UB2Q1_HUMAN - dbPTM
UB2Q1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UB2Q1_HUMAN
UniProt AC Q7Z7E8
Protein Name Ubiquitin-conjugating enzyme E2 Q1
Gene Name UBE2Q1
Organism Homo sapiens (Human).
Sequence Length 422
Subcellular Localization Nucleus . Cell projection, filopodium . Cytoplasm, cytosol .
Protein Description Catalyzes the covalent attachment of ubiquitin to other proteins. [PubMed: 22496338 May be involved in hormonal homeostasis in females. Involved in regulation of B4GALT1 cell surface expression, B4GALT1-mediated cell adhesion to laminin and embryoid body formation (By similarity]
Protein Sequence MQQPQPQGQQQPGPGQQLGGQGAAPGAGGGPGGGPGPGPCLRRELKLLESIFHRGHERFRIASACLDELSCEFLLAGAGGAGAGAAPGPHLPPRGSVPGDPVRIHCNITESYPAVPPIWSVESDDPNLAAVLERLVDIKKGNTLLLQHLKRIISDLCKLYNLPQHPDVEMLDQPLPAEQCTQEDVSSEDEDEEMPEDTEDLDHYEMKEEEPAEGKKSEDDGIGKENLAILEKIKKNQRQDYLNGAVSGSVQATDRLMKELRDIYRSQSFKGGNYAVELVNDSLYDWNVKLLKVDQDSALHNDLQILKEKEGADFILLNFSFKDNFPFDPPFVRVVSPVLSGGYVLGGGAICMELLTKQGWSSAYSIESVIMQISATLVKGKARVQFGANKSQYSLTRAQQSYKSLVQIHEKNGWYTPPKEDG
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-------MQQPQPQG
-------CCCCCCCC		8.2422223895
46UbiquitinationPCLRRELKLLESIFH
HHHHHHHHHHHHHHH		46.3923000965
46 (in isoform 1)Ubiquitination-46.3921890473
46UbiquitinationPCLRRELKLLESIFH
HHHHHHHHHHHHHHH		46.3921890473
46AcetylationPCLRRELKLLESIFH
HHHHHHHHHHHHHHH		46.3923236377
50PhosphorylationRELKLLESIFHRGHE
HHHHHHHHHHHHCHH		30.4428857561
96PhosphorylationPHLPPRGSVPGDPVR
CCCCCCCCCCCCCEE		26.81-
139SumoylationLERLVDIKKGNTLLL
HHHHHCHHCCCHHHH		50.60-
139SumoylationLERLVDIKKGNTLLL
HHHHHCHHCCCHHHH		50.60-
140UbiquitinationERLVDIKKGNTLLLQ
HHHHCHHCCCHHHHH		58.7029967540
217PhosphorylationEPAEGKKSEDDGIGK
CCCCCCCCCCCCCCH		50.1424719451
224UbiquitinationSEDDGIGKENLAILE
CCCCCCCHHHHHHHH		41.3229967540
232AcetylationENLAILEKIKKNQRQ
HHHHHHHHHHHCCCH		57.2820167786
232UbiquitinationENLAILEKIKKNQRQ
HHHHHHHHHHHCCCH		57.2833845483
234AcetylationLAILEKIKKNQRQDY
HHHHHHHHHCCCHHH		57.6620167786
241PhosphorylationKKNQRQDYLNGAVSG
HHCCCHHHHHCHHCC		8.17-
247PhosphorylationDYLNGAVSGSVQATD
HHHHCHHCCHHHHHH		25.4722817900
264PhosphorylationMKELRDIYRSQSFKG
HHHHHHHHHHCCCCC		14.43-
266PhosphorylationELRDIYRSQSFKGGN
HHHHHHHHCCCCCCC		17.1328450419
268PhosphorylationRDIYRSQSFKGGNYA
HHHHHHCCCCCCCEE		30.1228450419
274PhosphorylationQSFKGGNYAVELVND
CCCCCCCEEEEECCC		18.4628450419
307UbiquitinationHNDLQILKEKEGADF
HHHHHHHHHHCCCCE		69.2633845483
309UbiquitinationDLQILKEKEGADFIL
HHHHHHHHCCCCEEE		60.9233845483
320PhosphorylationDFILLNFSFKDNFPF
CEEEEECCCCCCCCC		30.2524719451
390UbiquitinationRVQFGANKSQYSLTR
EEEECCCHHHHCHHH		38.1029967540
390AcetylationRVQFGANKSQYSLTR
EEEECCCHHHHCHHH		38.1026051181
391PhosphorylationVQFGANKSQYSLTRA
EEECCCHHHHCHHHH		33.8728796482
393PhosphorylationFGANKSQYSLTRAQQ
ECCCHHHHCHHHHHH		16.8528796482
394PhosphorylationGANKSQYSLTRAQQS
CCCHHHHCHHHHHHH		18.6728857561
396PhosphorylationNKSQYSLTRAQQSYK
CHHHHCHHHHHHHHH		20.3028796482
401PhosphorylationSLTRAQQSYKSLVQI
CHHHHHHHHHHHHHH		23.5828857561
403UbiquitinationTRAQQSYKSLVQIHE
HHHHHHHHHHHHHHH		42.4332015554
404PhosphorylationRAQQSYKSLVQIHEK
HHHHHHHHHHHHHHH		26.0728857561
415PhosphorylationIHEKNGWYTPPKEDG
HHHHCCCCCCCCCCC		15.6922817900
416PhosphorylationHEKNGWYTPPKEDG-
HHHCCCCCCCCCCC-		26.9725159151
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 UB2Q1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UB2Q1_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 UB2Q1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
I2BPL_HUMANIRF2BPLphysical
19690564
RNF26_HUMANRNF26physical
19690564
RBX2_HUMANRNF7physical
19549727
ECM29_HUMANKIAA0368physical
20682791
CHIP_HUMANSTUB1physical
16275660
P53_HUMANTP53physical
25987028
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 UB2Q1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.

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