ERGI1_HUMAN - dbPTM
ERGI1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERGI1_HUMAN
UniProt AC Q969X5
Protein Name Endoplasmic reticulum-Golgi intermediate compartment protein 1
Gene Name ERGIC1
Organism Homo sapiens (Human).
Sequence Length 290
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Endoplasmic reticulum-Golgi intermediate compartment membrane
Multi-pass membrane protein . Golgi apparatus membrane
Multi-pass membrane protein . Cycles between the endoplasmic retic
Protein Description Possible role in transport between endoplasmic reticulum and Golgi..
Protein Sequence MPFDFRRFDIYRKVPKDLTQPTYTGAIISICCCLFILFLFLSELTGFITTEVVNELYVDDPDKDSGGKIDVSLNISLPNLHCELVGLDIQDEMGRHEVGHIDNSMKIPLNNGAGCRFEGQFSINKVPGNFHVSTHSATAQPQNPDMTHVIHKLSFGDTLQVQNIHGAFNALGGADRLTSNPLASHDYILKIVPTVYEDKSGKQRYSYQYTVANKEYVAYSHTGRIIPAIWFRYDLSPITVKYTERRQPLYRFITTICAIIGGTFTVAGILDSCIFTASEAWKKIQLGKMH
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
11PhosphorylationDFRRFDIYRKVPKDL
CCCCCCCCCCCCCCC		13.26-
14UbiquitinationRFDIYRKVPKDLTQP
CCCCCCCCCCCCCCC		5.4321963094
74N-linked_GlycosylationGKIDVSLNISLPNLH
CEEEEEEEEECCCCE		17.8115308636
98UbiquitinationDEMGRHEVGHIDNSM
CCCCCCCCCCCCCCC		5.7421890473
98 (in isoform 2)Ubiquitination-5.7421890473
106UbiquitinationGHIDNSMKIPLNNGA
CCCCCCCEEECCCCC		40.7821963094
122UbiquitinationCRFEGQFSINKVPGN
EEEEEEEEEEECCCC		19.8421963094
130UbiquitinationINKVPGNFHVSTHSA
EEECCCCEEEEECCC		8.1421963094
138O-linked_GlycosylationHVSTHSATAQPQNPD
EEEECCCCCCCCCCC		28.92OGP
149 (in isoform 2)Ubiquitination-3.4521890473
149UbiquitinationQNPDMTHVIHKLSFG
CCCCCCEEEEECCCC		3.4521890473
184PhosphorylationLTSNPLASHDYILKI
CCCCCCCCCCEEEEE		25.2828152594
187PhosphorylationNPLASHDYILKIVPT
CCCCCCCEEEEEECE		11.6128152594
190 (in isoform 1)Ubiquitination-31.9021890473
190AcetylationASHDYILKIVPTVYE
CCCCEEEEEECEEEE		31.9027452117
1902-HydroxyisobutyrylationASHDYILKIVPTVYE
CCCCEEEEEECEEEE		31.90-
190UbiquitinationASHDYILKIVPTVYE
CCCCEEEEEECEEEE		31.9021906983
196UbiquitinationLKIVPTVYEDKSGKQ
EEEECEEEECCCCCE		22.3827667366
196PhosphorylationLKIVPTVYEDKSGKQ
EEEECEEEECCCCCE		22.38-
1992-HydroxyisobutyrylationVPTVYEDKSGKQRYS
ECEEEECCCCCEEEE		49.52-
199UbiquitinationVPTVYEDKSGKQRYS
ECEEEECCCCCEEEE		49.5233845483
202UbiquitinationVYEDKSGKQRYSYQY
EEECCCCCEEEEEEE		38.40-
209PhosphorylationKQRYSYQYTVANKEY
CEEEEEEEEECCCEE		8.5718491316
214UbiquitinationYQYTVANKEYVAYSH
EEEEECCCEEEEEEC		40.4621890473
216PhosphorylationYTVANKEYVAYSHTG
EEECCCEEEEEECCC		7.62-
219PhosphorylationANKEYVAYSHTGRII
CCCEEEEEECCCCEE		7.31-
236PhosphorylationIWFRYDLSPITVKYT
EEEECCCCCCEEEEC		16.03-
238UbiquitinationFRYDLSPITVKYTER
EECCCCCCEEEECCC		6.5921963094
239PhosphorylationRYDLSPITVKYTERR
ECCCCCCEEEECCCC		17.8425599653
241UbiquitinationDLSPITVKYTERRQP
CCCCCEEEECCCCCH		37.4921963094
2412-HydroxyisobutyrylationDLSPITVKYTERRQP
CCCCCEEEECCCCCH		37.49-
241 (in isoform 1)Ubiquitination-37.4921890473
241AcetylationDLSPITVKYTERRQP
CCCCCEEEECCCCCH		37.4927452117
243PhosphorylationSPITVKYTERRQPLY
CCCEEEECCCCCHHH		19.8025599653
265UbiquitinationAIIGGTFTVAGILDS
HHHCCCCCHHHHHHH		14.8621890473
273S-palmitoylationVAGILDSCIFTASEA
HHHHHHHHCEECHHH		2.7129575903
288MalonylationWKKIQLGKMH-----
HHHHHCCCCC-----		42.2526320211
288UbiquitinationWKKIQLGKMH-----
HHHHHCCCCC-----		42.2533845483
312Ubiquitination-----------------------------
-----------------------------		27667366
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 ERGI1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERGI1_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 ERGI1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERGI3_HUMANERGIC3physical
15308636
FAF2_HUMANFAF2physical
22939629
GNAI2_HUMANGNAI2physical
22939629
TOM7_HUMANTOMM7physical
22939629
VATB1_HUMANATP6V1B1physical
22939629
HIG1A_HUMANHIGD1Aphysical
22939629
ITA2_HUMANITGA2physical
22939629
NDUV1_HUMANNDUFV1physical
22939629
RM11_HUMANMRPL11physical
22939629
RM32_HUMANMRPL32physical
22939629
UCRI_HUMANUQCRFS1physical
22939629
IST1_HUMANIST1physical
22939629
ICT1_HUMANICT1physical
22939629
GOGB1_HUMANGOLGB1physical
22939629
AINX_HUMANINAphysical
26186194
EFNB1_HUMANEFNB1physical
26186194
AINX_HUMANINAphysical
28514442
EFNB1_HUMANEFNB1physical
28514442
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 ERGI1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74, AND MASS SPECTROMETRY.
"Proteomics of endoplasmic reticulum-Golgi intermediate compartment(ERGIC) membranes from brefeldin A-treated HepG2 cells identifiesERGIC-32, a new cycling protein that interacts with human Erv46.";
Breuza L., Halbeisen R., Jenoe P., Otte S., Barlowe C., Hong W.,Hauri H.-P.;
J. Biol. Chem. 279:47242-47253(2004).
Cited for: PROTEIN SEQUENCE OF 177-199 AND 233-241, SUBCELLULAR LOCATION,TOPOLOGY, GLYCOSYLATION, AND INTERACTION WITH ERGIC3.

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