dbPTM

BUD13_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BUD13_HUMAN
UniProt AC	Q9BRD0
Protein Name	BUD13 homolog
Gene Name	BUD13
Organism	Homo sapiens (Human).
Sequence Length	619
Subcellular Localization
Protein Description
Protein Sequence	MAAAPPLSKAEYLKRYLSGADAGVDRGSESGRKRRKKRPKPGGAGGKGMRIVDDDVSWTAISTTKLEKEEEEDDGDLPVVAEFVDERPEEVKQMEAFRSSAKWKLLGGHNEDLPSNRHFRHDTPDSSPRRVRHGTPDPSPRKDRHDTPDPSPRRARHDTPDPSPLRGARHDSDTSPPRRIRHDSSDTSPPRRARHDSPDPSPPRRPQHNSSGASPRRVRHDSPDPSPPRRARHGSSDISSPRRVHNNSPDTSRRTLGSSDTQQLRRARHDSPDLAPNVTYSLPRTKSGKAPERASSKTSPHWKESGASHLSFPKNSKYEYDPDISPPRKKQAKSHFGDKKQLDSKGDCQKATDSDLSSPRHKQSPGHQDSDSDLSPPRNRPRHRSSDSDLSPPRRRQRTKSSDSDLSPPRRSQPPGKKAAHMYSGAKTGLVLTDIQREQQELKEQDQETMAFEAEFQYAETVFRDKSGRKRNLKLERLEQRRKAEKDSERDELYAQWGKGLAQSRQQQQNVEDAMKEMQKPLARYIDDEDLDRMLREQEREGDPMANFIKKNKAKENKNKKVRPRYSGPAPPPNRFNIWPGYRWDGVDRSNGFEQKRFARLASKKAVEELAYKWSVEDM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
16	Phosphorylation	KAEYLKRYLSGADAG HHHHHHHHHHCCCCC	12.02	29978859
18	Phosphorylation	EYLKRYLSGADAGVD HHHHHHHHCCCCCCC	24.01	25159151
26	Methylation	GADAGVDRGSESGRK CCCCCCCCCCHHHCC	48.40	-
28	Phosphorylation	DAGVDRGSESGRKRR CCCCCCCCHHHCCCC	29.50	25159151
30	Phosphorylation	GVDRGSESGRKRRKK CCCCCCHHHCCCCCC	45.66	30576142
40	Acetylation	KRRKKRPKPGGAGGK CCCCCCCCCCCCCCC	61.40	18585327
47	Acetylation	KPGGAGGKGMRIVDD CCCCCCCCCCEECCC	48.92	90929
57	Phosphorylation	RIVDDDVSWTAISTT EECCCCCCEEEEECC	26.21	28348404
59	Phosphorylation	VDDDVSWTAISTTKL CCCCCCEEEEECCCC	13.45	28348404
65	Sumoylation	WTAISTTKLEKEEEE EEEEECCCCCHHHHC	55.53	-
65	Sumoylation	WTAISTTKLEKEEEE EEEEECCCCCHHHHC	55.53	28112733
92	Ubiquitination	DERPEEVKQMEAFRS CCCHHHHHHHHHHHH	47.40	-
99	Phosphorylation	KQMEAFRSSAKWKLL HHHHHHHHHHHHHHH	28.35	28102081
100	Phosphorylation	QMEAFRSSAKWKLLG HHHHHHHHHHHHHHC	29.61	23917254
104	Ubiquitination	FRSSAKWKLLGGHNE HHHHHHHHHHCCCCC	32.88	-
115	Phosphorylation	GHNEDLPSNRHFRHD CCCCCCCCCCCCCCC	54.52	21406692
123	Phosphorylation	NRHFRHDTPDSSPRR CCCCCCCCCCCCCCC	23.91	23401153
126	Phosphorylation	FRHDTPDSSPRRVRH CCCCCCCCCCCCCCC	43.37	23401153
127	Phosphorylation	RHDTPDSSPRRVRHG CCCCCCCCCCCCCCC	29.79	29255136
135	Phosphorylation	PRRVRHGTPDPSPRK CCCCCCCCCCCCCCC	20.56	29255136
139	Phosphorylation	RHGTPDPSPRKDRHD CCCCCCCCCCCCCCC	44.72	29255136
147	Phosphorylation	PRKDRHDTPDPSPRR CCCCCCCCCCCCCCC	24.38	29255136
151	Phosphorylation	RHDTPDPSPRRARHD CCCCCCCCCCCCCCC	38.12	29255136
159	Phosphorylation	PRRARHDTPDPSPLR CCCCCCCCCCCCCCC	24.38	29255136
163	Phosphorylation	RHDTPDPSPLRGARH CCCCCCCCCCCCCCC	43.90	29255136
172	Phosphorylation	LRGARHDSDTSPPRR CCCCCCCCCCCCCCC	36.34	29255136
174	Phosphorylation	GARHDSDTSPPRRIR CCCCCCCCCCCCCCC	47.27	29255136
175	Phosphorylation	ARHDSDTSPPRRIRH CCCCCCCCCCCCCCC	37.59	29255136
184	Phosphorylation	PRRIRHDSSDTSPPR CCCCCCCCCCCCCCC	24.80	20164059
185	Phosphorylation	RRIRHDSSDTSPPRR CCCCCCCCCCCCCCH	51.47	20164059
187	Phosphorylation	IRHDSSDTSPPRRAR CCCCCCCCCCCCHHC	45.11	21955146
188	Phosphorylation	RHDSSDTSPPRRARH CCCCCCCCCCCHHCC	37.59	26055452
197	Phosphorylation	PRRARHDSPDPSPPR CCHHCCCCCCCCCCC	25.69	29255136
201	Phosphorylation	RHDSPDPSPPRRPQH CCCCCCCCCCCCCCC	55.72	29255136
201 (in isoform 2)	Phosphorylation	-	55.72	29743597
210	Phosphorylation	PRRPQHNSSGASPRR CCCCCCCCCCCCCCC	28.20	23927012
211	Phosphorylation	RRPQHNSSGASPRRV CCCCCCCCCCCCCCC	43.63	23927012
214	Phosphorylation	QHNSSGASPRRVRHD CCCCCCCCCCCCCCC	23.59	20201521
220 (in isoform 2)	Phosphorylation	-	36.72	29743597
222	Phosphorylation	PRRVRHDSPDPSPPR CCCCCCCCCCCCCCC	25.69	29255136
224 (in isoform 2)	Phosphorylation	-	61.33	29743597
226	Phosphorylation	RHDSPDPSPPRRARH CCCCCCCCCCCCCCC	55.72	29255136
235	Phosphorylation	PRRARHGSSDISSPR CCCCCCCCCCCCCCC	20.79	29255136
236	Phosphorylation	RRARHGSSDISSPRR CCCCCCCCCCCCCCC	43.48	29255136
239	Phosphorylation	RHGSSDISSPRRVHN CCCCCCCCCCCCCCC	39.00	29255136
240	Phosphorylation	HGSSDISSPRRVHNN CCCCCCCCCCCCCCC	23.82	29255136
248	Phosphorylation	PRRVHNNSPDTSRRT CCCCCCCCCCCCHHC	29.48	29255136
251	Phosphorylation	VHNNSPDTSRRTLGS CCCCCCCCCHHCCCC	27.76	29255136
252	Phosphorylation	HNNSPDTSRRTLGSS CCCCCCCCHHCCCCC	27.43	29255136
255	Phosphorylation	SPDTSRRTLGSSDTQ CCCCCHHCCCCCHHH	34.07	25159151
258	Phosphorylation	TSRRTLGSSDTQQLR CCHHCCCCCHHHHHH	28.31	25159151
259	Phosphorylation	SRRTLGSSDTQQLRR CHHCCCCCHHHHHHH	42.76	25159151
261	Phosphorylation	RTLGSSDTQQLRRAR HCCCCCHHHHHHHHH	21.84	29396449
271	Phosphorylation	LRRARHDSPDLAPNV HHHHHCCCCCCCCCC	17.75	29255136
279	Phosphorylation	PDLAPNVTYSLPRTK CCCCCCCEEECCCCC	17.65	25159151
280	Phosphorylation	DLAPNVTYSLPRTKS CCCCCCEEECCCCCC	12.15	21712546
281	Phosphorylation	LAPNVTYSLPRTKSG CCCCCEEECCCCCCC	23.64	25159151
295	Phosphorylation	GKAPERASSKTSPHW CCCCCCCCCCCCCCH	38.29	23403867
296	Phosphorylation	KAPERASSKTSPHWK CCCCCCCCCCCCCHH	38.68	23403867
298	Phosphorylation	PERASSKTSPHWKES CCCCCCCCCCCHHHC	49.81	26657352
299	Phosphorylation	ERASSKTSPHWKESG CCCCCCCCCCHHHCC	20.64	25159151
305	Phosphorylation	TSPHWKESGASHLSF CCCCHHHCCCCCCCC	35.61	21949786
308	Phosphorylation	HWKESGASHLSFPKN CHHHCCCCCCCCCCC	28.61	25159151
311	Phosphorylation	ESGASHLSFPKNSKY HCCCCCCCCCCCCCC	33.79	25159151
318	Phosphorylation	SFPKNSKYEYDPDIS CCCCCCCCCCCCCCC	21.39	23927012
320	Phosphorylation	PKNSKYEYDPDISPP CCCCCCCCCCCCCCC	29.68	23927012
325	Phosphorylation	YEYDPDISPPRKKQA CCCCCCCCCCCHHHH	35.91	19664994
352	Phosphorylation	KGDCQKATDSDLSSP CCCHHHCCCCCCCCC	42.97	24732914
354	Phosphorylation	DCQKATDSDLSSPRH CHHHCCCCCCCCCCH	35.78	30266825
357	Phosphorylation	KATDSDLSSPRHKQS HCCCCCCCCCCHHCC	43.20	30266825
358	Phosphorylation	ATDSDLSSPRHKQSP CCCCCCCCCCHHCCC	33.00	29255136
364	Phosphorylation	SSPRHKQSPGHQDSD CCCCHHCCCCCCCCC	37.34	23927012
365	Ubiquitination	SPRHKQSPGHQDSDS CCCHHCCCCCCCCCC	41.62	29967540
370	Phosphorylation	QSPGHQDSDSDLSPP CCCCCCCCCCCCCCC	32.23	23927012
372	Phosphorylation	PGHQDSDSDLSPPRN CCCCCCCCCCCCCCC	44.39	23927012
375	Phosphorylation	QDSDSDLSPPRNRPR CCCCCCCCCCCCCCC	37.54	23927012
382	Ubiquitination	SPPRNRPRHRSSDSD CCCCCCCCCCCCCCC	34.31	24816145
385	Phosphorylation	RNRPRHRSSDSDLSP CCCCCCCCCCCCCCC	32.16	27273156
386	Phosphorylation	NRPRHRSSDSDLSPP CCCCCCCCCCCCCCC	40.88	27273156
388	Phosphorylation	PRHRSSDSDLSPPRR CCCCCCCCCCCCCHH	42.26	27273156
391	Phosphorylation	RSSDSDLSPPRRRQR CCCCCCCCCCHHHHC	37.54	23401153
399	Phosphorylation	PPRRRQRTKSSDSDL CCHHHHCCCCCCCCC	27.26	25072903
401	Phosphorylation	RRRQRTKSSDSDLSP HHHHCCCCCCCCCCC	38.47	27273156
402	Phosphorylation	RRQRTKSSDSDLSPP HHHCCCCCCCCCCCC	42.56	27273156
404	Phosphorylation	QRTKSSDSDLSPPRR HCCCCCCCCCCCCCC	42.26	27273156
407	Phosphorylation	KSSDSDLSPPRRSQP CCCCCCCCCCCCCCC	37.54	23401153
423	Phosphorylation	GKKAAHMYSGAKTGL CCCHHHHHHCCCHHH	8.29	29396449
424	Phosphorylation	KKAAHMYSGAKTGLV CCHHHHHHCCCHHHH	25.38	28985074
427	Acetylation	AHMYSGAKTGLVLTD HHHHHCCCHHHHHHH	46.80	26051181
428	Phosphorylation	HMYSGAKTGLVLTDI HHHHCCCHHHHHHHH	34.90	20068231
433	Phosphorylation	AKTGLVLTDIQREQQ CCHHHHHHHHHHHHH	24.47	20068231
458	Phosphorylation	AFEAEFQYAETVFRD HHHHHHHHHHHHHCC	16.24	27642862
462	Ubiquitination	EFQYAETVFRDKSGR HHHHHHHHHCCCCCC	2.52	24816145
483	Ubiquitination	ERLEQRRKAEKDSER HHHHHHHHHHHHHHH	64.19	24816145
494	Phosphorylation	DSERDELYAQWGKGL HHHHHHHHHHHHHHH	8.49	28796482
499	Acetylation	ELYAQWGKGLAQSRQ HHHHHHHHHHHHHHH	48.03	26051181
499	Ubiquitination	ELYAQWGKGLAQSRQ HHHHHHHHHHHHHHH	48.03	29967540
516	Ubiquitination	QNVEDAMKEMQKPLA HCHHHHHHHHHHHHH	52.32	24816145
520	Acetylation	DAMKEMQKPLARYID HHHHHHHHHHHHHCC	40.46	25953088
563	Ubiquitination	ENKNKKVRPRYSGPA HCCCCCCCCCCCCCC	20.89	24816145
566	Phosphorylation	NKKVRPRYSGPAPPP CCCCCCCCCCCCCCC	22.21	19691289
567	Phosphorylation	KKVRPRYSGPAPPPN CCCCCCCCCCCCCCC	39.31	26055452
596	Ubiquitination	RSNGFEQKRFARLAS CCCCHHHHHHHHHHC	42.14	24816145
612	Phosphorylation	KAVEELAYKWSVEDM HHHHHHHHHCCCCCC	26.14	25159151

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
18	S	Phosphorylation	Kinase	CHEK1	O14757	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BUD13_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 BUD13_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
RBMX2_HUMAN	RBMX2	physical	22365833
GPKOW_HUMAN	GPKOW	physical	22365833

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 BUD13_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 THR-159; SER-163; SER-271;THR-279; SER-325 AND SER-358, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND MASSSPECTROMETRY.	19413330 [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 THR-159; SER-163; SER-222;SER-226; SER-271; SER-325; SER-354 AND SER-358, AND MASS SPECTROMETRY.	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-271; SER-281 ANDSER-325, AND MASS SPECTROMETRY.	18220336 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-159; SER-163 ANDSER-325, AND MASS SPECTROMETRY.	16964243 [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 THR-135; SER-139; THR-147;SER-151; THR-159; SER-163; SER-222; SER-226; SER-248; SER-271 ANDSER-325, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-255, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-494, AND MASSSPECTROMETRY.	15592455 [Abstract]