GSLG1_HUMAN - dbPTM
GSLG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GSLG1_HUMAN
UniProt AC Q92896
Protein Name Golgi apparatus protein 1
Gene Name GLG1
Organism Homo sapiens (Human).
Sequence Length 1179
Subcellular Localization Golgi apparatus membrane
Single-pass type I membrane protein .
Protein Description Binds fibroblast growth factor and E-selectin (cell-adhesion lectin on endothelial cells mediating the binding of neutrophils)..
Protein Sequence MAACGRVRRMFRLSAALHLLLLFAAGAEKLPGQGVHSQGQGPGANFVSFVGQAGGGGPAGQQLPQLPQSSQLQQQQQQQQQQQQPQPPQPPFPAGGPPARRGGAGAGGGWKLAEEESCREDVTRVCPKHTWSNNLAVLECLQDVREPENEISSDCNHLLWNYKLNLTTDPKFESVAREVCKSTITEIKECADEPVGKGYMVSCLVDHRGNITEYQCHQYITKMTAIIFSDYRLICGFMDDCKNDINILKCGSIRLGEKDAHSQGEVVSCLEKGLVKEAEEREPKIQVSELCKKAILRVAELSSDDFHLDRHLYFACRDDRERFCENTQAGEGRVYKCLFNHKFEESMSEKCREALTTRQKLIAQDYKVSYSLAKSCKSDLKKYRCNVENLPRSREARLSYLLMCLESAVHRGRQVSSECQGEMLDYRRMLMEDFSLSPEIILSCRGEIEHHCSGLHRKGRTLHCLMKVVRGEKGNLGMNCQQALQTLIQETDPGADYRIDRALNEACESVIQTACKHIRSGDPMILSCLMEHLYTEKMVEDCEHRLLELQYFISRDWKLDPVLYRKCQGDASRLCHTHGWNETSEFMPQGAVFSCLYRHAYRTEEQGRRLSRECRAEVQRILHQRAMDVKLDPALQDKCLIDLGKWCSEKTETGQELECLQDHLDDLVVECRDIVGNLTELESEDIQIEALLMRACEPIIQNFCHDVADNQIDSGDLMECLIQNKHQKDMNEKCAIGVTHFQLVQMKDFRFSYKFKMACKEDVLKLCPNIKKKVDVVICLSTTVRNDTLQEAKEHRVSLKCRRQLRVEELEMTEDIRLEPDLYEACKSDIKNFCSAVQYGNAQIIECLKENKKQLSTRCHQKVFKLQETEMMDPELDYTLMRVCKQMIKRFCPEADSKTMLQCLKQNKNSELMDPKCKQMITKRQITQNTDYRLNPMLRKACKADIPKFCHGILTKAKDDSELEGQVISCLKLRYADQRLSSDCEDQIRIIIQESALDYRLDPQLQLHCSDEISSLCAEEAAAQEQTGQVEECLKVNLLKIKTELCKKEVLNMLKESKADIFVDPVLHTACALDIKHHCAAITPGRGRQMSCLMEALEDKRVRLQPECKKRLNDRIEMWSYAAKVAPADGFSDLAMQVMTSPSKNYILSVISGSICILFLIGLMCGRITKRVTRELKDR
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
37O-linked_GlycosylationLPGQGVHSQGQGPGA
CCCCCCCCCCCCCCC
33.33OGP
69O-linked_GlycosylationQLPQLPQSSQLQQQQ
CCCCCCCHHHHHHHH
20.36OGP
70O-linked_GlycosylationLPQLPQSSQLQQQQQ
CCCCCCHHHHHHHHH
29.66OGP
117PhosphorylationWKLAEEESCREDVTR
CHHCCHHHHHCCHHH
23.04-
123PhosphorylationESCREDVTRVCPKHT
HHHHCCHHHHCCCCC
29.7023532336
165N-linked_GlycosylationLLWNYKLNLTTDPKF
HHHHCCCCCCCCHHH
31.05UniProtKB CARBOHYD
188AcetylationKSTITEIKECADEPV
HHHHHHHHHHCCCCC
40.2726051181
210N-linked_GlycosylationCLVDHRGNITEYQCH
EEECCCCCCCHHHHH
37.66UniProtKB CARBOHYD
238UbiquitinationYRLICGFMDDCKNDI
HHHHHCCCHHHCCCC
2.2929967540
242AcetylationCGFMDDCKNDINILK
HCCCHHHCCCCCEEE
65.7326051181
249UbiquitinationKNDINILKCGSIRLG
CCCCCEEECCCEECC
32.5229967540
258AcetylationGSIRLGEKDAHSQGE
CCEECCCCCCCCCCC
59.4226051181
261UbiquitinationRLGEKDAHSQGEVVS
ECCCCCCCCCCCHHH
30.6829967540
272UbiquitinationEVVSCLEKGLVKEAE
CHHHHHHHCCHHHHH
44.5929967540
272AcetylationEVVSCLEKGLVKEAE
CHHHHHHHCCHHHHH
44.5926051181
310MethylationSDDFHLDRHLYFACR
CCCCCCCHHHHEEEC
28.24-
349UbiquitinationKFEESMSEKCREALT
CCHHHHCHHHHHHHH
47.7529967540
360UbiquitinationEALTTRQKLIAQDYK
HHHHHHHHHHHCHHH
38.2729967540
370PhosphorylationAQDYKVSYSLAKSCK
HCHHHHHHHHHHHCH
15.64-
374 (in isoform 2)Ubiquitination-62.77-
374UbiquitinationKVSYSLAKSCKSDLK
HHHHHHHHHCHHHHH
62.77-
374AcetylationKVSYSLAKSCKSDLK
HHHHHHHHHCHHHHH
62.7726051181
383PhosphorylationCKSDLKKYRCNVENL
CHHHHHHHCCCHHCC
20.8624927040
416PhosphorylationVHRGRQVSSECQGEM
HHHCCCCCHHHCHHH
16.4523663014
417PhosphorylationHRGRQVSSECQGEML
HHCCCCCHHHCHHHH
43.4623663014
426PhosphorylationCQGEMLDYRRMLMED
HCHHHHHHHHHHHHC
8.9923663014
460MethylationSGLHRKGRTLHCLMK
CCCCCCCCHHHHHHH
36.83-
460DimethylationSGLHRKGRTLHCLMK
CCCCCCCCHHHHHHH
36.83-
467AcetylationRTLHCLMKVVRGEKG
CHHHHHHHHHHCCCC
25.3226051181
486O-linked_GlycosylationNCQQALQTLIQETDP
CHHHHHHHHHHHCCC
27.03OGP
491O-linked_GlycosylationLQTLIQETDPGADYR
HHHHHHHCCCCCCHH
30.99OGP
516 (in isoform 2)Ubiquitination-39.33-
516UbiquitinationSVIQTACKHIRSGDP
HHHHHHHHHHHCCCH
39.33-
551PhosphorylationHRLLELQYFISRDWK
HHHHHHHHHHHCCCC
18.59-
558 (in isoform 2)Ubiquitination-47.50-
558UbiquitinationYFISRDWKLDPVLYR
HHHHCCCCCCHHHHH
47.50-
564PhosphorylationWKLDPVLYRKCQGDA
CCCCHHHHHHCCCCH
14.3021406692
581N-linked_GlycosylationLCHTHGWNETSEFMP
HCCCCCCCCCCCCCC
47.46UniProtKB CARBOHYD
619UbiquitinationRECRAEVQRILHQRA
HHHHHHHHHHHHHHH
20.4322817900
627UbiquitinationRILHQRAMDVKLDPA
HHHHHHHCCCCCCHH
7.1122817900
630 (in isoform 2)Ubiquitination-42.8021906983
630UbiquitinationHQRAMDVKLDPALQD
HHHHCCCCCCHHHHC
42.8022817900
630 (in isoform 1)Ubiquitination-42.8021906983
638 (in isoform 2)Ubiquitination-20.2721906983
638UbiquitinationLDPALQDKCLIDLGK
CCHHHHCCCEEECCH
20.2722817900
638 (in isoform 1)Ubiquitination-20.2721906983
645UbiquitinationKCLIDLGKWCSEKTE
CCEEECCHHHCCCCC
52.9321906983
677N-linked_GlycosylationECRDIVGNLTELESE
HHHHHHCCCCCCCCC
32.6612754519
714PhosphorylationVADNQIDSGDLMECL
HHCCCCCCCCHHHHH
35.5228192239
739O-linked_GlycosylationEKCAIGVTHFQLVQM
HCCEECCEEEEEEEC
16.2655832601
747AcetylationHFQLVQMKDFRFSYK
EEEEEECCCCCCEEE
36.3090793
786N-linked_GlycosylationCLSTTVRNDTLQEAK
EECCCCCCCHHHHHH
42.13UniProtKB CARBOHYD
812SulfoxidationLRVEELEMTEDIRLE
HHHHHHCCCCCCCCC
8.5421406390
816UbiquitinationELEMTEDIRLEPDLY
HHCCCCCCCCCHHHH
4.3922817900
820UbiquitinationTEDIRLEPDLYEACK
CCCCCCCHHHHHHHH
41.3122817900
827UbiquitinationPDLYEACKSDIKNFC
HHHHHHHHHHHHHHH
59.2022817900
831 (in isoform 1)Ubiquitination-49.3021906983
831UbiquitinationEACKSDIKNFCSAVQ
HHHHHHHHHHHHHHH
49.3022817900
831 (in isoform 2)Ubiquitination-49.3021906983
851UbiquitinationIIECLKENKKQLSTR
HHHHHHHCHHHHHHH
56.0629967540
856PhosphorylationKENKKQLSTRCHQKV
HHCHHHHHHHHHHHH
16.0029116813
862UbiquitinationLSTRCHQKVFKLQET
HHHHHHHHHHHHHHH
26.4429967540
905AcetylationKTMLQCLKQNKNSEL
HHHHHHHHHCCCCCC
60.4927452117
922PhosphorylationPKCKQMITKRQITQN
HHHHHHHHHHHHHCC
18.1628555341
927PhosphorylationMITKRQITQNTDYRL
HHHHHHHHCCCCCCC
13.87-
927O-linked_GlycosylationMITKRQITQNTDYRL
HHHHHHHHCCCCCCC
13.87OGP
961PhosphorylationLTKAKDDSELEGQVI
HHCCCCCHHHHHHHH
54.9722617229
981PhosphorylationRYADQRLSSDCEDQI
HHCCHHCCCCCHHHH
26.7329449344
982PhosphorylationYADQRLSSDCEDQIR
HCCHHCCCCCHHHHH
51.3729449344
999PhosphorylationIQESALDYRLDPQLQ
HHHHHCCCCCCCCHH
17.58-
1029UbiquitinationAAQEQTGQVEECLKV
HHHHHCCCHHHHHHH
42.7232142685
1040UbiquitinationCLKVNLLKIKTELCK
HHHHCHHHHCHHHHH
45.3732142685
1042AcetylationKVNLLKIKTELCKKE
HHCHHHHCHHHHHHH
34.0727452117
1091PhosphorylationPGRGRQMSCLMEALE
CCCCHHHHHHHHHHH
8.8520068231
1120O-linked_GlycosylationNDRIEMWSYAAKVAP
HHHHHHHHHHHHCCC
12.00OGP
1179UbiquitinationVTRELKDR-------
HHHHHHCC-------
47.0222817900
1184 (in isoform 3)Phosphorylation-29052541
1188 (in isoform 3)Phosphorylation-30266825
1190 (in isoform 3)Phosphorylation-30266825
1190 (in isoform 2)Ubiquitination-21906983
1190Ubiquitination------------------
------------------
22817900
1195 (in isoform 2)Phosphorylation-29052541
1199 (in isoform 2)Phosphorylation-30266825
1201 (in isoform 2)Phosphorylation-30266825

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GSLG1_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 GSLG1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LYAM2_HUMANSELEphysical
11404363

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 GSLG1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-677.

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