SG1D2_HUMAN - dbPTM
SG1D2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SG1D2_HUMAN
UniProt AC O95969
Protein Name Secretoglobin family 1D member 2
Gene Name SCGB1D2
Organism Homo sapiens (Human).
Sequence Length 90
Subcellular Localization Secreted .
Protein Description May bind androgens and other steroids, may also bind estramustine, a chemotherapeutic agent used for prostate cancer. May be under transcriptional regulation of steroid hormones..
Protein Sequence MKLSVCLLLVTLALCCYQANAEFCPALVSELLDFFFISEPLFKLSLAKFDAPPEAVAAKLGVKRCTDQMSLQKRSLIAEVLVKILKKCSV
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

Oops, there are no PTM records of SG1D2_HUMAN !!

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 SG1D2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SG1D2_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 SG1D2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COEA1_HUMANCOL14A1physical
28514442
FSTL1_HUMANFSTL1physical
28514442
MBRL_HUMANTMEM259physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SG1D2_HUMAN

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Related Literatures of Post-Translational Modification

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