DDI2_HUMAN - dbPTM
DDI2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDI2_HUMAN
UniProt AC Q5TDH0
Protein Name Protein DDI1 homolog 2 {ECO:0000305}
Gene Name DDI2 {ECO:0000312|HGNC:HGNC:24578}
Organism Homo sapiens (Human).
Sequence Length 399
Subcellular Localization Cytoplasm, cytosol .
Protein Description Aspartic protease that mediates the cleavage of NFE2L1/NRF1 at 'Leu-104', thereby promoting release of NFE2L1/NRF1 from the endoplasmic reticulum membrane. [PubMed: 27676298]
Protein Sequence MLLTVYCVRRDLSEVTFSLQVDADFELHNFRALCELESGIPAAESQIVYAERPLTDNHRSLASYGLKDGDVVILRQKENADPRPPVQFPNLPRIDFSSIAVPGTSSPRQRQPPGTQQSHSSPGEITSSPQGLDNPALLRDMLLANPHELSLLKERNPPLAEALLSGDLEKFSRVLVEQQQDRARREQERIRLFSADPFDLEAQAKIEEDIRQQNIEENMTIAMEEAPESFGQVVMLYINCKVNGHPVKAFVDSGAQMTIMSQACAERCNIMRLVDRRWAGIAKGVGTQKIIGRVHLAQVQIEGDFLPCSFSILEEQPMDMLLGLDMLKRHQCSIDLKKNVLVIGTTGSQTTFLPEGELPECARLAYGAGREDVRPEEIADQELAEALQKSAEDAERQKP
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
4Phosphorylation----MLLTVYCVRRD
----CCEEEEEEECC		12.8824043423
6Phosphorylation--MLLTVYCVRRDLS
--CCEEEEEEECCHH		4.6825690035
67UbiquitinationSLASYGLKDGDVVIL
HHHHCCCCCCCEEEE		56.1322053931
67 (in isoform 2)Ubiquitination-56.1321890473
67 (in isoform 1)Ubiquitination-56.1321890473
67 (in isoform 3)Ubiquitination-56.1321890473
67UbiquitinationSLASYGLKDGDVVIL
HHHHCCCCCCCEEEE		56.1327667366
77 (in isoform 2)Ubiquitination-46.6421890473
77 (in isoform 1)Ubiquitination-46.6421890473
77 (in isoform 3)Ubiquitination-46.6421890473
77UbiquitinationDVVILRQKENADPRP
CEEEEECCCCCCCCC		46.6429967540
97PhosphorylationNLPRIDFSSIAVPGT
CCCCCCCCCEECCCC		19.6523403867
98PhosphorylationLPRIDFSSIAVPGTS
CCCCCCCCEECCCCC		17.9823927012
104PhosphorylationSSIAVPGTSSPRQRQ
CCEECCCCCCCCCCC		21.6922167270
105PhosphorylationSIAVPGTSSPRQRQP
CEECCCCCCCCCCCC		44.2322167270
105 (in isoform 3)Phosphorylation-44.2321406692
106 (in isoform 3)Phosphorylation-24.7621406692
106PhosphorylationIAVPGTSSPRQRQPP
EECCCCCCCCCCCCC		24.7622167270
108MethylationVPGTSSPRQRQPPGT
CCCCCCCCCCCCCCC		46.38-
115PhosphorylationRQRQPPGTQQSHSSP
CCCCCCCCCCCCCCC		29.2523401153
115 (in isoform 3)Phosphorylation-29.2521406692
118PhosphorylationQPPGTQQSHSSPGEI
CCCCCCCCCCCCCCC		18.6022167270
120PhosphorylationPGTQQSHSSPGEITS
CCCCCCCCCCCCCCC		43.4022167270
121PhosphorylationGTQQSHSSPGEITSS
CCCCCCCCCCCCCCC		31.3422167270
126PhosphorylationHSSPGEITSSPQGLD
CCCCCCCCCCCCCCC		20.8922167270
127PhosphorylationSSPGEITSSPQGLDN
CCCCCCCCCCCCCCC		45.7622167270
128PhosphorylationSPGEITSSPQGLDNP
CCCCCCCCCCCCCCH		16.7630278072
150PhosphorylationLANPHELSLLKERNP
HCCHHHHHHHHHHCC		28.7725159151
153 (in isoform 3)Ubiquitination-60.9821890473
153 (in isoform 2)Ubiquitination-60.9821890473
153 (in isoform 1)Ubiquitination-60.9821890473
153UbiquitinationPHELSLLKERNPPLA
HHHHHHHHHHCCHHH		60.9822053931
153UbiquitinationPHELSLLKERNPPLA
HHHHHHHHHHCCHHH		60.9823000965
170 (in isoform 3)Ubiquitination-56.8121890473
170UbiquitinationLLSGDLEKFSRVLVE
HHHCCHHHHHHHHHH		56.8123000965
170 (in isoform 1)Ubiquitination-56.8121890473
170 (in isoform 2)Ubiquitination-56.8121890473
170UbiquitinationLLSGDLEKFSRVLVE
HHHCCHHHHHHHHHH		56.8122053931
182MethylationLVEQQQDRARREQER
HHHHHHHHHHHHHHH		26.17-
194PhosphorylationQERIRLFSADPFDLE
HHHHHHEECCCCCHH		36.0325159151
194 (in isoform 3)Phosphorylation-36.0321406692
205UbiquitinationFDLEAQAKIEEDIRQ
CCHHHHHHHHHHHHH		38.2722053931
205UbiquitinationFDLEAQAKIEEDIRQ
CCHHHHHHHHHHHHH		38.2721906983
205 (in isoform 2)Ubiquitination-38.2721890473
205 (in isoform 1)Ubiquitination-38.2721890473
205 (in isoform 3)Ubiquitination-38.2721890473
283 (in isoform 1)Ubiquitination-52.8121890473
283AcetylationRRWAGIAKGVGTQKI
HHHHCCCCCCCHHHE		52.8126051181
283 (in isoform 3)Ubiquitination-52.8121890473
283UbiquitinationRRWAGIAKGVGTQKI
HHHHCCCCCCCHHHE		52.8123000965
289 (in isoform 3)Ubiquitination-35.8121890473
289UbiquitinationAKGVGTQKIIGRVHL
CCCCCHHHEEEEEEE		35.8123000965
289 (in isoform 1)Ubiquitination-35.8121890473
289AcetylationAKGVGTQKIIGRVHL
CCCCCHHHEEEEEEE		35.8125953088
333PhosphorylationMLKRHQCSIDLKKNV
HHHHCCCCCCCCCCE		16.7424961811
337UbiquitinationHQCSIDLKKNVLVIG
CCCCCCCCCCEEEEE		38.2629901268
338UbiquitinationQCSIDLKKNVLVIGT
CCCCCCCCCEEEEEC		60.6329967540
345PhosphorylationKNVLVIGTTGSQTTF
CCEEEEECCCCCCCC		19.5023286773
346PhosphorylationNVLVIGTTGSQTTFL
CEEEEECCCCCCCCC		29.6223286773
350PhosphorylationIGTTGSQTTFLPEGE
EECCCCCCCCCCCCC		22.6323286773
351PhosphorylationGTTGSQTTFLPEGEL
ECCCCCCCCCCCCCC		18.6123286773
361GlutathionylationPEGELPECARLAYGA
CCCCCCHHHHHHHCC		2.2322555962
389 (in isoform 1)Ubiquitination-53.1121890473
389UbiquitinationELAEALQKSAEDAER
HHHHHHHHHHHHHHH		53.1121963094
398UbiquitinationAEDAERQKP------
HHHHHHHCC------		59.9429967540
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 DDI2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDI2_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 DDI2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HYPK_HUMANHYPKphysical
22863883
VP26A_HUMANVPS26Aphysical
22863883
CCDC6_HUMANCCDC6physical
26344197
COA7_HUMANCOA7physical
26344197
HAT1_HUMANHAT1physical
26344197
TLN2_HUMANTLN2physical
26344197
TOM1_HUMANTOM1physical
26344197
TRM6_HUMANTRMT6physical
26344197
TTC4_HUMANTTC4physical
26344197
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 DDI2_HUMAN

loading...

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-106; SER-128 ANDSER-194, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.
"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-106 AND SER-194, 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-194, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory