P59510 (ATS20_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 20
Short name=ADAM-TS 20
Short name=ADAM-TS20
Short name=ADAMTS-20
EC=3.4.24.-

Gene names

Name:

ADAMTS20

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1910 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	May play a role in tissue-remodeling process occurring in both normal and pathological conditions.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Tissue specificity	Very sparingly expressed, although is detected at low levels in testis, prostate, ovary, heart, placenta, lung and pancreas. Overexpressed in several brain, colon and breast carcinomas.
Post-translational modification	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.
Sequence similarities	Contains 1 disintegrin domain. Contains 1 GON domain. Contains 1 peptidase M12B domain. Contains 15 TSP type-1 domains.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P59510-1)

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.

Isoform 2 (identifier: P59510-2)

The sequence of this isoform differs from the canonical sequence as follows:
     683-693: THDICVQGQCM → SYNIDCNCVLK
     1429-1504: CSASCGKGRK...QRDVYCRLKG → EDLKVKLLPQ...GDLKYYKNSL
     1505-1910: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Propeptide	22 – 253	232	By similarity		PRO_0000029206
	Chain	254 – 1910	1657	A disintegrin and metalloproteinase with thrombospondin motifs 20		PRO_0000029207
Regions
	Domain	259 – 467	209	Peptidase M12B
	Domain	468 – 555	88	Disintegrin
	Domain	556 – 611	56	TSP type-1 1
	Domain	846 – 904	59	TSP type-1 2
	Domain	905 – 961	57	TSP type-1 3
	Domain	966 – 1023	58	TSP type-1 4
	Domain	1024 – 1073	50	TSP type-1 5
	Domain	1076 – 1135	60	TSP type-1 6
	Domain	1152 – 1206	55	TSP type-1 7
	Domain	1207 – 1264	58	TSP type-1 8
	Domain	1304 – 1356	53	TSP type-1 9
	Domain	1358 – 1416	59	TSP type-1 10
	Domain	1417 – 1475	59	TSP type-1 11
	Domain	1476 – 1531	56	TSP type-1 12
	Domain	1535 – 1588	54	TSP type-1 13
	Domain	1589 – 1652	64	TSP type-1 14
	Domain	1654 – 1710	57	TSP type-1 15
	Domain	1711 – 1910	200	GON
	Region	724 – 846	123	Spacer
	Compositional bias	612 – 723	112	Cys-rich
Sites
	Active site	404	1	By similarity
	Metal binding	403	1	Zinc; catalytic By similarity
	Metal binding	407	1	Zinc; catalytic By similarity
	Metal binding	413	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	92	1	N-linked (GlcNAc...) Potential
	Glycosylation	191	1	N-linked (GlcNAc...) Potential
	Glycosylation	445	1	N-linked (GlcNAc...) Potential
	Glycosylation	702	1	N-linked (GlcNAc...) Potential
	Glycosylation	717	1	N-linked (GlcNAc...) Potential
	Glycosylation	728	1	N-linked (GlcNAc...) Potential
	Glycosylation	809	1	N-linked (GlcNAc...) Potential
	Glycosylation	870	1	N-linked (GlcNAc...) Potential
	Glycosylation	1061	1	N-linked (GlcNAc...) Potential
	Glycosylation	1456	1	N-linked (GlcNAc...) Potential
	Glycosylation	1542	1	N-linked (GlcNAc...) Potential
	Glycosylation	1572	1	N-linked (GlcNAc...) Potential
	Glycosylation	1763	1	N-linked (GlcNAc...) Potential
	Glycosylation	1781	1	N-linked (GlcNAc...) Potential
	Glycosylation	1852	1	N-linked (GlcNAc...) Potential
	Disulfide bond	381 ↔ 462		By similarity
	Disulfide bond	419 ↔ 446		By similarity
	Disulfide bond	568 ↔ 605		By similarity
	Disulfide bond	572 ↔ 610		By similarity
	Disulfide bond	583 ↔ 595		By similarity
Natural variations
	Alternative sequence	683 – 693	11	THDICVQGQCM → SYNIDCNCVLK in isoform 2.		VSP_007106
	Alternative sequence	1429 – 1504	76	CSASC…CRLKG → EDLKVKLLPQRTIILWELMK NIFCHGKHSHMYLINVVTDH LLYPRHCDPETIETYFLSLW SLQFTWGDLKYYKNSL in isoform 2.		VSP_007107
	Alternative sequence	1505 – 1910	406	Missing in isoform 2.		VSP_007108
	Natural variant	876	1	K → M. Corresponds to variant rs7302446 [ dbSNP | Ensembl ].		VAR_057088
	Natural variant	1000	1	R → H. Corresponds to variant rs7297737 [ dbSNP | Ensembl ].		VAR_057089
	Natural variant	1273	1	S → F. Corresponds to variant rs7310011 [ dbSNP | Ensembl ].		VAR_057090
Experimental info
	Sequence conflict	152	1	T → V in CAD56159. Ref.2
	Sequence conflict	152	1	T → V in CAD56160. Ref.2
	Sequence conflict	360	1	E → Y in CAD56159. Ref.2
	Sequence conflict	360	1	E → Y in CAD56160. Ref.2
	Sequence conflict	371	1	M → T in AAO15766. Ref.1
	Sequence conflict	456	1	D → E in CAD56159. Ref.2
	Sequence conflict	456	1	D → E in CAD56160. Ref.2
	Sequence conflict	648	1	I → V in CAD56159. Ref.2
	Sequence conflict	648	1	I → V in CAD56160. Ref.2
	Sequence conflict	792 – 793	2	Missing in CAD56159. Ref.2
	Sequence conflict	792 – 793	2	Missing in CAD56160. Ref.2
	Sequence conflict	818 – 821	4	ILIE → LILQ in AAO15766. Ref.1
	Sequence conflict	908 – 912	5	WHVIG → GMLLAK in AAO15766. Ref.1
	Sequence conflict	1315	1	S → Q in CAD56159. Ref.2
	Sequence conflict	1315	1	S → Q in CAD56160. Ref.2
	Sequence conflict	1327	1	R → T in AAO15766. Ref.1
	Sequence conflict	1816	1	T → A in CAD56159. Ref.2
	Sequence conflict	1881	1	E → Q in CAD56159. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: D7FFCB0D56F4B6D9	FASTA	1,910	214,721
	10 20 30 40 50 60 MWVAKWLTGL LYHLSLFITR SWEVDFHPRQ EALVRTLTSY EVVIPERVNE FGEVFPQSHH 70 80 90 100 110 120 FSRQKRSSEA LEPMPFRTHY RFTAYGQLFQ LNLTADASFL AAGYTEVHLG TPERGAWESD 130 140 150 160 170 180 AGPSDLRHCF YRGQVNSQED YKAVVSLCGG LTGTFKGQNG EYFLEPIMKA DGNEYEDGHN 190 200 210 220 230 240 KPHLIYRQDL NNSFLQTLKY CSVSESQIKE TSLPFHTYSN MNEDLNVMKE RVLGHTSKNV 250 260 270 280 290 300 PLKDERRHSR KKRLISYPRY IEIMVTADAK VVSAHGSNLQ NYILTLMSIV ATIYKDPSIG 310 320 330 340 350 360 NLIHIVVVKL VMIHREEEGP VINFDGATTL KNFCSWQQTQ NDLDDVHPSH HDTAVLITRE 370 380 390 400 410 420 DICSSKEKCN MLGLSYLGTI CDPLQSCFIN EEKGLISAFT IAHELGHTLG VQHDDNPRCK 430 440 450 460 470 480 EMKVTKYHVM APALSFHMSP WSWSNCSRKY VTEFLDTGYG ECLLDKPDEE IYNLPSELPG 490 500 510 520 530 540 SRYDGNKQCE LAFGPGSQMC PHINICMHLW CTSTEKLHKG CFTQHVPPAD GTDCGPGMHC 550 560 570 580 590 600 RHGLCVNKET ETRPVNGEWG PWEPYSSCSR TCGGGIESAT RRCNRPEPRN GGNYCVGRRM 610 620 630 640 650 660 KFRSCNTDSC PKGTQDFREK QCSDFNGKHL DISGIPSNVR WLPRYSGIGT KDRCKLYCQV 670 680 690 700 710 720 AGTNYFYLLK DMVEDGTPCG TETHDICVQG QCMAAGCDHV LNSSAKIDKC GVCGGDNSSC 730 740 750 760 770 780 KTITGVFNSS HYGYNVVVKI PAGATNVDIR QYSYSGQPDD SYLALSDAEG NFLFNGNFLL 790 800 810 820 830 840 STSKKEINVQ GTRTVIEYSG SNNAVERINS TNRQEKEILI EVLCVGNLYN PDVHYSFNIP 850 860 870 880 890 900 LEERSDMFTW DPYGPWEGCT KMCQGLQRRN ITCIHKSDHS VVSDKECDHL PLPSFVTQSC 910 920 930 940 950 960 NTDCELRWHV IGKSECSSQC GQGYRTLDIH CMKYSIHEGQ TVQVDDHYCG DQLKPPTQEL 970 980 990 1000 1010 1020 CHGNCVFTRW HYSEWSQCSR SCGGGERSRE SYCMNNFGHR LADNECQELS RVTRENCNEF 1030 1040 1050 1060 1070 1080 SCPSWAASEW SECLVTCGKG TKQRQVWCQL NVDHLSDGFC NSSTKPESLS PCELHTCASW 1090 1100 1110 1120 1130 1140 QVGPWGPCTT TCGHGYQMRD VKCVNELASA VLEDTECHEA SRPSDRQSCV LTPCSFISKL 1150 1160 1170 1180 1190 1200 ETALLPTVLI KKMAQWRHGS WTPCSVSCGR GTQARYVSCR DALDRIADES YCAHLPRPAE 1210 1220 1230 1240 1250 1260 IWDCFTPCGE WQAGDWSPCS ASCGHGKTTR QVLCMNYHQP IDENYCDPEV RPLMEQECSL 1270 1280 1290 1300 1310 1320 AACPPAHSHF PSSPVQPSYY LSTNLPLTQK LEDNENQVVH PSVRGNQWRT GPWGSCSSSC 1330 1340 1350 1360 1370 1380 SGGLQHRAVV CQDENGQSAS YCDAASKPPE LQQCGPGPCP QWNYGNWGEC SQTCGGGIKS 1390 1400 1410 1420 1430 1440 RLVICQFPNG QILEDHNCEI VNKPPSVIQC HMHACPADVS WHQEPWTSCS ASCGKGRKYR 1450 1460 1470 1480 1490 1500 EVFCIDQFQR KLEDTNCSQV QKPPTHKACR SVRCPSWKAN SWNECSVTCG SGVQQRDVYC 1510 1520 1530 1540 1550 1560 RLKGVGQVVE EMCDQSTRPC SQRRCWSQDC VQHKGMERGR LNCSTSCERK DSHQRMECTD 1570 1580 1590 1600 1610 1620 NQIRQVNEIV YNSSTISLTS KNCRNPPCNY IVVTADSSQC ANNCGFSYRQ RITYCTEIPS 1630 1640 1650 1660 1670 1680 TKKHKLHRLR PIVYQECPVV PSSQVYQCIN SCLHLATWKV GKWSKCSVTC GIGIMKRQVK 1690 1700 1710 1720 1730 1740 CITKHGLSSD LCLNHLKPGA QKKCYANDCK SFTTCKEIQV KNHIRKDGDY YLNIKGRIIK 1750 1760 1770 1780 1790 1800 IYCADMYLEN PKEYLTLVQG EENFSEVYGF RLKNPYQCPF NGSRREDCEC DNGHLAAGYT 1810 1820 1830 1840 1850 1860 VFSKIRIDLT SMQIKTTDLL FSKTIFGNAV PFATAGDCYS AFRCPQGQFS INLSGTGMKI 1870 1880 1890 1900 1910 SSTAKWLTQG SYTSVSIRRS EDGTRFFGKC GGYCGKCLPH MTTGLPIQVI
	Isoform 2 [UniParc]. Checksum: 2F9D75248EE885DF	FASTA	1,504	169,506
	10 20 30 40 50 60 MWVAKWLTGL LYHLSLFITR SWEVDFHPRQ EALVRTLTSY EVVIPERVNE FGEVFPQSHH 70 80 90 100 110 120 FSRQKRSSEA LEPMPFRTHY RFTAYGQLFQ LNLTADASFL AAGYTEVHLG TPERGAWESD 130 140 150 160 170 180 AGPSDLRHCF YRGQVNSQED YKAVVSLCGG LTGTFKGQNG EYFLEPIMKA DGNEYEDGHN 190 200 210 220 230 240 KPHLIYRQDL NNSFLQTLKY CSVSESQIKE TSLPFHTYSN MNEDLNVMKE RVLGHTSKNV 250 260 270 280 290 300 PLKDERRHSR KKRLISYPRY IEIMVTADAK VVSAHGSNLQ NYILTLMSIV ATIYKDPSIG 310 320 330 340 350 360 NLIHIVVVKL VMIHREEEGP VINFDGATTL KNFCSWQQTQ NDLDDVHPSH HDTAVLITRE 370 380 390 400 410 420 DICSSKEKCN MLGLSYLGTI CDPLQSCFIN EEKGLISAFT IAHELGHTLG VQHDDNPRCK 430 440 450 460 470 480 EMKVTKYHVM APALSFHMSP WSWSNCSRKY VTEFLDTGYG ECLLDKPDEE IYNLPSELPG 490 500 510 520 530 540 SRYDGNKQCE LAFGPGSQMC PHINICMHLW CTSTEKLHKG CFTQHVPPAD GTDCGPGMHC 550 560 570 580 590 600 RHGLCVNKET ETRPVNGEWG PWEPYSSCSR TCGGGIESAT RRCNRPEPRN GGNYCVGRRM 610 620 630 640 650 660 KFRSCNTDSC PKGTQDFREK QCSDFNGKHL DISGIPSNVR WLPRYSGIGT KDRCKLYCQV 670 680 690 700 710 720 AGTNYFYLLK DMVEDGTPCG TESYNIDCNC VLKAAGCDHV LNSSAKIDKC GVCGGDNSSC 730 740 750 760 770 780 KTITGVFNSS HYGYNVVVKI PAGATNVDIR QYSYSGQPDD SYLALSDAEG NFLFNGNFLL 790 800 810 820 830 840 STSKKEINVQ GTRTVIEYSG SNNAVERINS TNRQEKEILI EVLCVGNLYN PDVHYSFNIP 850 860 870 880 890 900 LEERSDMFTW DPYGPWEGCT KMCQGLQRRN ITCIHKSDHS VVSDKECDHL PLPSFVTQSC 910 920 930 940 950 960 NTDCELRWHV IGKSECSSQC GQGYRTLDIH CMKYSIHEGQ TVQVDDHYCG DQLKPPTQEL 970 980 990 1000 1010 1020 CHGNCVFTRW HYSEWSQCSR SCGGGERSRE SYCMNNFGHR LADNECQELS RVTRENCNEF 1030 1040 1050 1060 1070 1080 SCPSWAASEW SECLVTCGKG TKQRQVWCQL NVDHLSDGFC NSSTKPESLS PCELHTCASW 1090 1100 1110 1120 1130 1140 QVGPWGPCTT TCGHGYQMRD VKCVNELASA VLEDTECHEA SRPSDRQSCV LTPCSFISKL 1150 1160 1170 1180 1190 1200 ETALLPTVLI KKMAQWRHGS WTPCSVSCGR GTQARYVSCR DALDRIADES YCAHLPRPAE 1210 1220 1230 1240 1250 1260 IWDCFTPCGE WQAGDWSPCS ASCGHGKTTR QVLCMNYHQP IDENYCDPEV RPLMEQECSL 1270 1280 1290 1300 1310 1320 AACPPAHSHF PSSPVQPSYY LSTNLPLTQK LEDNENQVVH PSVRGNQWRT GPWGSCSSSC 1330 1340 1350 1360 1370 1380 SGGLQHRAVV CQDENGQSAS YCDAASKPPE LQQCGPGPCP QWNYGNWGEC SQTCGGGIKS 1390 1400 1410 1420 1430 1440 RLVICQFPNG QILEDHNCEI VNKPPSVIQC HMHACPADVS WHQEPWTSED LKVKLLPQRT 1450 1460 1470 1480 1490 1500 IILWELMKNI FCHGKHSHMY LINVVTDHLL YPRHCDPETI ETYFLSLWSL QFTWGDLKYY KNSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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).
[2]	"Identification and characterization of ADAMTS-20 defines a novel subfamily of metalloproteinases-disintegrins with multiple thrombospondin-1 repeats and a unique GON domain." Llamazares M., Cal S., Quesada V., Lopez-Otin C. J. Biol. Chem. 278:13382-13389(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Liver.
[3]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., 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., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF488804 mRNA. Translation: AAO15766.1. AJ515153 mRNA. Translation: CAD56159.3. AJ515154 mRNA. Translation: CAD56160.2. AC090525 Genomic DNA. No translation available. AC107018 Genomic DNA. No translation available. AC120104 Genomic DNA. No translation available.
IPI	IPI00414321. IPI00874153.
RefSeq	NP_079279.3. NM_025003.3.
UniGene	Hs.287554.
3D structure databases
ProteinModelPortal	P59510.
ModBase	Search...
Protein-protein interaction databases
IntAct	P59510. 1 interaction.
STRING	9606.ENSP00000374071.
Protein family/group databases
MEROPS	M12.246.
PTM databases
PhosphoSite	P59510.
Polymorphism databases
DMDM	218511943.
Proteomic databases
PaxDb	P59510.
PRIDE	P59510.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	80070.
KEGG	hsa:80070.
UCSC	uc010skx.2. human.
Organism-specific databases
CTD	80070.
GeneCards	GC12M043715.
HGNC	HGNC:17178. ADAMTS20.
HPA	HPA027608. HPA027609.
MIM	611681. gene.
neXtProt	NX_P59510.
PharmGKB	PA134901626.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG237764.
HOGENOM	HOG000004798.
HOVERGEN	HBG037334.
InParanoid	P59510.
KO	K09609.
OrthoDB	EOG4HHP1G.
Gene expression databases
ArrayExpress	P59510.
Bgee	P59510.
CleanEx	HS_ADAMTS20.
Genevestigator	P59510.
GermOnline	ENSG00000173157. Homo sapiens.
Family and domain databases
Gene3D	3.40.390.10. 1 hit.
InterPro	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]
Pfam	PF05986. ADAM_spacer1. 1 hit. PF08685. GON. 1 hit. PF01562. Pep_M12B_propep. 1 hit. PF01421. Reprolysin. 1 hit. PF00090. TSP_1. 11 hits. [Graphical view]
PRINTS	PR01857. ADAMTSFAMILY.
SMART	SM00209. TSP1. 13 hits. [Graphical view]
SUPFAM	SSF82895. TSP1. 12 hits.
PROSITE	PS50215. ADAM_MEPRO. 1 hit. PS00427. DISINTEGRIN_1. False negative. PS50214. DISINTEGRIN_2. False negative. PS51046. GON. 1 hit. PS50092. TSP1. 12 hits. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	80070.
NextBio	70275.
SOURCE	Search...

Entry information

Entry name

ATS20_HUMAN

Accession

Primary (citable) accession number: P59510
Secondary accession number(s): A6NNC9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2003
Last sequence update:	December 16, 2008
Last modified:	May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.