PADI1_HUMAN - dbPTM
PADI1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PADI1_HUMAN
UniProt AC Q9ULC6
Protein Name Protein-arginine deiminase type-1
Gene Name PADI1
Organism Homo sapiens (Human).
Sequence Length 663
Subcellular Localization Cytoplasm .
Protein Description Catalyzes the deimination of arginine residues of proteins..
Protein Sequence MAPKRVVQLSLKMPTHAVCVVGVEAHVDIHSDVPKGANSFRVSGSSGVEVFMVYNRTRVKEPIGKARWPLDTDADMVVSVGTASKELKDFKVRVSYFGEQEDQALGRSVLYLTGVDISLEVDTGRTGKVKRSQGDKKTWRWGPEGYGAILLVNCDRDNHRSAEPDLTHSWLMSLADLQDMSPMLLSCNGPDKLFDSHKLVLNVPFSDSKRVRVFCARGGNSLSDYKQVLGPQCLSYEVERQPGEQEIKFYVEGLTFPDADFLGLVSLSVSLVDPGTLPEVTLFTDTVGFRMAPWIMTPNTQPPEELYVCRVMDTHGSNEKFLEDMSYLTLKANCKLTICPQVENRNDRWIQDEMEFGYIEAPHKSFPVVFDSPRNRGLKDFPYKRILGPDFGYVTREIPLPGPSSLDSFGNLDVSPPVTVGGTEYPLGRILIGSSFPKSGGRQMARAVRNFLKAQQVQAPVELYSDWLSVGHVDEFLTFVPTSDQKGFRLLLASPSACLKLFQEKKEEGYGEAAQFDGLKHQAKRSINEMLADRHLQRDNLHAQKCIDWNRNVLKRELGLAESDIVDIPQLFFLKNFYAEAFFPDMVNMVVLGKYLGIPKPYGPIINGRCCLEEKVQSLLEPLGLHCIFIDDYLSYHELQGEIHCGTNVRRKPFPFKWWNMVP
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
39PhosphorylationDVPKGANSFRVSGSS
CCCCCCCCEEEECCC
17.56-
45PhosphorylationNSFRVSGSSGVEVFM
CCEEEECCCCEEEEE
19.2021712546
57PhosphorylationVFMVYNRTRVKEPIG
EEEEEECCCCCCCCC
35.8621712546
72PhosphorylationKARWPLDTDADMVVS
CCCCCCCCCCCEEEE
40.55-
132PhosphorylationRTGKVKRSQGDKKTW
CCCCEECCCCCCCCE
32.5620393185
175UbiquitinationHSWLMSLADLQDMSP
HHHHHHHHHHHHCCC
14.2516196087
196PhosphorylationGPDKLFDSHKLVLNV
CCCCCCCCCEEEEEC
18.39-
206PhosphorylationLVLNVPFSDSKRVRV
EEEECCCCCCCCEEE
34.60-
208PhosphorylationLNVPFSDSKRVRVFC
EECCCCCCCCEEEEE
22.59-
226AcetylationGNSLSDYKQVLGPQC
CCCHHHHHHHHCHHC
38.6371333
226UbiquitinationGNSLSDYKQVLGPQC
CCCHHHHHHHHCHHC
38.6316196087
326PhosphorylationEKFLEDMSYLTLKAN
HHHHHHCCHHHHCCC
29.3419835603
327PhosphorylationKFLEDMSYLTLKANC
HHHHHCCHHHHCCCC
9.3219835603
329PhosphorylationLEDMSYLTLKANCKL
HHHCCHHHHCCCCEE
20.2730619164
372PhosphorylationSFPVVFDSPRNRGLK
CCCEEECCCCCCCCC
17.8124719451
439PhosphorylationIGSSFPKSGGRQMAR
ECCCCCCCCHHHHHH
46.8718452278
494PhosphorylationGFRLLLASPSACLKL
CHHHEEECHHHHHHH
21.25-
595PhosphorylationNMVVLGKYLGIPKPY
HHHHHHHHCCCCCCC
14.36-
602PhosphorylationYLGIPKPYGPIINGR
HCCCCCCCCCCCCCE
41.48-

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 PADI1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PADI1_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 PADI1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STAP2_HUMANSTAP2physical
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
DB00155L-Citrulline
Regulatory Network of PADI1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP