P58397 (ATS12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 12
Short name=ADAM-TS 12
Short name=ADAM-TS12
Short name=ADAMTS-12
EC=3.4.24.-

Gene names

Name:	ADAMTS12
ORF Names:	UNQ1918/PRO4389

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	1594 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Metalloprotease that may play a role in the degradation of COMP. Cleaves also alpha-2 macroglobulin and aggregan. Has anti-tumorigenic properties. Ref.5 Ref.6 Ref.7
Cofactor	Binds 1 zinc ion per subunit By similarity.
Enzyme regulation	Inhibited by alpha-2 macroglobulin. Ref.7
Subunit structure	Interacts with COMP. Ref.5
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Tissue specificity	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. Ref.1 Ref.5
Induction	By IFN-alpha and by IL1B/interleukin-1 beta. Up-regulated in articular cartilage and synovium from arthritis patients. Up-regulared in chondrocytes. Ref.5 Ref.7
Domain	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.
Post-translational modification	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.
Sequence similarities	Contains 1 disintegrin domain. Contains 1 peptidase M12B domain. Contains 1 PLAC domain. Contains 8 TSP type-1 domains.
Biophysicochemical properties	pH dependence: Optimum pH is between 7.5 and 9.5 with COMP for substrate.

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 Phosphoprotein 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 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P58397-1)

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: P58397-2)

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

Isoform 3 (identifier: P58397-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Propeptide	26 – 240	215	By similarity		PRO_0000029186
	Chain	241 – 1594	1354	A disintegrin and metalloproteinase with thrombospondin motifs 12		PRO_0000029187
Regions
	Domain	246 – 456	211	Peptidase M12B
	Domain	465 – 544	80	Disintegrin
	Domain	542 – 597	56	TSP type-1 1
	Domain	823 – 883	61	TSP type-1 2
	Domain	887 – 943	57	TSP type-1 3
	Domain	944 – 997	54	TSP type-1 4
	Domain	1313 – 1366	54	TSP type-1 5
	Domain	1368 – 1422	55	TSP type-1 6
	Domain	1423 – 1471	49	TSP type-1 7
	Domain	1472 – 1532	61	TSP type-1 8
	Domain	1535 – 1575	41	PLAC
	Region	701 – 827	127	Spacer 1
	Region	997 – 1316	320	Spacer 2
	Motif	208 – 213	6	Cysteine switch By similarity
	Compositional bias	302 – 305	4	Poly-Glu
	Compositional bias	597 – 700	104	Cys-rich
Sites
	Active site	393	1	By similarity
	Metal binding	208	1	Zinc; in inhibited form By similarity
	Metal binding	392	1	Zinc; catalytic By similarity
	Metal binding	396	1	Zinc; catalytic By similarity
	Metal binding	402	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	982	1	Phosphothreonine By similarity
	Glycosylation	105	1	N-linked (GlcNAc...) Potential
	Glycosylation	125	1	N-linked (GlcNAc...) Potential
	Glycosylation	215	1	N-linked (GlcNAc...) Potential
	Glycosylation	485	1	N-linked (GlcNAc...) Potential
	Glycosylation	685	1	N-linked (GlcNAc...) Potential
	Glycosylation	790	1	N-linked (GlcNAc...) Potential
	Glycosylation	952	1	N-linked (GlcNAc...) Potential
	Glycosylation	1105	1	N-linked (GlcNAc...) Potential
	Glycosylation	1276	1	N-linked (GlcNAc...) Potential
	Glycosylation	1301	1	N-linked (GlcNAc...) Potential
	Glycosylation	1321	1	N-linked (GlcNAc...) Potential
	Glycosylation	1372	1	N-linked (GlcNAc...) Potential
	Glycosylation	1379	1	N-linked (GlcNAc...) Potential
	Glycosylation	1504	1	N-linked (GlcNAc...) Potential
	Disulfide bond	370 ↔ 451		By similarity
	Disulfide bond	409 ↔ 435		By similarity
	Disulfide bond	554 ↔ 591		By similarity
	Disulfide bond	558 ↔ 596		By similarity
	Disulfide bond	569 ↔ 581		By similarity
Natural variations
	Alternative sequence	212 – 229	18	DSVNI…EKWER → GIVTHMSSWVEESVLFFW in isoform 2.		VSP_013141
	Alternative sequence	230 – 1594	1365	Missing in isoform 2.		VSP_013142
	Alternative sequence	630 – 714	85	Missing in isoform 3.		VSP_038151
	Natural variant	110	1	Q → E. Corresponds to variant rs16891862 [ dbSNP | Ensembl ].		VAR_057074
	Natural variant	1000	1	R → Q. Corresponds to variant rs13362345 [ dbSNP | Ensembl ].		VAR_057075
	Natural variant	1177	1	W → R. Corresponds to variant rs3813474 [ dbSNP | Ensembl ].		VAR_059761
	Natural variant	1495	1	T → I. Ref.1 Corresponds to variant rs25754 [ dbSNP | Ensembl ].		VAR_058972
	Natural variant	1591	1	S → P. Corresponds to variant rs16891281 [ dbSNP | Ensembl ].		VAR_059762
Experimental info
	Sequence conflict	824	1	Missing in CAC20419. Ref.1
	Sequence conflict	1336	1	R → K in CAC20419. Ref.1
	Sequence conflict	1341	1	S → T in CAC20419. Ref.1
	Sequence conflict	1578	1	H → R in AAI31734. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 22, 2009. Version 2. Checksum: C88563125F0F90D8	FASTA	1,594	177,676
	10 20 30 40 50 60 MPCAQRSWLA NLSVVAQLLN FGALCYGRQP QPGPVRFPDR RQEHFIKGLP EYHVVGPVRV 70 80 90 100 110 120 DASGHFLSYG LHYPITSSRR KRDLDGSEDW VYYRISHEEK DLFFNLTVNQ GFLSNSYIME 130 140 150 160 170 180 KRYGNLSHVK MMASSAPLCH LSGTVLQQGT RVGTAALSAC HGLTGFFQLP HGDFFIEPVK 190 200 210 220 230 240 KHPLVEGGYH PHIVYRRQKV PETKEPTCGL KDSVNISQKQ ELWREKWERH NLPSRSLSRR 250 260 270 280 290 300 SISKERWVET LVVADTKMIE YHGSENVESY ILTIMNMVTG LFHNPSIGNA IHIVVVRLIL 310 320 330 340 350 360 LEEEEQGLKI VHHAEKTLSS FCKWQKSINP KSDLNPVHHD VAVLLTRKDI CAGFNRPCET 370 380 390 400 410 420 LGLSHLSGMC QPHRSCNINE DSGLPLAFTI AHELGHSFGI QHDGKENDCE PVGRHPYIMS 430 440 450 460 470 480 RQLQYDPTPL TWSKCSEEYI TRFLDRGWGF CLDDIPKKKG LKSKVIAPGV IYDVHHQCQL 490 500 510 520 530 540 QYGPNATFCQ EVENVCQTLW CSVKGFCRSK LDAAADGTQC GEKKWCMAGK CITVGKKPES 550 560 570 580 590 600 IPGGWGRWSP WSHCSRTCGA GVQSAERLCN NPEPKFGGKY CTGERKRYRL CNVHPCRSEA 610 620 630 640 650 660 PTFRQMQCSE FDTVPYKNEL YHWFPIFNPA HPCELYCRPI DGQFSEKMLD AVIDGTPCFE 670 680 690 700 710 720 GGNSRNVCIN GICKMVGCDY EIDSNATEDR CGVCLGDGSS CQTVRKMFKQ KEGSGYVDIG 730 740 750 760 770 780 LIPKGARDIR VMEIEGAGNF LAIRSEDPEK YYLNGGFIIQ WNGNYKLAGT VFQYDRKGDL 790 800 810 820 830 840 EKLMATGPTN ESVWIQLLFQ VTNPGIKYEY TIQKDGLDND VEQQMYFWQY GHWTECSVTC 850 860 870 880 890 900 GTGIRRQTAH CIKKGRGMVK ATFCDPETQP NGRQKKCHEK ACPPRWWAGE WEACSATCGP 910 920 930 940 950 960 HGEKKRTVLC IQTMVSDEQA LPPTDCQHLL KPKTLLSCNR DILCPSDWTV GNWSECSVSC 970 980 990 1000 1010 1020 GGGVRIRSVT CAKNHDEPCD VTRKPNSRAL CGLQQCPSSR RVLKPNKGTI SNGKNPPTLK 1030 1040 1050 1060 1070 1080 PVPPPTSRPR MLTTPTGPES MSTSTPAISS PSPTTASKEG DLGGKQWQDS STQPELSSRY 1090 1100 1110 1120 1130 1140 LISTGSTSQP ILTSQSLSIQ PSEENVSSSD TGPTSEGGLV ATTTSGSGLS SSRNPITWPV 1150 1160 1170 1180 1190 1200 TPFYNTLTKG PEMEIHSGSG EEREQPEDKD ESNPVIWTKI RVPGNDAPVE STEMPLAPPL 1210 1220 1230 1240 1250 1260 TPDLSRESWW PPFSTVMEGL LPSQRPTTSE TGTPRVEGMV TEKPANTLLP LGGDHQPEPS 1270 1280 1290 1300 1310 1320 GKTANRNHLK LPNNMNQTKS SEPVLTEEDA TSLITEGFLL NASNYKQLTN GHGSAHWIVG 1330 1340 1350 1360 1370 1380 NWSECSTTCG LGAYWRRVEC STQMDSDCAA IQRPDPAKRC HLRPCAGWKV GNWSKCSRNC 1390 1400 1410 1420 1430 1440 SGGFKIREIQ CVDSRDHRNL RPFHCQFLAG IPPPLSMSCN PEPCEAWQVE PWSQCSRSCG 1450 1460 1470 1480 1490 1500 GGVQERGVFC PGGLCDWTKR PTSTMSCNEH LCCHWATGNW DLCSTSCGGG FQKRTVQCVP 1510 1520 1530 1540 1550 1560 SEGNKTEDQD QCLCDHKPRP PEFKKCNQQA CKKSADLLCT KDKLSASFCQ TLKAMKKCSV 1570 1580 1590 PTVRAECCFS CPQTHITHTQ RQRRQRLLQK SKEL
	Isoform 2 [UniParc]. Checksum: 11FBCB40E82091F6	FASTA	229	26,003
	10 20 30 40 50 60 MPCAQRSWLA NLSVVAQLLN FGALCYGRQP QPGPVRFPDR RQEHFIKGLP EYHVVGPVRV 70 80 90 100 110 120 DASGHFLSYG LHYPITSSRR KRDLDGSEDW VYYRISHEEK DLFFNLTVNQ GFLSNSYIME 130 140 150 160 170 180 KRYGNLSHVK MMASSAPLCH LSGTVLQQGT RVGTAALSAC HGLTGFFQLP HGDFFIEPVK 190 200 210 220 KHPLVEGGYH PHIVYRRQKV PETKEPTCGL KGIVTHMSSW VEESVLFFW
	Isoform 3 [UniParc]. Checksum: 5BF525F456FC8EE5	FASTA	1,509	168,460
	10 20 30 40 50 60 MPCAQRSWLA NLSVVAQLLN FGALCYGRQP QPGPVRFPDR RQEHFIKGLP EYHVVGPVRV 70 80 90 100 110 120 DASGHFLSYG LHYPITSSRR KRDLDGSEDW VYYRISHEEK DLFFNLTVNQ GFLSNSYIME 130 140 150 160 170 180 KRYGNLSHVK MMASSAPLCH LSGTVLQQGT RVGTAALSAC HGLTGFFQLP HGDFFIEPVK 190 200 210 220 230 240 KHPLVEGGYH PHIVYRRQKV PETKEPTCGL KDSVNISQKQ ELWREKWERH NLPSRSLSRR 250 260 270 280 290 300 SISKERWVET LVVADTKMIE YHGSENVESY ILTIMNMVTG LFHNPSIGNA IHIVVVRLIL 310 320 330 340 350 360 LEEEEQGLKI VHHAEKTLSS FCKWQKSINP KSDLNPVHHD VAVLLTRKDI CAGFNRPCET 370 380 390 400 410 420 LGLSHLSGMC QPHRSCNINE DSGLPLAFTI AHELGHSFGI QHDGKENDCE PVGRHPYIMS 430 440 450 460 470 480 RQLQYDPTPL TWSKCSEEYI TRFLDRGWGF CLDDIPKKKG LKSKVIAPGV IYDVHHQCQL 490 500 510 520 530 540 QYGPNATFCQ EVENVCQTLW CSVKGFCRSK LDAAADGTQC GEKKWCMAGK CITVGKKPES 550 560 570 580 590 600 IPGGWGRWSP WSHCSRTCGA GVQSAERLCN NPEPKFGGKY CTGERKRYRL CNVHPCRSEA 610 620 630 640 650 660 PTFRQMQCSE FDTVPYKNEL YHWFPIFNPG YVDIGLIPKG ARDIRVMEIE GAGNFLAIRS 670 680 690 700 710 720 EDPEKYYLNG GFIIQWNGNY KLAGTVFQYD RKGDLEKLMA TGPTNESVWI QLLFQVTNPG 730 740 750 760 770 780 IKYEYTIQKD GLDNDVEQQM YFWQYGHWTE CSVTCGTGIR RQTAHCIKKG RGMVKATFCD 790 800 810 820 830 840 PETQPNGRQK KCHEKACPPR WWAGEWEACS ATCGPHGEKK RTVLCIQTMV SDEQALPPTD 850 860 870 880 890 900 CQHLLKPKTL LSCNRDILCP SDWTVGNWSE CSVSCGGGVR IRSVTCAKNH DEPCDVTRKP 910 920 930 940 950 960 NSRALCGLQQ CPSSRRVLKP NKGTISNGKN PPTLKPVPPP TSRPRMLTTP TGPESMSTST 970 980 990 1000 1010 1020 PAISSPSPTT ASKEGDLGGK QWQDSSTQPE LSSRYLISTG STSQPILTSQ SLSIQPSEEN 1030 1040 1050 1060 1070 1080 VSSSDTGPTS EGGLVATTTS GSGLSSSRNP ITWPVTPFYN TLTKGPEMEI HSGSGEEREQ 1090 1100 1110 1120 1130 1140 PEDKDESNPV IWTKIRVPGN DAPVESTEMP LAPPLTPDLS RESWWPPFST VMEGLLPSQR 1150 1160 1170 1180 1190 1200 PTTSETGTPR VEGMVTEKPA NTLLPLGGDH QPEPSGKTAN RNHLKLPNNM NQTKSSEPVL 1210 1220 1230 1240 1250 1260 TEEDATSLIT EGFLLNASNY KQLTNGHGSA HWIVGNWSEC STTCGLGAYW RRVECSTQMD 1270 1280 1290 1300 1310 1320 SDCAAIQRPD PAKRCHLRPC AGWKVGNWSK CSRNCSGGFK IREIQCVDSR DHRNLRPFHC 1330 1340 1350 1360 1370 1380 QFLAGIPPPL SMSCNPEPCE AWQVEPWSQC SRSCGGGVQE RGVFCPGGLC DWTKRPTSTM 1390 1400 1410 1420 1430 1440 SCNEHLCCHW ATGNWDLCST SCGGGFQKRT VQCVPSEGNK TEDQDQCLCD HKPRPPEFKK 1450 1460 1470 1480 1490 1500 CNQQACKKSA DLLCTKDKLS ASFCQTLKAM KKCSVPTVRA ECCFSCPQTH ITHTQRQRRQ RLLQKSKEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00036578. IPI00432310. IPI00944649.
RefSeq	NP_112217.2. NM_030955.2.
UniGene	Hs.12680.
3D structure databases
ProteinModelPortal	P58397.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000344847.
Protein family/group databases
MEROPS	M12.237.
PTM databases
PhosphoSite	P58397.
Polymorphism databases
DMDM	259016182.
Proteomic databases
PaxDb	P58397.
PRIDE	P58397.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000352040; ENSP00000344847; ENSG00000151388. ENST00000504830; ENSP00000422554; ENSG00000151388.
GeneID	81792.
KEGG	hsa:81792.
UCSC	uc003jia.1. human. uc010iuq.1. human.
Organism-specific databases
CTD	81792.
GeneCards	GC05M033495.
HGNC	HGNC:14605. ADAMTS12.
HPA	HPA035973.
MIM	606184. gene.
neXtProt	NX_P58397.
PharmGKB	PA24538.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG237764.
HOGENOM	HOG000015092.
HOVERGEN	HBG050620.
InParanoid	P58397.
KO	K08626.
OMA	LLCTKDK.
OrthoDB	EOG4XPQF0.
PhylomeDB	P58397.
Gene expression databases
ArrayExpress	P58397.
Bgee	P58397.
CleanEx	HS_ADAMTS12.
Genevestigator	P58397.
GermOnline	ENSG00000151388. Homo sapiens.
Family and domain databases
Gene3D	3.40.390.10. 2 hits.
InterPro	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]
Pfam	PF05986. ADAM_spacer1. 1 hit. PF01562. Pep_M12B_propep. 1 hit. PF01421. Reprolysin. 1 hit. PF00090. TSP_1. 8 hits. [Graphical view]
PRINTS	PR01857. ADAMTSFAMILY.
SMART	SM00209. TSP1. 8 hits. [Graphical view]
SUPFAM	SSF82895. TSP1. 8 hits.
PROSITE	PS50215. ADAM_MEPRO. 1 hit. PS00546. CYSTEINE_SWITCH. False negative. PS00427. DISINTEGRIN_1. False negative. PS50214. DISINTEGRIN_2. False negative. PS50900. PLAC. 1 hit. PS50092. TSP1. 6 hits. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ADAMTS12. human.
GenomeRNAi	81792.
NextBio	72100.
SOURCE	Search...

Entry information

Entry name

ATS12_HUMAN

Accession

Primary (citable) accession number: P58397
Secondary accession number(s): A2RRN9, A5D6V6, Q6UWL3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	September 22, 2009
Last modified:	May 1, 2013
This is version 121 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.