dbPTM

UBXN7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBXN7_HUMAN
UniProt AC	O94888
Protein Name	UBX domain-containing protein 7
Gene Name	UBXN7
Organism	Homo sapiens (Human).
Sequence Length	489
Subcellular Localization	Nucleus .
Protein Description	Ubiquitin-binding adapter that links a subset of NEDD8-associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates..
Protein Sequence	MAAHGGSAASSALKGLIQQFTTITGASESVGKHMLEACNNNLEMAVTMFLDGGGIAEEPSTSSASVSTVRPHTEEEVRAPIPQKQEILVEPEPLFGAPKRRRPARSIFDGFRDFQTETIRQEQELRNGGAIDKKLTTLADLFRPPIDLMHKGSFETAKECGQMQNKWLMINIQNVQDFACQCLNRDVWSNEAVKNIIREHFIFWQVYHDSEEGQRYIQFYKLGDFPYVSILDPRTGQKLVEWHQLDVSSFLDQVTGFLGEHGQLDGLSSSPPKKCARSESLIDASEDSQLEAAIRASLQETHFDSTQTKQDSRSDEESESELFSGSEEFISVCGSDEEEEVENLAKSRKSPHKDLGHRKEENRRPLTEPPVRTDPGTATNHQGLPAVDSEILEMPPEKADGVVEGIDVNGPKAQLMLRYPDGKREQITLPEQAKLLALVKHVQSKGYPNERFELLTNFPRRKLSHLDYDITLQEAGLCPQETVFVQERN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAHGGSAA ------CCCCCHHHH	14.25	19413330
7	Phosphorylation	-MAAHGGSAASSALK -CCCCCHHHHHHHHH	25.84	25159151
10	Ubiquitination	AHGGSAASSALKGLI CCCHHHHHHHHHHHH	18.83	21963094
10	Phosphorylation	AHGGSAASSALKGLI CCCHHHHHHHHHHHH	18.83	21406692
11	Phosphorylation	HGGSAASSALKGLIQ CCHHHHHHHHHHHHH	32.66	21406692
14	Ubiquitination	SAASSALKGLIQQFT HHHHHHHHHHHHHHH	51.92	23000965
24	Phosphorylation	IQQFTTITGASESVG HHHHHHHCCCCHHHH	25.30	27690223
27	Phosphorylation	FTTITGASESVGKHM HHHHCCCCHHHHHHH	31.58	27251275
29	Phosphorylation	TITGASESVGKHMLE HHCCCCHHHHHHHHH	33.40	25159151
46	Ubiquitination	NNNLEMAVTMFLDGG CCCHHHEEEEEECCC	3.73	21890473
51	Ubiquitination	MAVTMFLDGGGIAEE HEEEEEECCCCCCCC	42.29	23000965
60	Phosphorylation	GGIAEEPSTSSASVS CCCCCCCCCCCCCEE	44.17	30576142
61	Phosphorylation	GIAEEPSTSSASVST CCCCCCCCCCCCEEE	37.10	30576142
63	Phosphorylation	AEEPSTSSASVSTVR CCCCCCCCCCEEECC	25.34	30576142
66	Ubiquitination	PSTSSASVSTVRPHT CCCCCCCEEECCCCC	5.78	23000965
73	Ubiquitination	VSTVRPHTEEEVRAP EEECCCCCHHHHCCC	48.01	21963094
84	Acetylation	VRAPIPQKQEILVEP HCCCCCCCCEEEECC	44.54	25953088
84	Ubiquitination	VRAPIPQKQEILVEP HCCCCCCCCEEEECC	44.54	23000965
84	Sumoylation	VRAPIPQKQEILVEP HCCCCCCCCEEEECC	44.54	28112733
99	Ubiquitination	EPLFGAPKRRRPARS CCCCCCCCCCCCCHH	58.99	23000965
100	Ubiquitination	PLFGAPKRRRPARSI CCCCCCCCCCCCHHH	38.49	23000965
101	Ubiquitination	LFGAPKRRRPARSIF CCCCCCCCCCCHHHH	55.87	23000965
106	Phosphorylation	KRRRPARSIFDGFRD CCCCCCHHHHCCCHH	29.70	27499020
116	Phosphorylation	DGFRDFQTETIRQEQ CCCHHHHHHHHHHHH	34.78	20044836
118	Ubiquitination	FRDFQTETIRQEQEL CHHHHHHHHHHHHHH	25.50	21890473
118	Phosphorylation	FRDFQTETIRQEQEL CHHHHHHHHHHHHHH	25.50	20044836
125	Ubiquitination	TIRQEQELRNGGAID HHHHHHHHHCCCCCC	5.28	21963094
133	Ubiquitination	RNGGAIDKKLTTLAD HCCCCCCHHHHHHHH	43.50	23000965
134	Ubiquitination	NGGAIDKKLTTLADL CCCCCCHHHHHHHHH	47.52	23000965
151	Ubiquitination	PPIDLMHKGSFETAK CCCCCCCCCCHHHHH	42.14	21906983
158	Ubiquitination	KGSFETAKECGQMQN CCCHHHHHHHHCCCC	62.04	21963094
161	Ubiquitination	FETAKECGQMQNKWL HHHHHHHHCCCCCEE	27.38	23000965
163	Sulfoxidation	TAKECGQMQNKWLMI HHHHHHCCCCCEEEE	2.62	30846556
188	Ubiquitination	QCLNRDVWSNEAVKN HHHCCCCCCHHHHHH	10.34	21963094
189	Phosphorylation	CLNRDVWSNEAVKNI HHCCCCCCHHHHHHH	25.33	24670416
194	Ubiquitination	VWSNEAVKNIIREHF CCCHHHHHHHHHHHH	49.86	23000965
221	Ubiquitination	QRYIQFYKLGDFPYV CEEEEEEEECCCCEE	47.48	21906983
227	Phosphorylation	YKLGDFPYVSILDPR EEECCCCEEEEECCC	13.56	-
248	Phosphorylation	EWHQLDVSSFLDQVT EEHHCCHHHHHHHHH	18.29	28450419
249	Phosphorylation	WHQLDVSSFLDQVTG EHHCCHHHHHHHHHH	29.67	28450419
255	Phosphorylation	SSFLDQVTGFLGEHG HHHHHHHHHHHCCCC	19.31	28450419
268	Phosphorylation	HGQLDGLSSSPPKKC CCCCCCCCCCCCCHH	34.01	25159151
269	Phosphorylation	GQLDGLSSSPPKKCA CCCCCCCCCCCCHHC	52.48	25159151
270	Phosphorylation	QLDGLSSSPPKKCAR CCCCCCCCCCCHHCC	41.67	25159151
273	Ubiquitination	GLSSSPPKKCARSES CCCCCCCCHHCCCCC	64.96	29967540
276	Ubiquitination	SSPPKKCARSESLID CCCCCHHCCCCCCCC	27.24	21963094
278	Phosphorylation	PPKKCARSESLIDAS CCCHHCCCCCCCCCC	17.01	20201521
280	Phosphorylation	KKCARSESLIDASED CHHCCCCCCCCCCCH	31.69	20201521
285	Phosphorylation	SESLIDASEDSQLEA CCCCCCCCCHHHHHH	37.88	23927012
286	Ubiquitination	ESLIDASEDSQLEAA CCCCCCCCHHHHHHH	64.50	23000965
288	Phosphorylation	LIDASEDSQLEAAIR CCCCCCHHHHHHHHH	32.39	19664994
292	Ubiquitination	SEDSQLEAAIRASLQ CCHHHHHHHHHHHHH	19.44	21890473
297	Ubiquitination	LEAAIRASLQETHFD HHHHHHHHHHHHCCC	22.27	23000965
297	Phosphorylation	LEAAIRASLQETHFD HHHHHHHHHHHHCCC	22.27	23663014
301	Phosphorylation	IRASLQETHFDSTQT HHHHHHHHCCCCCCC	18.19	23186163
305	Phosphorylation	LQETHFDSTQTKQDS HHHHCCCCCCCCCCC	22.82	29255136
306	Phosphorylation	QETHFDSTQTKQDSR HHHCCCCCCCCCCCC	41.94	17525332
308	Phosphorylation	THFDSTQTKQDSRSD HCCCCCCCCCCCCCC	30.66	29255136
309	Ubiquitination	HFDSTQTKQDSRSDE CCCCCCCCCCCCCCH	42.14	21963094
312	Phosphorylation	STQTKQDSRSDEESE CCCCCCCCCCCHHHH	31.06	-
314	Phosphorylation	QTKQDSRSDEESESE CCCCCCCCCHHHHHH	54.01	27362937
318	Phosphorylation	DSRSDEESESELFSG CCCCCHHHHHHHHCC	44.36	27362937
320	Phosphorylation	RSDEESESELFSGSE CCCHHHHHHHHCCCH	49.21	24461736
347	Phosphorylation	EVENLAKSRKSPHKD HHHHHHHHCCCCCCC	39.06	26074081
350	Phosphorylation	NLAKSRKSPHKDLGH HHHHHCCCCCCCCCC	31.00	23663014
359	Ubiquitination	HKDLGHRKEENRRPL CCCCCCCCCCCCCCC	64.80	29967540
398	Ubiquitination	ILEMPPEKADGVVEG HHHCCHHHCCCEEEE	58.51	29967540
401	Ubiquitination	MPPEKADGVVEGIDV CCHHHCCCEEEEECC	30.17	23000965
407	Ubiquitination	DGVVEGIDVNGPKAQ CCEEEEECCCCCCEE	38.39	21890473
412	Ubiquitination	GIDVNGPKAQLMLRY EECCCCCCEEEEEEC	50.60	23000965
428	Phosphorylation	DGKREQITLPEQAKL CCCCEECCCHHHHHH	35.63	-
434	Ubiquitination	ITLPEQAKLLALVKH CCCHHHHHHHHHHHH	43.67	23000965
434	Acetylation	ITLPEQAKLLALVKH CCCHHHHHHHHHHHH	43.67	23236377
440	Ubiquitination	AKLLALVKHVQSKGY HHHHHHHHHHHHCCC	38.62	23000965
445	Ubiquitination	LVKHVQSKGYPNERF HHHHHHHCCCCCHHH	45.43	23000965
464	Phosphorylation	NFPRRKLSHLDYDIT CCCHHHCCCCCCCEE	25.66	24275569

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 UBXN7_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UBXN7_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 UBXN7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TERA_HUMAN	VCP	physical	18775313
NPL4_HUMAN	NPLOC4	physical	18775313
UFD1_HUMAN	UFD1L	physical	18775313
CUL1_HUMAN	CUL1	physical	18775313
CUL2_HUMAN	CUL2	physical	18775313
CUL3_HUMAN	CUL3	physical	18775313
UBR1_HUMAN	UBR1	physical	18775313
PSMD2_HUMAN	PSMD2	physical	18775313
HIF1A_HUMAN	HIF1A	physical	18775313
PPB1_HUMAN	ALPP	physical	18775313
SKP1_HUMAN	SKP1	physical	18775313
RBX1_HUMAN	RBX1	physical	18775313
ELOB_HUMAN	TCEB2	physical	18775313
ELOC_HUMAN	TCEB1	physical	18775313
VHL_HUMAN	VHL	physical	18775313
KLH12_HUMAN	KLHL12	physical	18775313
KLH13_HUMAN	KLHL13	physical	18775313
KLH22_HUMAN	KLHL22	physical	18775313
KBTB7_HUMAN	KBTBD7	physical	18775313
KBTB2_HUMAN	KBTBD2	physical	18775313
KLDC3_HUMAN	KLHDC3	physical	18775313
CUL4A_HUMAN	CUL4A	physical	18775313
CUL4B_HUMAN	CUL4B	physical	18775313
DDB1_HUMAN	DDB1	physical	18775313
DCAF1_HUMAN	VPRBP	physical	18775313
WDR26_HUMAN	WDR26	physical	18775313
WDR11_HUMAN	WDR11	physical	18775313
BRWD1_HUMAN	BRWD1	physical	18775313
BRWD3_HUMAN	BRWD3	physical	18775313
AMFR_HUMAN	AMFR	physical	18775313
UBR2_HUMAN	UBR2	physical	18775313
UBR4_HUMAN	UBR4	physical	18775313
PJA2_HUMAN	PJA2	physical	18775313
BIRC2_HUMAN	BIRC2	physical	18775313
TOPRS_HUMAN	TOPORS	physical	18775313
UBR5_HUMAN	UBR5	physical	18775313
CUL2_HUMAN	CUL2	physical	22537386
ELOC_HUMAN	TCEB1	physical	22537386
RBX1_HUMAN	RBX1	physical	22537386
NEDD8_HUMAN	NEDD8	physical	22537386
HIF1A_HUMAN	HIF1A	physical	22537386
CUL2_HUMAN	CUL2	physical	22466964
CUL4A_HUMAN	CUL4A	physical	22466964
CUL1_HUMAN	CUL1	physical	22466964
CUL3_HUMAN	CUL3	physical	22466964
NEDD8_HUMAN	NEDD8	physical	22466964
CUL4B_HUMAN	CUL4B	physical	22466964
A4_HUMAN	APP	physical	21832049
VATF_HUMAN	ATP6V1F	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
ANCHR_HUMAN	ZFYVE19	physical	22939629
ZYX_HUMAN	ZYX	physical	22939629
UCHL3_HUMAN	UCHL3	physical	22939629
VP26A_HUMAN	VPS26A	physical	22939629
ZPR1_HUMAN	ZPR1	physical	22939629
ZRAB2_HUMAN	ZRANB2	physical	22939629
UFC1_HUMAN	UFC1	physical	22939629
UFM1_HUMAN	UFM1	physical	22939629
YAP1_HUMAN	YAP1	physical	22939629
USP9X_HUMAN	USP9X	physical	22939629
UBC_HUMAN	UBC	physical	18775313
UBC_HUMAN	UBC	physical	22466964
TERA_HUMAN	VCP	physical	22466964
ACD11_HUMAN	ACAD11	physical	26389662
ERCC3_HUMAN	ERCC3	physical	26389662
KC1G3_HUMAN	CSNK1G3	physical	26389662
ASPC1_HUMAN	ASPSCR1	physical	26389662
TERA_HUMAN	VCP	physical	26389662
WDR11_HUMAN	WDR11	physical	26389662
CUL2_HUMAN	CUL2	physical	26389662
BACD3_HUMAN	KCTD10	physical	26389662
KLH12_HUMAN	KLHL12	physical	26389662
BTBD9_HUMAN	BTBD9	physical	26389662
BACD1_HUMAN	KCTD13	physical	26389662
TOPRS_HUMAN	TOPORS	physical	26389662
ABCF1_HUMAN	ABCF1	physical	26389662
JUN_HUMAN	JUN	physical	26389662
RNBP6_HUMAN	RANBP6	physical	26389662
SETD7_HUMAN	SETD7	physical	26389662
RN138_HUMAN	RNF138	physical	26389662
KIFC1_HUMAN	KIFC1	physical	26389662
MO4L2_HUMAN	MORF4L2	physical	26389662
BRWD3_HUMAN	BRWD3	physical	26389662
PHF6_HUMAN	PHF6	physical	26389662
PHIP_HUMAN	PHIP	physical	26389662
KC1E_HUMAN	CSNK1E	physical	26389662
PO3F2_HUMAN	POU3F2	physical	26389662
CSTF1_HUMAN	CSTF1	physical	26389662
FAF2_HUMAN	FAF2	physical	26389662
NPL4_HUMAN	NPLOC4	physical	26389662
NSF1C_HUMAN	NSFL1C	physical	26389662
UFD1_HUMAN	UFD1L	physical	26389662
VCIP1_HUMAN	VCPIP1	physical	26389662
BRWD1_HUMAN	BRWD1	physical	26389662
FAF1_HUMAN	FAF1	physical	26389662
F91A1_HUMAN	FAM91A1	physical	26389662
KLDC2_HUMAN	KLHDC2	physical	26389662
KLDC3_HUMAN	KLHDC3	physical	26389662
KLD10_HUMAN	KLHDC10	physical	26389662
IMA4_HUMAN	KPNA3	physical	26389662
BACD2_HUMAN	TNFAIP1	physical	26389662

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 UBXN7_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-288, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction."; Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; Mol. Cell. Proteomics 6:1952-1967(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASSSPECTROMETRY.	17693683 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-288, ANDMASS SPECTROMETRY.	16083285 [Abstract]
"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 THR-306, AND MASSSPECTROMETRY.	17525332 [Abstract]
Ubiquitylation
Reference	PubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-99, AND MASSSPECTROMETRY.	18781797 [Abstract]