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P58397

- ATS12_HUMAN

UniProt

P58397 - ATS12_HUMAN

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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 12

Gene
ADAMTS12, UNQ1918/PRO4389
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Metalloprotease that may play a role in the degradation of COMP. Cleaves also alpha-2 macroglobulin and aggregan. Has anti-tumorigenic properties.3 Publications

Cofactori

Binds 1 zinc ion per subunit By similarity.

Enzyme regulationi

Inhibited by alpha-2 macroglobulin.1 Publication

pH dependencei

Optimum pH is between 7.5 and 9.5 with COMP for substrate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi208 – 2081Zinc; in inhibited form By similarity
Metal bindingi392 – 3921Zinc; catalytic By similarity
Active sitei393 – 3931 By similarity
Metal bindingi396 – 3961Zinc; catalytic By similarity
Metal bindingi402 – 4021Zinc; catalytic By similarity

GO - Molecular functioni

  1. metalloendopeptidase activity Source: BHF-UCL
  2. protein binding Source: IntAct
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell-matrix adhesion Source: BHF-UCL
  2. cell migration Source: BHF-UCL
  3. cellular response to BMP stimulus Source: BHF-UCL
  4. cellular response to interleukin-1 Source: BHF-UCL
  5. cellular response to tumor necrosis factor Source: BHF-UCL
  6. negative regulation of cellular response to hepatocyte growth factor stimulus Source: BHF-UCL
  7. negative regulation of cellular response to vascular endothelial growth factor stimulus Source: BHF-UCL
  8. negative regulation of chondrocyte differentiation Source: BHF-UCL
  9. negative regulation of hepatocyte growth factor receptor signaling pathway Source: BHF-UCL
  10. proteoglycan catabolic process Source: BHF-UCL
  11. proteolysis involved in cellular protein catabolic process Source: BHF-UCL
  12. regulation of endothelial tube morphogenesis Source: BHF-UCL
  13. regulation of inflammatory response Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_200626. O-glycosylation of TSR domain-containing proteins.

Protein family/group databases

MEROPSiM12.237.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 12 (EC:3.4.24.-)
Short name:
ADAM-TS 12
Short name:
ADAM-TS12
Short name:
ADAMTS-12
Gene namesi
ORF Names:UNQ1918/PRO4389
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:14605. ADAMTS12.

Subcellular locationi

GO - Cellular componenti

  1. extracellular matrix Source: BHF-UCL
  2. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24538.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525 Reviewed predictionAdd
BLAST
Propeptidei26 – 240215 By similarityPRO_0000029186Add
BLAST
Chaini241 – 15941354A disintegrin and metalloproteinase with thrombospondin motifs 12PRO_0000029187Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi105 – 1051N-linked (GlcNAc...) Reviewed prediction
Glycosylationi125 – 1251N-linked (GlcNAc...) Reviewed prediction
Glycosylationi215 – 2151N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi322 ↔ 376 By similarity
Disulfide bondi351 ↔ 358 By similarity
Disulfide bondi370 ↔ 451 By similarity
Disulfide bondi409 ↔ 435 By similarity
Disulfide bondi478 ↔ 501 By similarity
Glycosylationi485 – 4851N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi489 ↔ 507 By similarity
Disulfide bondi496 ↔ 526 By similarity
Disulfide bondi520 ↔ 531 By similarity
Disulfide bondi554 ↔ 591 By similarity
Disulfide bondi558 ↔ 596 By similarity
Disulfide bondi569 ↔ 581 By similarity
Glycosylationi685 – 6851N-linked (GlcNAc...) Reviewed prediction
Glycosylationi790 – 7901N-linked (GlcNAc...) Reviewed prediction
Glycosylationi952 – 9521N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1105 – 11051N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1276 – 12761N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1301 – 13011N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1321 – 13211N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1372 – 13721N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1379 – 13791N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1504 – 15041N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.
Subjected to an intracellular maturation process yielding a 120 kDa N-terminal fragment containing the metalloproteinase, disintegrin, one TSP type-1 and the Cys-rich domains and a 83 kDa C-terminal fragment containing the spacer 2 and four TSP type-1 domains.
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.

Keywords - PTMi

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

Proteomic databases

PaxDbiP58397.
PRIDEiP58397.

PTM databases

PhosphoSiteiP58397.

Expressioni

Tissue specificityi

Expressed in skeletal muscle and fat. Detected at significant levels in fetal lung. Widely expressed in gastric carcinomas and in cancer cells of diverse origin.2 Publications

Inductioni

By IFN-alpha and by IL1B/interleukin-1 beta. Up-regulated in articular cartilage and synovium from arthritis patients. Up-regulared in chondrocytes.2 Publications

Gene expression databases

ArrayExpressiP58397.
BgeeiP58397.
CleanExiHS_ADAMTS12.
GenevestigatoriP58397.

Organism-specific databases

HPAiHPA035973.

Interactioni

Subunit structurei

Interacts with COMP.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
COMPP497473EBI-9028051,EBI-2531022
CompQ9R0G63EBI-9028051,EBI-9028018From a different organism.

Protein-protein interaction databases

IntActiP58397. 3 interactions.
STRINGi9606.ENSP00000344847.

Structurei

3D structure databases

ProteinModelPortaliP58397.
SMRiP58397. Positions 246-810.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini246 – 456211Peptidase M12BAdd
BLAST
Domaini465 – 54480DisintegrinAdd
BLAST
Domaini542 – 59756TSP type-1 1Add
BLAST
Domaini823 – 88361TSP type-1 2Add
BLAST
Domaini887 – 94357TSP type-1 3Add
BLAST
Domaini944 – 99754TSP type-1 4Add
BLAST
Domaini1313 – 136654TSP type-1 5Add
BLAST
Domaini1368 – 142255TSP type-1 6Add
BLAST
Domaini1423 – 147149TSP type-1 7Add
BLAST
Domaini1472 – 153261TSP type-1 8Add
BLAST
Domaini1535 – 157541PLACAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni701 – 827127Spacer 1Add
BLAST
Regioni997 – 1316320Spacer 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi208 – 2136Cysteine switch By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi302 – 3054Poly-Glu
Compositional biasi597 – 700104Cys-richAdd
BLAST

Domaini

The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix By similarity.
The C-terminal four TSP1-like repeats are necessary and sufficient for binding COMP.
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.
Contains 1 PLAC domain.
Contains 8 TSP type-1 domains.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG237764.
HOGENOMiHOG000015092.
HOVERGENiHBG050620.
InParanoidiP58397.
KOiK08626.
OMAiPFIMSRQ.
OrthoDBiEOG7V765X.
PhylomeDBiP58397.
TreeFamiTF313537.

Family and domain databases

Gene3Di3.40.390.10. 2 hits.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR010909. PLAC.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 8 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 8 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 8 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 6 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P58397-1) [UniParc]FASTAAdd to Basket

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

MPCAQRSWLA NLSVVAQLLN FGALCYGRQP QPGPVRFPDR RQEHFIKGLP     50
EYHVVGPVRV DASGHFLSYG LHYPITSSRR KRDLDGSEDW VYYRISHEEK 100
DLFFNLTVNQ GFLSNSYIME KRYGNLSHVK MMASSAPLCH LSGTVLQQGT 150
RVGTAALSAC HGLTGFFQLP HGDFFIEPVK KHPLVEGGYH PHIVYRRQKV 200
PETKEPTCGL KDSVNISQKQ ELWREKWERH NLPSRSLSRR SISKERWVET 250
LVVADTKMIE YHGSENVESY ILTIMNMVTG LFHNPSIGNA IHIVVVRLIL 300
LEEEEQGLKI VHHAEKTLSS FCKWQKSINP KSDLNPVHHD VAVLLTRKDI 350
CAGFNRPCET LGLSHLSGMC QPHRSCNINE DSGLPLAFTI AHELGHSFGI 400
QHDGKENDCE PVGRHPYIMS RQLQYDPTPL TWSKCSEEYI TRFLDRGWGF 450
CLDDIPKKKG LKSKVIAPGV IYDVHHQCQL QYGPNATFCQ EVENVCQTLW 500
CSVKGFCRSK LDAAADGTQC GEKKWCMAGK CITVGKKPES IPGGWGRWSP 550
WSHCSRTCGA GVQSAERLCN NPEPKFGGKY CTGERKRYRL CNVHPCRSEA 600
PTFRQMQCSE FDTVPYKNEL YHWFPIFNPA HPCELYCRPI DGQFSEKMLD 650
AVIDGTPCFE GGNSRNVCIN GICKMVGCDY EIDSNATEDR CGVCLGDGSS 700
CQTVRKMFKQ KEGSGYVDIG LIPKGARDIR VMEIEGAGNF LAIRSEDPEK 750
YYLNGGFIIQ WNGNYKLAGT VFQYDRKGDL EKLMATGPTN ESVWIQLLFQ 800
VTNPGIKYEY TIQKDGLDND VEQQMYFWQY GHWTECSVTC GTGIRRQTAH 850
CIKKGRGMVK ATFCDPETQP NGRQKKCHEK ACPPRWWAGE WEACSATCGP 900
HGEKKRTVLC IQTMVSDEQA LPPTDCQHLL KPKTLLSCNR DILCPSDWTV 950
GNWSECSVSC GGGVRIRSVT CAKNHDEPCD VTRKPNSRAL CGLQQCPSSR 1000
RVLKPNKGTI SNGKNPPTLK PVPPPTSRPR MLTTPTGPES MSTSTPAISS 1050
PSPTTASKEG DLGGKQWQDS STQPELSSRY LISTGSTSQP ILTSQSLSIQ 1100
PSEENVSSSD TGPTSEGGLV ATTTSGSGLS SSRNPITWPV TPFYNTLTKG 1150
PEMEIHSGSG EEREQPEDKD ESNPVIWTKI RVPGNDAPVE STEMPLAPPL 1200
TPDLSRESWW PPFSTVMEGL LPSQRPTTSE TGTPRVEGMV TEKPANTLLP 1250
LGGDHQPEPS GKTANRNHLK LPNNMNQTKS SEPVLTEEDA TSLITEGFLL 1300
NASNYKQLTN GHGSAHWIVG NWSECSTTCG LGAYWRRVEC STQMDSDCAA 1350
IQRPDPAKRC HLRPCAGWKV GNWSKCSRNC SGGFKIREIQ CVDSRDHRNL 1400
RPFHCQFLAG IPPPLSMSCN PEPCEAWQVE PWSQCSRSCG GGVQERGVFC 1450
PGGLCDWTKR PTSTMSCNEH LCCHWATGNW DLCSTSCGGG FQKRTVQCVP 1500
SEGNKTEDQD QCLCDHKPRP PEFKKCNQQA CKKSADLLCT KDKLSASFCQ 1550
TLKAMKKCSV PTVRAECCFS CPQTHITHTQ RQRRQRLLQK SKEL 1594
Length:1,594
Mass (Da):177,676
Last modified:September 22, 2009 - v2
Checksum:iC88563125F0F90D8
GO
Isoform 2 (identifier: P58397-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     212-229: DSVNISQKQELWREKWER → GIVTHMSSWVEESVLFFW
     230-1594: Missing.

Show »
Length:229
Mass (Da):26,003
Checksum:i11FBCB40E82091F6
GO
Isoform 3 (identifier: P58397-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     630-714: Missing.

Note: No experimental confirmation available.

Show »
Length:1,509
Mass (Da):168,460
Checksum:i5BF525F456FC8EE5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti110 – 1101Q → E.
Corresponds to variant rs16891862 [ dbSNP | Ensembl ].
VAR_057074
Natural varianti1000 – 10001R → Q.
Corresponds to variant rs13362345 [ dbSNP | Ensembl ].
VAR_057075
Natural varianti1177 – 11771W → R.
Corresponds to variant rs3813474 [ dbSNP | Ensembl ].
VAR_059761
Natural varianti1495 – 14951T → I.1 Publication
Corresponds to variant rs25754 [ dbSNP | Ensembl ].
VAR_058972
Natural varianti1591 – 15911S → P.
Corresponds to variant rs16891281 [ dbSNP | Ensembl ].
VAR_059762

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei212 – 22918DSVNI…EKWER → GIVTHMSSWVEESVLFFW in isoform 2. VSP_013141Add
BLAST
Alternative sequencei230 – 15941365Missing in isoform 2. VSP_013142Add
BLAST
Alternative sequencei630 – 71485Missing in isoform 3. VSP_038151Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti824 – 8241Missing in CAC20419. 1 Publication
Sequence conflicti1336 – 13361R → K in CAC20419. 1 Publication
Sequence conflicti1341 – 13411S → T in CAC20419. 1 Publication
Sequence conflicti1578 – 15781H → R in AAI31734. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ250725 mRNA. Translation: CAC20419.1.
AY358745 mRNA. Translation: AAQ89105.1.
AC008880 Genomic DNA. No translation available.
AC034232 Genomic DNA. No translation available.
AC109491 Genomic DNA. No translation available.
AC139777 Genomic DNA. No translation available.
BC058841 mRNA. Translation: AAH58841.1.
BC131733 mRNA. Translation: AAI31734.1.
BC139900 mRNA. Translation: AAI39901.1.
CCDSiCCDS34140.1. [P58397-1]
RefSeqiNP_112217.2. NM_030955.2. [P58397-1]
UniGeneiHs.12680.

Genome annotation databases

EnsembliENST00000352040; ENSP00000344847; ENSG00000151388. [P58397-3]
ENST00000504830; ENSP00000422554; ENSG00000151388. [P58397-1]
GeneIDi81792.
KEGGihsa:81792.
UCSCiuc003jia.1. human. [P58397-1]
uc010iuq.1. human. [P58397-3]

Polymorphism databases

DMDMi259016182.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ250725 mRNA. Translation: CAC20419.1 .
AY358745 mRNA. Translation: AAQ89105.1 .
AC008880 Genomic DNA. No translation available.
AC034232 Genomic DNA. No translation available.
AC109491 Genomic DNA. No translation available.
AC139777 Genomic DNA. No translation available.
BC058841 mRNA. Translation: AAH58841.1 .
BC131733 mRNA. Translation: AAI31734.1 .
BC139900 mRNA. Translation: AAI39901.1 .
CCDSi CCDS34140.1. [P58397-1 ]
RefSeqi NP_112217.2. NM_030955.2. [P58397-1 ]
UniGenei Hs.12680.

3D structure databases

ProteinModelPortali P58397.
SMRi P58397. Positions 246-810.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P58397. 3 interactions.
STRINGi 9606.ENSP00000344847.

Protein family/group databases

MEROPSi M12.237.

PTM databases

PhosphoSitei P58397.

Polymorphism databases

DMDMi 259016182.

Proteomic databases

PaxDbi P58397.
PRIDEi P58397.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000352040 ; ENSP00000344847 ; ENSG00000151388 . [P58397-3 ]
ENST00000504830 ; ENSP00000422554 ; ENSG00000151388 . [P58397-1 ]
GeneIDi 81792.
KEGGi hsa:81792.
UCSCi uc003jia.1. human. [P58397-1 ]
uc010iuq.1. human. [P58397-3 ]

Organism-specific databases

CTDi 81792.
GeneCardsi GC05M033495.
HGNCi HGNC:14605. ADAMTS12.
HPAi HPA035973.
MIMi 606184. gene.
neXtProti NX_P58397.
PharmGKBi PA24538.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG237764.
HOGENOMi HOG000015092.
HOVERGENi HBG050620.
InParanoidi P58397.
KOi K08626.
OMAi PFIMSRQ.
OrthoDBi EOG7V765X.
PhylomeDBi P58397.
TreeFami TF313537.

Enzyme and pathway databases

Reactomei REACT_200626. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

ChiTaRSi ADAMTS12. human.
GeneWikii ADAMTS12.
GenomeRNAii 81792.
NextBioi 72100.
PROi P58397.
SOURCEi Search...

Gene expression databases

ArrayExpressi P58397.
Bgeei P58397.
CleanExi HS_ADAMTS12.
Genevestigatori P58397.

Family and domain databases

Gene3Di 3.40.390.10. 2 hits.
InterProi IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR010909. PLAC.
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. 8 hits.
[Graphical view ]
PRINTSi PR01857. ADAMTSFAMILY.
SMARTi SM00209. TSP1. 8 hits.
[Graphical view ]
SUPFAMi SSF82895. SSF82895. 8 hits.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 6 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification, characterization, and intracellular processing of ADAM-TS12, a novel human disintegrin with a complex structural organization involving multiple thrombospondin-1 repeats."
    Cal S., Argueelles J.M., Fernandez P.L., Lopez-Otin C.
    J. Biol. Chem. 276:17932-17940(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT ILE-1495.
    Tissue: Fetal lung.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORMS 2 AND 3).
  5. "ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein."
    Liu C.-J., Kong W., Xu K., Luan Y., Ilalov K., Sehgal B., Yu S., Howell R.D., Di Cesare P.E.
    J. Biol. Chem. 281:15800-15808(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH COMP, PH DEPENDENCE, TISSUE SPECIFICITY, INDUCTION.
  6. "The ADAMTS12 metalloproteinase exhibits anti-tumorigenic properties through modulation of the Ras-dependent ERK signalling pathway."
    Llamazares M., Obaya A.J., Moncada-Pazos A., Heljasvaara R., Espada J., Lopez-Otin C., Cal S.
    J. Cell Sci. 120:3544-3552(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Inhibition of ADAMTS-7 and ADAMTS-12 degradation of cartilage oligomeric matrix protein by alpha-2-macroglobulin."
    Luan Y., Kong L., Howell D.R., Ilalov K., Fajardo M., Bai X.-H., Di Cesare P.E., Goldring M.B., Abramson S.B., Liu C.-J.
    Osteoarthritis Cartilage 16:1413-1420(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, INDUCTION.

Entry informationi

Entry nameiATS12_HUMAN
AccessioniPrimary (citable) accession number: P58397
Secondary accession number(s): A2RRN9, A5D6V6, Q6UWL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: September 22, 2009
Last modified: September 3, 2014
This is version 132 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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