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Q9P2N4

- ATS9_HUMAN

UniProt

Q9P2N4 - ATS9_HUMAN

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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 9

Gene

ADAMTS9

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

Functioni

Cleaves the large aggregating proteoglycans, aggrecan and versican. Has a protease-independent function in promoting the transport from the endoplasmic reticulum to the Golgi apparatus of a variety of secretory cargos.2 Publications

Catalytic activityi

Cleaves aggrecan at the 1838-Glu-|-Ala-1839 site and versican at the 1428-Glu-|-Ala-1429 site.

Cofactori

Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi223 – 2231Zinc; in inhibited formBy similarity
Metal bindingi434 – 4341Zinc; catalyticBy similarity
Active sitei435 – 4351PROSITE-ProRule annotation
Metal bindingi438 – 4381Zinc; catalyticBy similarity
Metal bindingi444 – 4441Zinc; catalyticBy similarity

GO - Molecular functioni

  1. metalloendopeptidase activity Source: InterPro
  2. metallopeptidase activity Source: MGI
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. glycoprotein catabolic process Source: ProtInc
  2. multicellular organismal development Source: ProtInc
  3. positive regulation of melanocyte differentiation Source: Ensembl
  4. protein transport Source: UniProtKB-KW
  5. proteolysis Source: MGI
  6. vesicle-mediated transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

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

MEROPSiM12.021.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 9 (EC:3.4.24.-)
Short name:
ADAM-TS 9
Short name:
ADAM-TS9
Short name:
ADAMTS-9
Gene namesi
Name:ADAMTS9
Synonyms:KIAA1312
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:13202. ADAMTS9.

Subcellular locationi

Secretedextracellular spaceextracellular matrix By similarity. Endoplasmic reticulum 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. extracellular space Source: Ensembl
  3. proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24553.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Propeptidei19 – 287269PRO_0000029182Add
BLAST
Chaini288 – 19351648A disintegrin and metalloproteinase with thrombospondin motifs 9PRO_0000029183Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi135 – 1351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi271 – 2711N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi368 ↔ 418By similarity
Disulfide bondi394 ↔ 400By similarity
Disulfide bondi412 ↔ 494By similarity
Disulfide bondi450 ↔ 478By similarity
Disulfide bondi521 ↔ 543By similarity
Disulfide bondi532 ↔ 553By similarity
Disulfide bondi538 ↔ 572By similarity
Disulfide bondi566 ↔ 577By similarity
Disulfide bondi600 ↔ 637By similarity
Disulfide bondi604 ↔ 642By similarity
Disulfide bondi615 ↔ 627By similarity
Glycosylationi749 – 7491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi840 – 8401N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi890 ↔ 931By similarity
Disulfide bondi894 ↔ 935By similarity
Disulfide bondi904 ↔ 918By similarity
Glycosylationi1213 – 12131N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1250 ↔ 1290By similarity
Disulfide bondi1254 ↔ 1295By similarity
Disulfide bondi1265 ↔ 1278By similarity
Glycosylationi1267 – 12671N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1624 ↔ 1670By similarity
Disulfide bondi1628 ↔ 1675By similarity
Disulfide bondi1639 ↔ 1659By similarity
Glycosylationi1788 – 17881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1806 – 18061N-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

PaxDbiQ9P2N4.
PRIDEiQ9P2N4.

PTM databases

PhosphoSiteiQ9P2N4.

Miscellaneous databases

PMAP-CutDBQ9P2N4.

Expressioni

Tissue specificityi

Highly expressed in all fetal tissues. Expressed in a number of adult tissues with highest expression in heart, placenta and skeletal muscle.

Gene expression databases

BgeeiQ9P2N4.
CleanExiHS_ADAMTS9.
ExpressionAtlasiQ9P2N4. baseline and differential.
GenevestigatoriQ9P2N4.

Organism-specific databases

HPAiHPA028567.
HPA028577.

Interactioni

Protein-protein interaction databases

IntActiQ9P2N4. 1 interaction.
STRINGi9606.ENSP00000418735.

Structurei

3D structure databases

ProteinModelPortaliQ9P2N4.
SMRiQ9P2N4. Positions 293-759.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini293 – 499207Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini509 – 58779DisintegrinAdd
BLAST
Domaini588 – 64356TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini878 – 93659TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini939 – 99759TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini998 – 104952TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini1052 – 110958TSP type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini1110 – 116657TSP type-1 6PROSITE-ProRule annotationAdd
BLAST
Domaini1182 – 124059TSP type-1 7PROSITE-ProRule annotationAdd
BLAST
Domaini1241 – 129656TSP type-1 8PROSITE-ProRule annotationAdd
BLAST
Domaini1328 – 137952TSP type-1 9PROSITE-ProRule annotationAdd
BLAST
Domaini1382 – 144059TSP type-1 10PROSITE-ProRule annotationAdd
BLAST
Domaini1441 – 149454TSP type-1 11PROSITE-ProRule annotationAdd
BLAST
Domaini1497 – 155559TSP type-1 12PROSITE-ProRule annotationAdd
BLAST
Domaini1556 – 161156TSP type-1 13PROSITE-ProRule annotationAdd
BLAST
Domaini1612 – 167665TSP type-1 14PROSITE-ProRule annotationAdd
BLAST
Domaini1677 – 173458TSP type-1 15PROSITE-ProRule annotationAdd
BLAST
Domaini1735 – 1935201GONPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni753 – 877125SpacerAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi221 – 2288Cysteine switchBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi88 – 969Poly-Ser
Compositional biasi644 – 752109Cys-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 ancillary domains, including the TSRs domain, are required for specific extracellular localization and for its versicanase and aggrecanase activities.
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.
The GON domain mediates protease-independent function in ER to Golgi transport.

Sequence similaritiesi

Contains 1 disintegrin domain.Curated
Contains 1 GON domain.PROSITE-ProRule annotation
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
Contains 15 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG237764.
GeneTreeiENSGT00760000118885.
HOGENOMiHOG000004798.
HOVERGENiHBG037334.
InParanoidiQ9P2N4.
KOiK08624.
OMAiCQGERKR.
PhylomeDBiQ9P2N4.
TreeFamiTF331949.

Family and domain databases

Gene3Di3.40.390.10. 2 hits.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR012314. Pept_M12B_GON-ADAMTSs.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF08685. GON. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 13 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 15 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 14 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS51046. GON. 1 hit.
PS50092. TSP1. 14 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9P2N4-3) [UniParc]FASTAAdd to Basket

Also known as: ADAMTS-9B

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

        10         20         30         40         50
MQFVSWATLL TLLVRDLAEM GSPDAAAAVR KDRLHPRQVK LLETLSEYEI
60 70 80 90 100
VSPIRVNALG EPFPTNVHFK RTRRSINSAT DPWPAFASSS SSSTSSQAHY
110 120 130 140 150
RLSAFGQQFL FNLTANAGFI APLFTVTLLG TPGVNQTKFY SEEEAELKHC
160 170 180 190 200
FYKGYVNTNS EHTAVISLCS GMLGTFRSHD GDYFIEPLQS MDEQEDEEEQ
210 220 230 240 250
NKPHIIYRRS APQREPSTGR HACDTSEHKN RHSKDKKKTR ARKWGERINL
260 270 280 290 300
AGDVAALNSG LATEAFSAYG NKTDNTREKR THRRTKRFLS YPRFVEVLVV
310 320 330 340 350
ADNRMVSYHG ENLQHYILTL MSIVASIYKD PSIGNLINIV IVNLIVIHNE
360 370 380 390 400
QDGPSISFNA QTTLKNFCQW QHSKNSPGGI HHDTAVLLTR QDICRAHDKC
410 420 430 440 450
DTLGLAELGT ICDPYRSCSI SEDSGLSTAF TIAHELGHVF NMPHDDNNKC
460 470 480 490 500
KEEGVKSPQH VMAPTLNFYT NPWMWSKCSR KYITEFLDTG YGECLLNEPE
510 520 530 540 550
SRPYPLPVQL PGILYNVNKQ CELIFGPGSQ VCPYMMQCRR LWCNNVNGVH
560 570 580 590 600
KGCRTQHTPW ADGTECEPGK HCKYGFCVPK EMDVPVTDGS WGSWSPFGTC
610 620 630 640 650
SRTCGGGIKT AIRECNRPEP KNGGKYCVGR RMKFKSCNTE PCLKQKRDFR
660 670 680 690 700
DEQCAHFDGK HFNINGLLPN VRWVPKYSGI LMKDRCKLFC RVAGNTAYYQ
710 720 730 740 750
LRDRVIDGTP CGQDTNDICV QGLCRQAGCD HVLNSKARRD KCGVCGGDNS
760 770 780 790 800
SCKTVAGTFN TVHYGYNTVV RIPAGATNID VRQHSFSGET DDDNYLALSS
810 820 830 840 850
SKGEFLLNGN FVVTMAKREI RIGNAVVEYS GSETAVERIN STDRIEQELL
860 870 880 890 900
LQVLSVGKLY NPDVRYSFNI PIEDKPQQFY WNSHGPWQAC SKPCQGERKR
910 920 930 940 950
KLVCTRESDQ LTVSDQRCDR LPQPGHITEP CGTDCDLRWH VASRSECSAQ
960 970 980 990 1000
CGLGYRTLDI YCAKYSRLDG KTEKVDDGFC SSHPKPSNRE KCSGECNTGG
1010 1020 1030 1040 1050
WRYSAWTECS KSCDGGTQRR RAICVNTRND VLDDSKCTHQ EKVTIQRCSE
1060 1070 1080 1090 1100
FPCPQWKSGD WSECLVTCGK GHKHRQVWCQ FGEDRLNDRM CDPETKPTSM
1110 1120 1130 1140 1150
QTCQQPECAS WQAGPWGQCS VTCGQGYQLR AVKCIIGTYM SVVDDNDCNA
1160 1170 1180 1190 1200
ATRPTDTQDC ELPSCHPPPA APETRRSTYS APRTQWRFGS WTPCSATCGK
1210 1220 1230 1240 1250
GTRMRYVSCR DENGSVADES ACATLPRPVA KEECSVTPCG QWKALDWSSC
1260 1270 1280 1290 1300
SVTCGQGRAT RQVMCVNYSD HVIDRSECDQ DYIPETDQDC SMSPCPQRTP
1310 1320 1330 1340 1350
DSGLAQHPFQ NEDYRPRSAS PSRTHVLGGN QWRTGPWGAC SSTCAGGSQR
1360 1370 1380 1390 1400
RVVVCQDENG YTANDCVERI KPDEQRACES GPCPQWAYGN WGECTKLCGG
1410 1420 1430 1440 1450
GIRTRLVVCQ RSNGERFPDL SCEILDKPPD REQCNTHACP HDAAWSTGPW
1460 1470 1480 1490 1500
SSCSVSCGRG HKQRNVYCMA KDGSHLESDY CKHLAKPHGH RKCRGGRCPK
1510 1520 1530 1540 1550
WKAGAWSQCS VSCGRGVQQR HVGCQIGTHK IARETECNPY TRPESERDCQ
1560 1570 1580 1590 1600
GPRCPLYTWR AEEWQECTKT CGEGSRYRKV VCVDDNKNEV HGARCDVSKR
1610 1620 1630 1640 1650
PVDRESCSLQ PCEYVWITGE WSECSVTCGK GYKQRLVSCS EIYTGKENYE
1660 1670 1680 1690 1700
YSYQTTINCP GTQPPSVHPC YLRDCPVSAT WRVGNWGSCS VSCGVGVMQR
1710 1720 1730 1740 1750
SVQCLTNEDQ PSHLCHTDLK PEERKTCRNV YNCELPQNCK EVKRLKGASE
1760 1770 1780 1790 1800
DGEYFLMIRG KLLKIFCAGM HSDHPKEYVT LVHGDSENFS EVYGHRLHNP
1810 1820 1830 1840 1850
TECPYNGSRR DDCQCRKDYT AAGFSSFQKI RIDLTSMQII TTDLQFARTS
1860 1870 1880 1890 1900
EGHPVPFATA GDCYSAAKCP QGRFSINLYG TGLSLTESAR WISQGNYAVS
1910 1920 1930
DIKKSPDGTR VVGKCGGYCG KCTPSSGTGL EVRVL
Length:1,935
Mass (Da):216,491
Last modified:November 4, 2008 - v4
Checksum:i150B78D4C5CC2CCC
GO
Isoform 2 (identifier: Q9P2N4-1) [UniParc]FASTAAdd to Basket

Also known as: Long

The sequence of this isoform differs from the canonical sequence as follows:
     1624-1629: CSVTCG → VPSWEL
     1630-1935: Missing.

Note: May result from the retention of an intron in the cDNA leading to a prematurate stop codon.

Show »
Length:1,629
Mass (Da):182,680
Checksum:iE72B933CEED67809
GO
Isoform 3 (identifier: Q9P2N4-2) [UniParc]FASTAAdd to Basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     1064-1072: CLVTCGKGH → VRWEGCYFP
     1073-1935: Missing.

Show »
Length:1,072
Mass (Da):120,717
Checksum:i85251C8E59449E0C
GO
Isoform 4 (identifier: Q9P2N4-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     324-351: Missing.

Note: No experimental confirmation available.

Show »
Length:1,907
Mass (Da):213,420
Checksum:i24BD2199B1142022
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461S → G in AAF89106. (PubMed:10936055)Curated
Sequence conflicti182 – 1821D → G in AAO15765. (PubMed:12514189)Curated
Sequence conflicti367 – 3671F → L in AAF89106. (PubMed:10936055)Curated
Sequence conflicti1117 – 11171G → V in AAO15765. (PubMed:12514189)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti96 – 961S → P.1 Publication
Corresponds to variant rs36115950 [ dbSNP | Ensembl ].
VAR_047081
Natural varianti96 – 961S → T.
Corresponds to variant rs36115950 [ dbSNP | Ensembl ].
VAR_051592
Natural varianti1579 – 15791K → E.
Corresponds to variant rs17071010 [ dbSNP | Ensembl ].
VAR_047082
Natural varianti1674 – 16741D → E.1 Publication
Corresponds to variant rs6787633 [ dbSNP | Ensembl ].
VAR_047083
Natural varianti1740 – 17401K → R.
Corresponds to variant rs17070967 [ dbSNP | Ensembl ].
VAR_047084
Natural varianti1791 – 17911E → Q.
Corresponds to variant rs3796381 [ dbSNP | Ensembl ].
VAR_047085
Natural varianti1921 – 19211K → E.
Corresponds to variant rs17070909 [ dbSNP | Ensembl ].
VAR_051593
Natural varianti1933 – 19331R → Q.
Corresponds to variant rs17070905 [ dbSNP | Ensembl ].
VAR_047086

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei324 – 35128Missing in isoform 4. 1 PublicationVSP_053399Add
BLAST
Alternative sequencei1064 – 10729CLVTCGKGH → VRWEGCYFP in isoform 3. 1 PublicationVSP_005499
Alternative sequencei1073 – 1935863Missing in isoform 3. 1 PublicationVSP_005500Add
BLAST
Alternative sequencei1624 – 16296CSVTCG → VPSWEL in isoform 2. 1 PublicationVSP_007548
Alternative sequencei1630 – 1935306Missing in isoform 2. 1 PublicationVSP_007549Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF261918 mRNA. Translation: AAF89106.1.
AF488803 mRNA. Translation: AAO15765.1.
AC096888 Genomic DNA. No translation available.
AC122178 Genomic DNA. No translation available.
BC130578 mRNA. Translation: AAI30579.1.
BC171764 mRNA. Translation: AAI71764.1.
AB037733 mRNA. Translation: BAA92550.1.
CCDSiCCDS2903.1. [Q9P2N4-3]
RefSeqiNP_891550.1. NM_182920.1. [Q9P2N4-3]
XP_005265386.1. XM_005265329.1. [Q9P2N4-4]
UniGeneiHs.656071.

Genome annotation databases

EnsembliENST00000295903; ENSP00000295903; ENSG00000163638. [Q9P2N4-4]
ENST00000498707; ENSP00000418735; ENSG00000163638. [Q9P2N4-3]
GeneIDi56999.
KEGGihsa:56999.
UCSCiuc003dmg.3. human. [Q9P2N4-3]
uc003dmh.1. human. [Q9P2N4-1]
uc003dmk.1. human. [Q9P2N4-2]
uc011bfo.2. human.

Polymorphism databases

DMDMi212276516.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF261918 mRNA. Translation: AAF89106.1 .
AF488803 mRNA. Translation: AAO15765.1 .
AC096888 Genomic DNA. No translation available.
AC122178 Genomic DNA. No translation available.
BC130578 mRNA. Translation: AAI30579.1 .
BC171764 mRNA. Translation: AAI71764.1 .
AB037733 mRNA. Translation: BAA92550.1 .
CCDSi CCDS2903.1. [Q9P2N4-3 ]
RefSeqi NP_891550.1. NM_182920.1. [Q9P2N4-3 ]
XP_005265386.1. XM_005265329.1. [Q9P2N4-4 ]
UniGenei Hs.656071.

3D structure databases

ProteinModelPortali Q9P2N4.
SMRi Q9P2N4. Positions 293-759.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9P2N4. 1 interaction.
STRINGi 9606.ENSP00000418735.

Protein family/group databases

MEROPSi M12.021.

PTM databases

PhosphoSitei Q9P2N4.

Polymorphism databases

DMDMi 212276516.

Proteomic databases

PaxDbi Q9P2N4.
PRIDEi Q9P2N4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000295903 ; ENSP00000295903 ; ENSG00000163638 . [Q9P2N4-4 ]
ENST00000498707 ; ENSP00000418735 ; ENSG00000163638 . [Q9P2N4-3 ]
GeneIDi 56999.
KEGGi hsa:56999.
UCSCi uc003dmg.3. human. [Q9P2N4-3 ]
uc003dmh.1. human. [Q9P2N4-1 ]
uc003dmk.1. human. [Q9P2N4-2 ]
uc011bfo.2. human.

Organism-specific databases

CTDi 56999.
GeneCardsi GC03M064501.
HGNCi HGNC:13202. ADAMTS9.
HPAi HPA028567.
HPA028577.
MIMi 605421. gene.
neXtProti NX_Q9P2N4.
PharmGKBi PA24553.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG237764.
GeneTreei ENSGT00760000118885.
HOGENOMi HOG000004798.
HOVERGENi HBG037334.
InParanoidi Q9P2N4.
KOi K08624.
OMAi CQGERKR.
PhylomeDBi Q9P2N4.
TreeFami TF331949.

Enzyme and pathway databases

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

GeneWikii ADAMTS9.
GenomeRNAii 56999.
NextBioi 35481460.
PMAP-CutDB Q9P2N4.
PROi Q9P2N4.
SOURCEi Search...

Gene expression databases

Bgeei Q9P2N4.
CleanExi HS_ADAMTS9.
ExpressionAtlasi Q9P2N4. baseline and differential.
Genevestigatori Q9P2N4.

Family and domain databases

Gene3Di 3.40.390.10. 2 hits.
InterProi IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR012314. Pept_M12B_GON-ADAMTSs.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view ]
Pfami PF05986. ADAM_spacer1. 1 hit.
PF08685. GON. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 13 hits.
[Graphical view ]
PRINTSi PR01857. ADAMTSFAMILY.
SMARTi SM00209. TSP1. 15 hits.
[Graphical view ]
SUPFAMi SSF82895. SSF82895. 14 hits.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS51046. GON. 1 hit.
PS50092. TSP1. 14 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "ADAMTS 9, a novel member of the ADAM-TS/Metallospondin gene family."
    Clark M.E., Kelner G.S., Turbeville L.A., Boyer A., Arden K.A., Maki R.A.
    Genomics 67:343-350(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Fetus.
  2. "Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1."
    Somerville R.P., Longpre J.-M., Jungers K.A., Engle J.M., Ross M., Evanko S., Wight T.N., Leduc R., Apte S.S.
    J. Biol. Chem. 278:9503-9513(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, VARIANTS PRO-96 AND GLU-1674.
  3. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [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 1 AND 4).
  5. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 159-1935 (ISOFORM 2).
    Tissue: Brain.
  6. "Identification of a novel ADAMTS9/GON-1 function for protein transport from the ER to the Golgi."
    Yoshina S., Sakaki K., Yonezumi-Hayashi A., Gengyo-Ando K., Inoue H., Iino Y., Mitani S.
    Mol. Biol. Cell 23:1728-1741(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSPORT, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiATS9_HUMAN
AccessioniPrimary (citable) accession number: Q9P2N4
Secondary accession number(s): A1L4L0
, B7ZVX9, B9ZVN0, Q9NR29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 4, 2008
Last modified: October 29, 2014
This is version 139 of the entry and version 4 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 3
    Human chromosome 3: 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