UFC1_HUMAN - dbPTM
UFC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UFC1_HUMAN
UniProt AC Q9Y3C8
Protein Name Ubiquitin-fold modifier-conjugating enzyme 1
Gene Name UFC1
Organism Homo sapiens (Human).
Sequence Length 167
Subcellular Localization
Protein Description E2-like enzyme which forms an intermediate with UFM1 via a thioester linkage..
Protein Sequence MADEATRRVVSEIPVLKTNAGPRDRELWVQRLKEEYQSLIRYVENNKNADNDWFRLESNKEGTRWFGKCWYIHDLLKYEFDIEFDIPITYPTTAPEIAVPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGLAHLMALGLGPWLAVEIPDLIQKGVIQHKEKCNQ
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-------MADEATRR
-------CCHHHHHH
10.80-
17UbiquitinationVSEIPVLKTNAGPRD
HHCCCEECCCCCCCC
39.7132015554
33AcetylationELWVQRLKEEYQSLI
HHHHHHHHHHHHHHH
51.1723749302
33UbiquitinationELWVQRLKEEYQSLI
HHHHHHHHHHHHHHH
51.1723000965
33UbiquitinationELWVQRLKEEYQSLI
HHHHHHHHHHHHHHH
51.1721890473
36PhosphorylationVQRLKEEYQSLIRYV
HHHHHHHHHHHHHHH
12.4222817900
38PhosphorylationRLKEEYQSLIRYVEN
HHHHHHHHHHHHHHH
25.5124719451
42PhosphorylationEYQSLIRYVENNKNA
HHHHHHHHHHHCCCC
12.7222817900
47UbiquitinationIRYVENNKNADNDWF
HHHHHHCCCCCCCCE
66.1629967540
60UbiquitinationWFRLESNKEGTRWFG
CEEEEECCCCCEEEE
67.7933845483
68UbiquitinationEGTRWFGKCWYIHDL
CCCEEEEEEEEHHHH
16.4832015554
114UbiquitinationAKMYRGGKICLTDHF
EEEECCCEEEECCCC
32.8229967540
114AcetylationAKMYRGGKICLTDHF
EEEECCCEEEECCCC
32.8225953088
116S-nitrosocysteineMYRGGKICLTDHFKP
EECCCEEEECCCCHH
3.69-
116S-nitrosylationMYRGGKICLTDHFKP
EECCCEEEECCCCHH
3.6919483679
118PhosphorylationRGGKICLTDHFKPLW
CCCEEEECCCCHHHH
24.0225159151
122AcetylationICLTDHFKPLWARNV
EEECCCCHHHHHCCC
35.4621791702
122UbiquitinationICLTDHFKPLWARNV
EEECCCCHHHHHCCC
35.4622817900
122UbiquitinationICLTDHFKPLWARNV
EEECCCCHHHHHCCC
35.4621890473

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 UFC1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UFC1_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 UFC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UFM1_HUMANUFM1physical
15071506
UFM1_HUMANUFM1physical
22939629
VATF_HUMANATP6V1Fphysical
22939629
UNK_HUMANUNKphysical
22939629
ZPR1_HUMANZPR1physical
22939629
USP9X_HUMANUSP9Xphysical
22939629
ANCHR_HUMANZFYVE19physical
22939629
VATB2_HUMANATP6V1B2physical
22939629
ZYX_HUMANZYXphysical
22939629
VINC_HUMANVCLphysical
22939629
UFM1_HUMANUFM1physical
24966333
CATA_HUMANCATphysical
26344197
COX17_HUMANCOX17physical
26344197
ETFA_HUMANETFAphysical
26344197
FKB1A_HUMANFKBP1Aphysical
26344197
LDHB_HUMANLDHBphysical
26344197
LYPA2_HUMANLYPLA2physical
26344197
NECP2_HUMANNECAP2physical
26344197
NEDD8_HUMANNEDD8physical
26344197
TAGL2_HUMANTAGLN2physical
26344197
TALDO_HUMANTALDO1physical
26344197
UFM1_HUMANUFM1physical
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 UFC1_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.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-122, AND MASS SPECTROMETRY.

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