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P49862

- KLK7_HUMAN

UniProt

P49862 - KLK7_HUMAN

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Protein

Kallikrein-7

Gene
KLK7, PRSS6, SCCE
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. Cleaves insulin A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6-Leu-|-Cys-7', '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' and '26-Tyr-|-Thr-27'. Could play a role in the activation of precursors to inflammatory cytokines.1 Publication

Catalytic activityi

Cleavage of proteins with aromatic side chains in the P1 position.

Enzyme regulationi

Inhibited by Zn2+ and Cu2+ at low micromolar concentrations. Inhibited by SERPINA12.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei70 – 701Charge relay system1 Publication
Sitei109 – 1091Major binding site for inhibitory zinc or copper
Active sitei112 – 1121Charge relay system1 Publication
Active sitei205 – 2051Charge relay system1 Publication

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
  2. serine-type peptidase activity Source: ProtInc

GO - Biological processi

  1. epidermis development Source: ProtInc
  2. extracellular matrix disassembly Source: Reactome
  3. extracellular matrix organization Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.117. 1154.
ReactomeiREACT_118572. Degradation of the extracellular matrix.

Protein family/group databases

MEROPSiS01.300.

Names & Taxonomyi

Protein namesi
Recommended name:
Kallikrein-7 (EC:3.4.21.117)
Short name:
hK7
Alternative name(s):
Serine protease 6
Stratum corneum chymotryptic enzyme
Short name:
hSCCE
Gene namesi
Name:KLK7
Synonyms:PRSS6, SCCE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:6368. KLK7.

Subcellular locationi

Secreted
Note: In ovarian carcinoma, secreted and also observed at the apical membrane and in cytoplasm at the invasive front.1 Publication

GO - Cellular componenti

  1. epidermal lamellar body Source: UniProtKB
  2. extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi54 – 541H → F: No effect on zinc inhibition. 1 Publication
Mutagenesisi109 – 1091H → A: No zinc inhibition. 1 Publication

Organism-specific databases

PharmGKBiPA30157.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Propeptidei23 – 297Activation peptidePRO_0000027942
Chaini30 – 253224Kallikrein-7PRO_0000027943Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi36 ↔ 1652 Publications
Disulfide bondi55 ↔ 712 Publications
Disulfide bondi137 ↔ 2392 Publications
Disulfide bondi144 ↔ 2112 Publications
Disulfide bondi176 ↔ 1902 Publications
Disulfide bondi201 ↔ 2262 Publications
Glycosylationi246 – 2461N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP49862.
PRIDEiP49862.

PTM databases

PhosphoSiteiP49862.

Miscellaneous databases

PMAP-CutDBP49862.

Expressioni

Tissue specificityi

Abundantly expressed in the skin and is expressed by keratinocytes in the epidermis. Also expressed in the brain, mammary gland, cerebellum, spinal cord and kidney. Lower levels in salivary glands, uterus, thymus, thyroid, placenta, trachea and testis. Up-regulated in ovarian carcinoma, especially late-stage serous carcinoma, compared with normal ovaries and benign adenomas (at protein level).2 Publications

Inductioni

By estrogens and glucocorticoids in a breast carcinoma cell line.2 Publications

Gene expression databases

ArrayExpressiP49862.
BgeeiP49862.
CleanExiHS_KLK7.
GenevestigatoriP49862.

Organism-specific databases

HPAiCAB026342.
HPA018994.

Interactioni

Protein-protein interaction databases

BioGridi111631. 3 interactions.
STRINGi9606.ENSP00000304791.

Structurei

Secondary structure

1
253
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 496
Beta strandi52 – 6110
Beta strandi64 – 674
Helixi69 – 713
Beta strandi76 – 816
Beta strandi90 – 956
Beta strandi97 – 1004
Turni106 – 1083
Beta strandi114 – 1174
Beta strandi143 – 1508
Beta strandi152 – 1565
Beta strandi164 – 1718
Helixi173 – 1808
Helixi181 – 1833
Beta strandi188 – 1925
Beta strandi208 – 2114
Beta strandi214 – 2218
Beta strandi224 – 2263
Beta strandi233 – 2375
Helixi238 – 2403
Helixi242 – 25110

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QXGX-ray2.60A/B30-253[»]
2QXHX-ray2.00A30-253[»]
2QXIX-ray1.00A30-253[»]
2QXJX-ray2.10A30-253[»]
3BSQX-ray2.80A/B/C30-250[»]
ProteinModelPortaliP49862.
SMRiP49862. Positions 30-253.

Miscellaneous databases

EvolutionaryTraceiP49862.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 250221Peptidase S1Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP49862.
KOiK08668.
OMAiVLVNERW.
PhylomeDBiP49862.
TreeFamiTF331065.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

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

Isoform 1 (identifier: P49862-1) [UniParc]FASTAAdd to Basket

Also known as: Long

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

MARSLLLPLQ ILLLSLALET AGEEAQGDKI IDGAPCARGS HPWQVALLSG    50
NQLHCGGVLV NERWVLTAAH CKMNEYTVHL GSDTLGDRRA QRIKASKSFR 100
HPGYSTQTHV NDLMLVKLNS QARLSSMVKK VRLPSRCEPP GTTCTVSGWG 150
TTTSPDVTFP SDLMCVDVKL ISPQDCTKVY KDLLENSMLC AGIPDSKKNA 200
CNGDSGGPLV CRGTLQGLVS WGTFPCGQPN DPGVYTQVCK FTKWINDTMK 250
KHR 253
Length:253
Mass (Da):27,525
Last modified:October 1, 1996 - v1
Checksum:i2D68B6B15A76A668
GO
Isoform 2 (identifier: P49862-2) [UniParc]FASTAAdd to Basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.

Show »
Length:181
Mass (Da):19,887
Checksum:i86A28A03B80C2D78
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7272Missing in isoform 2. VSP_013581Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti226 – 2261C → W in AAH32005. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L33404 mRNA. Translation: AAC37551.1.
AF166330 Genomic DNA. Translation: AAD49718.1.
AF243527 Genomic DNA. Translation: AAG33360.1.
AF332583 Genomic DNA. Translation: AAK69624.1.
AF411214 mRNA. Translation: AAN03662.1.
AF411215 mRNA. Translation: AAN03663.1.
AY601109 mRNA. Translation: AAU04540.1.
AK289660 mRNA. Translation: BAF82349.1.
CH471135 Genomic DNA. Translation: EAW71959.1.
BC032005 mRNA. Translation: AAH32005.1.
CCDSiCCDS12812.1. [P49862-1]
CCDS59414.1. [P49862-2]
PIRiA53968.
RefSeqiNP_001193982.1. NM_001207053.1. [P49862-2]
NP_001230055.1. NM_001243126.1.
NP_005037.1. NM_005046.3. [P49862-1]
NP_644806.1. NM_139277.2. [P49862-1]
UniGeneiHs.151254.

Genome annotation databases

EnsembliENST00000391807; ENSP00000375683; ENSG00000169035. [P49862-1]
ENST00000595820; ENSP00000470538; ENSG00000169035. [P49862-1]
ENST00000597707; ENSP00000469950; ENSG00000169035. [P49862-2]
GeneIDi5650.
KEGGihsa:5650.
UCSCiuc002puo.3. human. [P49862-1]

Polymorphism databases

DMDMi1710878.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L33404 mRNA. Translation: AAC37551.1 .
AF166330 Genomic DNA. Translation: AAD49718.1 .
AF243527 Genomic DNA. Translation: AAG33360.1 .
AF332583 Genomic DNA. Translation: AAK69624.1 .
AF411214 mRNA. Translation: AAN03662.1 .
AF411215 mRNA. Translation: AAN03663.1 .
AY601109 mRNA. Translation: AAU04540.1 .
AK289660 mRNA. Translation: BAF82349.1 .
CH471135 Genomic DNA. Translation: EAW71959.1 .
BC032005 mRNA. Translation: AAH32005.1 .
CCDSi CCDS12812.1. [P49862-1 ]
CCDS59414.1. [P49862-2 ]
PIRi A53968.
RefSeqi NP_001193982.1. NM_001207053.1. [P49862-2 ]
NP_001230055.1. NM_001243126.1.
NP_005037.1. NM_005046.3. [P49862-1 ]
NP_644806.1. NM_139277.2. [P49862-1 ]
UniGenei Hs.151254.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2QXG X-ray 2.60 A/B 30-253 [» ]
2QXH X-ray 2.00 A 30-253 [» ]
2QXI X-ray 1.00 A 30-253 [» ]
2QXJ X-ray 2.10 A 30-253 [» ]
3BSQ X-ray 2.80 A/B/C 30-250 [» ]
ProteinModelPortali P49862.
SMRi P49862. Positions 30-253.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111631. 3 interactions.
STRINGi 9606.ENSP00000304791.

Chemistry

BindingDBi P49862.
ChEMBLi CHEMBL2443.

Protein family/group databases

MEROPSi S01.300.

PTM databases

PhosphoSitei P49862.

Polymorphism databases

DMDMi 1710878.

Proteomic databases

PaxDbi P49862.
PRIDEi P49862.

Protocols and materials databases

DNASUi 5650.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000391807 ; ENSP00000375683 ; ENSG00000169035 . [P49862-1 ]
ENST00000595820 ; ENSP00000470538 ; ENSG00000169035 . [P49862-1 ]
ENST00000597707 ; ENSP00000469950 ; ENSG00000169035 . [P49862-2 ]
GeneIDi 5650.
KEGGi hsa:5650.
UCSCi uc002puo.3. human. [P49862-1 ]

Organism-specific databases

CTDi 5650.
GeneCardsi GC19M051479.
HGNCi HGNC:6368. KLK7.
HPAi CAB026342.
HPA018994.
MIMi 604438. gene.
neXtProti NX_P49862.
PharmGKBi PA30157.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000251820.
HOVERGENi HBG013304.
InParanoidi P49862.
KOi K08668.
OMAi VLVNERW.
PhylomeDBi P49862.
TreeFami TF331065.

Enzyme and pathway databases

BRENDAi 3.4.21.117. 1154.
Reactomei REACT_118572. Degradation of the extracellular matrix.

Miscellaneous databases

EvolutionaryTracei P49862.
GeneWikii KLK7.
GenomeRNAii 5650.
NextBioi 21952.
PMAP-CutDB P49862.
PROi P49862.
SOURCEi Search...

Gene expression databases

ArrayExpressi P49862.
Bgeei P49862.
CleanExi HS_KLK7.
Genevestigatori P49862.

Family and domain databases

InterProi IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression, and characterization of stratum corneum chymotryptic enzyme. A skin-specific human serine proteinase."
    Hansson L., Stroemqvist M., Baeckman A., Wallbrandt P., Carlstein A., Egelrud T.
    J. Biol. Chem. 269:19420-19426(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 23-53.
    Tissue: Skin.
  2. "The KLK7 (PRSS6) gene, encoding for the stratum corneum chymotryptic enzyme is a new member of the human kallikrein gene family -- genomic characterization, mapping, tissue expression and hormonal regulation."
    Yousef G.M., Scorilas A., Magklara A., Soosaipillai A., Diamandis E.P.
    Gene 254:119-128(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION.
    Tissue: Keratinocyte.
  3. "Sequencing and expression analysis of the serine protease gene cluster located in chromosome 19q13 region."
    Gan L., Lee I., Smith R., Argonza-Barrett R., Lei H., McCuaig J., Moss P., Paeper B., Wang K.
    Gene 257:119-130(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Epidermal overexpression of stratum corneum chymotryptic enzyme in mice: a model for chronic itchy dermatitis."
    Hansson L., Backman A., Ny A., Edlund M., Ekholm E., Ekstrand Hammarstrom B., Tornell J., Wallbrandt P., Wennbo H., Egelrud T.
    J. Invest. Dermatol. 118:444-449(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Differential splicing of KLK5 and KLK7 in epithelial ovarian cancer produces novel variants with potential as cancer biomarkers."
    Dong Y., Kaushal A., Brattsand M., Nicklin J., Clements J.A.
    Clin. Cancer Res. 9:1710-1720(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Ovarian carcinoma.
  6. "Prostate epithelial cells KLK7 protein."
    Mo Z., Yang X.
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Prostate.
  7. "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: Amygdala.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORM 1).
    Tissue: Skin.
  10. "Primary substrate specificity of recombinant human stratum corneum chymotryptic enzyme."
    Skytt A., Stroemqvist M., Egelrud T.
    Biochem. Biophys. Res. Commun. 211:586-589(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  11. Cited for: FUNCTION, CLEAVAGE SPECIFICITY FOR INSULIN, ENZYME REGULATION.
  12. "Chymotryptic specificity determinants in the 1.0 A structure of the zinc-inhibited human tissue kallikrein 7."
    Debela M., Hess P., Magdolen V., Schechter N.M., Steiner T., Huber R., Bode W., Goettig P.
    Proc. Natl. Acad. Sci. U.S.A. 104:16086-16091(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 30-253 IN COMPLEX WITH ZINC OR COPPER, ACTIVE SITE, DISULFIDE BONDS, MUTAGENESIS OF HIS-54 AND HIS-109.
  13. "Crystal structure of human epidermal kallikrein 7 (hK7) synthesized directly in its native state in E. coli: insights into the atomic basis of its inhibition by LEKTI domain 6 (LD6)."
    Fernandez I.S., Standker L., Magert H.J., Forssmann W.G., Gimenez-Gallego G., Romero A.
    J. Mol. Biol. 377:1488-1497(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-250, DISULFIDE BONDS.

Entry informationi

Entry nameiKLK7_HUMAN
AccessioniPrimary (citable) accession number: P49862
Secondary accession number(s): A8K0U5, Q8N5N9, Q8NFV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 133 of the entry and version 1 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

Keywords - Technical termi

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

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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