ERGI3_HUMAN - dbPTM
ERGI3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERGI3_HUMAN
UniProt AC Q9Y282
Protein Name Endoplasmic reticulum-Golgi intermediate compartment protein 3
Gene Name ERGIC3
Organism Homo sapiens (Human).
Sequence Length 383
Subcellular Localization Endoplasmic reticulum-Golgi intermediate compartment membrane
Multi-pass membrane protein . Golgi apparatus, cis-Golgi network membrane
Multi-pass membrane protein . Endoplasmic reticulum membrane
Multi-pass membrane protein . Cycles between th
Protein Description Possible role in transport between endoplasmic reticulum and Golgi..
Protein Sequence MEALGKLKQFDAYPKTLEDFRVKTCGGATVTIVSGLLMLLLFLSELQYYLTTEVHPELYVDKSRGDKLKINIDVLFPHMPCAYLSIDAMDVAGEQQLDVEHNLFKQRLDKDGIPVSSEAERHELGKVEVTVFDPDSLDPDRCESCYGAEAEDIKCCNTCEDVREAYRRRGWAFKNPDTIEQCRREGFSQKMQEQKNEGCQVYGFLEVNKVAGNFHFAPGKSFQQSHVHVHDLQSFGLDNINMTHYIQHLSFGEDYPGIVNPLDHTNVTAPQASMMFQYFVKVVPTVYMKVDGEVLRTNQFSVTRHEKVANGLLGDQGLPGVFVLYELSPMMVKLTEKHRSFTHFLTGVCAIIGGMFTVAGLIDSLIYHSARAIQKKIDLGKTT
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
1Acetylation-------MEALGKLK
-------CCCCHHHH
6.4925944712
62-Hydroxyisobutyrylation--MEALGKLKQFDAY
--CCCCHHHHHCCCC
54.05-
6Ubiquitination--MEALGKLKQFDAY
--CCCCHHHHHCCCC
54.05-
8UbiquitinationMEALGKLKQFDAYPK
CCCCHHHHHCCCCCC
53.0221890473
82-HydroxyisobutyrylationMEALGKLKQFDAYPK
CCCCHHHHHCCCCCC
53.02-
8 (in isoform 1)Ubiquitination-53.0221890473
8 (in isoform 3)Ubiquitination-53.0221890473
8 (in isoform 2)Ubiquitination-53.0221890473
13PhosphorylationKLKQFDAYPKTLEDF
HHHHCCCCCCCHHHC
13.7027762562
15UbiquitinationKQFDAYPKTLEDFRV
HHCCCCCCCHHHCCC
53.7321890473
15 (in isoform 1)Ubiquitination-53.7321890473
15 (in isoform 3)Ubiquitination-53.7321890473
15 (in isoform 2)Ubiquitination-53.7321890473
83PhosphorylationFPHMPCAYLSIDAMD
CCCCCCEEEEEECCC
14.01-
1102-HydroxyisobutyrylationLFKQRLDKDGIPVSS
HHHHHCCCCCCCCCC
63.55-
110UbiquitinationLFKQRLDKDGIPVSS
HHHHHCCCCCCCCCC
63.55-
116 (in isoform 3)Phosphorylation-19.6727251275
116PhosphorylationDKDGIPVSSEAERHE
CCCCCCCCCHHHHHC
19.6729255136
117PhosphorylationKDGIPVSSEAERHEL
CCCCCCCCHHHHHCC
40.8529255136
126UbiquitinationAERHELGKVEVTVFD
HHHHCCCCEEEEEEC
48.09-
130PhosphorylationELGKVEVTVFDPDSL
CCCCEEEEEECHHHC
11.2730177828
130O-linked_GlycosylationELGKVEVTVFDPDSL
CCCCEEEEEECHHHC
11.27OGP
136PhosphorylationVTVFDPDSLDPDRCE
EEEECHHHCCHHHCC
39.8130177828
174 (in isoform 2)Ubiquitination-60.8821890473
174 (in isoform 1)Ubiquitination-60.8821890473
174 (in isoform 3)Ubiquitination-60.8821890473
174UbiquitinationRRRGWAFKNPDTIEQ
HHCCCCCCCHHHHHH
60.8821906983
190 (in isoform 2)Ubiquitination-41.1621890473
190 (in isoform 1)Ubiquitination-41.1621890473
190 (in isoform 3)Ubiquitination-41.1621890473
190SumoylationRREGFSQKMQEQKNE
HHCCHHHHHHHHHCC
41.16-
190UbiquitinationRREGFSQKMQEQKNE
HHCCHHHHHHHHHCC
41.161906983
190SumoylationRREGFSQKMQEQKNE
HHCCHHHHHHHHHCC
41.16-
195UbiquitinationSQKMQEQKNEGCQVY
HHHHHHHHCCCCEEE
57.10-
202PhosphorylationKNEGCQVYGFLEVNK
HCCCCEEEEEEEEEE
4.01-
209UbiquitinationYGFLEVNKVAGNFHF
EEEEEEEEEECEEEC
38.34-
241N-linked_GlycosylationSFGLDNINMTHYIQH
HCCCCCCCCHHHHHH
35.2419159218
266N-linked_GlycosylationVNPLDHTNVTAPQAS
CCCCCCCCCCCCCHH
26.23UniProtKB CARBOHYD
289UbiquitinationVVPTVYMKVDGEVLR
CCCEEEEEECCEEEE
21.35-
337UbiquitinationMMVKLTEKHRSFTHF
HHHHHHHHHHHHHHH
38.80-
381UbiquitinationQKKIDLGKTT-----
HHHHCCCCCC-----
57.18-
382PhosphorylationKKIDLGKTT------
HHHCCCCCC------
35.6221712546
383PhosphorylationKIDLGKTT-------
HHCCCCCC-------
39.8521712546

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 ERGI3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERGI3_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 ERGI3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COX16_HUMANCOX16physical
26186194
PXMP2_HUMANPXMP2physical
26186194
AT1A3_HUMANATP1A3physical
26186194
TM87A_HUMANTMEM87Aphysical
26186194
ZNT9_HUMANSLC30A9physical
26186194
DJC11_HUMANDNAJC11physical
26186194
FLVC1_HUMANFLVCR1physical
26186194
PARL_HUMANPARLphysical
26186194
MFAP3_HUMANMFAP3physical
26186194
TM192_HUMANTMEM192physical
26186194
FACR2_HUMANFAR2physical
26186194
ARV1_HUMANARV1physical
26186194
CLPT1_HUMANCLPTM1physical
26186194
ABCB6_HUMANABCB6physical
26186194
S38AA_HUMANSLC38A10physical
26186194
S26A2_HUMANSLC26A2physical
26186194
EXT1_HUMANEXT1physical
26186194
PSN2_HUMANPSEN2physical
26186194
TM246_HUMANTMEM246physical
26186194
GPAT4_HUMANAGPAT6physical
26186194
STOM_HUMANSTOMphysical
26186194
STAR3_HUMANSTARD3physical
26186194
VMP1_HUMANVMP1physical
26186194
ERGI2_HUMANERGIC2physical
26186194
AN13D_HUMANANKRD13Dphysical
26186194
AN13A_HUMANANKRD13Aphysical
26186194
LMBD2_HUMANLMBRD2physical
26186194
T184B_HUMANTMEM184Bphysical
26186194
PM34_HUMANSLC25A17physical
26186194
TM223_HUMANTMEM223physical
26186194
CHPT1_HUMANCHPT1physical
26186194
GLPK_HUMANGKphysical
26186194
NDC1_HUMANNDC1physical
26186194
PIGU_HUMANPIGUphysical
26186194
BDH_HUMANBDH1physical
26186194
SFXN5_HUMANSFXN5physical
26186194
WRB_HUMANWRBphysical
26186194
TM186_HUMANTMEM186physical
26186194
TIM16_HUMANPAM16physical
26186194
COT2_HUMANNR2F2physical
26186194
RER1_HUMANRER1physical
26186194
YIPF3_HUMANYIPF3physical
26186194
MOT13_HUMANSLC16A13physical
26186194
S2546_HUMANSLC25A46physical
26186194
SGPP1_HUMANSGPP1physical
26186194
BSCL2_HUMANBSCL2physical
26186194
PTPM1_HUMANPTPMT1physical
26186194
DOLK_HUMANDOLKphysical
26186194
MTFP1_HUMANMTFP1physical
26186194
ALG3_HUMANALG3physical
26186194
ERGI2_HUMANERGIC2physical
28514442
AN13D_HUMANANKRD13Dphysical
28514442
DOLK_HUMANDOLKphysical
28514442
MOT13_HUMANSLC16A13physical
28514442
CLPT1_HUMANCLPTM1physical
28514442
TM87A_HUMANTMEM87Aphysical
28514442
EXT1_HUMANEXT1physical
28514442
COPG1_HUMANCOPG1physical
28514442
S26A2_HUMANSLC26A2physical
28514442
T184B_HUMANTMEM184Bphysical
28514442
SFXN5_HUMANSFXN5physical
28514442
TM223_HUMANTMEM223physical
28514442
TM192_HUMANTMEM192physical
28514442
ZNT9_HUMANSLC30A9physical
28514442
STAR3_HUMANSTARD3physical
28514442
PXMP2_HUMANPXMP2physical
28514442
CHPT1_HUMANCHPT1physical
28514442
SPP2B_HUMANSPPL2Bphysical
28514442
COT2_HUMANNR2F2physical
28514442
LMBD2_HUMANLMBRD2physical
28514442
S2546_HUMANSLC25A46physical
28514442
ADT3_HUMANSLC25A6physical
28514442
NDC1_HUMANNDC1physical
28514442
MFAP3_HUMANMFAP3physical
28514442
PARL_HUMANPARLphysical
28514442
COX16_HUMANCOX16physical
28514442
BDH_HUMANBDH1physical
28514442
TIM29_HUMANC19orf52physical
28514442
STOM_HUMANSTOMphysical
28514442
WRB_HUMANWRBphysical
28514442
SSRA_HUMANSSR1physical
28514442
TPPC5_HUMANTRAPPC5physical
28514442
AN13A_HUMANANKRD13Aphysical
28514442
SGPP1_HUMANSGPP1physical
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 ERGI3_HUMAN

loading...

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-241, AND MASSSPECTROMETRY.

TOP