GOLI4_HUMAN - dbPTM
GOLI4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GOLI4_HUMAN
UniProt AC O00461
Protein Name Golgi integral membrane protein 4
Gene Name GOLIM4
Organism Homo sapiens (Human).
Sequence Length 696
Subcellular Localization Golgi apparatus, Golgi stack membrane
Single-pass type II membrane protein. Endosome membrane
Single-pass type II membrane protein. Membrane
Lipid-anchor . Localizes to cis and medial Golgi cisternae. Probably cycles between early Golgi and dista
Protein Description Plays a role in endosome to Golgi protein trafficking; mediates protein transport along the late endosome-bypass pathway from the early endosome to the Golgi..
Protein Sequence MGNGMCSRKQKRIFQTLLLLTVVFGFLYGAMLYYELQTQLRKAEAVALKYQQHQESLSAQLQVVYEHRSRLEKSLQKERLEHKKAKEDFLVYKLEAQETLNKGRQDSNSRYSALNVQHQMLKSQHEELKKQHSDLEEEHRKQGEDFSRTFNDHKQKYLQLQQEKEQELSKLKETVYNLREENRQLRKAHQDIHTQLQDVKQQHKNLLSEHEQLVVTLEDHKSALAAAQTQVAEYKQLKDTLNRIPSLRKPDPAEQQNVTQVAHSPQGYNTAREKPTREVQEVSRNNDVWQNHEAVPGRAEDTKLYAPTHKEAEFQAPPEPIQQEVERREPEEHQVEEEHRKALEEEEMEQVGQAEHLEEEHDPSPEEQDREWKEQHEQREAANLLEGHARAEVYPSAKPMIKFQSPYEEQLEQQRLAVQQVEEAQQLREHQEALHQQRLQGHLLRQQEQQQQQVAREMALQRQAELEEGRPQHQEQLRQQAHYDAMDNDIVQGAEDQGIQGEEGAYERDNQHQDEAEGDPGNRHEPREQGPREADPESEADRAAVEDINPADDPNNQGEDEFEEAEQVREENLPDENEEQKQSNQKQENTEVEEHLVMAGNPDQQEDNVDEQYQEEAEEEVQEDLTEEKKRELEHNAEETYGENDENTDDKNNDGEEQEVRDDNRPKGREEHYEEEEEEEEDGAAVAEKSHRRAEM
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
2Myristoylation------MGNGMCSRK
------CCCCCCCHH		39.1225255805
6S-palmitoylation--MGNGMCSRKQKRI
--CCCCCCCHHHHHH		3.6429575903
21PhosphorylationFQTLLLLTVVFGFLY
HHHHHHHHHHHHHHH		18.0022210691
38PhosphorylationMLYYELQTQLRKAEA
HHHHHHHHHHHHHHH		42.0424719451
422-HydroxyisobutyrylationELQTQLRKAEAVALK
HHHHHHHHHHHHHHH		60.20-
102UbiquitinationEAQETLNKGRQDSNS
HHHHHHHCCCCCCCH		59.59-
141AcetylationDLEEEHRKQGEDFSR
HHHHHHHHHCCCHHH		65.6430589005
1562-HydroxyisobutyrylationTFNDHKQKYLQLQQE
HHHHHHHHHHHHHHH		53.37-
156AcetylationTFNDHKQKYLQLQQE
HHHHHHHHHHHHHHH		53.3727452117
1642-HydroxyisobutyrylationYLQLQQEKEQELSKL
HHHHHHHHHHHHHHH		61.43-
169PhosphorylationQEKEQELSKLKETVY
HHHHHHHHHHHHHHH		34.8826074081
170SumoylationEKEQELSKLKETVYN
HHHHHHHHHHHHHHH		75.98-
170SumoylationEKEQELSKLKETVYN
HHHHHHHHHHHHHHH		75.98-
174PhosphorylationELSKLKETVYNLREE
HHHHHHHHHHHHHHH		27.0626074081
176PhosphorylationSKLKETVYNLREENR
HHHHHHHHHHHHHHH		18.8526074081
194O-linked_GlycosylationKAHQDIHTQLQDVKQ
HHHHHHHHHHHHHHH		31.1755826935
208O-linked_GlycosylationQQHKNLLSEHEQLVV
HHHHHHCHHHHHHEE		39.82OGP
216O-linked_GlycosylationEHEQLVVTLEDHKSA
HHHHHEEEHHHHHHH		19.5655832977
222O-linked_GlycosylationVTLEDHKSALAAAQT
EEHHHHHHHHHHHHH		25.7055833817
229O-linked_GlycosylationSALAAAQTQVAEYKQ
HHHHHHHHHHHHHHH		21.9355833821
246O-linked_GlycosylationDTLNRIPSLRKPDPA
HHHHCCCHHCCCCHH		38.13OGP
246PhosphorylationDTLNRIPSLRKPDPA
HHHHCCCHHCCCCHH		38.1324719451
257N-linked_GlycosylationPDPAEQQNVTQVAHS
CCHHHHCCCCEEECC		38.20UniProtKB CARBOHYD
259O-linked_GlycosylationPAEQQNVTQVAHSPQ
HHHHCCCCEEECCCC		25.52OGP
264O-linked_GlycosylationNVTQVAHSPQGYNTA
CCCEEECCCCCCCCC		14.80OGP
264PhosphorylationNVTQVAHSPQGYNTA
CCCEEECCCCCCCCC		14.8029214152
270O-linked_GlycosylationHSPQGYNTAREKPTR
CCCCCCCCCCCCCCH		20.7155830239
276PhosphorylationNTAREKPTREVQEVS
CCCCCCCCHHHHHHH		50.99-
276O-linked_GlycosylationNTAREKPTREVQEVS
CCCCCCCCHHHHHHH		50.9955824949
283PhosphorylationTREVQEVSRNNDVWQ
CHHHHHHHCCCCCHH		28.6522496350
283O-linked_GlycosylationTREVQEVSRNNDVWQ
CHHHHHHHCCCCCHH		28.6567054043
302O-linked_GlycosylationVPGRAEDTKLYAPTH
CCCCCCCCCCCCCCC		17.9155834973
305PhosphorylationRAEDTKLYAPTHKEA
CCCCCCCCCCCCCCC		16.4627642862
308O-linked_GlycosylationDTKLYAPTHKEAEFQ
CCCCCCCCCCCCCCC		37.0955826277
364PhosphorylationLEEEHDPSPEEQDRE
HHHHCCCCHHHHHHH		51.5028102081
394PhosphorylationGHARAEVYPSAKPMI
HHHHHHCCCCCCCCE		5.2922817900
396PhosphorylationARAEVYPSAKPMIKF
HHHHCCCCCCCCEEC		31.1022817900
396O-linked_GlycosylationARAEVYPSAKPMIKF
HHHHCCCCCCCCEEC		31.1017081983
405O-linked_GlycosylationKPMIKFQSPYEEQLE
CCCEECCCCHHHHHH		32.3655831377
405PhosphorylationKPMIKFQSPYEEQLE
CCCEECCCCHHHHHH		32.36-
407PhosphorylationMIKFQSPYEEQLEQQ
CEECCCCHHHHHHHH		37.0327642862
483PhosphorylationQLRQQAHYDAMDNDI
HHHHHHHHHHCCCHH		14.3827642862
506PhosphorylationIQGEEGAYERDNQHQ
CCCCCCCCCCCCCCC		23.5027642862
538PhosphorylationPREADPESEADRAAV
CCCCCCCCHHHHHHH		43.4029255136
583PhosphorylationENEEQKQSNQKQENT
CCHHHHHHHHHHHHH		48.5429255136
613PhosphorylationEDNVDEQYQEEAEEE
CCCCCHHHHHHHHHH		18.8224275569
626PhosphorylationEEVQEDLTEEKKREL
HHHHHHHHHHHHHHH		55.1922468782
640PhosphorylationLEHNAEETYGENDEN
HHHCHHHHCCCCCCC		28.4728355574
641PhosphorylationEHNAEETYGENDENT
HHCHHHHCCCCCCCC		26.2325159151
648PhosphorylationYGENDENTDDKNNDG
CCCCCCCCCCCCCCC		43.4529496963
673PhosphorylationPKGREEHYEEEEEEE
CCCCHHHCHHHHHHH		28.4628355574
690PhosphorylationGAAVAEKSHRRAEM-
HHHHHHHHHHHHCC-		17.46-
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 GOLI4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GOLI4_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 GOLI4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
THIOM_HUMANTXN2physical
22939629
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 GOLI4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-394 AND SER-396, ANDMASS SPECTROMETRY.

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