CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009131
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 A disintegrin and metalloproteinase with thrombospondin motifs 12 
Protein Synonyms/Alias
 ADAM-TS 12; ADAM-TS12; ADAMTS-12 
Gene Name
 ADAMTS12 
Gene Synonyms/Alias
 UNQ1918/PRO4389 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
536GKCITVGKKPESIPGmethylation[1]
Reference
 [1] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510
Functional Description
 Metalloprotease that may play a role in the degradation of COMP. Cleaves also alpha-2 macroglobulin and aggregan. Has anti-tumorigenic properties. 
Sequence Annotation
 DOMAIN 246 456 Peptidase M12B.
 DOMAIN 465 544 Disintegrin.
 DOMAIN 542 597 TSP type-1 1.
 DOMAIN 823 883 TSP type-1 2.
 DOMAIN 887 943 TSP type-1 3.
 DOMAIN 944 997 TSP type-1 4.
 DOMAIN 1313 1366 TSP type-1 5.
 DOMAIN 1368 1422 TSP type-1 6.
 DOMAIN 1423 1471 TSP type-1 7.
 DOMAIN 1472 1532 TSP type-1 8.
 DOMAIN 1535 1575 PLAC.
 REGION 701 827 Spacer 1.
 REGION 997 1316 Spacer 2.
 MOTIF 208 213 Cysteine switch (By similarity).
 ACT_SITE 393 393 By similarity.
 METAL 208 208 Zinc; in inhibited form (By similarity).
 METAL 392 392 Zinc; catalytic (By similarity).
 METAL 396 396 Zinc; catalytic (By similarity).
 METAL 402 402 Zinc; catalytic (By similarity).
 MOD_RES 982 982 Phosphothreonine (By similarity).
 CARBOHYD 105 105 N-linked (GlcNAc...) (Potential).
 CARBOHYD 125 125 N-linked (GlcNAc...) (Potential).
 CARBOHYD 215 215 N-linked (GlcNAc...) (Potential).
 CARBOHYD 485 485 N-linked (GlcNAc...) (Potential).
 CARBOHYD 685 685 N-linked (GlcNAc...) (Potential).
 CARBOHYD 790 790 N-linked (GlcNAc...) (Potential).
 CARBOHYD 952 952 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1105 1105 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1276 1276 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1301 1301 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1321 1321 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1372 1372 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1379 1379 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1504 1504 N-linked (GlcNAc...) (Potential).
 DISULFID 370 451 By similarity.
 DISULFID 409 435 By similarity.
 DISULFID 554 591 By similarity.
 DISULFID 558 596 By similarity.
 DISULFID 569 581 By similarity.  
Keyword
 Alternative splicing; Cleavage on pair of basic residues; Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein; Polymorphism; Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1594 AA 
Protein Sequence
MPCAQRSWLA NLSVVAQLLN FGALCYGRQP QPGPVRFPDR RQEHFIKGLP EYHVVGPVRV 60
DASGHFLSYG LHYPITSSRR KRDLDGSEDW VYYRISHEEK DLFFNLTVNQ GFLSNSYIME 120
KRYGNLSHVK MMASSAPLCH LSGTVLQQGT RVGTAALSAC HGLTGFFQLP HGDFFIEPVK 180
KHPLVEGGYH PHIVYRRQKV PETKEPTCGL KDSVNISQKQ ELWREKWERH NLPSRSLSRR 240
SISKERWVET LVVADTKMIE YHGSENVESY ILTIMNMVTG LFHNPSIGNA IHIVVVRLIL 300
LEEEEQGLKI VHHAEKTLSS FCKWQKSINP KSDLNPVHHD VAVLLTRKDI CAGFNRPCET 360
LGLSHLSGMC QPHRSCNINE DSGLPLAFTI AHELGHSFGI QHDGKENDCE PVGRHPYIMS 420
RQLQYDPTPL TWSKCSEEYI TRFLDRGWGF CLDDIPKKKG LKSKVIAPGV IYDVHHQCQL 480
QYGPNATFCQ EVENVCQTLW CSVKGFCRSK LDAAADGTQC GEKKWCMAGK CITVGKKPES 540
IPGGWGRWSP WSHCSRTCGA GVQSAERLCN NPEPKFGGKY CTGERKRYRL CNVHPCRSEA 600
PTFRQMQCSE FDTVPYKNEL YHWFPIFNPA HPCELYCRPI DGQFSEKMLD AVIDGTPCFE 660
GGNSRNVCIN GICKMVGCDY EIDSNATEDR CGVCLGDGSS CQTVRKMFKQ KEGSGYVDIG 720
LIPKGARDIR VMEIEGAGNF LAIRSEDPEK YYLNGGFIIQ WNGNYKLAGT VFQYDRKGDL 780
EKLMATGPTN ESVWIQLLFQ VTNPGIKYEY TIQKDGLDND VEQQMYFWQY GHWTECSVTC 840
GTGIRRQTAH CIKKGRGMVK ATFCDPETQP NGRQKKCHEK ACPPRWWAGE WEACSATCGP 900
HGEKKRTVLC IQTMVSDEQA LPPTDCQHLL KPKTLLSCNR DILCPSDWTV GNWSECSVSC 960
GGGVRIRSVT CAKNHDEPCD VTRKPNSRAL CGLQQCPSSR RVLKPNKGTI SNGKNPPTLK 1020
PVPPPTSRPR MLTTPTGPES MSTSTPAISS PSPTTASKEG DLGGKQWQDS STQPELSSRY 1080
LISTGSTSQP ILTSQSLSIQ PSEENVSSSD TGPTSEGGLV ATTTSGSGLS SSRNPITWPV 1140
TPFYNTLTKG PEMEIHSGSG EEREQPEDKD ESNPVIWTKI RVPGNDAPVE STEMPLAPPL 1200
TPDLSRESWW PPFSTVMEGL LPSQRPTTSE TGTPRVEGMV TEKPANTLLP LGGDHQPEPS 1260
GKTANRNHLK LPNNMNQTKS SEPVLTEEDA TSLITEGFLL NASNYKQLTN GHGSAHWIVG 1320
NWSECSTTCG LGAYWRRVEC STQMDSDCAA IQRPDPAKRC HLRPCAGWKV GNWSKCSRNC 1380
SGGFKIREIQ CVDSRDHRNL RPFHCQFLAG IPPPLSMSCN PEPCEAWQVE PWSQCSRSCG 1440
GGVQERGVFC PGGLCDWTKR PTSTMSCNEH LCCHWATGNW DLCSTSCGGG FQKRTVQCVP 1500
SEGNKTEDQD QCLCDHKPRP PEFKKCNQQA CKKSADLLCT KDKLSASFCQ TLKAMKKCSV 1560
PTVRAECCFS CPQTHITHTQ RQRRQRLLQK SKEL 1594 
Gene Ontology
 GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
 GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
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. 
Pfam
 PF05986; ADAM_spacer1
 PF01562; Pep_M12B_propep
 PF01421; Reprolysin
 PF00090; TSP_1 
SMART
 SM00209; TSP1 
PROSITE
 PS50215; ADAM_MEPRO
 PS00546; CYSTEINE_SWITCH
 PS00427; DISINTEGRIN_1
 PS50214; DISINTEGRIN_2
 PS50900; PLAC
 PS50092; TSP1
 PS00142; ZINC_PROTEASE 
PRINTS
 PR01857; ADAMTSFAMILY.