dbPTM

DREB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DREB_HUMAN
UniProt AC	Q16643
Protein Name	Drebrin
Gene Name	DBN1
Organism	Homo sapiens (Human).
Sequence Length	649
Subcellular Localization	Cytoplasm . Cytoplasm, cell cortex . Cell junction . Cell projection . Cell projection, growth cone . In the absence of antigen, evenly distributed throughout subcortical regions of the T-cell membrane and cytoplasm. In the presence of antigen, distr
Protein Description	Drebrins might play some role in cell migration, extension of neuronal processes and plasticity of dendrites. Required for actin polymerization at immunological synapses (IS) and for CXCR4 recruitment to IS..
Protein Sequence	MAGVSFSGHRLELLAAYEEVIREESAADWALYTYEDGSDDLKLAASGEGGLQELSGHFENQKVMYGFCSVKDSQAALPKYVLINWVGEDVPDARKCACASHVAKVAEFFQGVDVIVNASSVEDIDAGAIGQRLSNGLARLSSPVLHRLRLREDENAEPVGTTYQKTDAAVEMKRINREQFWEQAKKEEELRKEEERKKALDERLRFEQERMEQERQEQEERERRYREREQQIEEHRRKQQTLEAEEAKRRLKEQSIFGDHRDEEEETHMKKSESEVEEAAAIIAQRPDNPREFFKQQERVASASAGSCDVPSPFNHRPGSHLDSHRRMAPTPIPTRSPSDSSTASTPVAEQIERALDEVTSSQPPPLPPPPPPAQETQEPSPILDSEETRAAAPQAWAGPMEEPPQAQAPPRGPGSPAEDLMFMESAEQAVLAAPVEPATADATEIHDAADTIETDTATADTTVANNVPPAATSLIDLWPGNGEGASTLQGEPRAPTPPSGTEVTLAEVPLLDEVAPEPLLPAGEGCATLLNFDELPEPPATFCDPEEVEGESLAAPQTPTLPSALEELEQEQEPEPHLLTNGETTQKEGTQASEGYFSQSQEEEFAQSEELCAKAPPPVFYNKPPEIDITCWDADPVPEEEEGFEGGD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGVSFSGH ------CCCCCCCHH	27.39	19413330
5	Phosphorylation	---MAGVSFSGHRLE ---CCCCCCCHHHHH	16.87	25159151
6	Phosphorylation	--MAGVSFSGHRLEL --CCCCCCCHHHHHH	10.61	32142685
7	Phosphorylation	-MAGVSFSGHRLELL -CCCCCCCHHHHHHH	26.61	28355574
8	Ubiquitination	MAGVSFSGHRLELLA CCCCCCCHHHHHHHH	14.13	23000965
17	Phosphorylation	RLELLAAYEEVIREE HHHHHHHHHHHHHHH	13.66	28674151
32	Phosphorylation	SAADWALYTYEDGSD CCCCEEEEEECCCCC	10.26	28796482
33	Phosphorylation	AADWALYTYEDGSDD CCCEEEEEECCCCCC	22.68	28796482
34	Phosphorylation	ADWALYTYEDGSDDL CCEEEEEECCCCCCC	9.85	28796482
34 (in isoform 2)	Phosphorylation	-	9.85	27642862
36 (in isoform 2)	Phosphorylation	-	52.03	27642862
51	Ubiquitination	AASGEGGLQELSGHF ECCCCCHHHHHHCCC	5.41	23000965
60	Ubiquitination	ELSGHFENQKVMYGF HHHCCCCCCEEEEEE	46.13	23000965
62	Ubiquitination	SGHFENQKVMYGFCS HCCCCCCEEEEEEEC	40.32	-
62	Acetylation	SGHFENQKVMYGFCS HCCCCCCEEEEEEEC	40.32	26051181
62	Ubiquitination	SGHFENQKVMYGFCS HCCCCCCEEEEEEEC	40.32	23000965
63	Phosphorylation	GHFENQKVMYGFCSV CCCCCCEEEEEEECH	2.29	32142685
64	Sulfoxidation	HFENQKVMYGFCSVK CCCCCEEEEEEECHH	3.31	30846556
64	Ubiquitination	HFENQKVMYGFCSVK CCCCCEEEEEEECHH	3.31	23000965
65	Phosphorylation	FENQKVMYGFCSVKD CCCCEEEEEEECHHC	15.27	25159151
67	Phosphorylation	NQKVMYGFCSVKDSQ CCEEEEEEECHHCHH	1.22	-
69	Phosphorylation	KVMYGFCSVKDSQAA EEEEEEECHHCHHHC	29.91	32142685
70	Ubiquitination	VMYGFCSVKDSQAAL EEEEEECHHCHHHCC	9.33	32015554
71	Ubiquitination	MYGFCSVKDSQAALP EEEEECHHCHHHCCC	35.05	21906983
71	Acetylation	MYGFCSVKDSQAALP EEEEECHHCHHHCCC	35.05	26051181
71	Phosphorylation	MYGFCSVKDSQAALP EEEEECHHCHHHCCC	35.05	32142685
71	Ubiquitination	MYGFCSVKDSQAALP EEEEECHHCHHHCCC	35.05	23000965
71 (in isoform 1)	Ubiquitination	-	35.05	21906983
73	Phosphorylation	GFCSVKDSQAALPKY EEECHHCHHHCCCCE	18.92	27251275
73	Ubiquitination	GFCSVKDSQAALPKY EEECHHCHHHCCCCE	18.92	23000965
73 (in isoform 2)	Ubiquitination	-	18.92	21906983
75	Phosphorylation	CSVKDSQAALPKYVL ECHHCHHHCCCCEEE	18.21	27251275
78	Phosphorylation	KDSQAALPKYVLINW HCHHHCCCCEEEEEC	22.62	32645325
79	Acetylation	DSQAALPKYVLINWV CHHHCCCCEEEEECC	49.17	26051181
79	Ubiquitination	DSQAALPKYVLINWV CHHHCCCCEEEEECC	49.17	29967540
80	Phosphorylation	SQAALPKYVLINWVG HHHCCCCEEEEECCC	9.88	28796482
81	Ubiquitination	QAALPKYVLINWVGE HHCCCCEEEEECCCC	5.59	29967540
96	S-nitrosylation	DVPDARKCACASHVA CCCCHHHHHHHHHHH	2.91	2212679
110	Ubiquitination	AKVAEFFQGVDVIVN HHHHHHHCCCCEEEC	57.21	24816145
113	Phosphorylation	AEFFQGVDVIVNASS HHHHCCCCEEECCCC	31.11	32142685
134	Phosphorylation	GAIGQRLSNGLARLS CHHHHHHHHHHHHHC	30.92	30266825
136	Phosphorylation	IGQRLSNGLARLSSP HHHHHHHHHHHHCCH	19.82	20068231
141	Phosphorylation	SNGLARLSSPVLHRL HHHHHHHCCHHHHHH	27.35	25159151
142	Phosphorylation	NGLARLSSPVLHRLR HHHHHHCCHHHHHHH	24.50	29255136
142 (in isoform 3)	Phosphorylation	-	24.50	-
143	Phosphorylation	GLARLSSPVLHRLRL HHHHHCCHHHHHHHC	29.34	20068231
144	Phosphorylation	LARLSSPVLHRLRLR HHHHCCHHHHHHHCC	8.31	18707149
161	Phosphorylation	ENAEPVGTTYQKTDA CCCCCCCCCEECCHH	23.67	21945579
162	Phosphorylation	NAEPVGTTYQKTDAA CCCCCCCCEECCHHH	20.30	21945579
162	Ubiquitination	NAEPVGTTYQKTDAA CCCCCCCCEECCHHH	20.30	24816145
163	Phosphorylation	AEPVGTTYQKTDAAV CCCCCCCEECCHHHH	14.09	21945579
165	Acetylation	PVGTTYQKTDAAVEM CCCCCEECCHHHHHH	37.65	26051181
165	Phosphorylation	PVGTTYQKTDAAVEM CCCCCEECCHHHHHH	37.65	-
172	Ubiquitination	KTDAAVEMKRINREQ CCHHHHHHHHHCHHH	2.58	32142685
173	Ubiquitination	TDAAVEMKRINREQF CHHHHHHHHHCHHHH	36.30	-
173	2-Hydroxyisobutyrylation	TDAAVEMKRINREQF CHHHHHHHHHCHHHH	36.30	-
173	Acetylation	TDAAVEMKRINREQF CHHHHHHHHHCHHHH	36.30	25953088
173	Ubiquitination	TDAAVEMKRINREQF CHHHHHHHHHCHHHH	36.30	32015554
175	Ubiquitination	AAVEMKRINREQFWE HHHHHHHHCHHHHHH	4.80	27667366
227	Ubiquitination	ERERRYREREQQIEE HHHHHHHHHHHHHHH	52.19	27667366
232	Ubiquitination	YREREQQIEEHRRKQ HHHHHHHHHHHHHHH	7.20	23000965
238	Ubiquitination	QIEEHRRKQQTLEAE HHHHHHHHHHHHHHH	46.87	-
238	Ubiquitination	QIEEHRRKQQTLEAE HHHHHHHHHHHHHHH	46.87	27667366
240	Ubiquitination	EEHRRKQQTLEAEEA HHHHHHHHHHHHHHH	51.60	27667366
241	Phosphorylation	EHRRKQQTLEAEEAK HHHHHHHHHHHHHHH	24.87	20068231
243	Phosphorylation	RRKQQTLEAEEAKRR HHHHHHHHHHHHHHH	58.38	20068231
247	Ubiquitination	QTLEAEEAKRRLKEQ HHHHHHHHHHHHHHC	11.36	32142685
248	Ubiquitination	TLEAEEAKRRLKEQS HHHHHHHHHHHHHCH	41.13	32142685
250	Ubiquitination	EAEEAKRRLKEQSIF HHHHHHHHHHHCHHH	49.78	32142685
251	Ubiquitination	AEEAKRRLKEQSIFG HHHHHHHHHHCHHHC	9.22	32015554
252	Acetylation	EEAKRRLKEQSIFGD HHHHHHHHHCHHHCC	52.47	26051181
252	Ubiquitination	EEAKRRLKEQSIFGD HHHHHHHHHCHHHCC	52.47	32015554
254	Ubiquitination	AKRRLKEQSIFGDHR HHHHHHHCHHHCCCC	39.99	32015554
255	Phosphorylation	KRRLKEQSIFGDHRD HHHHHHCHHHCCCCC	22.45	28348404
257	Phosphorylation	RLKEQSIFGDHRDEE HHHHCHHHCCCCCHH	13.09	27251275
267	Phosphorylation	HRDEEEETHMKKSES CCCHHHHHHHHHCHH	30.46	27135362
271	Ubiquitination	EEETHMKKSESEVEE HHHHHHHHCHHHHHH	52.46	29967540
272	Phosphorylation	EETHMKKSESEVEEA HHHHHHHCHHHHHHH	40.62	30266825
273	Phosphorylation	ETHMKKSESEVEEAA HHHHHHCHHHHHHHH	60.85	32142685
273	Ubiquitination	ETHMKKSESEVEEAA HHHHHHCHHHHHHHH	60.85	29967540
274	Phosphorylation	THMKKSESEVEEAAA HHHHHCHHHHHHHHH	54.77	30266825
276	Phosphorylation	MKKSESEVEEAAAII HHHCHHHHHHHHHHH	12.87	32142685
284	Ubiquitination	EEAAAIIAQRPDNPR HHHHHHHHCCCCCHH	8.00	23000965
295	Acetylation	DNPREFFKQQERVAS CCHHHHHHHHHHHHH	57.29	-
295	Ubiquitination	DNPREFFKQQERVAS CCHHHHHHHHHHHHH	57.29	-
295	Acetylation	DNPREFFKQQERVAS CCHHHHHHHHHHHHH	57.29	25953088
295	Malonylation	DNPREFFKQQERVAS CCHHHHHHHHHHHHH	57.29	26320211
295	Succinylation	DNPREFFKQQERVAS CCHHHHHHHHHHHHH	57.29	23954790
295	Ubiquitination	DNPREFFKQQERVAS CCHHHHHHHHHHHHH	57.29	23000965
297	Acetylation	PREFFKQQERVASAS HHHHHHHHHHHHHCC	40.84	-
297	Ubiquitination	PREFFKQQERVASAS HHHHHHHHHHHHHCC	40.84	23000965
302	Phosphorylation	KQQERVASASAGSCD HHHHHHHHCCCCCCC	21.65	24732914
304	Phosphorylation	QERVASASAGSCDVP HHHHHHCCCCCCCCC	30.57	24732914
307	Phosphorylation	VASASAGSCDVPSPF HHHCCCCCCCCCCCC	13.58	24732914
309	Phosphorylation	SASAGSCDVPSPFNH HCCCCCCCCCCCCCC	57.99	27251275
312	Phosphorylation	AGSCDVPSPFNHRPG CCCCCCCCCCCCCCC	41.81	23401153
314	Phosphorylation	SCDVPSPFNHRPGSH CCCCCCCCCCCCCCC	16.45	20068231
320	Phosphorylation	PFNHRPGSHLDSHRR CCCCCCCCCCCCCCC	24.45	28348404
322	Phosphorylation	NHRPGSHLDSHRRMA CCCCCCCCCCCCCCC	8.49	27251275
322 (in isoform 3)	Phosphorylation	-	8.49	28985074
324	Phosphorylation	RPGSHLDSHRRMAPT CCCCCCCCCCCCCCC	25.83	24732914
326	Phosphorylation	GSHLDSHRRMAPTPI CCCCCCCCCCCCCCC	33.74	-
328	Sulfoxidation	HLDSHRRMAPTPIPT CCCCCCCCCCCCCCC	5.44	21406390
329 (in isoform 3)	Phosphorylation	-	11.73	26552605
331	Phosphorylation	SHRRMAPTPIPTRSP CCCCCCCCCCCCCCC	25.06	29255136
331 (in isoform 3)	Phosphorylation	-	25.06	26552605
333	Phosphorylation	RRMAPTPIPTRSPSD CCCCCCCCCCCCCCC	6.31	32645325
334 (in isoform 3)	Phosphorylation	-	23.98	26552605
335	Phosphorylation	MAPTPIPTRSPSDSS CCCCCCCCCCCCCCC	44.49	29255136
335 (in isoform 3)	Phosphorylation	-	44.49	24719451
336 (in isoform 3)	Phosphorylation	-	41.01	26552605
337	Phosphorylation	PTPIPTRSPSDSSTA CCCCCCCCCCCCCCC	31.10	29255136
337 (in isoform 3)	Phosphorylation	-	31.10	26552605
338 (in isoform 3)	Phosphorylation	-	38.57	26552605
339	Phosphorylation	PIPTRSPSDSSTAST CCCCCCCCCCCCCCC	51.90	29255136
339 (in isoform 3)	Phosphorylation	-	51.90	26552605
340 (in isoform 3)	Phosphorylation	-	50.41	26552605
341	Phosphorylation	PTRSPSDSSTASTPV CCCCCCCCCCCCCHH	33.65	29255136
341 (in isoform 3)	Phosphorylation	-	33.65	26552605
342	Phosphorylation	TRSPSDSSTASTPVA CCCCCCCCCCCCHHH	32.74	29255136
342 (in isoform 3)	Phosphorylation	-	32.74	28985074
343	Phosphorylation	RSPSDSSTASTPVAE CCCCCCCCCCCHHHH	28.69	29255136
344	Phosphorylation	SPSDSSTASTPVAEQ CCCCCCCCCCHHHHH	17.23	15345747
345	Phosphorylation	PSDSSTASTPVAEQI CCCCCCCCCHHHHHH	33.08	22167270
346	Phosphorylation	SDSSTASTPVAEQIE CCCCCCCCHHHHHHH	21.22	23927012
347	Phosphorylation	DSSTASTPVAEQIER CCCCCCCHHHHHHHH	22.33	19664995
348	Phosphorylation	SSTASTPVAEQIERA CCCCCCHHHHHHHHH	10.43	19664995
360	Phosphorylation	ERALDEVTSSQPPPL HHHHHHHHCCCCCCC	22.18	24732914
361	Phosphorylation	RALDEVTSSQPPPLP HHHHHHHCCCCCCCC	31.95	24732914
362	Phosphorylation	ALDEVTSSQPPPLPP HHHHHHCCCCCCCCC	37.02	24732914
376	Phosphorylation	PPPPPAQETQEPSPI CCCCCCCCCCCCCCC	55.34	32142685
377	Phosphorylation	PPPPAQETQEPSPIL CCCCCCCCCCCCCCC	26.59	30266825
377 (in isoform 3)	Phosphorylation	-	26.59	27762562
379	Phosphorylation	PPAQETQEPSPILDS CCCCCCCCCCCCCCC	55.98	18669648
381	Phosphorylation	AQETQEPSPILDSEE CCCCCCCCCCCCCHH	24.66	30266825
382	Phosphorylation	QETQEPSPILDSEET CCCCCCCCCCCCHHH	41.71	32142685
383	Phosphorylation	ETQEPSPILDSEETR CCCCCCCCCCCHHHH	8.61	32142685
384	Phosphorylation	TQEPSPILDSEETRA CCCCCCCCCCHHHHH	7.23	32142685
385	Phosphorylation	QEPSPILDSEETRAA CCCCCCCCCHHHHHH	55.51	32142685
386	Phosphorylation	EPSPILDSEETRAAA CCCCCCCCHHHHHHC	33.61	30266825
389	Phosphorylation	PILDSEETRAAAPQA CCCCCHHHHHHCCCC	22.89	24732914
391	Phosphorylation	LDSEETRAAAPQAWA CCCHHHHHHCCCCCC	18.52	32645325
392	Phosphorylation	DSEETRAAAPQAWAG CCHHHHHHCCCCCCC	19.18	32645325
401	Sulfoxidation	PQAWAGPMEEPPQAQ CCCCCCCCCCCCCCC	9.97	30846556
416	Phosphorylation	APPRGPGSPAEDLMF CCCCCCCCCHHHHHC	24.87	26074081
418	Phosphorylation	PRGPGSPAEDLMFME CCCCCCCHHHHHCHH	25.32	-
426	Phosphorylation	EDLMFMESAEQAVLA HHHHCHHHHHHHHHH	25.89	32142685
427	Phosphorylation	DLMFMESAEQAVLAA HHHCHHHHHHHHHHC	10.30	32142685
487	Phosphorylation	PGNGEGASTLQGEPR CCCCCCCCCCCCCCC	40.27	26074081
488	Phosphorylation	GNGEGASTLQGEPRA CCCCCCCCCCCCCCC	23.67	26074081
497	Phosphorylation	QGEPRAPTPPSGTEV CCCCCCCCCCCCCEE	47.01	26074081
499	Phosphorylation	EPRAPTPPSGTEVTL CCCCCCCCCCCEEEE	48.12	-
500	Phosphorylation	PRAPTPPSGTEVTLA CCCCCCCCCCEEEEE	60.60	26074081
502	Phosphorylation	APTPPSGTEVTLAEV CCCCCCCCEEEEEEC	31.45	26074081
505	Phosphorylation	PPSGTEVTLAEVPLL CCCCCEEEEEECCCC	17.64	26074081
559	Phosphorylation	ESLAAPQTPTLPSAL CCCCCCCCCCCCHHH	19.72	26074081
561	Phosphorylation	LAAPQTPTLPSALEE CCCCCCCCCCHHHHH	55.47	26074081
564	Phosphorylation	PQTPTLPSALEELEQ CCCCCCCHHHHHHHH	48.90	26074081
566	Phosphorylation	TPTLPSALEELEQEQ CCCCCHHHHHHHHHC	6.53	17081983
591	Phosphorylation	ETTQKEGTQASEGYF CCCCCCCCCCCCCCC	23.27	28122231
594	Phosphorylation	QKEGTQASEGYFSQS CCCCCCCCCCCCCCC	23.03	30266825
597	Phosphorylation	GTQASEGYFSQSQEE CCCCCCCCCCCCHHH	8.94	30266825
599	Phosphorylation	QASEGYFSQSQEEEF CCCCCCCCCCHHHHH	22.04	30266825
601	Phosphorylation	SEGYFSQSQEEEFAQ CCCCCCCCHHHHHHH	38.06	30266825
603	Phosphorylation	GYFSQSQEEEFAQSE CCCCCCHHHHHHHHH	65.82	19664995
609	Phosphorylation	QEEEFAQSEELCAKA HHHHHHHHHHHHHCC	29.61	30266825
611	Phosphorylation	EEFAQSEELCAKAPP HHHHHHHHHHHCCCC	55.16	-
622	Phosphorylation	KAPPPVFYNKPPEID CCCCCCCCCCCCCCC	23.63	28796482
624	Phosphorylation	PPPVFYNKPPEIDIT CCCCCCCCCCCCCEE	51.04	15592455
631	Phosphorylation	KPPEIDITCWDADPV CCCCCCEEEECCCCC	12.09	28796482
632	Glutathionylation	PPEIDITCWDADPVP CCCCCEEEECCCCCC	2.94	22555962
646	Phosphorylation	PEEEEGFEGGD---- CHHHCCCCCCC----	73.46	32142685
647	Phosphorylation	EEEEGFEGGD----- HHHCCCCCCC-----	43.22	32142685

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
142	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
142	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
342	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
647	S	Phosphorylation	Kinase	ATM	Q13315	PSP

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TPM1_HUMAN	TPM1	physical	22939629
ZC3H4_HUMAN	ZC3H4	physical	22939629
TPM4_HUMAN	TPM4	physical	22939629
RLA0_HUMAN	RPLP0	physical	22939629
TXND5_HUMAN	TXNDC5	physical	22939629
FLNA_HUMAN	FLNA	physical	22939629
NU133_HUMAN	NUP133	physical	22939629
PLAK_HUMAN	JUP	physical	22939629
ECE1_HUMAN	ECE1	physical	22939629
SPTB2_HUMAN	SPTBN1	physical	22939629
SPTN1_HUMAN	SPTAN1	physical	22939629
HNRL1_HUMAN	HNRNPUL1	physical	22939629
MARCS_HUMAN	MARCKS	physical	22939629
ACTG_HUMAN	ACTG1	physical	26496610
ACTN4_HUMAN	ACTN4	physical	26496610
ACTN1_HUMAN	ACTN1	physical	26496610
AP2A1_HUMAN	AP2A1	physical	26496610
AP2A2_HUMAN	AP2A2	physical	26496610
AP2B1_HUMAN	AP2B1	physical	26496610
ANXA2_HUMAN	ANXA2	physical	26496610
VATA_HUMAN	ATP6V1A	physical	26496610
VAS1_HUMAN	ATP6AP1	physical	26496610
DYST_HUMAN	DST	physical	26496610
KCC2G_HUMAN	CAMK2G	physical	26496610
CAZA2_HUMAN	CAPZA2	physical	26496610
CAPZB_HUMAN	CAPZB	physical	26496610
CAV1_HUMAN	CAV1	physical	26496610
CD44_HUMAN	CD44	physical	26496610
CD59_HUMAN	CD59	physical	26496610
CDC42_HUMAN	CDC42	physical	26496610
COF1_HUMAN	CFL1	physical	26496610
COF2_HUMAN	CFL2	physical	26496610
AP2M1_HUMAN	AP2M1	physical	26496610
CLCA_HUMAN	CLTA	physical	26496610
CLCB_HUMAN	CLTB	physical	26496610
CLH1_HUMAN	CLTC	physical	26496610
CBPM_HUMAN	CPM	physical	26496610
DAB2_HUMAN	DAB2	physical	26496610
DSG2_HUMAN	DSG2	physical	26496610
SRC8_HUMAN	CTTN	physical	26496610
STOM_HUMAN	STOM	physical	26496610
EPS15_HUMAN	EPS15	physical	26496610
FLII_HUMAN	FLII	physical	26496610
FLNA_HUMAN	FLNA	physical	26496610
FLNB_HUMAN	FLNB	physical	26496610
FLOT2_HUMAN	FLOT2	physical	26496610
PUR2_HUMAN	GART	physical	26496610
GNAS3_HUMAN	GNAS	physical	26496610
GNAS2_HUMAN	GNAS	physical	26496610
ALEX_HUMAN	GNAS	physical	26496610
GNAS1_HUMAN	GNAS	physical	26496610
GBB2_HUMAN	GNB2	physical	26496610
GELS_HUMAN	GSN	physical	26496610
HS90B_HUMAN	HSP90AB1	physical	26496610
SYIC_HUMAN	IARS	physical	26496610
IP3KA_HUMAN	ITPKA	physical	26496610
PLAK_HUMAN	JUP	physical	26496610
LEG1_HUMAN	LGALS1	physical	26496610
ABLM1_HUMAN	ABLIM1	physical	26496610
LMO7_HUMAN	LMO7	physical	26496610
MYO1B_HUMAN	MYO1B	physical	26496610
MYO1C_HUMAN	MYO1C	physical	26496610
MYO1E_HUMAN	MYO1E	physical	26496610
MYO5A_HUMAN	MYO5A	physical	26496610
MYO5B_HUMAN	MYO5B	physical	26496610
MYO6_HUMAN	MYO6	physical	26496610
MYPT1_HUMAN	PPP1R12A	physical	26496610
NP1L1_HUMAN	NAP1L1	physical	26496610
NP1L4_HUMAN	NAP1L4	physical	26496610
MERL_HUMAN	NF2	physical	26496610
PALM_HUMAN	PALM	physical	26496610
P3C2A_HUMAN	PIK3C2A	physical	26496610
PP1A_HUMAN	PPP1CA	physical	26496610
PP1G_HUMAN	PPP1CC	physical	26496610
TWF1_HUMAN	TWF1	physical	26496610
RAB1A_HUMAN	RAB1A	physical	26496610
SDC4_HUMAN	SDC4	physical	26496610
SIPA1_HUMAN	SIPA1	physical	26496610
FSCN1_HUMAN	FSCN1	physical	26496610
SPTN1_HUMAN	SPTAN1	physical	26496610
SPTB2_HUMAN	SPTBN1	physical	26496610
SSFA2_HUMAN	SSFA2	physical	26496610
SVIL_HUMAN	SVIL	physical	26496610
TMOD1_HUMAN	TMOD1	physical	26496610
TPM1_HUMAN	TPM1	physical	26496610
COR2A_HUMAN	CORO2A	physical	26496610
YES_HUMAN	YES1	physical	26496610
LUZP1_HUMAN	LUZP1	physical	26496610
CLH2_HUMAN	CLTCL1	physical	26496610
PICAL_HUMAN	PICALM	physical	26496610
SRBS2_HUMAN	SORBS2	physical	26496610
NUMB_HUMAN	NUMB	physical	26496610
IQGA1_HUMAN	IQGAP1	physical	26496610
RAI3_HUMAN	GPRC5A	physical	26496610
LRRF1_HUMAN	LRRFIP1	physical	26496610
LRRF2_HUMAN	LRRFIP2	physical	26496610
XPR1_HUMAN	XPR1	physical	26496610
ABCG2_HUMAN	ABCG2	physical	26496610
HOME3_HUMAN	HOMER3	physical	26496610
HOME1_HUMAN	HOMER1	physical	26496610
EPN4_HUMAN	CLINT1	physical	26496610
RHGBA_HUMAN	ARHGAP11A	physical	26496610
SC16A_HUMAN	SEC16A	physical	26496610
WDR1_HUMAN	WDR1	physical	26496610
ARPC5_HUMAN	ARPC5	physical	26496610
ARPC4_HUMAN	ARPC4	physical	26496610
ARPC3_HUMAN	ARPC3	physical	26496610
ARC1B_HUMAN	ARPC1B	physical	26496610
ARP3_HUMAN	ACTR3	physical	26496610
ARP2_HUMAN	ACTR2	physical	26496610
ARPC2_HUMAN	ARPC2	physical	26496610
FLOT1_HUMAN	FLOT1	physical	26496610
BASP1_HUMAN	BASP1	physical	26496610
DCTN2_HUMAN	DCTN2	physical	26496610
ARC1A_HUMAN	ARPC1A	physical	26496610
ERLN1_HUMAN	ERLIN1	physical	26496610
AKAP2_HUMAN	AKAP2	physical	26496610
SYNPO_HUMAN	SYNPO	physical	26496610
RRAS2_HUMAN	RRAS2	physical	26496610
CE162_HUMAN	CEP162	physical	26496610
TAB2_HUMAN	TAB2	physical	26496610
MPRIP_HUMAN	MPRIP	physical	26496610
COBL_HUMAN	COBL	physical	26496610
CYTSA_HUMAN	SPECC1L	physical	26496610
COR1C_HUMAN	CORO1C	physical	26496610
ZDHC5_HUMAN	ZDHHC5	physical	26496610
PKHG3_HUMAN	PLEKHG3	physical	26496610
RAI14_HUMAN	RAI14	physical	26496610
TIM13_HUMAN	TIMM13	physical	26496610
UHRF1_HUMAN	UHRF1	physical	26496610
PACN3_HUMAN	PACSIN3	physical	26496610
TMOD3_HUMAN	TMOD3	physical	26496610
CAR10_HUMAN	CARD10	physical	26496610
LIMA1_HUMAN	LIMA1	physical	26496610
GTSE1_HUMAN	GTSE1	physical	26496610
CN166_HUMAN	C14orf166	physical	26496610
PALMD_HUMAN	PALMD	physical	26496610
BMP2K_HUMAN	BMP2K	physical	26496610
NEB1_HUMAN	PPP1R9A	physical	26496610
ERBIN_HUMAN	ERBB2IP	physical	26496610
MYO5C_HUMAN	MYO5C	physical	26496610
CING_HUMAN	CGN	physical	26496610
RHG21_HUMAN	ARHGAP21	physical	26496610
AFAP1_HUMAN	AFAP1	physical	26496610
INF2_HUMAN	INF2	physical	26496610
CYBR1_HUMAN	CYBRD1	physical	26496610
MYO19_HUMAN	MYO19	physical	26496610
ARP5L_HUMAN	ARPC5L	physical	26496610
BACD3_HUMAN	KCTD10	physical	26496610
DCTN5_HUMAN	DCTN5	physical	26496610
NEB2_HUMAN	PPP1R9B	physical	26496610
STON2_HUMAN	STON2	physical	26496610
DIXC1_HUMAN	DIXDC1	physical	26496610
SSH2_HUMAN	SSH2	physical	26496610
NEXN_HUMAN	NEXN	physical	26496610
CYTSB_HUMAN	SPECC1	physical	26496610
FCHO2_HUMAN	FCHO2	physical	26496610
MISP_HUMAN	MISP	physical	26496610
CHM4B_HUMAN	CHMP4B	physical	26496610
PPR18_HUMAN	PPP1R18	physical	26496610
CAVN1_HUMAN	PTRF	physical	26496610
TPRN_HUMAN	TPRN	physical	26496610
MY18A_HUMAN	MYO18A	physical	26496610
HOME2_HUMAN	HOMER2	physical	28514442
ACTA_HUMAN	ACTA2	physical	28514442
GELS_HUMAN	GSN	physical	28514442
ACTB_HUMAN	ACTB	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442
TMOD2_HUMAN	TMOD2	physical	28514442

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 DREB_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-142; THR-331; THR-335; SER-337; SER-339;THR-343; SER-345; THR-346 AND SER-601, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides."; Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.; Nat. Biotechnol. 21:566-569(2003). Cited for: PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.	12665801 [Abstract]
Phosphorylation
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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-142; THR-331; THR-335; SER-337; SER-339;THR-343; SER-345; THR-346 AND SER-601, AND MASS SPECTROMETRY.	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 SER-142; THR-331; THR-335;SER-337; SER-339 AND THR-346, 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-142 AND THR-335, ANDMASS SPECTROMETRY.	18220336 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142 AND SER-339, ANDMASS SPECTROMETRY.	18088087 [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-142, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142 AND THR-346, ANDMASS SPECTROMETRY.	17287340 [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-339, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND MASSSPECTROMETRY.	16094384 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-142, ANDMASS SPECTROMETRY.	15302935 [Abstract]
"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-331 AND THR-346, ANDMASS SPECTROMETRY.	19690332 [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-622, AND MASSSPECTROMETRY.	15592455 [Abstract]