dbPTM

UBQL4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBQL4_HUMAN
UniProt AC	Q9NRR5
Protein Name	Ubiquilin-4
Gene Name	UBQLN4
Organism	Homo sapiens (Human).
Sequence Length	601
Subcellular Localization	Nucleus . Cytoplasm . Endoplasmic reticulum . Cytoplasm, perinuclear region . Cytoplasmic vesicle, autophagosome . Colocalizes with the proteasome, both in nucleus and cytoplasm.
Protein Description	Plays a role in the regulation of protein degradation via the ubiquitin-proteasome system (UPS). Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome (Ref. 6). Plays a role in the regulation of the proteasomal degradation of non-ubiquitinated GJA1 (By similarity). Acts as an adapter protein that recruits UBQLN1 to the autophagy machinery. Mediates the association of UBQLN1 with autophagosomes and the autophagy-related protein LC3 (MAP1LC3A/B/C) and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion. [PubMed: 23459205]
Protein Sequence	MAEPSGAETRPPIRVTVKTPKDKEEIVICDRASVKEFKEEISRRFKAQQDQLVLIFAGKILKDGDTLNQHGIKDGLTVHLVIKTPQKAQDPAAATASSPSTPDPASAPSTTPASPATPAQPSTSGSASSDAGSGSRRSSGGGPSPGAGEGSPSATASILSGFGGILGLGSLGLGSANFMELQQQMQRQLMSNPEMLSQIMENPLVQDMMSNPDLMRHMIMANPQMQQLMERNPEISHMLNNPELMRQTMELARNPAMMQEMMRNQDRALSNLESIPGGYNALRRMYTDIQEPMFSAAREQFGNNPFSSLAGNSDSSSSQPLRTENREPLPNPWSPSPPTSQAPGSGGEGTGGSGTSQVHPTVSNPFGINAASLGSGMFNSPEMQALLQQISENPQLMQNVISAPYMRSMMQTLAQNPDFAAQMMVNVPLFAGNPQLQEQLRLQLPVFLQQMQNPESLSILTNPRAMQALLQIQQGLQTLQTEAPGLVPSLGSFGISRTPAPSAGSNAGSTPEAPTSSPATPATSSPTGASSAQQQLMQQMIQLLAGSGNSQVQTPEVRFQQQLEQLNSMGFINREANLQALIATGGDINAAIERLLGSQLS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEPSGAET ------CCCCCCCCC	37.09	-
5	Phosphorylation	---MAEPSGAETRPP ---CCCCCCCCCCCC	41.98	30001349
9	Phosphorylation	AEPSGAETRPPIRVT CCCCCCCCCCCEEEE	48.19	30001349
16	Phosphorylation	TRPPIRVTVKTPKDK CCCCEEEEECCCCCC	13.36	20068231
18	Ubiquitination	PPIRVTVKTPKDKEE CCEEEEECCCCCCCC	50.14	-
19	Phosphorylation	PIRVTVKTPKDKEEI CEEEEECCCCCCCCE	31.10	20068231
21	Ubiquitination	RVTVKTPKDKEEIVI EEEECCCCCCCCEEE	83.26	-
23	Sumoylation	TVKTPKDKEEIVICD EECCCCCCCCEEEEE	64.47	28112733
23	2-Hydroxyisobutyrylation	TVKTPKDKEEIVICD EECCCCCCCCEEEEE	64.47	-
23	Sumoylation	TVKTPKDKEEIVICD EECCCCCCCCEEEEE	64.47	-
23	Ubiquitination	TVKTPKDKEEIVICD EECCCCCCCCEEEEE	64.47	-
35	Acetylation	ICDRASVKEFKEEIS EEECHHHHHHHHHHH	55.74	26051181
35	Ubiquitination	ICDRASVKEFKEEIS EEECHHHHHHHHHHH	55.74	-
42	Phosphorylation	KEFKEEISRRFKAQQ HHHHHHHHHHHHHHH	22.23	24719451
46	Ubiquitination	EEISRRFKAQQDQLV HHHHHHHHHHHHHEE	43.40	21890473
46	Ubiquitination	EEISRRFKAQQDQLV HHHHHHHHHHHHHEE	43.40	21890473
59	Ubiquitination	LVLIFAGKILKDGDT EEEEEECEECCCCCC	41.24	21890473
59	Ubiquitination	LVLIFAGKILKDGDT EEEEEECEECCCCCC	41.24	21890473
62	Ubiquitination	IFAGKILKDGDTLNQ EEECEECCCCCCCHH	64.24	21890473
62	Sumoylation	IFAGKILKDGDTLNQ EEECEECCCCCCCHH	64.24	28112733
62	Acetylation	IFAGKILKDGDTLNQ EEECEECCCCCCCHH	64.24	23954790
84	Phosphorylation	TVHLVIKTPQKAQDP EEEEEEECCCCCCCC	21.59	25159151
87	Ubiquitination	LVIKTPQKAQDPAAA EEEECCCCCCCCHHH	49.58	21890473
95	Phosphorylation	AQDPAAATASSPSTP CCCCHHHCCCCCCCC	23.50	29116813
97	Phosphorylation	DPAAATASSPSTPDP CCHHHCCCCCCCCCC	38.13	29116813
98	Phosphorylation	PAAATASSPSTPDPA CHHHCCCCCCCCCCC	22.02	30177828
100	Phosphorylation	AATASSPSTPDPASA HHCCCCCCCCCCCCC	55.29	29116813
101	Phosphorylation	ATASSPSTPDPASAP HCCCCCCCCCCCCCC	34.79	29116813
106	Phosphorylation	PSTPDPASAPSTTPA CCCCCCCCCCCCCCC	46.21	28450419
109	Phosphorylation	PDPASAPSTTPASPA CCCCCCCCCCCCCCC	44.63	28450419
110	Phosphorylation	DPASAPSTTPASPAT CCCCCCCCCCCCCCC	35.42	28450419
111	Phosphorylation	PASAPSTTPASPATP CCCCCCCCCCCCCCC	22.61	28450419
114	Phosphorylation	APSTTPASPATPAQP CCCCCCCCCCCCCCC	19.10	30175587
117	Phosphorylation	TTPASPATPAQPSTS CCCCCCCCCCCCCCC	23.65	28450419
122	Phosphorylation	PATPAQPSTSGSASS CCCCCCCCCCCCCCC	24.11	28450419
123	Phosphorylation	ATPAQPSTSGSASSD CCCCCCCCCCCCCCC	43.73	28450419
124	Phosphorylation	TPAQPSTSGSASSDA CCCCCCCCCCCCCCC	34.78	28450419
126	Phosphorylation	AQPSTSGSASSDAGS CCCCCCCCCCCCCCC	25.42	30177828
128	Phosphorylation	PSTSGSASSDAGSGS CCCCCCCCCCCCCCC	30.37	30206219
129	Phosphorylation	STSGSASSDAGSGSR CCCCCCCCCCCCCCC	31.06	30177828
133	Phosphorylation	SASSDAGSGSRRSSG CCCCCCCCCCCCCCC	35.00	23312004
135	Phosphorylation	SSDAGSGSRRSSGGG CCCCCCCCCCCCCCC	26.64	23312004
138	Phosphorylation	AGSGSRRSSGGGPSP CCCCCCCCCCCCCCC	32.02	24275569
139	Phosphorylation	GSGSRRSSGGGPSPG CCCCCCCCCCCCCCC	39.38	24275569
144	Phosphorylation	RSSGGGPSPGAGEGS CCCCCCCCCCCCCCC	38.96	30612738
160	Phosphorylation	SATASILSGFGGILG HHHHHHHHCCCCCCC	30.33	24247654
191	Phosphorylation	QMQRQLMSNPEMLSQ HHHHHHHHCHHHHHH	58.80	28122231
197	Phosphorylation	MSNPEMLSQIMENPL HHCHHHHHHHHHCHH	19.15	28122231
203 (in isoform 2)	Phosphorylation	-	22.17	20068231
263	Methylation	AMMQEMMRNQDRALS HHHHHHHHCHHHHHH	36.03	-
267	Methylation	EMMRNQDRALSNLES HHHHCHHHHHHCHHH	27.88	-
270	Phosphorylation	RNQDRALSNLESIPG HCHHHHHHCHHHCCC	38.08	27050516
274	Phosphorylation	RALSNLESIPGGYNA HHHHCHHHCCCHHHH	36.93	28152594
279	Phosphorylation	LESIPGGYNALRRMY HHHCCCHHHHHHHHH	11.81	28796482
283	Methylation	PGGYNALRRMYTDIQ CCHHHHHHHHHHHCC	20.93	-
286	Phosphorylation	YNALRRMYTDIQEPM HHHHHHHHHHCCCCH	10.23	29978859
287	Phosphorylation	NALRRMYTDIQEPMF HHHHHHHHHCCCCHH	19.79	28112733
295	Phosphorylation	DIQEPMFSAAREQFG HCCCCHHHHHHHHHC	18.11	28555341
307	Phosphorylation	QFGNNPFSSLAGNSD HHCCCCCHHHCCCCC	26.21	25850435
308	Phosphorylation	FGNNPFSSLAGNSDS HCCCCCHHHCCCCCC	23.71	25850435
313	Phosphorylation	FSSLAGNSDSSSSQP CHHHCCCCCCCCCCC	37.64	23663014
315	Phosphorylation	SLAGNSDSSSSQPLR HHCCCCCCCCCCCCC	31.76	23663014
316	Phosphorylation	LAGNSDSSSSQPLRT HCCCCCCCCCCCCCC	38.71	23663014
317	Phosphorylation	AGNSDSSSSQPLRTE CCCCCCCCCCCCCCC	36.62	23663014
318	Phosphorylation	GNSDSSSSQPLRTEN CCCCCCCCCCCCCCC	37.45	17525332
334	O-linked_Glycosylation	EPLPNPWSPSPPTSQ CCCCCCCCCCCCCCC	19.43	29351928
340	O-linked_Glycosylation	WSPSPPTSQAPGSGG CCCCCCCCCCCCCCC	30.07	29351928
598	Phosphorylation	AIERLLGSQLS---- HHHHHHCCCCC----	28.11	28985074

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
318	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
48	K	ubiquitylation	15280365
May undergo both 'Lys-48'- and 'Lys-63'-linked polyubiquitination.
318	S	Phosphorylation	30612738
Phosphorylated by ATM at Ser-318 in response to DNA damage, leading to localization in the nucleus and recruitment to sites of DNA damage.

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 UBQL4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ULA1_HUMAN	NAE1	physical	16169070
SNF5_HUMAN	SMARCB1	physical	16169070
RXRA_HUMAN	RXRA	physical	16169070
EF1A1_HUMAN	EEF1A1	physical	16169070
U119A_HUMAN	UNC119	physical	16169070
PTN_HUMAN	PTN	physical	16169070
SERPH_HUMAN	SERPINH1	physical	11162551
GRP78_HUMAN	HSPA5	physical	11162551
PRL_HUMAN	PRL	physical	11162551
FKBP7_HUMAN	FKBP7	physical	11162551
CATB_HUMAN	CTSB	physical	11162551
OSTP_HUMAN	SPP1	physical	11162551
HERP1_HUMAN	HERPUD1	physical	18307982
CXA1_HUMAN	GJA1	physical	20940304
CXA1_HUMAN	GJA1	physical	18079109
ADPGK_HUMAN	ADPGK	physical	16713569
AGR2_HUMAN	AGR2	physical	16713569
AREG_HUMAN	AREG	physical	16713569
BAG6_HUMAN	BAG6	physical	16713569
EAPP_HUMAN	EAPP	physical	16713569
UBR7_HUMAN	UBR7	physical	16713569
MYDGF_HUMAN	C19orf10	physical	16713569
C1QT1_HUMAN	C1QTNF1	physical	16713569
MTG8_HUMAN	RUNX1T1	physical	16713569
CCL21_HUMAN	CCL21	physical	16713569
CD99_HUMAN	CD99	physical	16713569
CDSN_HUMAN	CDSN	physical	16713569
CO8A1_HUMAN	COL8A1	physical	16713569
CPSF6_HUMAN	CPSF6	physical	16713569
CSTF2_HUMAN	CSTF2	physical	16713569
CSTFT_HUMAN	CSTF2T	physical	16713569
DAZP2_HUMAN	DAZAP2	physical	16713569
DKK3_HUMAN	DKK3	physical	16713569
DTX2_HUMAN	DTX2	physical	16713569
EDN1_HUMAN	EDN1	physical	16713569
FBLN4_HUMAN	EFEMP2	physical	16713569
ELF5_HUMAN	ELF5	physical	16713569
FGFP1_HUMAN	FGFBP1	physical	16713569
FKBP2_HUMAN	FKBP2	physical	16713569
RSRC2_HUMAN	RSRC2	physical	16713569
KLH26_HUMAN	KLHL26	physical	16713569
CC134_HUMAN	CCDC134	physical	16713569
ERP27_HUMAN	ERP27	physical	16713569
CCD33_HUMAN	CCDC33	physical	16713569
FZD7_HUMAN	FZD7	physical	16713569
GBRD_HUMAN	GABRD	physical	16713569
GKAP1_HUMAN	GKAP1	physical	16713569
GPX7_HUMAN	GPX7	physical	16713569
HAVR1_HUMAN	HAVCR1	physical	16713569
HXK2_HUMAN	HK2	physical	16713569
PA216_HUMAN	PLA2G16	physical	16713569
IBP6_HUMAN	IGFBP6	physical	16713569
KLH42_HUMAN	KLHL42	physical	16713569
IPIL1_HUMAN	ITPRIPL1	physical	16713569
ZG16B_HUMAN	ZG16B	physical	16713569
MK_HUMAN	MDK	physical	16713569
CA094_HUMAN	C1orf94	physical	16713569
AF17_HUMAN	MLLT6	physical	16713569
NDK3_HUMAN	NME3	physical	16713569
NPHP1_HUMAN	NPHP1	physical	16713569
ANF_HUMAN	NPPA	physical	16713569
NB5R1_HUMAN	CYB5R1	physical	16713569
NXF1_HUMAN	NXF1	physical	16713569
PDIA5_HUMAN	PDIA5	physical	16713569
PDLI7_HUMAN	PDLIM7	physical	16713569
PELI2_HUMAN	PELI2	physical	16713569
PIN1_HUMAN	PIN1	physical	16713569
PI42B_HUMAN	PIP4K2B	physical	16713569
BPIA1_HUMAN	BPIFA1	physical	16713569
PPIB_HUMAN	PPIB	physical	16713569
PPIC_HUMAN	PPIC	physical	16713569
SRGN_HUMAN	SRGN	physical	16713569
QSOX1_HUMAN	QSOX1	physical	16713569
RAI2_HUMAN	RAI2	physical	16713569
RIC8A_HUMAN	RIC8A	physical	16713569
RNPS1_HUMAN	RNPS1	physical	16713569
RPN1_HUMAN	RPN1	physical	16713569
SCMH1_HUMAN	SCMH1	physical	16713569
SEMG1_HUMAN	SEMG1	physical	16713569
PAI1_HUMAN	SERPINE1	physical	16713569
SPI2_HUMAN	SERPINI2	physical	16713569
7B2_HUMAN	SCG5	physical	16713569
MID49_HUMAN	MIEF2	physical	16713569
SPAG8_HUMAN	SPAG8	physical	16713569
SPIT1_HUMAN	SPINT1	physical	16713569
OSTP_HUMAN	SPP1	physical	16713569
STAM2_HUMAN	STAM2	physical	16713569
HSP13_HUMAN	HSPA13	physical	16713569
TFF1_HUMAN	TFF1	physical	16713569
PMEPA_HUMAN	PMEPA1	physical	16713569
TRI32_HUMAN	TRIM32	physical	16713569
UBQL1_HUMAN	UBQLN1	physical	16713569
USMG5_HUMAN	USMG5	physical	16713569
VIP_HUMAN	VIP	physical	16713569
NTAL_HUMAN	LAT2	physical	16713569
ZG16_HUMAN	ZG16	physical	16713569
ZN205_HUMAN	ZNF205	physical	16713569
UBQL4_HUMAN	UBQLN4	physical	16713569
MI4GD_HUMAN	MIF4GD	physical	16713569
ADA33_HUMAN	ADAM33	physical	16713569
ARL4C_HUMAN	ARL4C	physical	16713569
ATIF1_HUMAN	ATPIF1	physical	16713569
CEND_HUMAN	CEND1	physical	16713569
ERP29_HUMAN	ERP29	physical	16713569
CAC1G_HUMAN	CACNA1G	physical	16713569
CCD14_HUMAN	CCDC14	physical	16713569
COPB_HUMAN	COPB1	physical	16713569
CRIPT_HUMAN	CRIPT	physical	16713569
DMPK_HUMAN	DMPK	physical	16713569
EPDR1_HUMAN	EPDR1	physical	16713569
FA2H_HUMAN	FA2H	physical	16713569
SP20H_HUMAN	SUPT20H	physical	16713569
PR40A_HUMAN	PRPF40A	physical	16713569
GDIA_HUMAN	GDI1	physical	16713569
HGS_HUMAN	HGS	physical	16713569
MIC60_HUMAN	IMMT	physical	16713569
AN13D_HUMAN	ANKRD13D	physical	16713569
CC107_HUMAN	CCDC107	physical	16713569
CK049_HUMAN	C11orf49	physical	16713569
MOAP1_HUMAN	MOAP1	physical	16713569
CC136_HUMAN	CCDC136	physical	16713569
NOMO1_HUMAN	NOMO1	physical	16713569
NOMO3_HUMAN	NOMO3	physical	16713569
NT2NL_HUMAN	NOTCH2NL	physical	16713569
OAT_HUMAN	OAT	physical	16713569
PBIP1_HUMAN	PBXIP1	physical	16713569
PCD17_HUMAN	PCDH17	physical	16713569
PCDH8_HUMAN	PCDH8	physical	16713569
PNMA1_HUMAN	PNMA1	physical	16713569
PICK1_HUMAN	PICK1	physical	16713569
PTN_HUMAN	PTN	physical	16713569
PTPRN_HUMAN	PTPRN	physical	16713569
PTPR2_HUMAN	PTPRN2	physical	16713569
RBM10_HUMAN	RBM10	physical	16713569
ROBO2_HUMAN	ROBO2	physical	16713569
SCG2_HUMAN	SCG2	physical	16713569
SRSF2_HUMAN	SRSF2	physical	16713569
SFR19_HUMAN	SCAF1	physical	16713569
STMN1_HUMAN	STMN1	physical	16713569
TGFI1_HUMAN	TGFB1I1	physical	16713569
TNR6B_HUMAN	TNRC6B	physical	16713569
TRAF2_HUMAN	TRAF2	physical	16713569
TRIB2_HUMAN	TRIB2	physical	16713569
UBQL2_HUMAN	UBQLN2	physical	16713569
HEM4_HUMAN	UROS	physical	16713569
WAC_HUMAN	WAC	physical	16713569
1433T_HUMAN	YWHAQ	physical	16713569
ZDHC3_HUMAN	ZDHHC3	physical	16713569
FOG2_HUMAN	ZFPM2	physical	16713569
RD23A_HUMAN	RAD23A	physical	16713569
IMDH2_HUMAN	IMPDH2	physical	16713569
ANCHR_HUMAN	ZFYVE19	physical	22939629
ZPR1_HUMAN	ZPR1	physical	22939629
UBXN1_HUMAN	UBXN1	physical	22939629
VPS4B_HUMAN	VPS4B	physical	22939629
VP26A_HUMAN	VPS26A	physical	22939629
MLP3A_HUMAN	MAP1LC3A	physical	23459205
UBQL1_HUMAN	UBQLN1	physical	23459205
CXA1_HUMAN	GJA1	physical	24256120
PSMD2_HUMAN	PSMD2	physical	24256120
UBQL4_HUMAN	UBQLN4	physical	25416956
UBC_HUMAN	UBC	physical	20940304
ASNS_HUMAN	ASNS	physical	26344197
RD23A_HUMAN	RAD23A	physical	26344197
RD23B_HUMAN	RAD23B	physical	26344197
CXA5_HUMAN	GJA5	physical	25583071
CXG1_HUMAN	GJC1	physical	25583071
CXA1_HUMAN	GJA1	physical	25583071
CXB1_HUMAN	GJB1	physical	25583071
BAG6_HUMAN	BAG6	physical	27113755

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 UBQL4_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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 ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318, AND MASSSPECTROMETRY.	17525332 [Abstract]

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