| Tag | Content |
|---|
| CPLM ID | CPLM-018362 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | A disintegrin and metalloproteinase with thrombospondin motifs 14 |
Protein Synonyms/Alias | ADAM-TS 14; ADAM-TS14; ADAMTS-14 |
Gene Name | ADAMTS14 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 717 | NSHCRTVKGTLGKAS | acetylation | [1] | | 722 | TVKGTLGKASKQAGA | acetylation | [1] |
|
Reference | [1] Regulation of cellular metabolism by protein lysine acetylation. Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL. Science. 2010 Feb 19;327(5968):1000-4. [ PMID: 20167786] |
Functional Description | Has a aminoprocollagen type I activity processing activity in the absence of ADAMTS2. Seems to be synthesized as a latent enzyme that requires activation to display aminoprocollagen peptidase activity. |
Sequence Annotation | DOMAIN 259 460 Peptidase M12B.
DOMAIN 461 551 Disintegrin.
DOMAIN 552 607 TSP type-1 1.
DOMAIN 847 907 TSP type-1 2.
DOMAIN 908 967 TSP type-1 3.
DOMAIN 968 1022 TSP type-1 4.
DOMAIN 1059 1097 PLAC.
REGION 730 846 Spacer.
ACT_SITE 399 399 By similarity.
METAL 398 398 Zinc; catalytic (By similarity).
METAL 402 402 Zinc; catalytic (By similarity).
METAL 408 408 Zinc; catalytic (By similarity).
CARBOHYD 109 109 N-linked (GlcNAc...) (Potential).
CARBOHYD 475 475 N-linked (GlcNAc...) (Potential).
CARBOHYD 941 941 N-linked (GlcNAc...) (Potential).
CARBOHYD 1027 1027 N-linked (GlcNAc...) (Potential).
DISULFID 376 455 By similarity.
DISULFID 415 441 By similarity.
DISULFID 564 601 By similarity.
DISULFID 568 606 By similarity.
DISULFID 579 591 By similarity.
DISULFID 980 1016 By similarity.
DISULFID 984 1021 By similarity.
DISULFID 995 1005 By similarity. |
Keyword | Alternative promoter usage; Alternative splicing; Cleavage on pair of basic residues; Collagen degradation; Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Polymorphism; Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1223 AA |
Protein Sequence | MAPLRALLSY LLPLHCALCA AAGSRTPELH LSGKLSDYGV TVPCSTDFRG RFLSHVVSGP 60
AAASAGSMVV DTPPTLPRHS SHLRVARSPL HPGGTLWPGR VGRHSLYFNV TVFGKELHLR 120
LRPNRRLVVP GSSVEWQEDF RELFRQPLRQ ECVYTGGVTG MPGAAVAISN CDGLAGLIRT 180
DSTDFFIEPL ERGQQEKEAS GRTHVVYRRE AVQQEWAEPD GDLHNEAFGL GDLPNLLGLV 240
GDQLGDTERK RRHAKPGSYS IEVLLVVDDS VVRFHGKEHV QNYVLTLMNI VDEIYHDESL 300
GVHINIALVR LIMVGYRQSL SLIERGNPSR SLEQVCRWAH SQQRQDPSHA EHHDHVVFLT 360
RQDFGPSGYA PVTGMCHPLR SCALNHEDGF SSAFVIAHET GHVLGMEHDG QGNGCADETS 420
LGSVMAPLVQ AAFHRFHWSR CSKLELSRYL PSYDCLLDDP FDPAWPQPPE LPGINYSMDE 480
QCRFDFGSGY QTCLAFRTFE PCKQLWCSHP DNPYFCKTKK GPPLDGTECA PGKWCFKGHC 540
IWKSPEQTYG QDGGWSSWTK FGSCSRSCGG GVRSRSRSCN NPSPAYGGRL CLGPMFEYQV 600
CNSEECPGTY EDFRAQQCAK RNSYYVHQNA KHSWVPYEPD DDAQKCELIC QSADTGDVVF 660
MNQVVHDGTR CSYRDPYSVC ARGECVPVGC DKEVGSMKAD DKCGVCGGDN SHCRTVKGTL 720
GKASKQAGAL KLVQIPAGAR HIQIEALEKS PHRIVVKNQV TGSFILNPKG KEATSRTFTA 780
MGLEWEDAVE DAKESLKTSG PLPEAIAILA LPPTEGGPRS SLAYKYVIHE DLLPLIGSNN 840
VLLEEMDTYE WALKSWAPCS KACGGGIQFT KYGCRRRRDH HMVQRHLCDH KKRPKPIRRR 900
CNQHPCSQPV WVTEEWGACS RSCGKLGVQT RGIQCLLPLS NGTHKVMPAK ACAGDRPEAR 960
RPCLRVPCPA QWRLGAWSQC SATCGEGIQQ RQVVCRTNAN SLGHCEGDRP DTVQVCSLPA 1020
CGGNHQNSTV RADVWELGTP EGQWVPQSEP LHPINKISST EPCTGDRSVF CQMEVLDRYC 1080
SIPGYHRLCC VSCIKKASGP NPGPDPGPTS LPPFSTPGSP LPGPQDPADA AEPPGKPTGS 1140
EDHQHGRATQ LPGALDTSSP GTQHPFAPET PIPGASWSIS PTTPGGLPWG WTQTPTPVPE 1200
DKGQPGEDLR HPGTSLPAAS PVT 1223 |
Gene Ontology | GO:0005576; C:extracellular region; TAS:Reactome. 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:0030574; P:collagen catabolic process; IEA:UniProtKB-KW. GO:0030199; P:collagen fibril organization; IEA:Compara. GO:0030198; P:extracellular matrix organization; TAS:Reactome. GO:0006508; P:proteolysis; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |