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P07384

- CAN1_HUMAN

UniProt

P07384 - CAN1_HUMAN

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Protein

Calpain-1 catalytic subunit

Gene

CAPN1

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

Functioni

Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.

Catalytic activityi

Broad endopeptidase specificity.

Cofactori

Binds 4 calcium ions.

Enzyme regulationi

Activated by micromolar concentrations of calcium and inhibited by calpastatin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei15 – 162Cleavage; for 78 kDa form
Sitei27 – 282Cleavage; for 75 kDa form
Active sitei115 – 1151By similarity
Active sitei272 – 2721By similarity
Active sitei296 – 2961By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi99 – 10681
Calcium bindingi302 – 333322Add
BLAST
Calcium bindingi598 – 609123Add
BLAST
Calcium bindingi628 – 639124Add
BLAST

GO - Molecular functioni

  1. calcium-dependent cysteine-type endopeptidase activity Source: UniProtKB
  2. calcium ion binding Source: InterPro

GO - Biological processi

  1. extracellular matrix disassembly Source: Reactome
  2. extracellular matrix organization Source: Reactome
  3. positive regulation of cell proliferation Source: ProtInc
  4. proteolysis Source: UniProtKB
  5. receptor catabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.22.52. 2681.
ReactomeiREACT_118572. Degradation of the extracellular matrix.

Protein family/group databases

MEROPSiC02.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Calpain-1 catalytic subunit (EC:3.4.22.52)
Alternative name(s):
Calcium-activated neutral proteinase 1
Short name:
CANP 1
Calpain mu-type
Calpain-1 large subunit
Cell proliferation-inducing gene 30 protein
Micromolar-calpain
Short name:
muCANP
Gene namesi
Name:CAPN1
Synonyms:CANPL1
ORF Names:PIG30
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:1476. CAPN1.

Subcellular locationi

Cytoplasm 1 Publication. Cell membrane 1 Publication
Note: Translocates to the plasma membrane upon Ca2+ binding.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: BHF-UCL
  3. extracellular vesicular exosome Source: UniProtKB
  4. focal adhesion Source: UniProtKB
  5. membrane Source: BHF-UCL
  6. plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26057.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 714713Calpain-1 catalytic subunitPRO_0000207694Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications

Post-translational modificationi

Undergoes calcium-induced successive autoproteolytic cleavages that generate a membrane-bound 78 kDa active form and an intracellular 75 kDa active form. Calpastatin reduces with high efficiency the transition from 78 kDa to 75 kDa calpain forms.

Keywords - PTMi

Acetylation, Autocatalytic cleavage

Proteomic databases

MaxQBiP07384.
PaxDbiP07384.
PRIDEiP07384.

PTM databases

PhosphoSiteiP07384.

Miscellaneous databases

PMAP-CutDBP07384.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiP07384.
CleanExiHS_CAPN1.
ExpressionAtlasiP07384. baseline and differential.
GenevestigatoriP07384.

Organism-specific databases

HPAiHPA005992.

Interactioni

Subunit structurei

Forms a heterodimer with a small (regulatory) subunit (CAPNS1).

Binary interactionsi

WithEntry#Exp.IntActNotes
EZRP153112EBI-1542113,EBI-1056902
PTPN1P180314EBI-1542113,EBI-968788
STAT3P407632EBI-1542113,EBI-518675

Protein-protein interaction databases

BioGridi107273. 73 interactions.
IntActiP07384. 12 interactions.
MINTiMINT-5004023.
STRINGi9606.ENSP00000279247.

Structurei

Secondary structure

1
714
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 393
Helixi42 – 5110
Helixi65 – 684
Helixi78 – 803
Beta strandi84 – 863
Helixi88 – 914
Beta strandi99 – 1024
Helixi104 – 1063
Beta strandi111 – 1133
Helixi115 – 12410
Helixi128 – 1347
Beta strandi147 – 1559
Beta strandi158 – 1669
Beta strandi168 – 1714
Beta strandi174 – 1774
Helixi187 – 19812
Helixi203 – 2053
Helixi210 – 2167
Beta strandi217 – 2204
Beta strandi221 – 2266
Helixi227 – 2293
Helixi234 – 24411
Beta strandi247 – 2515
Beta strandi256 – 2583
Beta strandi274 – 28411
Beta strandi287 – 2959
Helixi312 – 3165
Helixi319 – 3257
Beta strandi331 – 3377
Helixi338 – 3447
Beta strandi347 – 3526

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZCMX-ray2.00A33-353[»]
2ARYX-ray2.40A/B29-360[»]
ProteinModelPortaliP07384.
SMRiP07384. Positions 13-713.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07384.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 354300Calpain catalyticPROSITE-ProRule annotationAdd
BLAST
Domaini541 – 57636EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini585 – 61834EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini615 – 65036EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini680 – 71435EF-hand 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni355 – 526172Domain IIIAdd
BLAST
Regioni527 – 54216LinkerAdd
BLAST
Regioni543 – 713171Domain IVAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C2 family.Curated
Contains 1 calpain catalytic domain.PROSITE-ProRule annotation
Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG327523.
GeneTreeiENSGT00760000118971.
HOGENOMiHOG000232035.
HOVERGENiHBG012645.
InParanoidiP07384.
KOiK01367.
OMAiPQSLGYK.
OrthoDBiEOG7RV9FM.
PhylomeDBiP07384.
TreeFamiTF314748.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR029643. CAPN1.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000169. Pept_cys_AS.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view]
PANTHERiPTHR10183:SF284. PTHR10183:SF284. 1 hit.
PfamiPF01067. Calpain_III. 1 hit.
PF13405. EF-hand_6. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
PRINTSiPR00704. CALPAIN.
SMARTiSM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
SM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF49758. SSF49758. 1 hit.
PROSITEiPS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P07384-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEEIITPVY CTGVSAQVQK QRARELGLGR HENAIKYLGQ DYEQLRVRCL
60 70 80 90 100
QSGTLFRDEA FPPVPQSLGY KDLGPNSSKT YGIKWKRPTE LLSNPQFIVD
110 120 130 140 150
GATRTDICQG ALGDCWLLAA IASLTLNDTL LHRVVPHGQS FQNGYAGIFH
160 170 180 190 200
FQLWQFGEWV DVVVDDLLPI KDGKLVFVHS AEGNEFWSAL LEKAYAKVNG
210 220 230 240 250
SYEALSGGST SEGFEDFTGG VTEWYELRKA PSDLYQIILK ALERGSLLGC
260 270 280 290 300
SIDISSVLDM EAITFKKLVK GHAYSVTGAK QVNYRGQVVS LIRMRNPWGE
310 320 330 340 350
VEWTGAWSDS SSEWNNVDPY ERDQLRVKME DGEFWMSFRD FMREFTRLEI
360 370 380 390 400
CNLTPDALKS RTIRKWNTTL YEGTWRRGST AGGCRNYPAT FWVNPQFKIR
410 420 430 440 450
LDETDDPDDY GDRESGCSFV LALMQKHRRR ERRFGRDMET IGFAVYEVPP
460 470 480 490 500
ELVGQPAVHL KRDFFLANAS RARSEQFINL REVSTRFRLP PGEYVVVPST
510 520 530 540 550
FEPNKEGDFV LRFFSEKSAG TVELDDQIQA NLPDEQVLSE EEIDENFKAL
560 570 580 590 600
FRQLAGEDME ISVKELRTIL NRIISKHKDL RTKGFSLESC RSMVNLMDRD
610 620 630 640 650
GNGKLGLVEF NILWNRIRNY LSIFRKFDLD KSGSMSAYEM RMAIESAGFK
660 670 680 690 700
LNKKLYELII TRYSEPDLAV DFDNFVCCLV RLETMFRFFK TLDTDLDGVV
710
TFDLFKWLQL TMFA
Length:714
Mass (Da):81,890
Last modified:April 1, 1988 - v1
Checksum:i1CB6D7C56D063498
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti548 – 5481K → N in AAH08751. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031T → A.1 Publication
Corresponds to variant rs17885718 [ dbSNP | Ensembl ].
VAR_021085
Natural varianti433 – 4331R → P.2 Publications
Corresponds to variant rs10895991 [ dbSNP | Ensembl ].
VAR_021086
Natural varianti492 – 4921G → R.1 Publication
Corresponds to variant rs17883283 [ dbSNP | Ensembl ].
VAR_021087
Natural varianti676 – 6761V → I.1 Publication
Corresponds to variant rs17884773 [ dbSNP | Ensembl ].
VAR_021088

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04366 mRNA. Translation: CAA27881.1.
AY550975 mRNA. Translation: AAT52221.1.
AY796340 Genomic DNA. Translation: AAV41878.1.
BC008751 mRNA. Translation: AAH08751.1.
BC017200 mRNA. Translation: AAH17200.1.
BC075862 mRNA. Translation: AAH75862.1.
CCDSiCCDS44644.1.
PIRiA26213. CIHUH.
RefSeqiNP_001185797.1. NM_001198868.1.
NP_001185798.1. NM_001198869.1.
NP_005177.2. NM_005186.3.
XP_006718761.1. XM_006718698.1.
UniGeneiHs.502842.
Hs.735492.

Genome annotation databases

EnsembliENST00000279247; ENSP00000279247; ENSG00000014216.
ENST00000524773; ENSP00000434176; ENSG00000014216.
ENST00000527323; ENSP00000431984; ENSG00000014216.
ENST00000533129; ENSP00000431686; ENSG00000014216.
ENST00000533820; ENSP00000435272; ENSG00000014216.
GeneIDi823.
KEGGihsa:823.
UCSCiuc001odf.2. human.

Polymorphism databases

DMDMi115574.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

CaBP

Calpain

Calpains homepage
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04366 mRNA. Translation: CAA27881.1 .
AY550975 mRNA. Translation: AAT52221.1 .
AY796340 Genomic DNA. Translation: AAV41878.1 .
BC008751 mRNA. Translation: AAH08751.1 .
BC017200 mRNA. Translation: AAH17200.1 .
BC075862 mRNA. Translation: AAH75862.1 .
CCDSi CCDS44644.1.
PIRi A26213. CIHUH.
RefSeqi NP_001185797.1. NM_001198868.1.
NP_001185798.1. NM_001198869.1.
NP_005177.2. NM_005186.3.
XP_006718761.1. XM_006718698.1.
UniGenei Hs.502842.
Hs.735492.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZCM X-ray 2.00 A 33-353 [» ]
2ARY X-ray 2.40 A/B 29-360 [» ]
ProteinModelPortali P07384.
SMRi P07384. Positions 13-713.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107273. 73 interactions.
IntActi P07384. 12 interactions.
MINTi MINT-5004023.
STRINGi 9606.ENSP00000279247.

Chemistry

BindingDBi P07384.
ChEMBLi CHEMBL2111357.

Protein family/group databases

MEROPSi C02.001.

PTM databases

PhosphoSitei P07384.

Polymorphism databases

DMDMi 115574.

Proteomic databases

MaxQBi P07384.
PaxDbi P07384.
PRIDEi P07384.

Protocols and materials databases

DNASUi 823.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000279247 ; ENSP00000279247 ; ENSG00000014216 .
ENST00000524773 ; ENSP00000434176 ; ENSG00000014216 .
ENST00000527323 ; ENSP00000431984 ; ENSG00000014216 .
ENST00000533129 ; ENSP00000431686 ; ENSG00000014216 .
ENST00000533820 ; ENSP00000435272 ; ENSG00000014216 .
GeneIDi 823.
KEGGi hsa:823.
UCSCi uc001odf.2. human.

Organism-specific databases

CTDi 823.
GeneCardsi GC11P064950.
HGNCi HGNC:1476. CAPN1.
HPAi HPA005992.
MIMi 114220. gene.
neXtProti NX_P07384.
PharmGKBi PA26057.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG327523.
GeneTreei ENSGT00760000118971.
HOGENOMi HOG000232035.
HOVERGENi HBG012645.
InParanoidi P07384.
KOi K01367.
OMAi PQSLGYK.
OrthoDBi EOG7RV9FM.
PhylomeDBi P07384.
TreeFami TF314748.

Enzyme and pathway databases

BRENDAi 3.4.22.52. 2681.
Reactomei REACT_118572. Degradation of the extracellular matrix.

Miscellaneous databases

ChiTaRSi CAPN1. human.
EvolutionaryTracei P07384.
GeneWikii CAPN1.
GenomeRNAii 823.
NextBioi 3370.
PMAP-CutDB P07384.
PROi P07384.
SOURCEi Search...

Gene expression databases

Bgeei P07384.
CleanExi HS_CAPN1.
ExpressionAtlasi P07384. baseline and differential.
Genevestigatori P07384.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
InterProi IPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR029643. CAPN1.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000169. Pept_cys_AS.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view ]
PANTHERi PTHR10183:SF284. PTHR10183:SF284. 1 hit.
Pfami PF01067. Calpain_III. 1 hit.
PF13405. EF-hand_6. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view ]
PRINTSi PR00704. CALPAIN.
SMARTi SM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
SM00054. EFh. 3 hits.
[Graphical view ]
SUPFAMi SSF49758. SSF49758. 1 hit.
PROSITEi PS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP) deduced from its cDNA sequence."
    Aoki K., Imajoh S., Ohno S., Emori Y., Koike M., Kosaki G., Suzuki K.
    FEBS Lett. 205:313-317(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A novel member of the calcium-dependent cysteine protease family."
    Sorimachi H., Ohmi S., Emori Y., Kawasaki H., Saido T.C., Ohno S., Minami Y., Suzuki K.
    Biol. Chem. Hoppe-Seyler 371:171-176(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Identification of a human cell proliferation inducing gene."
    Kim J.W.
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. NIEHS SNPs program
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-103; PRO-433; ARG-492 AND ILE-676.
  5. "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 PRO-433.
    Tissue: Kidney, Pancreas and Placenta.
  6. "Modulation of the calpain autoproteolysis by calpastatin and phospholipids."
    Melloni E., Michetti M., Salamino F., Minafra R., Pontremoli S.
    Biochem. Biophys. Res. Commun. 229:193-197(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPROTEOLYTIC PROCESSING.
  7. "Autolysis of human erythrocyte calpain produces two active enzyme forms with different cell localization."
    Michetti M., Salamino F., Tedesco I., Averna M., Minafra R., Melloni E., Pontremoli S.
    FEBS Lett. 392:11-15(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION.
  8. "Calcium-binding properties of human erythrocyte calpain."
    Michetti M., Salamino F., Minafra R., Melloni E., Pontremoli S.
    Biochem. J. 325:721-726(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CALCIUM-BINDING DATA.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Molecular mode of action of a covalently inhibiting peptidomimetic on the human calpain protease core."
    Li Q., Hanzlik R.P., Weaver R.F., Schonbrunn E.
    Biochemistry 45:701-708(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 33-353 OF MUTANT ALA-213, CALCIUM-BINDING REGIONS.

Entry informationi

Entry nameiCAN1_HUMAN
AccessioniPrimary (citable) accession number: P07384
Secondary accession number(s): Q2TTR0, Q6DHV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: October 29, 2014
This is version 173 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, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3