ATS12_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATS12_HUMAN
• UniProt AC: P58397
• Protein Name: A disintegrin and metalloproteinase with thrombospondin motifs 12
• Gene Name: ADAMTS12
• Organism: Homo sapiens (Human).
• Sequence Length: 1594
• Subcellular Localization: Secreted, extracellular space, extracellular matrix.
• Protein Description: Metalloprotease that may play a role in the degradation of COMP. Cleaves also alpha-2 macroglobulin and aggregan. Has anti-tumorigenic properties..
• Protein Sequence: MPCAQRSWLANLSVVAQLLNFGALCYGRQPQPGPVRFPDRRQEHFIKGLPEYHVVGPVRVDASGHFLSYGLHYPITSSRRKRDLDGSEDWVYYRISHEEKDLFFNLTVNQGFLSNSYIMEKRYGNLSHVKMMASSAPLCHLSGTVLQQGTRVGTAALSACHGLTGFFQLPHGDFFIEPVKKHPLVEGGYHPHIVYRRQKVPETKEPTCGLKDSVNISQKQELWREKWERHNLPSRSLSRRSISKERWVETLVVADTKMIEYHGSENVESYILTIMNMVTGLFHNPSIGNAIHIVVVRLILLEEEEQGLKIVHHAEKTLSSFCKWQKSINPKSDLNPVHHDVAVLLTRKDICAGFNRPCETLGLSHLSGMCQPHRSCNINEDSGLPLAFTIAHELGHSFGIQHDGKENDCEPVGRHPYIMSRQLQYDPTPLTWSKCSEEYITRFLDRGWGFCLDDIPKKKGLKSKVIAPGVIYDVHHQCQLQYGPNATFCQEVENVCQTLWCSVKGFCRSKLDAAADGTQCGEKKWCMAGKCITVGKKPESIPGGWGRWSPWSHCSRTCGAGVQSAERLCNNPEPKFGGKYCTGERKRYRLCNVHPCRSEAPTFRQMQCSEFDTVPYKNELYHWFPIFNPAHPCELYCRPIDGQFSEKMLDAVIDGTPCFEGGNSRNVCINGICKMVGCDYEIDSNATEDRCGVCLGDGSSCQTVRKMFKQKEGSGYVDIGLIPKGARDIRVMEIEGAGNFLAIRSEDPEKYYLNGGFIIQWNGNYKLAGTVFQYDRKGDLEKLMATGPTNESVWIQLLFQVTNPGIKYEYTIQKDGLDNDVEQQMYFWQYGHWTECSVTCGTGIRRQTAHCIKKGRGMVKATFCDPETQPNGRQKKCHEKACPPRWWAGEWEACSATCGPHGEKKRTVLCIQTMVSDEQALPPTDCQHLLKPKTLLSCNRDILCPSDWTVGNWSECSVSCGGGVRIRSVTCAKNHDEPCDVTRKPNSRALCGLQQCPSSRRVLKPNKGTISNGKNPPTLKPVPPPTSRPRMLTTPTGPESMSTSTPAISSPSPTTASKEGDLGGKQWQDSSTQPELSSRYLISTGSTSQPILTSQSLSIQPSEENVSSSDTGPTSEGGLVATTTSGSGLSSSRNPITWPVTPFYNTLTKGPEMEIHSGSGEEREQPEDKDESNPVIWTKIRVPGNDAPVESTEMPLAPPLTPDLSRESWWPPFSTVMEGLLPSQRPTTSETGTPRVEGMVTEKPANTLLPLGGDHQPEPSGKTANRNHLKLPNNMNQTKSSEPVLTEEDATSLITEGFLLNASNYKQLTNGHGSAHWIVGNWSECSTTCGLGAYWRRVECSTQMDSDCAAIQRPDPAKRCHLRPCAGWKVGNWSKCSRNCSGGFKIREIQCVDSRDHRNLRPFHCQFLAGIPPPLSMSCNPEPCEAWQVEPWSQCSRSCGGGVQERGVFCPGGLCDWTKRPTSTMSCNEHLCCHWATGNWDLCSTSCGGGFQKRTVQCVPSEGNKTEDQDQCLCDHKPRPPEFKKCNQQACKKSADLLCTKDKLSASFCQTLKAMKKCSVPTVRAECCFSCPQTHITHTQRQRRQRLLQKSKEL

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
52	Phosphorylation	FIKGLPEYHVVGPVR HHCCCCCCEEECCEE	9.66	110747131
105	N-linked_Glycosylation	EEKDLFFNLTVNQGF HCCCEEEEEEECCCC	27.71	UniProtKB CARBOHYD
107	Phosphorylation	KDLFFNLTVNQGFLS CCEEEEEEECCCCCC	20.65	69338501
117	Phosphorylation	QGFLSNSYIMEKRYG CCCCCCCEEEEECCC	14.45	28842319
125	N-linked_Glycosylation	IMEKRYGNLSHVKMM EEEECCCCHHHHHHH	29.45	UniProtKB CARBOHYD
215	N-linked_Glycosylation	CGLKDSVNISQKQEL CCCCCCCCCHHHHHH	31.95	UniProtKB CARBOHYD
234	Phosphorylation	WERHNLPSRSLSRRS HHHCCCCCCCCCCCC	37.35	17081983
236	Phosphorylation	RHNLPSRSLSRRSIS HCCCCCCCCCCCCCC	34.73	17081983
428	Phosphorylation	RQLQYDPTPLTWSKC ECCCCCCCCCCCHHC	28.21	22817900
431	Phosphorylation	QYDPTPLTWSKCSEE CCCCCCCCCHHCCHH	28.97	30898595
433	Phosphorylation	DPTPLTWSKCSEEYI CCCCCCCHHCCHHHH	20.67	22817900
436	Phosphorylation	PLTWSKCSEEYITRF CCCCHHCCHHHHHHH	36.88	113136077
485	N-linked_Glycosylation	CQLQYGPNATFCQEV HHHHCCCCCCHHHHH	47.45	UniProtKB CARBOHYD
530	Acetylation	KKWCMAGKCITVGKK CEEEECCEEEEECCC	16.96	12436333
533	Phosphorylation	CMAGKCITVGKKPES EECCEEEEECCCCCC	32.45	46159189
536	Methylation	GKCITVGKKPESIPG CEEEEECCCCCCCCC	61.90	23644510
536	Trimethylation	GKCITVGKKPESIPG CEEEEECCCCCCCCC	61.90	-
536	Acetylation	GKCITVGKKPESIPG CEEEEECCCCCCCCC	61.90	12433507
549	Phosphorylation	PGGWGRWSPWSHCSR CCCCCCCCCCCHHHC	18.35	50563497
552	Phosphorylation	WGRWSPWSHCSRTCG CCCCCCCCHHHCCCC	20.28	50563503
555	Phosphorylation	WSPWSHCSRTCGAGV CCCCCHHHCCCCCCH	25.79	50563509
685	N-linked_Glycosylation	CDYEIDSNATEDRCG CCEEECCCCCCCCCC	47.32	UniProtKB CARBOHYD
716	Phosphorylation	KQKEGSGYVDIGLIP HCCCCCCCEEEEEEC	9.17	110747137
770	Phosphorylation	GNYKLAGTVFQYDRK CCEEEEEEEEEECCC	16.73	24719451
774	Phosphorylation	LAGTVFQYDRKGDLE EEEEEEEECCCCCHH	13.27	24719451
790	N-linked_Glycosylation	LMATGPTNESVWIQL HHHCCCCCHHHHHEE	42.55	UniProtKB CARBOHYD
862	Phosphorylation	GRGMVKATFCDPETQ CCCCEEEEEECCCCC	21.05	29759185
868	Phosphorylation	ATFCDPETQPNGRQK EEEECCCCCCCCCCC	55.50	29759185
952	N-linked_Glycosylation	PSDWTVGNWSECSVS CCCCCCCCCCCCEEE	34.46	UniProtKB CARBOHYD
987	Phosphorylation	DVTRKPNSRALCGLQ CCCCCCCCHHHCCCC	27.70	10529547
1014	Acetylation	KGTISNGKNPPTLKP CCCCCCCCCCCCCCC	71.21	88573
1070	Phosphorylation	GGKQWQDSSTQPELS CCCCCCCCCCCCCCC	21.86	27732954
1071	Phosphorylation	GKQWQDSSTQPELSS CCCCCCCCCCCCCCC	39.07	27732954
1072	Phosphorylation	KQWQDSSTQPELSSR CCCCCCCCCCCCCCC	52.69	27732954
1077	Phosphorylation	SSTQPELSSRYLIST CCCCCCCCCCEEEEC	15.88	27732954
1078	Phosphorylation	STQPELSSRYLISTG CCCCCCCCCEEEECC	37.25	27732954
1105	N-linked_Glycosylation	SIQPSEENVSSSDTG EECCCCCCCCCCCCC	34.61	UniProtKB CARBOHYD
1223	Phosphorylation	VMEGLLPSQRPTTSE HHHCCCCCCCCCCCC	38.50	24719451
1241	Phosphorylation	PRVEGMVTEKPANTL CCEEECEECCCCCEE	29.42	22210691
1247	O-linked_Glycosylation	VTEKPANTLLPLGGD EECCCCCEEECCCCC	31.60	OGP
1276	N-linked_Glycosylation	LKLPNNMNQTKSSEP CCCCCCCCCCCCCCC	48.79	UniProtKB CARBOHYD
1301	N-linked_Glycosylation	ITEGFLLNASNYKQL HHHCEEEECCCCEEE	43.39	UniProtKB CARBOHYD
1321	N-linked_Glycosylation	SAHWIVGNWSECSTT CEEEEECCHHHHCCC	28.36	UniProtKB CARBOHYD
1372	N-linked_Glycosylation	CAGWKVGNWSKCSRN CCCCEECCCHHCCCC	42.72	UniProtKB CARBOHYD
1379	N-linked_Glycosylation	NWSKCSRNCSGGFKI CCHHCCCCCCCCCEE	14.17	UniProtKB CARBOHYD
1504	N-linked_Glycosylation	QCVPSEGNKTEDQDQ EECCCCCCCCCCCCC	43.98	UniProtKB CARBOHYD

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ATS12_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATS12_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ATS12_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBR1_HUMAN	UBR1	physical	26186194
FKBP9_HUMAN	FKBP9	physical	26186194
SP3_HUMAN	SP3	physical	26186194
PPM1A_HUMAN	PPM1A	physical	26186194
SNRK_HUMAN	SNRK	physical	26186194
USF2_HUMAN	USF2	physical	26186194
USF1_HUMAN	USF1	physical	26186194
SNRK_HUMAN	SNRK	physical	28514442
USF1_HUMAN	USF1	physical	28514442
UBR1_HUMAN	UBR1	physical	28514442
PPM1A_HUMAN	PPM1A	physical	28514442
FKBP9_HUMAN	FKBP9	physical	28514442
USF2_HUMAN	USF2	physical	28514442
RUFY3_HUMAN	RUFY3	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-236, ANDMASS SPECTROMETRY.
PubMed: 17081983