

609 – 613

5

Helix

614 – 617

4

Helix

618 – 625

8

Sequences

	Sequence		Length	Mass (Da)
	P03952 [UniParc]. Last modified October 23, 1986. Version 1. Checksum: E62F9C1053838FB4	FASTA	638	71,370
	10 20 30 40 50 60 MILFKQATYF ISLFATVSCG CLTQLYENAF FRGGDVASMY TPNAQYCQMR CTFHPRCLLF 70 80 90 100 110 120 SFLPASSIND MEKRFGCFLK DSVTGTLPKV HRTGAVSGHS LKQCGHQISA CHRDIYKGVD 130 140 150 160 170 180 MRGVNFNVSK VSSVEECQKR CTNNIRCQFF SYATQTFHKA EYRNNCLLKY SPGGTPTAIK 190 200 210 220 230 240 VLSNVESGFS LKPCALSEIG CHMNIFQHLA FSDVDVARVL TPDAFVCRTI CTYHPNCLFF 250 260 270 280 290 300 TFYTNVWKIE SQRNVCLLKT SESGTPSSST PQENTISGYS LLTCKRTLPE PCHSKIYPGV 310 320 330 340 350 360 DFGGEELNVT FVKGVNVCQE TCTKMIRCQF FTYSLLPEDC KEEKCKCFLR LSMDGSPTRI 370 380 390 400 410 420 AYGTQGSSGY SLRLCNTGDN SVCTTKTSTR IVGGTNSSWG EWPWQVSLQV KLTAQRHLCG 430 440 450 460 470 480 GSLIGHQWVL TAAHCFDGLP LQDVWRIYSG ILNLSDITKD TPFSQIKEII IHQNYKVSEG 490 500 510 520 530 540 NHDIALIKLQ APLNYTEFQK PICLPSKGDT STIYTNCWVT GWGFSKEKGE IQNILQKVNI 550 560 570 580 590 600 PLVTNEECQK RYQDYKITQR MVCAGYKEGG KDACKGDSGG PLVCKHNGMW RLVGITSWGE 610 620 630 GCARREQPGV YTKVAEYMDW ILEKTQSSDG KAQMQSPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats." Chung D.W., Fujikawa K., McMullen B.A., Davie E.W. Biochemistry 25:2410-2417(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genomic structure of the human plasma prekallikrein gene, identification of allelic variants, and analysis in end-stage renal disease." Yu H., Anderson P.J., Freedman B.I., Rich S.S., Bowden D.W. Genomics 69:225-234(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-143; GLN-202 AND PRO-208.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[4]	SeattleSNPs variation discovery resource Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-143; THR-178; GLN-202; CYS-269; VAL-311; ALA-358; ALA-381; PRO-442 AND GLN-560.
[5]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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 GLN-560. Tissue: Colon.
[8]	"Location of the disulfide bonds in human plasma prekallikrein: the presence of four novel apple domains in the amino-terminal portion of the molecule." McMullen B.A., Fujikawa K., Davie E.W. Biochemistry 30:2050-2056(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS.
[9]	"Inactivation of human plasma kallikrein and factor XIa by protein C inhibitor." Meijers J.C., Kanters D.H., Vlooswijk R.A., van Erp H.E., Hessing M., Bouma B.N. Biochemistry 27:4231-4237(1988) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, HETERODIMER WITH SERPINA5.
[10]	"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." Zhang H., Li X.-J., Martin D.B., Aebersold R. Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-453.
[11]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-127; ASN-308; ASN-396; ASN-453 AND ASN-494, MASS SPECTROMETRY. Tissue: Plasma.
[12]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-308; ASN-396; ASN-453 AND ASN-494, MASS SPECTROMETRY. Tissue: Liver.
[13]	"Severe prekallikrein (Fletcher factor) deficiency due to a compound heterozygosis (383Trp stop codon and Cys529Tyr)." Lombardi A.M., Sartori M.T., Cabrio L., Fadin M., Zanon E., Girolami A. Thromb. Haemost. 90:1040-1045(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PKK DEFICIENCY TYR-548.
[14]	"A new type of plasma prekallikrein deficiency associated with homozygosity for Gly104Arg and Asn124Ser in apple domain 2 of the heavy-chain region." Katsuda I., Maruyama F., Ezaki K., Sawamura T., Ichihara Y. Eur. J. Haematol. 79:59-68(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PKK DEFICIENCY ARG-123 AND SER-143.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M13143 mRNA. Translation: AAA60153.1.
AF232742 , AF232734, AF232735, AF232736, AF232737, AF232738, AF232739, AF232740, AF232741 Genomic DNA. Translation: AAF79940.1.
AK313378 mRNA. Translation: BAG36176.1.
AY190920 Genomic DNA. Translation: AAN84794.1.
AC110771 Genomic DNA. Translation: AAY40900.1.
CH471056 Genomic DNA. Translation: EAX04623.1.
BC117349 mRNA. Translation: AAI17350.1.
BC117351 mRNA. Translation: AAI17352.1.

IPI

IPI00654888.

PIR

KQHUP. A00921.

RefSeq

NP_000883.2. NM_000892.3.

UniGene

Hs.237642.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ANW	X-ray	1.85	A	391-631	[»]
2ANY	X-ray	1.40	A	391-631	[»]

ProteinModelPortal

P03952.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000264690.

Protein family/group databases

MEROPS

S01.212.

PTM databases

PhosphoSite

P03952.

Polymorphism databases

DMDM

125184.

Proteomic databases

PaxDb

P03952.

PRIDE

P03952.

Protocols and materials databases

DNASU

3818.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264690; ENSP00000264690; ENSG00000164344.

GeneID

3818.

KEGG

hsa:3818.

UCSC

uc003iyy.3. human.

Organism-specific databases

CTD

3818.

GeneCards

GC04P187130.

HGNC

HGNC:6371. KLKB1.

HPA

HPA005634.

MIM

229000. gene.
612423. phenotype.

neXtProt

NX_P03952.

Orphanet

749. Congenital prekallikrein deficiency.

PharmGKB

PA30160.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5640.

HOGENOM

HOG000112467.

HOVERGEN

HBG000399.

InParanoid

P03952.

KO

K01324.

Enzyme and pathway databases

BRENDA

3.4.21.34. 2681.

Reactome

REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P03952.

Bgee

P03952.

CleanEx

HS_KLK3.
HS_KLKB1.

Genevestigator

P03952.

GermOnline

ENSG00000164344. Homo sapiens.

Family and domain databases

InterPro

IPR000177. Apple.
IPR003014. PAN-1_domain.
IPR003609. Pan_app.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]

Pfam

PF00024. PAN_1. 4 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]

PRINTS

PR00005. APPLEDOMAIN.
PR00722. CHYMOTRYPSIN.

SMART

SM00223. APPLE. 4 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.

PROSITE

PS00495. APPLE. 4 hits.
PS50948. PAN. 4 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P03952.

ChEMBL

CHEMBL2000.

EvolutionaryTrace

P03952.

GenomeRNAi

3818.

NextBio

15011.

PMAP-CutDB

Q4W5C3.

SOURCE

Search...

Entry information

Entry name

KLKB1_HUMAN

Accession

Primary (citable) accession number: P03952
Secondary accession number(s): A6NH96 , B2R8H9, Q17RE8, Q17RE9, Q4W5C3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 1986
Last sequence update:	October 23, 1986
Last modified:	May 1, 2013
This is version 155 of the entry and version 1 of the sequence. [Complete history]

Entry status

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.