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Q8TE59

- ATS19_HUMAN

UniProt

Q8TE59 - ATS19_HUMAN

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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 19

Gene

ADAMTS19

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

Functioni

Cofactori

Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi294 – 2941Zinc; in inhibited formBy similarity
Metal bindingi482 – 4821Zinc; catalyticBy similarity
Active sitei483 – 4831PROSITE-ProRule annotation
Metal bindingi486 – 4861Zinc; catalyticBy similarity
Metal bindingi492 – 4921Zinc; 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

MEROPSiM12.029.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 19 (EC:3.4.24.-)
Short name:
ADAM-TS 19
Short name:
ADAM-TS19
Short name:
ADAMTS-19
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:17111. ADAMTS19.

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

PharmGKBiPA24545.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Propeptidei22 – 316295By similarityPRO_0000029202Add
BLAST
Chaini317 – 1207891A disintegrin and metalloproteinase with thrombospondin motifs 19PRO_0000029203Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi260 – 2601N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi401 ↔ 466By similarity
Disulfide bondi441 ↔ 448By similarity
Disulfide bondi460 ↔ 540By similarity
Disulfide bondi499 ↔ 524By similarity
Disulfide bondi569 ↔ 593By similarity
Disulfide bondi580 ↔ 601By similarity
Disulfide bondi588 ↔ 620By similarity
Disulfide bondi614 ↔ 625By similarity
Disulfide bondi645 ↔ 680By similarity
Disulfide bondi649 ↔ 685By similarity
Disulfide bondi660 ↔ 670By similarity
Glycosylationi797 – 7971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi907 – 9071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi949 – 9491N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi988 ↔ 1031By similarity
Disulfide bondi992 ↔ 1036By similarity
Disulfide bondi1003 ↔ 1020By similarity
Glycosylationi1009 – 10091N-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

PaxDbiQ8TE59.
PRIDEiQ8TE59.

PTM databases

PhosphoSiteiQ8TE59.

Expressioni

Tissue specificityi

Expressed in fetal lung, but not in any adult tissues examined. Expression was detected in an osteosarcoma cDNA library.

Gene expression databases

BgeeiQ8TE59.
CleanExiHS_ADAMTS19.
ExpressionAtlasiQ8TE59. baseline and differential.
GenevestigatoriQ8TE59.

Organism-specific databases

HPAiHPA056171.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000274487.

Structurei

3D structure databases

ProteinModelPortaliQ8TE59.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini325 – 545221Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini546 – 63388DisintegrinAdd
BLAST
Domaini634 – 68653TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini915 – 97561TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini976 – 103762TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini1039 – 108345TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini1087 – 114458TSP type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini1160 – 119940PLACPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni791 – 914124SpacerAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi292 – 2998Cysteine switchBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi88 – 216129Pro-richAdd
BLAST
Compositional biasi687 – 790104Cys-richAdd
BLAST

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

Contains 1 disintegrin domain.Curated
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
Contains 1 PLAC domain.PROSITE-ProRule annotation
Contains 5 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG259740.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004800.
HOVERGENiHBG050621.
InParanoidiQ8TE59.
KOiK08633.
OMAiEKECKTK.
OrthoDBiEOG722J7P.
PhylomeDBiQ8TE59.
TreeFamiTF313537.

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.
IPR010909. PLAC.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF08686. PLAC. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 4 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 5 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 5 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 5 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8TE59-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRLTHICCCC LLYQLGFLSN GIVSELQFAP DREEWEVVFP ALWRREPVDP
60 70 80 90 100
AGGSGGSADP GWVRGVGGGG SARAQAAGSS REVRSVAPVP LEEPVEGRSE
110 120 130 140 150
SRLRPPPPSE GEEDEELESQ ELPRGSSGAA ALSPGAPASW QPPPPPQPPP
160 170 180 190 200
SPPPAQHAEP DGDEVLLRIP AFSRDLYLLL RRDGRFLAPR FAVEQRPNPG
210 220 230 240 250
PGPTGAASAP QPPAPPDAGC FYTGAVLRHP GSLASFSTCG GGLMGFIQLN
260 270 280 290 300
EDFIFIEPLN DTMAITGHPH RVYRQKRSME EKVTEKSALH SHYCGIISDK
310 320 330 340 350
GRPRSRKIAE SGRGKRYSYK LPQEYNIETV VVADPAMVSY HGADAARRFI
360 370 380 390 400
LTILNMVFNL FQHKSLSVQV NLRVIKLILL HETPPELYIG HHGEKMLESF
410 420 430 440 450
CKWQHEEFGK KNDIHLEMST NWGEDMTSVD AAILITRKDF CVHKDEPCDT
460 470 480 490 500
VGIAYLSGMC SEKRKCIIAE DNGLNLAFTI AHEMGHNMGI NHDNDHPSCA
510 520 530 540 550
DGLHIMSGEW IKGQNLGDVS WSRCSKEDLE RFLRSKASNC LLQTNPQSVN
560 570 580 590 600
SVMVPSKLPG MTYTADEQCQ ILFGPLASFC QEMQHVICTG LWCKVEGEKE
610 620 630 640 650
CRTKLDPPMD GTDCDLGKWC KAGECTSRTS APEHLAGEWS LWSPCSRTCS
660 670 680 690 700
AGISSRERKC PGLDSEARDC NGPRKQYRIC ENPPCPAGLP GFRDWQCQAY
710 720 730 740 750
SVRTSSPKHI LQWQAVLDEE KPCALFCSPV GKEQPILLSE KVMDGTSCGY
760 770 780 790 800
QGLDICANGR CQKVGCDGLL GSLAREDHCG VCNGNGKSCK IIKGDFNHTR
810 820 830 840 850
GAGYVEVLVI PAGARRIKVV EEKPAHSYLA LRDAGKQSIN SDWKIEHSGA
860 870 880 890 900
FNLAGTTVHY VRRGLWEKIS AKGPTTAPLH LLVLLFQDQN YGLHYEYTIP
910 920 930 940 950
SDPLPENQSS KAPEPLFMWT HTSWEDCDAT CGGGERKTTV SCTKIMSKNI
960 970 980 990 1000
SIVDNEKCKY LTKPEPQIRK CNEQPCQTRW MMTEWTPCSR TCGKGMQSRQ
1010 1020 1030 1040 1050
VACTQQLSNG TLIRARERDC IGPKPASAQR CEGQDCMTVW EAGVWSECSV
1060 1070 1080 1090 1100
KCGKGIRHRT VRCTNPRKKC VLSTRPREAE DCEDYSKCYV WRMGDWSKCS
1110 1120 1130 1140 1150
ITCGKGMQSR VIQCMHKITG RHGNECFSSE KPAAYRPCHL QPCNEKINVN
1160 1170 1180 1190 1200
TITSPRLAAL TFKCLGDQWP VYCRVIREKN LCQDMRWYQR CCETCRDFYA

QKLQQKS
Length:1,207
Mass (Da):134,048
Last modified:May 18, 2010 - v2
Checksum:i21EFB26660DEB6D9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti367 – 3671S → G in CAC84565. (PubMed:11867212)Curated
Sequence conflicti1048 – 10481C → F in CAC84565. (PubMed:11867212)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti360 – 3601L → I in a breast cancer sample; somatic mutation. 1 Publication
VAR_036154
Natural varianti582 – 5821E → G.
Corresponds to variant rs10062501 [ dbSNP | Ensembl ].
VAR_057087
Natural varianti1089 – 10891Y → F.
Corresponds to variant rs11749126 [ dbSNP | Ensembl ].
VAR_024599

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ311904 mRNA. Translation: CAC84565.1.
AC008425 Genomic DNA. No translation available.
AC008528 Genomic DNA. No translation available.
AC008591 Genomic DNA. No translation available.
AC106781 Genomic DNA. No translation available.
AC129713 Genomic DNA. No translation available.
CCDSiCCDS4146.1.
RefSeqiNP_598377.3. NM_133638.3.
UniGeneiHs.23751.

Genome annotation databases

EnsembliENST00000274487; ENSP00000274487; ENSG00000145808.
GeneIDi171019.
KEGGihsa:171019.
UCSCiuc003kvb.1. human.

Polymorphism databases

DMDMi296434402.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ311904 mRNA. Translation: CAC84565.1 .
AC008425 Genomic DNA. No translation available.
AC008528 Genomic DNA. No translation available.
AC008591 Genomic DNA. No translation available.
AC106781 Genomic DNA. No translation available.
AC129713 Genomic DNA. No translation available.
CCDSi CCDS4146.1.
RefSeqi NP_598377.3. NM_133638.3.
UniGenei Hs.23751.

3D structure databases

ProteinModelPortali Q8TE59.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000274487.

Protein family/group databases

MEROPSi M12.029.

PTM databases

PhosphoSitei Q8TE59.

Polymorphism databases

DMDMi 296434402.

Proteomic databases

PaxDbi Q8TE59.
PRIDEi Q8TE59.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000274487 ; ENSP00000274487 ; ENSG00000145808 .
GeneIDi 171019.
KEGGi hsa:171019.
UCSCi uc003kvb.1. human.

Organism-specific databases

CTDi 171019.
GeneCardsi GC05P128824.
H-InvDB HIX0024810.
HGNCi HGNC:17111. ADAMTS19.
HPAi HPA056171.
MIMi 607513. gene.
neXtProti NX_Q8TE59.
PharmGKBi PA24545.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG259740.
GeneTreei ENSGT00760000118880.
HOGENOMi HOG000004800.
HOVERGENi HBG050621.
InParanoidi Q8TE59.
KOi K08633.
OMAi EKECKTK.
OrthoDBi EOG722J7P.
PhylomeDBi Q8TE59.
TreeFami TF313537.

Enzyme and pathway databases

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

Miscellaneous databases

GenomeRNAii 171019.
NextBioi 89186.
PROi Q8TE59.
SOURCEi Search...

Gene expression databases

Bgeei Q8TE59.
CleanExi HS_ADAMTS19.
ExpressionAtlasi Q8TE59. baseline and differential.
Genevestigatori Q8TE59.

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.
IPR010909. PLAC.
IPR000884. Thrombospondin_1_rpt.
[Graphical view ]
Pfami PF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF08686. PLAC. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 4 hits.
[Graphical view ]
PRINTSi PR01857. ADAMTSFAMILY.
SMARTi SM00209. TSP1. 5 hits.
[Graphical view ]
SUPFAMi SSF82895. SSF82895. 5 hits.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 5 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 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].
  3. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-360.

Entry informationi

Entry nameiATS19_HUMAN
AccessioniPrimary (citable) accession number: Q8TE59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 116 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