dbPTM

UBB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBB_HUMAN
UniProt AC	P0CG47
Protein Name	Polyubiquitin-B
Gene Name	UBB
Organism	Homo sapiens (Human).
Sequence Length	229
Subcellular Localization	Ubiquitin: Cytoplasm. Nucleus.
Protein Description	Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling..
Protein Sequence	MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Sulfoxidation	-------MQIFVKTL -------CEEEEEEC	6.60	21406390
6	Sumoylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	-
6	Acetylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	25825284
6	Malonylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	26320211
6	Methylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	28640069
6	Sumoylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	-
6	Ubiquitination	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	16443603
6	Ubiquitination	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	21890473
7	Phosphorylation	-MQIFVKTLTGKTIT -CEEEEEECCCCEEE	25.01	24043423
9	Phosphorylation	QIFVKTLTGKTITLE EEEEEECCCCEEEEE	41.69	23401153
11	Sumoylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
11	Acetylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	23954790
11	Malonylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	26320211
11	Sumoylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
11	Ubiquitination	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	16443603
11	Ubiquitination	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	21890473
12	Phosphorylation	VKTLTGKTITLEVEP EEECCCCEEEEEECC	22.12	25159151
14	Phosphorylation	TLTGKTITLEVEPSD ECCCCEEEEEECCCC	23.30	25159151
20	Phosphorylation	ITLEVEPSDTIENVK EEEEECCCCHHHHHH	33.60	21712546
22	Phosphorylation	LEVEPSDTIENVKAK EEECCCCHHHHHHHH	34.23	25159151
27	Sumoylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
27	Acetylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	2993057
27	Sumoylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
27	Ubiquitination	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	20639865
27	Ubiquitination	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	21890473
29	Acetylation	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	2993057
29	Sumoylation	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	-
29	Ubiquitination	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	16543144
29	Ubiquitination	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	21890473
33	Acetylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	23236377
33	Malonylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	33225896
33	Sumoylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
33	Ubiquitination	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	20639865
33	Ubiquitination	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	21890473
48	Sumoylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
48	Acetylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	23954790
48	Malonylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	33225896
48	Sumoylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
48	Ubiquitination	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	16443603
48	Ubiquitination	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	21890473
55	Phosphorylation	KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC	35.82	25159151
57	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	23401153
59	Phosphorylation	DGRTLSDYNIQKEST CCCCCCCCCCCCHHE	15.70	23911959
63	Sumoylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	-
63	Acetylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	23236377
63	Malonylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	33225896
63	Methylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	66693193
63	Sumoylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	-
63	Ubiquitination	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	639865
63	Ubiquitination	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	21890473
65	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEEEEE	43.22	28355574
66	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEEEEEE	21.20	22617229
72	Methylation	STLHLVLRLRGGMQI HEEEEEEEECCCEEE	18.17	-
76	ADP-ribosylation	LVLRLRGGMQIFVKT EEEEECCCEEEEEEE	9.82	28525742
82	Sumoylation	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	-
82	Acetylation	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	25825284
82	Malonylation	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	26320211
82	Methylation	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	28640073
82	Sumoylation	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	-
82	Ubiquitination	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	-
83	Phosphorylation	GMQIFVKTLTGKTIT CEEEEEEECCCCEEE	25.01	24043423
85	Phosphorylation	QIFVKTLTGKTITLE EEEEEECCCCEEEEE	41.69	23401153
87	Sumoylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
87	Acetylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	25953088
87	Malonylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	26320211
87	Sumoylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
87	Ubiquitination	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
88	Phosphorylation	VKTLTGKTITLEVEP EEECCCCEEEEEECC	22.12	21712546
90	Phosphorylation	TLTGKTITLEVEPSD ECCCCEEEEEECCCC	23.30	25159151
96	Phosphorylation	ITLEVEPSDTIENVK EEEEECCCCHHHHHH	33.60	21712546
98	Phosphorylation	LEVEPSDTIENVKAK EEECCCCHHHHHHHH	34.23	25159151
103	Sumoylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
103	Acetylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	26051181
103	Sumoylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
103	Ubiquitination	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	20639865
105	Sumoylation	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	-
105	Ubiquitination	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	20639865
109	Acetylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	26051181
109	Malonylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	26320211
109	Sumoylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
109	Ubiquitination	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
124	Sumoylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
124	Acetylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	26051181
124	Malonylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	33225896
124	Sumoylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
124	Ubiquitination	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	20639865
131	Phosphorylation	KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC	35.82	25159151
133	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	23401153
135	Phosphorylation	DGRTLSDYNIQKEST CCCCCCCCCCCCHHE	15.70	23911959
139	Sumoylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	-
139	Acetylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	26051181
139	Malonylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	33225896
139	Methylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	66693199
139	Sumoylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	-
139	Ubiquitination	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	20639865
141	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEEEEE	43.22	28355574
142	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEEEEEE	21.20	22617229
148	Methylation	STLHLVLRLRGGMQI HEEEEEEEECCCEEE	18.17	-
158	Sumoylation	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	-
158	Acetylation	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	25825284
158	Malonylation	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	26320211
158	Methylation	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	28640077
158	Sumoylation	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	-
158	Ubiquitination	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	-
159	Phosphorylation	GMQIFVKTLTGKTIT CEEEEEEECCCCEEE	25.01	24043423
161	Phosphorylation	QIFVKTLTGKTITLE EEEEEECCCCEEEEE	41.69	23401153
163	Sumoylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
163	Acetylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	25953088
163	Malonylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	26320211
163	Sumoylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
163	Ubiquitination	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
164	Phosphorylation	VKTLTGKTITLEVEP EEECCCCEEEEEECC	22.12	21712546
166	Phosphorylation	TLTGKTITLEVEPSD ECCCCEEEEEECCCC	23.30	25159151
172	Phosphorylation	ITLEVEPSDTIENVK EEEEECCCCHHHHHH	33.60	21712546
174	Phosphorylation	LEVEPSDTIENVKAK EEECCCCHHHHHHHH	34.23	25159151
179	Sumoylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
179	Acetylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	26051181
179	Sumoylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
179	Ubiquitination	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	20639865
181	Sumoylation	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	-
181	Ubiquitination	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	20639865
185	Acetylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	26051181
185	Malonylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	26320211
185	Sumoylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
185	Ubiquitination	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
200	Sumoylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
200	Acetylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	26051181
200	Malonylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	33225896
200	Sumoylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
200	Ubiquitination	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	20639865
207	Phosphorylation	KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC	35.82	25159151
209	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	23401153
211	Phosphorylation	DGRTLSDYNIQKEST CCCCCCCCCCCCHHH	15.70	23911959
215	Sumoylation	LSDYNIQKESTLHLV CCCCCCCCHHHEEEE	50.24	-
215	Acetylation	LSDYNIQKESTLHLV CCCCCCCCHHHEEEE	50.24	26051181
215	Malonylation	LSDYNIQKESTLHLV CCCCCCCCHHHEEEE	50.24	26320211
215	Methylation	LSDYNIQKESTLHLV CCCCCCCCHHHEEEE	50.24	66712447
215	Sumoylation	LSDYNIQKESTLHLV CCCCCCCCHHHEEEE	50.24	-
215	Ubiquitination	LSDYNIQKESTLHLV CCCCCCCCHHHEEEE	50.24	-
217	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHHEEEEEE	43.22	28355574
218	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHHEEEEEEE	21.20	22617229
224	Methylation	STLHLVLRLRGGC-- HHEEEEEEECCCC--	18.17	-

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
65	S	Phosphorylation	Kinase	PINK1	Q9BXM7	Uniprot
65	S	Phosphorylation	Kinase	PINK1	Q9BXM7	PSP
66	T	Phosphorylation	Kinase	PINK1	Q9BXM7	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
65	S	Phosphorylation	24784582
[Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy.
65	S	ubiquitylation	24784582
[Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy.

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 UBB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DAZP2_HUMAN	DAZAP2	physical	16189514
UBE3A_HUMAN	UBE3A	physical	25416956
DAZP2_HUMAN	DAZAP2	physical	25416956
CACO2_HUMAN	CALCOCO2	physical	25416956
UBQL1_HUMAN	UBQLN1	physical	25416956
DDI1_YEAST	DDI1	physical	25703377
DAZP2_HUMAN	DAZAP2	physical	21516116

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 UBB_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-6 AND LYS-48, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-65, AND MASSSPECTROMETRY.	17081983 [Abstract]
Ubiquitylation
Reference	PubMed
"Polyubiquitination of proliferating cell nuclear antigen by HLTF andSHPRH prevents genomic instability from stalled replication forks."; Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X.,Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.; Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008). Cited for: UBIQUITINATION AT LYS-63, AND MUTAGENESIS OF LYS-48 AND LYS-63.	18719106 [Abstract]
"The proteomic reactor facilitates the analysis of affinity-purifiedproteins by mass spectrometry: application for identifyingubiquitinated proteins in human cells."; Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M.,Haines D.S., Figeys D.; J. Proteome Res. 6:298-305(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48, AND MASSSPECTROMETRY.	17203973 [Abstract]
"Mass spectrometric characterization of the affinity-purified human26S proteasome complex."; Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.; Biochemistry 46:3553-3565(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48, AND MASSSPECTROMETRY.	17323924 [Abstract]
"Differential regulation of EGF receptor internalization anddegradation by multiubiquitination within the kinase domain."; Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.; Mol. Cell 21:737-748(2006). Cited for: FUNCTION, UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63, ANDMASS SPECTROMETRY.	16543144 [Abstract]
"Alzheimer disease-specific conformation of hyperphosphorylated pairedhelical filament-tau is polyubiquitinated through Lys-48, Lys-11, andLys-6 ubiquitin conjugation."; Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.; J. Biol. Chem. 281:10825-10838(2006). Cited for: PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11AND LYS-48, AND MASS SPECTROMETRY.	16443603 [Abstract]

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