GSLG1_CAEEL - dbPTM
GSLG1_CAEEL - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GSLG1_CAEEL
UniProt AC Q19459
Protein Name Golgi apparatus protein 1 homolog
Gene Name F14E5.2
Organism Caenorhabditis elegans.
Sequence Length 1149
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description
Protein Sequence MWRFPLILASVCWLTTAQQQNVANDPDKKLASFDACKADIHKHCSRPDVDLTSDMSILECLQDAGFSETATLSEQCEQLVWDFKVKITQDERFVSAAKQYCEEELKGNAAMNLCTSQTQPGFALSCLMEFTKNVTETGKCHAFLARTERLAFSDFRLVGPFVTKCRAILDKFKCNVLTPDPAHKGVRVAHTQGMALECILDKVVKNAKTQADALQILGDDCKHEVLRLAEMQADDFHLDRPLFFACRLDRERYCKDVPSGEGKVFECLMMNRNDKFMDPECGNLLAERAYLMGRDYRMAHPLTKACQPELTRYKCEPQNQIESAAHFHLAWILLCLENGANQPEHKEVQPSKECAHEMITHRQMMMQHFRMAPELVLNCAQEIDKWCSPRGDIEAEGRTLHCLMEHAESRNETLKLGAQCLQAVQQVVKVADIGRNYKVDKVLYGSCRSLIDGPCAQDAVSETATLTCLMRNVDSPDMVPECEKRLLEVQYFMARDWTMDPQLYEACHQEAVSRCSALDNWHQQHNSDNTVDRGPQVLACLYRSAYDEQNPLSVKCGTQVRQLLHVRAVRVNLIPEIEDSCREALSEFCSHNVKPSEEMMCLQQNFETDNFKRKHPQCFAELTKFTEMEAKDTKLNRALSKACKPVISTHCAQFANEEIDHGDVLECLVNNKDAKEMNNKCRSYVNHFELISLRDYHFSYKFQKACASDIEQSCKGHNNDKGEIIRCLSEVRFEHKVLGSPKDLTDDCKKQLKVAYLQQEQVEFDDKEHMADADPKLSQKCEQEIKMYKCNQADTFEDTIECLRLNFEHLGPECKSMIFYREKIEAVDNSMDDELQKKCRYDIGKFCANSDSENVLECLTNTKIVRLLQRECKAIVKERMQESARDVRLRPQLLTSCRKEAEQYCPEDMKKINMPQYSQTVLDGVVVSCLRDKFRQSISDQNHIDFSPRCSAEVSRAIVEAEFDPQLDPPLYNACKSTINDHCSATIMESGGHFDNVMECLKNDFNKGLIRDKQCSEQVARRLQESLVDIHLDPVLHEACAMDIQRYCRDVPPGHSRIVMCLMDSADKQELSKECSTKLSDRNKLWMKAHSEFQMALPDSWHAFANLVMEHPERNSILGYLAGFIVFILLIGCCCGRVSKKQYIEMKNR
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
133N-linked_GlycosylationCLMEFTKNVTETGKC
HHHHHHCCCCCCCCC
42.77-
411N-linked_GlycosylationMEHAESRNETLKLGA
HHHHHHHHHHHHHHH
56.7517761667
830PhosphorylationKIEAVDNSMDDELQK
HHHHHCCCCCHHHHH
21.0828854356
850PhosphorylationIGKFCANSDSENVLE
HHHHHCCCCCCCHHH
24.8030078680
1072PhosphorylationSADKQELSKECSTKL
CCCHHHHHHHHHHHH
26.1719530675
1076PhosphorylationQELSKECSTKLSDRN
HHHHHHHHHHHHHHH
29.6619530675
1077PhosphorylationELSKECSTKLSDRNK
HHHHHHHHHHHHHHC
47.8919530675

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 GSLG1_CAEEL !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GSLG1_CAEEL !!

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 GSLG1_CAEEL !!

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

Oops, there are no PPI records of GSLG1_CAEEL !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GSLG1_CAEEL

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditiselegans and suggests an atypical translocation mechanism for integralmembrane proteins.";
Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,Taoka M., Takahashi N., Isobe T.;
Mol. Cell. Proteomics 6:2100-2109(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-411, AND MASSSPECTROMETRY.
"Lectin affinity capture, isotope-coded tagging and mass spectrometryto identify N-linked glycoproteins.";
Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,Kasai K., Takahashi N., Isobe T.;
Nat. Biotechnol. 21:667-672(2003).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-411, AND MASSSPECTROMETRY.

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