STYL1_HUMAN - dbPTM
STYL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STYL1_HUMAN
UniProt AC Q9Y6J8
Protein Name Serine/threonine/tyrosine-interacting-like protein 1
Gene Name STYXL1
Organism Homo sapiens (Human).
Sequence Length 313
Subcellular Localization Mitochondrion matrix .
Protein Description Catalytically inactive phosphatase. [PubMed: 20180778]
Protein Sequence MPGLLLCEPTELYNILNQATKLSRLTDPNYLCLLDVRSKWEYDESHVITALRVKKKNNEYLLPESVDLECVKYCVVYDNNSSTLEILLKDDDDDSDSDGDGKDLVPQAAIEYGRILTRLTHHPVYILKGGYERFSGTYHFLRTQKIIWMPQELDAFQPYPIEIVPGKVFVGNFSQACDPKIQKDLKIKAHVNVSMDTGPFFAGDADKLLHIRIEDSPEAQILPFLRHMCHFIEIHHHLGSVILIFSTQGISRSCAAIIAYLMHSNEQTLQRSWAYVKKCKNNMCPNRGLVSQLLEWEKTILGDSITNIMDPLY
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
20PhosphorylationYNILNQATKLSRLTD
HHHHHHHHHHHHCCC
23.8226074081
21UbiquitinationNILNQATKLSRLTDP
HHHHHHHHHHHCCCC
47.70-
38PhosphorylationLCLLDVRSKWEYDES
EEEEECCCCCCCCHH
41.8023403867
39 (in isoform 5)Ubiquitination-33.2221906983
39UbiquitinationCLLDVRSKWEYDESH
EEEECCCCCCCCHHH
33.2221906983
39 (in isoform 4)Ubiquitination-33.2221906983
39 (in isoform 3)Ubiquitination-33.2221906983
39 (in isoform 2)Ubiquitination-33.2221906983
39 (in isoform 1)Ubiquitination-33.2221906983
45PhosphorylationSKWEYDESHVITALR
CCCCCCHHHEEEEEE
21.8423403867
49PhosphorylationYDESHVITALRVKKK
CCHHHEEEEEEEEEC
20.6724719451
56UbiquitinationTALRVKKKNNEYLLP
EEEEEEECCCCEECC
60.32-
60PhosphorylationVKKKNNEYLLPESVD
EEECCCCEECCCCCC
18.7028152594
65PhosphorylationNEYLLPESVDLECVK
CCEECCCCCCCEEEE
20.9928152594
95PhosphorylationLKDDDDDSDSDGDGK
ECCCCCCCCCCCCCC
46.11-
97PhosphorylationDDDDDSDSDGDGKDL
CCCCCCCCCCCCCCC
47.66-
102UbiquitinationSDSDGDGKDLVPQAA
CCCCCCCCCCHHHHH
53.26-
128 (in isoform 1)Ubiquitination-40.5121906983
128 (in isoform 2)Ubiquitination-40.5121906983
128 (in isoform 3)Ubiquitination-40.5121906983
128UbiquitinationHHPVYILKGGYERFS
CCCEEEEECCCCCCC
40.5121906983
137PhosphorylationGYERFSGTYHFLRTQ
CCCCCCEEEEEEEEC
16.7822210691
145 (in isoform 1)Ubiquitination-35.2321906983
145 (in isoform 2)Ubiquitination-35.2321906983
145UbiquitinationYHFLRTQKIIWMPQE
EEEEEECEEEEECCC
35.232190698
145 (in isoform 3)Ubiquitination-35.2321906983
180UbiquitinationFSQACDPKIQKDLKI
HHHCCCHHHCCCCEE
44.51-
278UbiquitinationRSWAYVKKCKNNMCP
HHHHHHHHHCCCCCC
40.16-

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 STYL1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STYL1_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 STYL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AES_HUMANAESphysical
17353931
SMC1A_HUMANSMC1Aphysical
17353931
RS29_HUMANRPS29physical
17353931
ATX10_HUMANATXN10physical
17353931
EHD4_HUMANEHD4physical
17353931
SERB_HUMANPSPHphysical
17353931
ACTS_HUMANACTA1physical
27880917
MYO1B_HUMANMYO1Bphysical
27880917
MYO1C_HUMANMYO1Cphysical
27880917
SPTN1_HUMANSPTAN1physical
27880917
SPTB2_HUMANSPTBN1physical
27880917
VIME_HUMANVIMphysical
27880917

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 STYL1_HUMAN

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Related Literatures of Post-Translational Modification

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