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Protein

Interstitial collagenase

Gene

MMP1

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

Functioni

Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.1 Publication

Catalytic activityi

Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Can be activated without removal of the activation peptide.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi92Zinc 2; in inhibited formCombined sources1
Metal bindingi124Calcium 1Combined sources1
Metal bindingi158Calcium 2Combined sources1
Metal bindingi168Zinc 1Combined sources1
Metal bindingi170Zinc 1Combined sources1
Metal bindingi175Calcium 3Combined sources1
Metal bindingi176Calcium 3; via carbonyl oxygenCombined sources1
Metal bindingi178Calcium 3; via carbonyl oxygenCombined sources1
Metal bindingi180Calcium 3; via carbonyl oxygenCombined sources1
Metal bindingi183Zinc 1Combined sources1
Metal bindingi190Calcium 2; via carbonyl oxygenCombined sources1
Metal bindingi192Calcium 2; via carbonyl oxygenCombined sources1
Metal bindingi194Calcium 2Combined sources1
Metal bindingi196Zinc 1Combined sources1
Metal bindingi198Calcium 3Combined sources1
Metal bindingi199Calcium 1Combined sources1
Metal bindingi201Calcium 3Combined sources1
Metal bindingi218Zinc 2; catalyticCombined sources1
Active sitei2191
Metal bindingi222Zinc 2; catalyticCombined sources1
Metal bindingi228Zinc 2; catalyticCombined sources1
Metal bindingi285Calcium 4; via carbonyl oxygenCombined sources1
Metal bindingi329Calcium 4; via carbonyl oxygenCombined sources1
Metal bindingi378Calcium 4; via carbonyl oxygenCombined sources1
Metal bindingi427Calcium 4; via carbonyl oxygenCombined sources1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • endopeptidase activity Source: ParkinsonsUK-UCL
  • metalloendopeptidase activity Source: BHF-UCL
  • serine-type endopeptidase activity Source: Reactome
  • zinc ion binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation, Host-virus interaction

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:G66-33949-MONOMER.
BRENDAi3.4.24.7. 2681.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1592389. Activation of Matrix Metalloproteinases.
R-HSA-210991. Basigin interactions.
R-HSA-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Protein family/group databases

MEROPSiM10.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Interstitial collagenase (EC:3.4.24.7)
Alternative name(s):
Fibroblast collagenase
Matrix metalloproteinase-1
Short name:
MMP-1
Cleaved into the following 2 chains:
Gene namesi
Name:MMP1
Synonyms:CLG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:7155. MMP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi360Y → F: Partial reduction of tyrosine phosphorylation in the presence of PKDCC/VLK. 1 Publication1

Organism-specific databases

DisGeNETi4312.
MalaCardsiMMP1.
OpenTargetsiENSG00000196611.
Orphaneti79408. Severe generalized recessive dystrophic epidermolysis bullosa.
PharmGKBiPA30867.

Chemistry databases

ChEMBLiCHEMBL332.
DrugBankiDB00786. Marimastat.
GuidetoPHARMACOLOGYi1628.

Polymorphism and mutation databases

BioMutaiMMP1.
DMDMi116852.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Add BLAST19
PropeptideiPRO_000002870320 – 99Activation peptide1 PublicationAdd BLAST80
ChainiPRO_0000028704100 – 469Interstitial collagenaseAdd BLAST370
ChainiPRO_0000028705100 – 26922 kDa interstitial collagenaseAdd BLAST170
ChainiPRO_0000028706270 – 46927 kDa interstitial collagenaseAdd BLAST200

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei57Phosphoserine1 Publication1
GlycosylationiCAR_000105120N-linked (GlcNAc...)1 Publication1
Modified residuei274Phosphothreonine1 Publication1
Disulfide bondi278 ↔ 466By similarity
Modified residuei360Phosphotyrosine; by PKDCC1 Publication1

Post-translational modificationi

Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase.1 Publication
Tyrosine phosphorylated in platelets by PKDCC/VLK.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei143Not glycosylated1 Publication1
Sitei269 – 270Cleavage; by autolysis1 Publication2

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

PaxDbiP03956.
PeptideAtlasiP03956.
PRIDEiP03956.

PTM databases

iPTMnetiP03956.
PhosphoSitePlusiP03956.
UniCarbKBiP03956.

Miscellaneous databases

PMAP-CutDBP03956.

Expressioni

Gene expression databases

BgeeiENSG00000196611.
CleanExiHS_MMP1.
GenevisibleiP03956. HS.

Organism-specific databases

HPAiCAB017558.

Interactioni

Subunit structurei

Interacts with HIV-1 Tat.1 Publication

Protein-protein interaction databases

BioGridi110456. 6 interactors.
DIPiDIP-529N.
IntActiP03956. 2 interactors.
MINTiMINT-198818.
STRINGi9606.ENSP00000322788.

Chemistry databases

BindingDBiP03956.

Structurei

Secondary structure

1469
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi33 – 41Combined sources9
Helixi59 – 70Combined sources12
Helixi81 – 87Combined sources7
Beta strandi103 – 106Combined sources4
Beta strandi112 – 118Combined sources7
Beta strandi123 – 125Combined sources3
Helixi127 – 142Combined sources16
Beta strandi144 – 146Combined sources3
Beta strandi148 – 151Combined sources4
Beta strandi153 – 155Combined sources3
Beta strandi158 – 164Combined sources7
Beta strandi169 – 171Combined sources3
Beta strandi176 – 179Combined sources4
Beta strandi182 – 184Combined sources3
Beta strandi187 – 189Combined sources3
Turni190 – 193Combined sources4
Beta strandi195 – 198Combined sources4
Beta strandi204 – 209Combined sources6
Helixi212 – 223Combined sources12
Beta strandi237 – 239Combined sources3
Helixi250 – 260Combined sources11
Beta strandi285 – 290Combined sources6
Beta strandi293 – 298Combined sources6
Beta strandi301 – 304Combined sources4
Beta strandi309 – 311Combined sources3
Beta strandi313 – 316Combined sources4
Helixi317 – 319Combined sources3
Beta strandi330 – 334Combined sources5
Helixi335 – 337Combined sources3
Beta strandi339 – 344Combined sources6
Beta strandi347 – 352Combined sources6
Beta strandi361 – 363Combined sources3
Helixi364 – 368Combined sources5
Beta strandi379 – 382Combined sources4
Turni384 – 386Combined sources3
Beta strandi388 – 393Combined sources6
Beta strandi396 – 401Combined sources6
Turni402 – 405Combined sources4
Beta strandi412 – 414Combined sources3
Helixi415 – 418Combined sources4
Beta strandi427 – 432Combined sources6
Beta strandi435 – 440Combined sources6
Beta strandi443 – 448Combined sources6
Turni449 – 452Combined sources4
Beta strandi453 – 459Combined sources7
Turni460 – 463Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AYKNMR-A101-269[»]
1CGEX-ray1.90A102-269[»]
1CGFX-ray2.10A/B102-263[»]
1CGLX-ray2.40A/B101-269[»]
1HFCX-ray1.50A101-269[»]
1SU3X-ray2.20A/B20-469[»]
2AYKNMR-A101-269[»]
2CLTX-ray2.67A/B100-466[»]
2J0TX-ray2.54A/B/C101-269[»]
2TCLX-ray2.20A101-269[»]
3AYKNMR-A101-269[»]
3SHIX-ray2.20A/G/M106-261[»]
4AUOX-ray3.00A/B100-466[»]
4AYKNMR-A101-269[»]
966CX-ray1.90A108-264[»]
ProteinModelPortaliP03956.
SMRiP03956.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03956.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati275 – 324Hemopexin 1Add BLAST50
Repeati325 – 371Hemopexin 2Add BLAST47
Repeati374 – 422Hemopexin 3Add BLAST49
Repeati423 – 466Hemopexin 4Add BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni98 – 276MetalloproteaseAdd BLAST179

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi90 – 97Cysteine switchBy similarity8

Domaini

There are two distinct domains in this protein; the catalytic N-terminal, and the C-terminal which is involved in substrate specificity and in binding TIMP (tissue inhibitor of metalloproteinases).
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Sequence similaritiesi

Belongs to the peptidase M10A family.Curated
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP03956.
KOiK01388.
OMAiFPGIGHK.
OrthoDBiEOG091G03DP.
PhylomeDBiP03956.
TreeFamiTF315428.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P03956-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHSFPPLLLL LFWGVVSHSF PATLETQEQD VDLVQKYLEK YYNLKNDGRQ
60 70 80 90 100
VEKRRNSGPV VEKLKQMQEF FGLKVTGKPD AETLKVMKQP RCGVPDVAQF
110 120 130 140 150
VLTEGNPRWE QTHLTYRIEN YTPDLPRADV DHAIEKAFQL WSNVTPLTFT
160 170 180 190 200
KVSEGQADIM ISFVRGDHRD NSPFDGPGGN LAHAFQPGPG IGGDAHFDED
210 220 230 240 250
ERWTNNFREY NLHRVAAHEL GHSLGLSHST DIGALMYPSY TFSGDVQLAQ
260 270 280 290 300
DDIDGIQAIY GRSQNPVQPI GPQTPKACDS KLTFDAITTI RGEVMFFKDR
310 320 330 340 350
FYMRTNPFYP EVELNFISVF WPQLPNGLEA AYEFADRDEV RFFKGNKYWA
360 370 380 390 400
VQGQNVLHGY PKDIYSSFGF PRTVKHIDAA LSEENTGKTY FFVANKYWRY
410 420 430 440 450
DEYKRSMDPG YPKMIAHDFP GIGHKVDAVF MKDGFFYFFH GTRQYKFDPK
460
TKRILTLQKA NSWFNCRKN
Length:469
Mass (Da):54,007
Last modified:December 1, 1992 - v3
Checksum:i4B1361DCF4C54B20
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti43N → K in AAA35700 (PubMed:3027129).Curated1
Sequence conflicti64Missing in AAA35700 (PubMed:3027129).Curated1
Sequence conflicti115T → R in AAA35699 (PubMed:3009463).Curated1
Sequence conflicti200D → H in CAA28858 (PubMed:3030290).Curated1
Sequence conflicti208R → T in CAA28858 (PubMed:3030290).Curated1
Sequence conflicti317I → T in CAA28858 (PubMed:3030290).Curated1
Sequence conflicti410G → S in AAA35699 (PubMed:3009463).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01196929Q → P.Corresponds to variant rs554499dbSNPEnsembl.1
Natural variantiVAR_021024191I → V.1 PublicationCorresponds to variant rs17879973dbSNPEnsembl.1
Natural variantiVAR_011970252D → G.Corresponds to variant rs513964dbSNPEnsembl.1
Natural variantiVAR_054005262R → S.Corresponds to variant rs12282811dbSNPEnsembl.1
Natural variantiVAR_021025405R → Q.1 PublicationCorresponds to variant rs17879165dbSNPEnsembl.1
Natural variantiVAR_021026406S → T.1 PublicationCorresponds to variant rs17884120dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54925 mRNA. Translation: CAA38691.1.
X05231 mRNA. Translation: CAA28858.1.
M13509 mRNA. Translation: AAA35699.1.
U78045 Genomic DNA. Translation: AAB36941.1.
BT006874 mRNA. Translation: AAP35520.1.
AY769434 Genomic DNA. Translation: AAV28732.1.
BC013875 mRNA. Translation: AAH13875.1.
M16567 Genomic DNA. Translation: AAA52033.1.
M15996 mRNA. Translation: AAA35700.1.
CCDSiCCDS8322.1.
PIRiA37308. KCHUI.
RefSeqiNP_002412.1. NM_002421.3.
UniGeneiHs.83169.

Genome annotation databases

EnsembliENST00000315274; ENSP00000322788; ENSG00000196611.
GeneIDi4312.
KEGGihsa:4312.
UCSCiuc001phi.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Collagenase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54925 mRNA. Translation: CAA38691.1.
X05231 mRNA. Translation: CAA28858.1.
M13509 mRNA. Translation: AAA35699.1.
U78045 Genomic DNA. Translation: AAB36941.1.
BT006874 mRNA. Translation: AAP35520.1.
AY769434 Genomic DNA. Translation: AAV28732.1.
BC013875 mRNA. Translation: AAH13875.1.
M16567 Genomic DNA. Translation: AAA52033.1.
M15996 mRNA. Translation: AAA35700.1.
CCDSiCCDS8322.1.
PIRiA37308. KCHUI.
RefSeqiNP_002412.1. NM_002421.3.
UniGeneiHs.83169.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AYKNMR-A101-269[»]
1CGEX-ray1.90A102-269[»]
1CGFX-ray2.10A/B102-263[»]
1CGLX-ray2.40A/B101-269[»]
1HFCX-ray1.50A101-269[»]
1SU3X-ray2.20A/B20-469[»]
2AYKNMR-A101-269[»]
2CLTX-ray2.67A/B100-466[»]
2J0TX-ray2.54A/B/C101-269[»]
2TCLX-ray2.20A101-269[»]
3AYKNMR-A101-269[»]
3SHIX-ray2.20A/G/M106-261[»]
4AUOX-ray3.00A/B100-466[»]
4AYKNMR-A101-269[»]
966CX-ray1.90A108-264[»]
ProteinModelPortaliP03956.
SMRiP03956.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110456. 6 interactors.
DIPiDIP-529N.
IntActiP03956. 2 interactors.
MINTiMINT-198818.
STRINGi9606.ENSP00000322788.

Chemistry databases

BindingDBiP03956.
ChEMBLiCHEMBL332.
DrugBankiDB00786. Marimastat.
GuidetoPHARMACOLOGYi1628.

Protein family/group databases

MEROPSiM10.001.

PTM databases

iPTMnetiP03956.
PhosphoSitePlusiP03956.
UniCarbKBiP03956.

Polymorphism and mutation databases

BioMutaiMMP1.
DMDMi116852.

Proteomic databases

PaxDbiP03956.
PeptideAtlasiP03956.
PRIDEiP03956.

Protocols and materials databases

DNASUi4312.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000315274; ENSP00000322788; ENSG00000196611.
GeneIDi4312.
KEGGihsa:4312.
UCSCiuc001phi.3. human.

Organism-specific databases

CTDi4312.
DisGeNETi4312.
GeneCardsiMMP1.
H-InvDBHIX0201751.
HGNCiHGNC:7155. MMP1.
HPAiCAB017558.
MalaCardsiMMP1.
MIMi120353. gene.
neXtProtiNX_P03956.
OpenTargetsiENSG00000196611.
Orphaneti79408. Severe generalized recessive dystrophic epidermolysis bullosa.
PharmGKBiPA30867.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP03956.
KOiK01388.
OMAiFPGIGHK.
OrthoDBiEOG091G03DP.
PhylomeDBiP03956.
TreeFamiTF315428.

Enzyme and pathway databases

BioCyciZFISH:G66-33949-MONOMER.
BRENDAi3.4.24.7. 2681.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1592389. Activation of Matrix Metalloproteinases.
R-HSA-210991. Basigin interactions.
R-HSA-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Miscellaneous databases

EvolutionaryTraceiP03956.
GeneWikiiMMP1.
GenomeRNAii4312.
PMAP-CutDBP03956.
PROiP03956.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000196611.
CleanExiHS_MMP1.
GenevisibleiP03956. HS.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMMP1_HUMAN
AccessioniPrimary (citable) accession number: P03956
Secondary accession number(s): P08156
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: December 1, 1992
Last modified: November 30, 2016
This is version 196 of the entry and version 3 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 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.