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Protein

Matrix metalloproteinase-14

Gene

MMP14

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

Functioni

Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro-MMP2.3 Publications

Catalytic activityi

Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
  • Ca2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi93Zinc; in inhibited formBy similarity1
Metal bindingi239Zinc; catalytic1
Active sitei240PROSITE-ProRule annotation1
Metal bindingi243Zinc; catalytic1
Metal bindingi249Zinc; catalytic1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • metalloaminopeptidase activity Source: ParkinsonsUK-UCL
  • metalloendopeptidase activity Source: UniProtKB
  • peptidase activator activity Source: Ensembl
  • serine-type endopeptidase activity Source: Reactome
  • zinc ion binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000157227-MONOMER.
ZFISH:ENSG00000157227-MONOMER.
BRENDAi3.4.24.80. 2681.
3.4.24.B5. 2681.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1592389. Activation of Matrix Metalloproteinases.
SIGNORiP50281.

Protein family/group databases

MEROPSiM10.014.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-14 (EC:3.4.24.80)
Short name:
MMP-14
Alternative name(s):
MMP-X1
Membrane-type matrix metalloproteinase 1
Short name:
MT-MMP 1
Short name:
MTMMP1
Membrane-type-1 matrix metalloproteinase
Short name:
MT1-MMP
Short name:
MT1MMP
Gene namesi
Name:MMP14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:7160. MMP14.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini112 – 541ExtracellularSequence analysisAdd BLAST430
Transmembranei542 – 562HelicalSequence analysisAdd BLAST21
Topological domaini563 – 582CytoplasmicSequence analysisAdd BLAST20

GO - Cellular componenti

  • cytoplasmic vesicle Source: UniProtKB
  • extracellular matrix Source: InterPro
  • focal adhesion Source: UniProtKB
  • Golgi lumen Source: Reactome
  • integral component of plasma membrane Source: ProtInc
  • macropinosome Source: UniProtKB
  • melanosome Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Involvement in diseasei

Winchester syndrome (WNCHRS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by severe osteolysis in the hands and feet, generalized osteoporosis, bone thinning, and absence of subcutaneous nodules. Various additional features include coarse face, corneal opacities, gum hypertrophy, and EKG changes.
See also OMIM:277950
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07056717T → R in WNCHRS; results in increased MMP14 proteosomal degradation and reduced protein localization to cell membrane. 1 PublicationCorresponds to variant rs587777039dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi4323.
MalaCardsiMMP14.
MIMi277950. phenotype.
OpenTargetsiENSG00000157227.
Orphaneti85196. Nodulosis-arthropathy-osteolysis syndrome.
3460. Torg-Winchester syndrome.
PharmGKBiPA30872.

Chemistry databases

ChEMBLiCHEMBL3869.
DrugBankiDB00786. Marimastat.
GuidetoPHARMACOLOGYi1638.

Polymorphism and mutation databases

BioMutaiMMP14.
DMDMi317373419.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000002879821 – 111Activation peptide1 PublicationAdd BLAST91
ChainiPRO_0000028799112 – 582Matrix metalloproteinase-14Add BLAST471

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi319 ↔ 508By similarity
Modified residuei399Phosphotyrosine; by PKDCC1 Publication1

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity
Tyrosine phosphorylated by PKDCC/VLK.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Phosphoprotein, Zymogen

Proteomic databases

EPDiP50281.
MaxQBiP50281.
PaxDbiP50281.
PeptideAtlasiP50281.
PRIDEiP50281.

PTM databases

iPTMnetiP50281.
PhosphoSitePlusiP50281.
SwissPalmiP50281.

Expressioni

Tissue specificityi

Expressed in stromal cells of colon, breast, and head and neck. Expressed in lung tumors.1 Publication

Inductioni

Up-regulated by NANOS1.1 Publication

Gene expression databases

BgeeiENSG00000157227.
CleanExiHS_MMP14.
ExpressionAtlasiP50281. baseline and differential.
GenevisibleiP50281. HS.

Organism-specific databases

HPAiCAB009918.
HPA051432.

Interactioni

Subunit structurei

Interacts (via C-terminal cytoplasmic tail) with BST2. Interacts with DLL1; inhibits DLL1-induced Notch signaling (PubMed:21572390).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADI1Q9BV574EBI-992788,EBI-992807
BCAR1P569453EBI-992788,EBI-702093
CCDC155Q8N6L03EBI-992788,EBI-749265
Gorasp2Q9R06414EBI-992788,EBI-4422912From a different organism.
LIMK1P536674EBI-992788,EBI-444403
LUMP518842EBI-992788,EBI-725780
TIMP2P160352EBI-992788,EBI-1033507

Protein-protein interaction databases

BioGridi110466. 9 interactors.
DIPiDIP-35111N.
IntActiP50281. 34 interactors.
MINTiMINT-246780.
STRINGi9606.ENSP00000308208.

Chemistry databases

BindingDBiP50281.

Structurei

Secondary structure

1582
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi120 – 128Combined sources9
Turni133 – 135Combined sources3
Helixi137 – 154Combined sources18
Beta strandi158 – 161Combined sources4
Helixi164 – 168Combined sources5
Beta strandi171 – 173Combined sources3
Beta strandi176 – 182Combined sources7
Beta strandi187 – 190Combined sources4
Beta strandi194 – 202Combined sources9
Turni208 – 211Combined sources4
Beta strandi213 – 216Combined sources4
Beta strandi230 – 232Combined sources3
Helixi233 – 244Combined sources12
Beta strandi258 – 260Combined sources3
Helixi273 – 283Combined sources11
Helixi318 – 320Combined sources3
Beta strandi324 – 329Combined sources6
Beta strandi332 – 337Combined sources6
Beta strandi340 – 345Combined sources6
Beta strandi354 – 356Combined sources3
Helixi357 – 360Combined sources4
Beta strandi370 – 373Combined sources4
Beta strandi375 – 377Combined sources3
Beta strandi379 – 383Combined sources5
Beta strandi386 – 391Combined sources6
Beta strandi400 – 402Combined sources3
Helixi403 – 405Combined sources3
Beta strandi416 – 420Combined sources5
Turni422 – 424Combined sources3
Beta strandi427 – 431Combined sources5
Beta strandi434 – 439Combined sources6
Turni440 – 443Combined sources4
Beta strandi450 – 452Combined sources3
Helixi453 – 455Combined sources3
Beta strandi464 – 468Combined sources5
Beta strandi472 – 479Combined sources8
Beta strandi482 – 487Combined sources6
Turni488 – 491Combined sources4
Helixi501 – 504Combined sources4
Beta strandi569 – 575Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BQQX-ray2.75M114-287[»]
1BUVX-ray2.75M114-287[»]
2MQSNMR-A316-511[»]
3C7XX-ray1.70A316-511[»]
3MA2X-ray2.05A/D112-292[»]
3X23X-ray2.40B563-582[»]
4P3CX-ray1.94M215-227[»]
4P3DX-ray1.95C/M215-227[»]
4QXUX-ray2.30K218-228[»]
ProteinModelPortaliP50281.
SMRiP50281.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50281.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati316 – 364Hemopexin 1Add BLAST49
Repeati365 – 410Hemopexin 2Add BLAST46
Repeati412 – 460Hemopexin 3Add BLAST49
Repeati461 – 508Hemopexin 4Add BLAST48

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi91 – 98Cysteine switchBy similarity8

Domaini

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, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiP50281.
KOiK07763.
OMAiNPESWLQ.
OrthoDBiEOG091G03DP.
PhylomeDBiP50281.
TreeFamiTF352396.

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.
IPR028693. MMP14.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021805. Pept_M10A_metallopeptidase_C.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF24. PTHR10201:SF24. 1 hit.
PfamiPF11857. DUF3377. 1 hit.
PF00045. 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.

P50281-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPAPRPPRC LLLPLLTLGT ALASLGSAQS SSFSPEAWLQ QYGYLPPGDL
60 70 80 90 100
RTHTQRSPQS LSAAIAAMQK FYGLQVTGKA DADTMKAMRR PRCGVPDKFG
110 120 130 140 150
AEIKANVRRK RYAIQGLKWQ HNEITFCIQN YTPKVGEYAT YEAIRKAFRV
160 170 180 190 200
WESATPLRFR EVPYAYIREG HEKQADIMIF FAEGFHGDST PFDGEGGFLA
210 220 230 240 250
HAYFPGPNIG GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE LGHALGLEHS
260 270 280 290 300
SDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYGGESGFP TKMPPQPRTT
310 320 330 340 350
SRPSVPDKPK NPTYGPNICD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM
360 370 380 390 400
DGYPMPIGQF WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP
410 420 430 440 450
KHIKELGRGL PTDKIDAALF WMPNGKTYFF RGNKYYRFNE ELRAVDSEYP
460 470 480 490 500
KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG NKYWKFNNQK LKVEPGYPKS
510 520 530 540 550
ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGGGAVSAA AVVLPVLLLL
560 570 580
LVLAVGLAVF FFRRHGTPRR LLYCQRSLLD KV
Length:582
Mass (Da):65,894
Last modified:January 11, 2011 - v3
Checksum:i3722DE286A4BBCDE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti338E → K in BAA05519 (PubMed:8015608).Curated1
Sequence conflicti500S → P in CAA62432 (PubMed:8706726).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0210294A → T.1 PublicationCorresponds to variant rs17882219dbSNPEnsembl.1
Natural variantiVAR_0210306R → K.1 PublicationCorresponds to variant rs17884647dbSNPEnsembl.1
Natural variantiVAR_0210318P → S.7 PublicationsCorresponds to variant rs1042703dbSNPEnsembl.1
Natural variantiVAR_07056717T → R in WNCHRS; results in increased MMP14 proteosomal degradation and reduced protein localization to cell membrane. 1 PublicationCorresponds to variant rs587777039dbSNPEnsembl.1
Natural variantiVAR_021032233I → V.1 PublicationCorresponds to variant rs17884841dbSNPEnsembl.1
Natural variantiVAR_021033273D → N.1 PublicationCorresponds to variant rs1042704dbSNPEnsembl.1
Natural variantiVAR_021034302R → W.1 PublicationCorresponds to variant rs17884719dbSNPEnsembl.1
Natural variantiVAR_021035355M → I.1 PublicationCorresponds to variant rs17880989dbSNPEnsembl.1
Natural variantiVAR_031267431R → H.Corresponds to variant rs3751489dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26512 mRNA. Translation: BAA05519.1.
X83535 mRNA. Translation: CAA58519.1.
Z48481 mRNA. Translation: CAA88372.1.
U41078 mRNA. Translation: AAA83770.1.
X90925 mRNA. Translation: CAA62432.1.
AK291325 mRNA. Translation: BAF84014.1.
AY795074 Genomic DNA. Translation: AAV40837.1.
AL135998 Genomic DNA. No translation available.
BC064803 mRNA. Translation: AAH64803.1.
CCDSiCCDS9577.1.
PIRiI38028.
RefSeqiNP_004986.1. NM_004995.3.
UniGeneiHs.2399.

Genome annotation databases

EnsembliENST00000311852; ENSP00000308208; ENSG00000157227.
GeneIDi4323.
KEGGihsa:4323.
UCSCiuc001whc.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26512 mRNA. Translation: BAA05519.1.
X83535 mRNA. Translation: CAA58519.1.
Z48481 mRNA. Translation: CAA88372.1.
U41078 mRNA. Translation: AAA83770.1.
X90925 mRNA. Translation: CAA62432.1.
AK291325 mRNA. Translation: BAF84014.1.
AY795074 Genomic DNA. Translation: AAV40837.1.
AL135998 Genomic DNA. No translation available.
BC064803 mRNA. Translation: AAH64803.1.
CCDSiCCDS9577.1.
PIRiI38028.
RefSeqiNP_004986.1. NM_004995.3.
UniGeneiHs.2399.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BQQX-ray2.75M114-287[»]
1BUVX-ray2.75M114-287[»]
2MQSNMR-A316-511[»]
3C7XX-ray1.70A316-511[»]
3MA2X-ray2.05A/D112-292[»]
3X23X-ray2.40B563-582[»]
4P3CX-ray1.94M215-227[»]
4P3DX-ray1.95C/M215-227[»]
4QXUX-ray2.30K218-228[»]
ProteinModelPortaliP50281.
SMRiP50281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110466. 9 interactors.
DIPiDIP-35111N.
IntActiP50281. 34 interactors.
MINTiMINT-246780.
STRINGi9606.ENSP00000308208.

Chemistry databases

BindingDBiP50281.
ChEMBLiCHEMBL3869.
DrugBankiDB00786. Marimastat.
GuidetoPHARMACOLOGYi1638.

Protein family/group databases

MEROPSiM10.014.

PTM databases

iPTMnetiP50281.
PhosphoSitePlusiP50281.
SwissPalmiP50281.

Polymorphism and mutation databases

BioMutaiMMP14.
DMDMi317373419.

Proteomic databases

EPDiP50281.
MaxQBiP50281.
PaxDbiP50281.
PeptideAtlasiP50281.
PRIDEiP50281.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311852; ENSP00000308208; ENSG00000157227.
GeneIDi4323.
KEGGihsa:4323.
UCSCiuc001whc.5. human.

Organism-specific databases

CTDi4323.
DisGeNETi4323.
GeneCardsiMMP14.
H-InvDBHIX0202102.
HGNCiHGNC:7160. MMP14.
HPAiCAB009918.
HPA051432.
MalaCardsiMMP14.
MIMi277950. phenotype.
600754. gene.
neXtProtiNX_P50281.
OpenTargetsiENSG00000157227.
Orphaneti85196. Nodulosis-arthropathy-osteolysis syndrome.
3460. Torg-Winchester syndrome.
PharmGKBiPA30872.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiP50281.
KOiK07763.
OMAiNPESWLQ.
OrthoDBiEOG091G03DP.
PhylomeDBiP50281.
TreeFamiTF352396.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000157227-MONOMER.
ZFISH:ENSG00000157227-MONOMER.
BRENDAi3.4.24.80. 2681.
3.4.24.B5. 2681.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1592389. Activation of Matrix Metalloproteinases.
SIGNORiP50281.

Miscellaneous databases

ChiTaRSiMMP14. human.
EvolutionaryTraceiP50281.
GeneWikiiMMP14.
GenomeRNAii4323.
PROiP50281.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000157227.
CleanExiHS_MMP14.
ExpressionAtlasiP50281. baseline and differential.
GenevisibleiP50281. 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.
IPR028693. MMP14.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021805. Pept_M10A_metallopeptidase_C.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF24. PTHR10201:SF24. 1 hit.
PfamiPF11857. DUF3377. 1 hit.
PF00045. 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 nameiMMP14_HUMAN
AccessioniPrimary (citable) accession number: P50281
Secondary accession number(s): A8K5L0, Q6GSF3, Q92678
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: November 30, 2016
This is version 178 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 14
    Human chromosome 14: 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.