Tag | Content |
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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 |
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536 | GKCITVGKKPESIPG | methylation | [1] |
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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 | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |