CTGE5_HUMAN - dbPTM
CTGE5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTGE5_HUMAN
UniProt AC O15320
Protein Name Endoplasmic reticulum export factor CTAGE5 {ECO:0000305}
Gene Name CTAGE5 {ECO:0000312|HGNC:HGNC:7057}
Organism Homo sapiens (Human).
Sequence Length 804
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type I membrane protein . Endoplasmic reticulum exit sites.
Protein Description Plays a role in the transport of cargos that are too large to fit into COPII-coated vesicles and require specific mechanisms to be incorporated into membrane-bound carriers and exported from the endoplasmic reticulum. This protein is required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers and recruiting PREB/SEC12 at the endoplasmic reticulum exit sites..
Protein Sequence MEEPGVTPQPYLGLLLEELRRVVAALPEGMRPDSNLYGFPWELVICAAVVGFFAVLFFLWRSFRSVRSRLYVGREKKLALMLSGLIEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLDNPPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPYALDVPNTAFGREHSPYGPSPLGWPSSETRAFLSPPTLLEGPLRLSPLLPGGGGRGSRGPGNPLDHQITNERGESSCDRLTDPHRAPSDTGSLSPPWDQDRRMMFPPPGQSYPDSALPPQRQDRFCSNSGRLSGPAELRSFNMPSLDKMDGSMPSEMESSRNDTKDDLGNLNVPDSSLPAENEATGPGFVPPPLAPIRGPLFPVDARGPFLRRGPPFPPPPPGAMFGASRDYFPPGDFPGPPPAPFAMRNVYPPRGFPPYLPPRPGFFPPPPHSEGRSEFPSGLIPPSNEPATEHPEPQQET
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
62 (in isoform 6)Phosphorylation-17.27-
64 (in isoform 6)Phosphorylation-35.17-
108 (in isoform 3)Phosphorylation-6.96-
110 (in isoform 3)Phosphorylation-46.26-
137 (in isoform 2)Phosphorylation-43.57-
139 (in isoform 2)Phosphorylation-44.82-
142 (in isoform 5)Phosphorylation-49.9327251275
144 (in isoform 5)Phosphorylation-28.6127251275
321AcetylationKKLIHAAKLNASLKT
HHHHHHHHHCHHHHH		42.9525953088
442 (in isoform 6)Phosphorylation-6.4519081932
444 (in isoform 6)Phosphorylation-52.16-
447 (in isoform 6)Phosphorylation-21.6019081932
461 (in isoform 6)Phosphorylation-37.50-
464 (in isoform 6)Phosphorylation-8.08-
473 (in isoform 6)Phosphorylation-34.40-
484 (in isoform 6)Phosphorylation-45.74-
488 (in isoform 3)Phosphorylation-3.86-
490 (in isoform 3)Phosphorylation-51.20-
493 (in isoform 3)Phosphorylation-11.41-
503 (in isoform 2)Phosphorylation-29.9024719451
507 (in isoform 3)Phosphorylation-4.02-
508 (in isoform 6)Phosphorylation-31.92-
510 (in isoform 3)Phosphorylation-19.79-
514 (in isoform 2)Methylation-31.81-
515 (in isoform 6)Phosphorylation-49.44-
516 (in isoform 2)Phosphorylation-32.4827050516
517 (in isoform 6)Phosphorylation-18.31-
519 (in isoform 3)Phosphorylation-44.69-
519 (in isoform 6)Phosphorylation-44.69-
521 (in isoform 6)Phosphorylation-27.25-
522 (in isoform 5)Phosphorylation-28.5227251275
527 (in isoform 5)Phosphorylation-26.6127251275
528 (in isoform 2)Phosphorylation-34.0124719451
530 (in isoform 3)Phosphorylation-46.80-
540 (in isoform 2)Phosphorylation-5.17-
541 (in isoform 5)Phosphorylation-8.6627251275
547 (in isoform 2)Phosphorylation-9.01-
549 (in isoform 2)Phosphorylation-42.37-
551 (in isoform 2)Phosphorylation-4.15-
553 (in isoform 2)Phosphorylation-47.55-
553 (in isoform 5)Phosphorylation-47.5527251275
554 (in isoform 3)Phosphorylation-33.18-
556 (in isoform 6)Phosphorylation-33.77-
560 (in isoform 6)Phosphorylation-59.14-
561 (in isoform 3)Phosphorylation-35.84-
563 (in isoform 3)Phosphorylation-51.73-
564 (in isoform 5)Phosphorylation-36.7727251275
565 (in isoform 3)Phosphorylation-45.11-
567 (in isoform 3)Phosphorylation-32.66-
572 (in isoform 6)Phosphorylation-38.30-
588 (in isoform 2)Phosphorylation-12.62-
588 (in isoform 5)Phosphorylation-12.6227251275
592 (in isoform 2)Phosphorylation-32.76-
599 (in isoform 5)Phosphorylation-21.2027251275
601 (in isoform 5)Phosphorylation-42.0927251275
602 (in isoform 3)Phosphorylation-37.37-
604 (in isoform 2)Phosphorylation-29.25-
606 (in isoform 3)Phosphorylation-4.29-
618 (in isoform 3)Phosphorylation-31.31-
636 (in isoform 5)Phosphorylation-29.9927251275
640 (in isoform 5)Phosphorylation-6.3727251275
652 (in isoform 5)Phosphorylation-52.3227251275
764 (in isoform 4)Methylation-19.60-
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 CTGE5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTGE5_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 CTGE5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRB2_HUMANGRB2physical
21988832
PSA3_HUMANPSMA3physical
25416956
NGAP_HUMANRASAL2physical
25416956
CEP57_HUMANCEP57physical
25416956
EMIL1_HUMANEMILIN1physical
25416956
CREST_HUMANSS18L1physical
25416956
CCHCR_HUMANCCHCR1physical
25416956
TT23L_HUMANTTC23Lphysical
25416956
MAGBI_HUMANMAGEB18physical
25416956
CTGE2_HUMANCTAGE1physical
28514442
CTGE8_HUMANCTAGE8physical
28514442
CTGE4_HUMANCTAGE8physical
28514442
TGO1_HUMANMIA3physical
28514442
ATF1_HUMANATF1physical
28514442
RGPD8_HUMANRGPD8physical
28514442
CREB1_HUMANCREB1physical
28514442
ABCBA_HUMANABCB10physical
28514442
TRAF4_HUMANTRAF4physical
28514442
RGPD5_HUMANRGPD5physical
28514442
MPRIP_HUMANMPRIPphysical
28514442
CEP55_HUMANCEP55physical
28514442
CREM_HUMANCREMphysical
28514442
CCD22_HUMANCCDC22physical
28514442
IDE_HUMANIDEphysical
28514442
EF1A2_HUMANEEF1A2physical
28514442
RGPD3_HUMANRGPD3physical
28514442
MTFR1_HUMANMTFR1physical
28514442
COMD3_HUMANCOMMD3physical
28514442
EMAL4_HUMANEML4physical
28514442
COMD2_HUMANCOMMD2physical
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 CTGE5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536 AND SER-548, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-517; SER-522;SER-536 AND SER-635, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517 AND SER-536, ANDMASS SPECTROMETRY.
"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 SER-536 AND SER-635, ANDMASS SPECTROMETRY.

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