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O75173

- ATS4_HUMAN

UniProt

O75173 - ATS4_HUMAN

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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 4

Gene

ADAMTS4

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

Functioni

Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. Could also be a critical factor in the exacerbation of neurodegeneration in Alzheimer disease. Cleaves aggrecan at the '392-Glu-|-Ala-393' site.

Catalytic activityi

Glutamyl endopeptidase; bonds cleaved include 370-Thr-Glu-Gly-Glu-|-Ala-Arg-Gly-Ser-377 in the interglobular domain of mammalian aggrecan.

Cofactori

Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi194 – 1941Zinc; in inhibited formBy similarity
Metal bindingi361 – 3611Zinc; catalytic
Active sitei362 – 36211 PublicationPROSITE-ProRule annotation
Metal bindingi365 – 3651Zinc; catalytic
Metal bindingi371 – 3711Zinc; catalytic

GO - Molecular functioni

  1. metalloendopeptidase activity Source: Ensembl
  2. metallopeptidase activity Source: ProtInc
  3. peptidase activity Source: ProtInc
  4. protease binding Source: BHF-UCL
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. defense response to bacterium Source: Ensembl
  2. extracellular matrix disassembly Source: Reactome
  3. extracellular matrix organization Source: Reactome
  4. proteolysis Source: ProtInc
  5. skeletal system development Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000158859-MONOMER.
BRENDAi3.4.24.82. 2681.
ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_200626. O-glycosylation of TSR domain-containing proteins.
REACT_201925. Degradation of the extracellular matrix.

Protein family/group databases

MEROPSiM12.221.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 4 (EC:3.4.24.82)
Short name:
ADAM-TS 4
Short name:
ADAM-TS4
Short name:
ADAMTS-4
Alternative name(s):
ADMP-1
Aggrecanase-1
Gene namesi
Name:ADAMTS4
Synonyms:KIAA0688
ORF Names:UNQ769/PRO1563
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:220. ADAMTS4.

Subcellular locationi

GO - Cellular componenti

  1. extracellular matrix Source: UniProtKB
  2. extracellular region Source: Reactome
  3. extracellular space Source: BHF-UCL
  4. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24548.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5151Sequence AnalysisAdd
BLAST
Propeptidei52 – 212161PRO_0000029164Add
BLAST
Chaini213 – 837625A disintegrin and metalloproteinase with thrombospondin motifs 4PRO_0000029165Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi293 ↔ 3451 Publication
Disulfide bondi322 ↔ 3271 Publication
Disulfide bondi339 ↔ 4231 Publication
Disulfide bondi377 ↔ 4071 Publication
Disulfide bondi449 ↔ 4721 Publication
Disulfide bondi460 ↔ 4821 Publication
Disulfide bondi467 ↔ 5011 Publication
Disulfide bondi495 ↔ 5061 Publication
Disulfide bondi532 ↔ 569By similarity
Disulfide bondi536 ↔ 574By similarity
Disulfide bondi547 ↔ 559By similarity

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.
Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity).By similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiO75173.
PRIDEiO75173.

PTM databases

PhosphoSiteiO75173.

Miscellaneous databases

PMAP-CutDBO75173.

Expressioni

Tissue specificityi

Expressed in brain, lung and heart. Expressed at very low level in placenta and skeletal muscles.

Inductioni

By IL1/interleukin-1.

Gene expression databases

BgeeiO75173.
CleanExiHS_ADAMTS4.
ExpressionAtlasiO75173. baseline and differential.
GenevestigatoriO75173.

Organism-specific databases

HPAiCAB025876.

Interactioni

Subunit structurei

Interacts with SRPX2.2 Publications

Protein-protein interaction databases

BioGridi114885. 4 interactions.
IntActiO75173. 2 interactions.
STRINGi9606.ENSP00000356975.

Structurei

Secondary structure

1
837
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi218 – 2269
Helixi228 – 2347
Helixi235 – 2373
Helixi238 – 25215
Helixi256 – 2583
Beta strandi262 – 27110
Beta strandi274 – 2763
Helixi285 – 29612
Turni297 – 2993
Beta strandi304 – 3063
Beta strandi311 – 3177
Turni322 – 3243
Beta strandi331 – 3333
Turni341 – 3433
Beta strandi345 – 3495
Helixi355 – 36612
Helixi375 – 3817
Beta strandi393 – 3953
Helixi406 – 41712
Turni418 – 4214
Helixi422 – 4243
Helixi439 – 4424
Helixi445 – 4539
Beta strandi463 – 4653
Turni466 – 4683
Beta strandi472 – 4765
Beta strandi479 – 4835
Beta strandi494 – 4963
Beta strandi499 – 5024
Beta strandi505 – 5073

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RJPX-ray2.80A/B/C/D213-520[»]
3B2ZX-ray2.80A/B/C/D/E/F/G/H213-520[»]
ProteinModelPortaliO75173.
SMRiO75173. Positions 215-805.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75173.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini218 – 428211Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini437 – 51983DisintegrinAdd
BLAST
Domaini520 – 57556TSP type-1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni686 – 837152SpacerAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi192 – 1998Cysteine switchBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi247 – 2526Poly-Ala
Compositional biasi577 – 685109Cys-richAdd
BLAST

Domaini

The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.
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

Contains 1 disintegrin domain.Curated
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
Contains 1 TSP type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG271890.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004799.
HOVERGENiHBG004313.
InParanoidiO75173.
KOiK07764.
OMAiHAGCDRI.
OrthoDBiEOG7WDN1M.
PhylomeDBiO75173.
TreeFamiTF331949.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 1 hit.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 1 hit.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O75173-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQTGSHPGR GLAGRWLWGA QPCLLLPIVP LSWLVWLLLL LLASLLPSAR
60 70 80 90 100
LASPLPREEE IVFPEKLNGS VLPGSGAPAR LLCRLQAFGE TLLLELEQDS
110 120 130 140 150
GVQVEGLTVQ YLGQAPELLG GAEPGTYLTG TINGDPESVA SLHWDGGALL
160 170 180 190 200
GVLQYRGAEL HLQPLEGGTP NSAGGPGAHI LRRKSPASGQ GPMCNVKAPL
210 220 230 240 250
GSPSPRPRRA KRFASLSRFV ETLVVADDKM AAFHGAGLKR YLLTVMAAAA
260 270 280 290 300
KAFKHPSIRN PVSLVVTRLV ILGSGEEGPQ VGPSAAQTLR SFCAWQRGLN
310 320 330 340 350
TPEDSDPDHF DTAILFTRQD LCGVSTCDTL GMADVGTVCD PARSCAIVED
360 370 380 390 400
DGLQSAFTAA HELGHVFNML HDNSKPCISL NGPLSTSRHV MAPVMAHVDP
410 420 430 440 450
EEPWSPCSAR FITDFLDNGY GHCLLDKPEA PLHLPVTFPG KDYDADRQCQ
460 470 480 490 500
LTFGPDSRHC PQLPPPCAAL WCSGHLNGHA MCQTKHSPWA DGTPCGPAQA
510 520 530 540 550
CMGGRCLHMD QLQDFNIPQA GGWGPWGPWG DCSRTCGGGV QFSSRDCTRP
560 570 580 590 600
VPRNGGKYCE GRRTRFRSCN TEDCPTGSAL TFREEQCAAY NHRTDLFKSF
610 620 630 640 650
PGPMDWVPRY TGVAPQDQCK LTCQAQALGY YYVLEPRVVD GTPCSPDSSS
660 670 680 690 700
VCVQGRCIHA GCDRIIGSKK KFDKCMVCGG DGSGCSKQSG SFRKFRYGYN
710 720 730 740 750
NVVTIPAGAT HILVRQQGNP GHRSIYLALK LPDGSYALNG EYTLMPSPTD
760 770 780 790 800
VVLPGAVSLR YSGATAASET LSGHGPLAQP LTLQVLVAGN PQDTRLRYSF
810 820 830
FVPRPTPSTP RPTPQDWLHR RAQILEILRR RPWAGRK
Length:837
Mass (Da):90,197
Last modified:January 11, 2011 - v3
Checksum:i0C05299D7FB23A8D
GO

Sequence cautioni

The sequence BAA31663.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti306 – 3061D → G in AAQ89245. (PubMed:12975309)Curated
Sequence conflicti682 – 6821G → R in AAL02262. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41T → I.1 Publication
Corresponds to variant rs17855814 [ dbSNP | Ensembl ].
VAR_030636
Natural varianti77 – 771A → T.1 Publication
Corresponds to variant rs34448954 [ dbSNP | Ensembl ].
VAR_057073
Natural varianti304 – 3041D → N.1 Publication
Corresponds to variant rs17855813 [ dbSNP | Ensembl ].
VAR_030637
Natural varianti369 – 3691M → V.1 Publication
Corresponds to variant rs17855812 [ dbSNP | Ensembl ].
VAR_030638
Natural varianti552 – 5521P → T.1 Publication
Corresponds to variant rs17855815 [ dbSNP | Ensembl ].
VAR_030639
Natural varianti564 – 5641T → A.1 Publication
Corresponds to variant rs17855816 [ dbSNP | Ensembl ].
VAR_030640
Natural varianti626 – 6261Q → R.3 Publications
Corresponds to variant rs4233367 [ dbSNP | Ensembl ].
VAR_022450
Natural varianti836 – 8361R → K.
Corresponds to variant rs11807350 [ dbSNP | Ensembl ].
VAR_030641

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF148213 mRNA. Translation: AAD41494.1.
AY044847 Genomic DNA. Translation: AAL02262.1.
AB014588 mRNA. Translation: BAA31663.2. Different initiation.
AY358886 mRNA. Translation: AAQ89245.1.
AL590714 Genomic DNA. Translation: CAH72146.1.
BC063293 mRNA. Translation: AAH63293.1.
CCDSiCCDS1223.1.
PIRiT00355.
RefSeqiNP_005090.3. NM_005099.4.
UniGeneiHs.211604.

Genome annotation databases

EnsembliENST00000367996; ENSP00000356975; ENSG00000158859.
GeneIDi9507.
KEGGihsa:9507.
UCSCiuc001fyt.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF148213 mRNA. Translation: AAD41494.1 .
AY044847 Genomic DNA. Translation: AAL02262.1 .
AB014588 mRNA. Translation: BAA31663.2 . Different initiation.
AY358886 mRNA. Translation: AAQ89245.1 .
AL590714 Genomic DNA. Translation: CAH72146.1 .
BC063293 mRNA. Translation: AAH63293.1 .
CCDSi CCDS1223.1.
PIRi T00355.
RefSeqi NP_005090.3. NM_005099.4.
UniGenei Hs.211604.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2RJP X-ray 2.80 A/B/C/D 213-520 [» ]
3B2Z X-ray 2.80 A/B/C/D/E/F/G/H 213-520 [» ]
ProteinModelPortali O75173.
SMRi O75173. Positions 215-805.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114885. 4 interactions.
IntActi O75173. 2 interactions.
STRINGi 9606.ENSP00000356975.

Chemistry

BindingDBi O75173.
ChEMBLi CHEMBL2318.
DrugBanki DB06822. Tinzaparin.

Protein family/group databases

MEROPSi M12.221.

PTM databases

PhosphoSitei O75173.

Proteomic databases

PaxDbi O75173.
PRIDEi O75173.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367996 ; ENSP00000356975 ; ENSG00000158859 .
GeneIDi 9507.
KEGGi hsa:9507.
UCSCi uc001fyt.4. human.

Organism-specific databases

CTDi 9507.
GeneCardsi GC01M161159.
H-InvDB HIX0001237.
HGNCi HGNC:220. ADAMTS4.
HPAi CAB025876.
MIMi 603876. gene.
neXtProti NX_O75173.
PharmGKBi PA24548.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG271890.
GeneTreei ENSGT00760000118880.
HOGENOMi HOG000004799.
HOVERGENi HBG004313.
InParanoidi O75173.
KOi K07764.
OMAi HAGCDRI.
OrthoDBi EOG7WDN1M.
PhylomeDBi O75173.
TreeFami TF331949.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000158859-MONOMER.
BRENDAi 3.4.24.82. 2681.
Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_200626. O-glycosylation of TSR domain-containing proteins.
REACT_201925. Degradation of the extracellular matrix.

Miscellaneous databases

ChiTaRSi ADAMTS4. human.
EvolutionaryTracei O75173.
GeneWikii ADAMTS4.
GenomeRNAii 9507.
NextBioi 35624.
PMAP-CutDB O75173.
PROi O75173.
SOURCEi Search...

Gene expression databases

Bgeei O75173.
CleanExi HS_ADAMTS4.
ExpressionAtlasi O75173. baseline and differential.
Genevestigatori O75173.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
InterProi IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view ]
Pfami PF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 1 hit.
[Graphical view ]
PRINTSi PR01857. ADAMTSFAMILY.
SMARTi SM00209. TSP1. 1 hit.
[Graphical view ]
SUPFAMi SSF82895. SSF82895. 1 hit.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-626.
  2. "ADAMTS-4 genomic locus."
    Sawaji Y., Nagase H., Saklatvala J., Clark A.R.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS THR-77 AND ARG-626.
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-626.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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], VARIANTS ILE-4; ASN-304; VAL-369; THR-552 AND ALA-564.
    Tissue: Brain.
  7. "The thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage."
    Tortorella M.D., Pratta M.A., Liu R.-Q., Abbaszade I., Ross H., Burn T.C., Arner E.C.
    J. Biol. Chem. 275:25791-25797(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
  8. "Epileptic and developmental disorders of the speech cortex: ligand/receptor interaction of wild-type and mutant SRPX2 with the plasminogen activator receptor uPAR."
    Royer-Zemmour B., Ponsole-Lenfant M., Gara H., Roll P., Leveque C., Massacrier A., Ferracci G., Cillario J., Robaglia-Schlupp A., Vincentelli R., Cau P., Szepetowski P.
    Hum. Mol. Genet. 17:3617-3630(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRPX2.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 213-520 ALONE AND IN COMPLEX WITH INHIBITOR, ACTIVE SITE, COFACTOR, ZINC-BINDING SITES, DISULFIDE BONDS.

Entry informationi

Entry nameiATS4_HUMAN
AccessioniPrimary (citable) accession number: O75173
Secondary accession number(s): Q5VTW2
, Q6P4Q8, Q6UWA8, Q9UN83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 11, 2011
Last modified: October 29, 2014
This is version 154 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

Caution

Has sometimes been referred to as ADAMTS2.Curated

Keywords - Technical termi

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

Documents

  1. Human chromosome 1
    Human chromosome 1: 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