ATS1_HUMAN - dbPTM
ATS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATS1_HUMAN
UniProt AC Q9UHI8
Protein Name A disintegrin and metalloproteinase with thrombospondin motifs 1
Gene Name ADAMTS1
Organism Homo sapiens (Human).
Sequence Length 967
Subcellular Localization Secreted, extracellular space, extracellular matrix.
Protein Description Cleaves aggrecan, a cartilage proteoglycan, at the '1938-Glu-|-Leu-1939' site (within the chondroitin sulfate attachment domain), 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..
Protein Sequence MQRAVPEGFGRRKLGSDMGNAERAPGSRSFGPVPTLLLLAAALLAVSDALGRPSEEDEELVVPELERAPGHGTTRLRLHAFDQQLDLELRPDSSFLAPGFTLQNVGRKSGSETPLPETDLAHCFYSGTVNGDPSSAAALSLCEGVRGAFYLLGEAYFIQPLPAASERLATAAPGEKPPAPLQFHLLRRNRQGDVGGTCGVVDDEPRPTGKAETEDEDEGTEGEDEGAQWSPQDPALQGVGQPTGTGSIRKKRFVSSHRYVETMLVADQSMAEFHGSGLKHYLLTLFSVAARLYKHPSIRNSVSLVVVKILVIHDEQKGPEVTSNAALTLRNFCNWQKQHNPPSDRDAEHYDTAILFTRQDLCGSQTCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDAKQCASLNGVNQDSHMMASMLSNLDHSQPWSPCSAYMITSFLDNGHGECLMDKPQNPIQLPGDLPGTSYDANRQCQFTFGEDSKHCPDAASTCSTLWCTGTSGGVLVCQTKHFPWADGTSCGEGKWCINGKCVNKTDRKHFDTPFHGSWGMWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNLEDCPDNNGKTFREEQCEAHNEFSKASFGSGPAVEWIPKYAGVSPKDRCKLICQAKGIGYFFVLQPKVVDGTPCSPDSTSVCVQGQCVKAGCDRIIDSKKKFDKCGVCGGNGSTCKKISGSVTSAKPGYHDIITIPTGATNIEVKQRNQRGSRNNGSFLAIKAADGTYILNGDYTLSTLEQDIMYKGVVLRYSGSSAALERIRSFSPLKEPLTIQVLTVGNALRPKIKYTYFVKKKKESFNAIPTFSAWVIEEWGECSKSCELGWQRRLVECRDINGQPASECAKEVKPASTRPCADHPCPQWQLGEWSSCSKTCGKGYKKRSLKCLSHDGGVLSHESCDPLKKPKHFIDFCTMAECS
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 Orthologous
Protein Cluster
16PhosphorylationFGRRKLGSDMGNAER
CCCCCCCCCCCCCCC
34.5668703167
170O-linked_GlycosylationAASERLATAAPGEKP
HHHHHHHHCCCCCCC
28.1355825523
197O-linked_GlycosylationRQGDVGGTCGVVDDE
CCCCCCCCCEECCCC
10.5255827657
208O-linked_GlycosylationVDDEPRPTGKAETED
CCCCCCCCCCCCCCC
53.2255827661
213PhosphorylationRPTGKAETEDEDEGT
CCCCCCCCCCCCCCC
54.3026471730
220PhosphorylationTEDEDEGTEGEDEGA
CCCCCCCCCCCCCCC
38.4826471730
230PhosphorylationEDEGAQWSPQDPALQ
CCCCCCCCCCCHHHC
10.7026471730
281PhosphorylationHGSGLKHYLLTLFSV
CCCCHHHHHHHHHHH
11.2125072903
284PhosphorylationGLKHYLLTLFSVAAR
CHHHHHHHHHHHHHH
24.1425072903
287PhosphorylationHYLLTLFSVAARLYK
HHHHHHHHHHHHHHC
17.6025072903
293PhosphorylationFSVAARLYKHPSIRN
HHHHHHHHCCHHHHH
11.1625072903
297PhosphorylationARLYKHPSIRNSVSL
HHHHCCHHHHHCEEE
33.6225072903
547N-linked_GlycosylationCINGKCVNKTDRKHF
EECCEECCCCCCCCC
51.48UniProtKB CARBOHYD
574PhosphorylationPWGDCSRTCGGGVQY
CCCCCCCCCCCCCEE
10.1450563479
581PhosphorylationTCGGGVQYTMRECDN
CCCCCCEEEEEECCC
10.4950563485
582PhosphorylationCGGGVQYTMRECDNP
CCCCCEEEEEECCCC
7.8350563491
620PhosphorylationCPDNNGKTFREEQCE
CCCCCCCCCHHHHHH
29.3523403867
639PhosphorylationFSKASFGSGPAVEWI
HHHHHCCCCCCHHCC
39.3228348404
720N-linked_GlycosylationKCGVCGGNGSTCKKI
CCCCCCCCCCCCCEE
26.90UniProtKB CARBOHYD
730PhosphorylationTCKKISGSVTSAKPG
CCCEEECCCCCCCCC
18.5521214269
732PhosphorylationKKISGSVTSAKPGYH
CEEECCCCCCCCCCC
25.3521214269
735UbiquitinationSGSVTSAKPGYHDII
ECCCCCCCCCCCCEE
38.4521890473
738PhosphorylationVTSAKPGYHDIITIP
CCCCCCCCCCEEEEC
12.5921214269
749PhosphorylationITIPTGATNIEVKQR
EEECCCCCCEEEECC
37.7721214269
764N-linked_GlycosylationNQRGSRNNGSFLAIK
CCCCCCCCCCEEEEE
46.50UniProtKB CARBOHYD
838PhosphorylationALRPKIKYTYFVKKK
HHCCCEEEEEEEECC
15.3322817900
840PhosphorylationRPKIKYTYFVKKKKE
CCCEEEEEEEECCHH
11.8622817900
901PhosphorylationKEVKPASTRPCADHP
HCCCCCCCCCCCCCC
40.5129978859
918PhosphorylationQWQLGEWSSCSKTCG
CCCCCCCCCCCCCCC
19.7129978859
919PhosphorylationWQLGEWSSCSKTCGK
CCCCCCCCCCCCCCC
24.3929978859
921PhosphorylationLGEWSSCSKTCGKGY
CCCCCCCCCCCCCCC
32.7129978859

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of ATS1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATS1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ATS1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VEGFA_HUMANVEGFAphysical
12716911

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.
Regulatory Network of ATS1_HUMAN

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Related Literatures of Post-Translational Modification

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