CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022945
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 A disintegrin and metalloproteinase with thrombospondin motifs 1 
Protein Synonyms/Alias
 ADAM-TS 1; ADAM-TS1; ADAMTS-1; METH-1 
Gene Name
 ADAMTS1 
Gene Synonyms/Alias
 KIAA1346; METH1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
735SGSVTSAKPGYHDIIubiquitination[1, 2]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
 Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover (By similarity). Has angiogenic inhibitor activity. Active metalloprotease, which may be associated with various inflammatory processes as well as development of cancer cachexia. May play a critical role in follicular rupture. 
Sequence Annotation
 DOMAIN 258 467 Peptidase M12B.
 DOMAIN 476 559 Disintegrin.
 DOMAIN 559 614 TSP type-1 1.
 DOMAIN 854 905 TSP type-1 2.
 DOMAIN 908 967 TSP type-1 3.
 REGION 725 849 Spacer.
 MOTIF 196 203 Cysteine switch (By similarity).
 ACT_SITE 402 402 By similarity.
 METAL 198 198 Zinc; in inhibited form (By similarity).
 METAL 401 401 Zinc; catalytic (By similarity).
 METAL 405 405 Zinc; catalytic (By similarity).
 METAL 411 411 Zinc; catalytic (By similarity).
 CARBOHYD 547 547 N-linked (GlcNAc...) (Potential).
 CARBOHYD 720 720 N-linked (GlcNAc...) (Potential).
 CARBOHYD 764 764 N-linked (GlcNAc...) (Potential).
 DISULFID 379 462 By similarity.
 DISULFID 417 446 By similarity.
 DISULFID 571 608 By similarity.
 DISULFID 575 613 By similarity.
 DISULFID 586 598 By similarity.  
Keyword
 3D-structure; Cleavage on pair of basic residues; Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein; Heparin-binding; Hydrolase; Metal-binding; Metalloprotease; Polymorphism; Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 967 AA 
Protein Sequence
MQRAVPEGFG RRKLGSDMGN AERAPGSRSF GPVPTLLLLA AALLAVSDAL GRPSEEDEEL 60
VVPELERAPG HGTTRLRLHA FDQQLDLELR PDSSFLAPGF TLQNVGRKSG SETPLPETDL 120
AHCFYSGTVN GDPSSAAALS LCEGVRGAFY LLGEAYFIQP LPAASERLAT AAPGEKPPAP 180
LQFHLLRRNR QGDVGGTCGV VDDEPRPTGK AETEDEDEGT EGEDEGAQWS PQDPALQGVG 240
QPTGTGSIRK KRFVSSHRYV ETMLVADQSM AEFHGSGLKH YLLTLFSVAA RLYKHPSIRN 300
SVSLVVVKIL VIHDEQKGPE VTSNAALTLR NFCNWQKQHN PPSDRDAEHY DTAILFTRQD 360
LCGSQTCDTL GMADVGTVCD PSRSCSVIED DGLQAAFTTA HELGHVFNMP HDDAKQCASL 420
NGVNQDSHMM ASMLSNLDHS QPWSPCSAYM ITSFLDNGHG ECLMDKPQNP IQLPGDLPGT 480
SYDANRQCQF TFGEDSKHCP DAASTCSTLW CTGTSGGVLV CQTKHFPWAD GTSCGEGKWC 540
INGKCVNKTD RKHFDTPFHG SWGMWGPWGD CSRTCGGGVQ YTMRECDNPV PKNGGKYCEG 600
KRVRYRSCNL EDCPDNNGKT FREEQCEAHN EFSKASFGSG PAVEWIPKYA GVSPKDRCKL 660
ICQAKGIGYF FVLQPKVVDG TPCSPDSTSV CVQGQCVKAG CDRIIDSKKK FDKCGVCGGN 720
GSTCKKISGS VTSAKPGYHD IITIPTGATN IEVKQRNQRG SRNNGSFLAI KAADGTYILN 780
GDYTLSTLEQ DIMYKGVVLR YSGSSAALER IRSFSPLKEP LTIQVLTVGN ALRPKIKYTY 840
FVKKKKESFN AIPTFSAWVI EEWGECSKSC ELGWQRRLVE CRDINGQPAS ECAKEVKPAS 900
TRPCADHPCP QWQLGEWSSC SKTCGKGYKK RSLKCLSHDG GVLSHESCDP LKKPKHFIDF 960
CTMAECS 967 
Gene Ontology
 GO:0005604; C:basement membrane; IEA:Compara.
 GO:0031410; C:cytoplasmic vesicle; IEA:Compara.
 GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
 GO:0004222; F:metalloendopeptidase activity; IEA:Compara.
 GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0060347; P:heart trabecula formation; IEA:Compara.
 GO:0007229; P:integrin-mediated signaling pathway; TAS:ProtInc.
 GO:0001822; P:kidney development; IEA:Compara.
 GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
 GO:0001542; P:ovulation from ovarian follicle; IEA:Compara.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR006586; ADAM_Cys-rich.
 IPR010294; ADAM_spacer1.
 IPR024079; MetalloPept_cat_dom.
 IPR013274; Pept_M12B_ADAM-TS1.
 IPR001590; Peptidase_M12B.
 IPR013273; Peptidase_M12B_ADAM-TS.
 IPR002870; Peptidase_M12B_N.
 IPR000884; Thrombospondin_1_rpt. 
Pfam
 PF05986; ADAM_spacer1
 PF01562; Pep_M12B_propep
 PF01421; Reprolysin
 PF00090; TSP_1 
SMART
 SM00608; ACR
 SM00209; TSP1 
PROSITE
 PS50215; ADAM_MEPRO
 PS00427; DISINTEGRIN_1
 PS50214; DISINTEGRIN_2
 PS50092; TSP1
 PS00142; ZINC_PROTEASE 
PRINTS
 PR01858; ADAMTS1.
 PR01857; ADAMTSFAMILY.