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Q8TE58

- ATS15_HUMAN

UniProt

Q8TE58 - ATS15_HUMAN

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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 15

Gene

ADAMTS15

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi174 – 1741Zinc; in inhibited formBy similarity
Metal bindingi361 – 3611Zinc; catalyticBy similarity
Active sitei362 – 3621PROSITE-ProRule annotation
Metal bindingi365 – 3651Zinc; catalyticBy similarity
Metal bindingi371 – 3711Zinc; catalyticBy similarity

GO - Molecular functioni

  1. metalloendopeptidase activity Source: InterPro
  2. zinc ion binding Source: InterPro
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

MEROPSiM12.025.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 15 (EC:3.4.24.-)
Short name:
ADAM-TS 15
Short name:
ADAM-TS15
Short name:
ADAMTS-15
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:16305. ADAMTS15.

Subcellular locationi

GO - Cellular componenti

  1. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24541.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 212195By similarityPRO_0000029192Add
BLAST
Chaini213 – 950738A disintegrin and metalloproteinase with thrombospondin motifs 15PRO_0000029193Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi141 – 1411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi293 ↔ 345By similarity
Disulfide bondi322 ↔ 327By similarity
Disulfide bondi339 ↔ 422By similarity
Disulfide bondi377 ↔ 406By similarity
Disulfide bondi448 ↔ 470By similarity
Disulfide bondi459 ↔ 480By similarity
Disulfide bondi465 ↔ 499By similarity
Disulfide bondi493 ↔ 504By similarity
Disulfide bondi528 ↔ 565By similarity
Disulfide bondi532 ↔ 570By similarity
Disulfide bondi543 ↔ 555By similarity
Glycosylationi591 – 5911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi623 – 6231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi679 – 6791N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity
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

PaxDbiQ8TE58.
PRIDEiQ8TE58.

PTM databases

PhosphoSiteiQ8TE58.

Expressioni

Tissue specificityi

Expressed in fetal liver and kidney, but not in any of the adult tissues examined.

Gene expression databases

BgeeiQ8TE58.
CleanExiHS_ADAMTS15.
GenevestigatoriQ8TE58.

Organism-specific databases

HPAiHPA042867.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000299164.

Structurei

3D structure databases

ProteinModelPortaliQ8TE58.
SMRiQ8TE58. Positions 218-690.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini218 – 427210Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini428 – 51588DisintegrinAdd
BLAST
Domaini516 – 57156TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini839 – 89557TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini896 – 94954TSP type-1 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni701 – 838138SpacerAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi172 – 1798Cysteine switchBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi572 – 700129Cys-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 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 3 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG240910.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004799.
HOVERGENiHBG004313.
InParanoidiQ8TE58.
KOiK08629.
OMAiRGFKRRP.
OrthoDBiEOG7WDN1M.
PhylomeDBiQ8TE58.
TreeFamiTF331949.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR013277. Pept_M12B_ADAM-TS8.
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. 3 hits.
[Graphical view]
PRINTSiPR01861. ADAMTS8.
PR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 3 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 3 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 3 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8TE58-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLLGILTLA FAGRTAGGSE PEREVVVPIR LDPDINGRRY YWRGPEDSGD
60 70 80 90 100
QGLIFQITAF QEDFYLHLTP DAQFLAPAFS TEHLGVPLQG LTGGSSDLRR
110 120 130 140 150
CFYSGDVNAE PDSFAAVSLC GGLRGAFGYR GAEYVISPLP NASAPAAQRN
160 170 180 190 200
SQGAHLLQRR GVPGGPSGDP TSRCGVASGW NPAILRALDP YKPRRAGFGE
210 220 230 240 250
SRSRRRSGRA KRFVSIPRYV ETLVVADESM VKFHGADLEH YLLTLLATAA
260 270 280 290 300
RLYRHPSILN PINIVVVKVL LLRDRDSGPK VTGNAALTLR NFCAWQKKLN
310 320 330 340 350
KVSDKHPEYW DTAILFTRQD LCGATTCDTL GMADVGTMCD PKRSCSVIED
360 370 380 390 400
DGLPSAFTTA HELGHVFNMP HDNVKVCEEV FGKLRANHMM SPTLIQIDRA
410 420 430 440 450
NPWSACSAAI ITDFLDSGHG DCLLDQPSKP ISLPEDLPGA SYTLSQQCEL
460 470 480 490 500
AFGVGSKPCP YMQYCTKLWC TGKAKGQMVC QTRHFPWADG TSCGEGKLCL
510 520 530 540 550
KGACVERHNL NKHRVDGSWA KWDPYGPCSR TCGGGVQLAR RQCTNPTPAN
560 570 580 590 600
GGKYCEGVRV KYRSCNLEPC PSSASGKSFR EEQCEAFNGY NHSTNRLTLA
610 620 630 640 650
VAWVPKYSGV SPRDKCKLIC RANGTGYFYV LAPKVVDGTL CSPDSTSVCV
660 670 680 690 700
QGKCIKAGCD GNLGSKKRFD KCGVCGGDNK SCKKVTGLFT KPMHGYNFVV
710 720 730 740 750
AIPAGASSID IRQRGYKGLI GDDNYLALKN SQGKYLLNGH FVVSAVERDL
760 770 780 790 800
VVKGSLLRYS GTGTAVESLQ ASRPILEPLT VEVLSVGKMT PPRVRYSFYL
810 820 830 840 850
PKEPREDKSS HPKDPRGPSV LHNSVLSLSN QVEQPDDRPP ARWVAGSWGP
860 870 880 890 900
CSASCGSGLQ KRAVDCRGSA GQRTVPACDA AHRPVETQAC GEPCPTWELS
910 920 930 940 950
AWSPCSKSCG RGFQRRSLKC VGHGGRLLAR DQCNLHRKPQ ELDFCVLRPC
Length:950
Mass (Da):103,287
Last modified:June 1, 2002 - v1
Checksum:i5DFBE18285CCCC3B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti623 – 6231N → S.
Corresponds to variant rs11222114 [ dbSNP | Ensembl ].
VAR_051594
Natural varianti770 – 7701Q → R in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036150
Natural varianti878 – 8781C → G in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036151

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ315733 mRNA. Translation: CAC86014.1.
BC109114 mRNA. Translation: AAI09115.1.
CCDSiCCDS8488.1.
RefSeqiNP_620686.1. NM_139055.2.
UniGeneiHs.534221.

Genome annotation databases

EnsembliENST00000299164; ENSP00000299164; ENSG00000166106.
GeneIDi170689.
KEGGihsa:170689.
UCSCiuc010scd.2. human.

Polymorphism databases

DMDMi48474504.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ315733 mRNA. Translation: CAC86014.1 .
BC109114 mRNA. Translation: AAI09115.1 .
CCDSi CCDS8488.1.
RefSeqi NP_620686.1. NM_139055.2.
UniGenei Hs.534221.

3D structure databases

ProteinModelPortali Q8TE58.
SMRi Q8TE58. Positions 218-690.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000299164.

Protein family/group databases

MEROPSi M12.025.

PTM databases

PhosphoSitei Q8TE58.

Polymorphism databases

DMDMi 48474504.

Proteomic databases

PaxDbi Q8TE58.
PRIDEi Q8TE58.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000299164 ; ENSP00000299164 ; ENSG00000166106 .
GeneIDi 170689.
KEGGi hsa:170689.
UCSCi uc010scd.2. human.

Organism-specific databases

CTDi 170689.
GeneCardsi GC11P130318.
HGNCi HGNC:16305. ADAMTS15.
HPAi HPA042867.
MIMi 607509. gene.
neXtProti NX_Q8TE58.
PharmGKBi PA24541.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG240910.
GeneTreei ENSGT00760000118880.
HOGENOMi HOG000004799.
HOVERGENi HBG004313.
InParanoidi Q8TE58.
KOi K08629.
OMAi RGFKRRP.
OrthoDBi EOG7WDN1M.
PhylomeDBi Q8TE58.
TreeFami TF331949.

Enzyme and pathway databases

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

Miscellaneous databases

GenomeRNAii 170689.
NextBioi 89098.
PROi Q8TE58.
SOURCEi Search...

Gene expression databases

Bgeei Q8TE58.
CleanExi HS_ADAMTS15.
Genevestigatori Q8TE58.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
InterProi IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR013277. Pept_M12B_ADAM-TS8.
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. 3 hits.
[Graphical view ]
PRINTSi PR01861. ADAMTS8.
PR01857. ADAMTSFAMILY.
SMARTi SM00209. TSP1. 3 hits.
[Graphical view ]
SUPFAMi SSF82895. SSF82895. 3 hits.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 3 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains."
    Cal S., Obaya A.J., Llamazares M., Garabaya C., Quesada V., Lopez-Otin C.
    Gene 283:49-62(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
  3. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-770 AND GLY-878.

Entry informationi

Entry nameiATS15_HUMAN
AccessioniPrimary (citable) accession number: Q8TE58
Secondary accession number(s): Q32MI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: June 1, 2002
Last modified: November 26, 2014
This is version 116 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

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. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3