dbPTM

UFL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UFL1_HUMAN
UniProt AC	O94874
Protein Name	E3 UFM1-protein ligase 1 {ECO:0000305}
Gene Name	UFL1 {ECO:0000312\|HGNC:HGNC:23039}
Organism	Homo sapiens (Human).
Sequence Length	794
Subcellular Localization	Endoplasmic reticulum . Cytoplasm, cytosol .
Protein Description	E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to substrate proteins, a post-translational modification on lysine residues of proteins that may play a crucial role in a number of cellular processes. Mediates DDRGK1 ufmylation and may regulate the proteasomal degradation of DDRGK1 and CDK5RAP3 thereby modulating NF-kappa-B signaling. [PubMed: 20018847]
Protein Sequence	MADAWEEIRRLAADFQRAQFAEATQRLSERNCIEIVNKLIAQKQLEVVHTLDGKEYITPAQISKEMRDELHVRGGRVNIVDLQQVINVDLIHIENRIGDIIKSEKHVQLVLGQLIDENYLDRLAEEVNDKLQESGQVTISELCKTYDLPGNFLTQALTQRLGRIISGHIDLDNRGVIFTEAFVARHKARIRGLFSAITRPTAVNSLISKYGFQEQLLYSVLEELVNSGRLRGTVVGGRQDKAVFVPDIYSRTQSTWVDSFFRQNGYLEFDALSRLGIPDAVSYIKKRYKTTQLLFLKAACVGQGLVDQVEASVEEAISSGTWVDIAPLLPTSLSVEDAAILLQQVMRAFSKQASTVVFSDTVVVSEKFINDCTELFRELMHQKAEKEMKNNPVHLITEEDLKQISTLESVSTSKKDKKDERRRKATEGSGSMRGGGGGNAREYKIKKVKKKGRKDDDSDDESQSSHTGKKKPEISFMFQDEIEDFLRKHIQDAPEEFISELAEYLIKPLNKTYLEVVRSVFMSSTTSASGTGRKRTIKDLQEEVSNLYNNIRLFEKGMKFFADDTQAALTKHLLKSVCTDITNLIFNFLASDLMMAVDDPAAITSEIRKKILSKLSEETKVALTKLHNSLNEKSIEDFISCLDSAAEACDIMVKRGDKKRERQILFQHRQALAEQLKVTEDPALILHLTSVLLFQFSTHSMLHAPGRCVPQIIAFLNSKIPEDQHALLVKYQGLVVKQLVSQSKKTGQGDYPLNNELDKEQEDVASTTRKELQELSSSIKDLVLKSRKSSVTEE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADAWEEIR ------CHHHHHHHH	18.41	22223895
9	Methylation	ADAWEEIRRLAADFQ HHHHHHHHHHHHHHH	30.73	115919501
24	Phosphorylation	RAQFAEATQRLSERN HHHHHHHHHHHHHHH	13.01	27251275
28	Phosphorylation	AEATQRLSERNCIEI HHHHHHHHHHHHHHH	36.38	27251275
38	Ubiquitination	NCIEIVNKLIAQKQL HHHHHHHHHHHHHCC	30.31	22817900
43	Ubiquitination	VNKLIAQKQLEVVHT HHHHHHHHCCEEEEE	48.07	21890473
43	Ubiquitination	VNKLIAQKQLEVVHT HHHHHHHHCCEEEEE	48.07	21890473
43	Ubiquitination	VNKLIAQKQLEVVHT HHHHHHHHCCEEEEE	48.07	22817900
43	Ubiquitination	VNKLIAQKQLEVVHT HHHHHHHHCCEEEEE	48.07	21890473
63	Phosphorylation	YITPAQISKEMRDEL CCCHHHHCHHHHHHH	15.52	-
73	Methylation	MRDELHVRGGRVNIV HHHHHEECCCCEEEE	30.97	115919497
102	Acetylation	NRIGDIIKSEKHVQL CCHHHHHHCHHHHHH	53.55	26051181
105	2-Hydroxyisobutyrylation	GDIIKSEKHVQLVLG HHHHHCHHHHHHHHH	57.05	-
119	Phosphorylation	GQLIDENYLDRLAEE HHHCCHHHHHHHHHH	14.13	-
122	Methylation	IDENYLDRLAEEVND CCHHHHHHHHHHHHH	32.95	115919493
195	Phosphorylation	ARIRGLFSAITRPTA HHHHHHHHHHCCHHH	24.65	21406692
198	Phosphorylation	RGLFSAITRPTAVNS HHHHHHHCCHHHHHH	30.25	21406692
201	Phosphorylation	FSAITRPTAVNSLIS HHHHCCHHHHHHHHH	39.69	21406692
205	Phosphorylation	TRPTAVNSLISKYGF CCHHHHHHHHHHHCH	22.08	24719451
208	Phosphorylation	TAVNSLISKYGFQEQ HHHHHHHHHHCHHHH	25.72	21406692
241	Acetylation	VVGGRQDKAVFVPDI EECCCCCCEEEECCC	37.80	25953088
241	Ubiquitination	VVGGRQDKAVFVPDI EECCCCCCEEEECCC	37.80	24816145
250	Phosphorylation	VFVPDIYSRTQSTWV EEECCCHHCCCCHHH	29.23	24719451
259	Phosphorylation	TQSTWVDSFFRQNGY CCCHHHHHHHHHCCC	19.37	24719451
266	Phosphorylation	SFFRQNGYLEFDALS HHHHHCCCCCHHHHH	15.59	-
282	Phosphorylation	LGIPDAVSYIKKRYK CCCCHHHHHHHHHCC	23.90	28152594
283	Phosphorylation	GIPDAVSYIKKRYKT CCCHHHHHHHHHCCH	15.34	28152594
289	2-Hydroxyisobutyrylation	SYIKKRYKTTQLLFL HHHHHHCCHHHHHHH	49.48	-
289	Malonylation	SYIKKRYKTTQLLFL HHHHHHCCHHHHHHH	49.48	26320211
354	Phosphorylation	RAFSKQASTVVFSDT HHHHHCCCEEEECCC	21.17	-
355	Phosphorylation	AFSKQASTVVFSDTV HHHHCCCEEEECCCE	24.57	-
383	2-Hydroxyisobutyrylation	FRELMHQKAEKEMKN HHHHHHHHHHHHHHC	43.78	-
386	Acetylation	LMHQKAEKEMKNNPV HHHHHHHHHHHCCCC	68.89	19823545
389	Acetylation	QKAEKEMKNNPVHLI HHHHHHHHCCCCEEE	55.45	19823553
402	Ubiquitination	LITEEDLKQISTLES EECHHHHHHHHCHHH	58.89	29967540
406	Phosphorylation	EDLKQISTLESVSTS HHHHHHHCHHHHCCC	35.85	24173317
409	Phosphorylation	KQISTLESVSTSKKD HHHHCHHHHCCCCCC	25.20	25159151
411	Phosphorylation	ISTLESVSTSKKDKK HHCHHHHCCCCCCHH	35.92	25159151
412	Phosphorylation	STLESVSTSKKDKKD HCHHHHCCCCCCHHH	42.27	25159151
413	Phosphorylation	TLESVSTSKKDKKDE CHHHHCCCCCCHHHH	30.15	25159151
414	Ubiquitination	LESVSTSKKDKKDER HHHHCCCCCCHHHHH	66.15	32015554
426	Phosphorylation	DERRRKATEGSGSMR HHHHHHHHCCCCCCC	43.87	23403867
429	Phosphorylation	RRKATEGSGSMRGGG HHHHHCCCCCCCCCC	22.82	25262027
431	Phosphorylation	KATEGSGSMRGGGGG HHHCCCCCCCCCCCC	13.65	25262027
433	Methylation	TEGSGSMRGGGGGNA HCCCCCCCCCCCCCH	42.15	30987737
449	Ubiquitination	EYKIKKVKKKGRKDD HHCCEECHHCCCCCC	58.61	24816145
458	Phosphorylation	KGRKDDDSDDESQSS CCCCCCCCCCCCHHC	54.69	29255136
462	Phosphorylation	DDDSDDESQSSHTGK CCCCCCCCHHCCCCC	42.21	23927012
464	Phosphorylation	DSDDESQSSHTGKKK CCCCCCHHCCCCCCC	33.11	23927012
465	Phosphorylation	SDDESQSSHTGKKKP CCCCCHHCCCCCCCC	19.89	28176443
467	Phosphorylation	DESQSSHTGKKKPEI CCCHHCCCCCCCCCE	53.28	20068231
488	Ubiquitination	EIEDFLRKHIQDAPE HHHHHHHHHHCCCCH	47.40	-
507	Ubiquitination	ELAEYLIKPLNKTYL HHHHHHHHHCCHHHH	40.64	29967540
512	Phosphorylation	LIKPLNKTYLEVVRS HHHHCCHHHHHHHHH	32.06	23663014
513	Phosphorylation	IKPLNKTYLEVVRSV HHHCCHHHHHHHHHH	11.50	23663014
519	Phosphorylation	TYLEVVRSVFMSSTT HHHHHHHHHHHCCCC	14.22	23663014
522	Sulfoxidation	EVVRSVFMSSTTSAS HHHHHHHHCCCCCCC	2.65	21406390
523	Phosphorylation	VVRSVFMSSTTSASG HHHHHHHCCCCCCCC	17.05	23663014
524	Phosphorylation	VRSVFMSSTTSASGT HHHHHHCCCCCCCCC	24.74	23663014
525	Phosphorylation	RSVFMSSTTSASGTG HHHHHCCCCCCCCCC	19.91	23663014
526	Phosphorylation	SVFMSSTTSASGTGR HHHHCCCCCCCCCCC	25.01	23663014
527	Phosphorylation	VFMSSTTSASGTGRK HHHCCCCCCCCCCCC	22.11	23663014
529	Phosphorylation	MSSTTSASGTGRKRT HCCCCCCCCCCCCCC	36.33	23663014
531	Phosphorylation	STTSASGTGRKRTIK CCCCCCCCCCCCCHH	31.17	23663014
536	Phosphorylation	SGTGRKRTIKDLQEE CCCCCCCCHHHHHHH	35.10	-
548	Phosphorylation	QEEVSNLYNNIRLFE HHHHHHHHHHHHHHH	15.48	-
556	Malonylation	NNIRLFEKGMKFFAD HHHHHHHHHHHHCCC	57.90	26320211
571	Malonylation	DTQAALTKHLLKSVC HHHHHHHHHHHHHHH	32.86	26320211
571	Acetylation	DTQAALTKHLLKSVC HHHHHHHHHHHHHHH	32.86	23236377
571	Ubiquitination	DTQAALTKHLLKSVC HHHHHHHHHHHHHHH	32.86	19608861
614	2-Hydroxyisobutyrylation	IRKKILSKLSEETKV HHHHHHHHCCHHHHH	53.22	-
614	Malonylation	IRKKILSKLSEETKV HHHHHHHHCCHHHHH	53.22	32601280
614	Ubiquitination	IRKKILSKLSEETKV HHHHHHHHCCHHHHH	53.22	29967540
614	Acetylation	IRKKILSKLSEETKV HHHHHHHHCCHHHHH	53.22	25953088
620	2-Hydroxyisobutyrylation	SKLSEETKVALTKLH HHCCHHHHHHHHHHH	28.88	-
625	Ubiquitination	ETKVALTKLHNSLNE HHHHHHHHHHHHCCC	48.91	29967540
625	Acetylation	ETKVALTKLHNSLNE HHHHHHHHHHHHCCC	48.91	25953088
652	Sulfoxidation	AAEACDIMVKRGDKK HHHHHCCEEECCCHH	1.53	21406390
654	Ubiquitination	EACDIMVKRGDKKRE HHHCCEEECCCHHHH	33.03	32015554
708	S-nitrosocysteine	MLHAPGRCVPQIIAF HCCCCCCCHHHHHHH	6.93	-
708	S-nitrosylation	MLHAPGRCVPQIIAF HCCCCCCCHHHHHHH	6.93	19483679
731	Phosphorylation	QHALLVKYQGLVVKQ HHHHHHHHHHHHHHH	10.59	30622161
741	Phosphorylation	LVVKQLVSQSKKTGQ HHHHHHHHCCCCCCC	37.01	27067055
745	Ubiquitination	QLVSQSKKTGQGDYP HHHHCCCCCCCCCCC	64.23	29967540
746	Phosphorylation	LVSQSKKTGQGDYPL HHHCCCCCCCCCCCC	38.17	26552605
751	Phosphorylation	KKTGQGDYPLNNELD CCCCCCCCCCCCCCC	19.22	26552605
770	Ubiquitination	DVASTTRKELQELSS HHHHHHHHHHHHHHH	61.76	29967540
776	Phosphorylation	RKELQELSSSIKDLV HHHHHHHHHHHHHHH	22.68	29255136
777	Phosphorylation	KELQELSSSIKDLVL HHHHHHHHHHHHHHH	49.02	29255136
778	Phosphorylation	ELQELSSSIKDLVLK HHHHHHHHHHHHHHH	30.22	29255136
780	Ubiquitination	QELSSSIKDLVLKSR HHHHHHHHHHHHHHH	47.13	29967540
785	Ubiquitination	SIKDLVLKSRKSSVT HHHHHHHHHHHCCCC	40.51	29967540
786	Phosphorylation	IKDLVLKSRKSSVTE HHHHHHHHHHCCCCC	40.56	26074081
789	Phosphorylation	LVLKSRKSSVTEE-- HHHHHHHCCCCCC--	29.00	25850435
790	Phosphorylation	VLKSRKSSVTEE--- HHHHHHCCCCCC---	35.77	25072903
792	Phosphorylation	KSRKSSVTEE----- HHHHCCCCCC-----	36.02	26074081

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
462	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
462	S	Phosphorylation		30886146
Phosphorylated at Ser-462 by ATM, enhancing protein ligase activity and promoting ATM activation in a positive feedback loop.

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 UFL1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of UFL1_HUMAN !!

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 UFL1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-571, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND MASSSPECTROMETRY.	18318008 [Abstract]
"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-458, AND MASSSPECTROMETRY.	17081983 [Abstract]

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