dbPTM

EXOC4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EXOC4_HUMAN
UniProt AC	Q96A65
Protein Name	Exocyst complex component 4
Gene Name	EXOC4
Organism	Homo sapiens (Human).
Sequence Length	974
Subcellular Localization	Midbody, Midbody ring . Cell projection . Colocalizes with CNTRL/centriolin at the midbody ring (PubMed:16213214). Localizes at the leading edge of migrating cells (By similarity).
Protein Description	Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane..
Protein Sequence	MAAEAAGGKYRSTVSKSKDPSGLLISVIRTLSTSDDVEDRENEKGRLEEAYEKCDRDLDELIVQHYTELTTAIRTYQSITERITNSRNKIKQVKENLLSCKMLLHCKRDELRKLWIEGIEHKHVLNLLDEIENIKQVPQKLEQCMASKHYLSATDMLVSAVESLEGPLLQVEGLSDLRLELHSKKMNLHLVLIDELHRHLYIKSTSRVVQRNKEKGKISSLVKDASVPLIDVTNLPTPRKFLDTSHYSTAGSSSVREINLQDIKEDLELDPEENSTLFMGILIKGLAKLKKIPETVKAIIERLEQELKQIVKRSTTQVADSGYQRGENVTVENQPRLLLELLELLFDKFNAVAAAHSVVLGYLQDTVVTPLTQQEDIKLYDMADVWVKIQDVLQMLLTEYLDMKNTRTASEPSAQLSYASTGREFAAFFAKKKPQRPKNSLFKFESSSHAISMSAYLREQRRELYSRSGELQGGPDDNLIEGGGTKFVCKPGARNITVIFHPLLRFIQEIEHALGLGPAKQCPLREFLTVYIKNIFLNQVLAEINKEIEGVTKTSDPLKILANADTMKVLGVQRPLLQSTIIVEKTVQDLLNLMHDLSAYSDQFLNMVCVKLQEYKDTCTAAYRGIVQSEEKLVISASWAKDDDISRLLKSLPNWMNMAQPKQLRPKREEEEDFIRAAFGKESEVLIGNLGDKLIPPQDILRDVSDLKALANMHESLEWLASRTKSAFSNLSTSQMLSPAQDSHTNTDLPPVSEQIMQTLSELAKSFQDMADRCLLVLHLEVRVHCFHYLIPLAKEGNYAIVANVESMDYDPLVVKLNKDISAIEEAMSASLQQHKFQYIFEGLGHLISCILINGAQYFRRISESGIKKMCRNIFVLQQNLTNITMSREADLDFARQYYEMLYNTADELLNLVVDQGVKYTELEYIHALTLLHRSQTGVGELTTQNTRLQRLKEIICEQAAIKQATKDKKITTV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAEAAGGK ------CCCCCCCCC	17.63	22814378
9	Acetylation	AAEAAGGKYRSTVSK CCCCCCCCCCCCCCC	36.25	19608861
9	Ubiquitination	AAEAAGGKYRSTVSK CCCCCCCCCCCCCCC	36.25	19608861
10	Phosphorylation	AEAAGGKYRSTVSKS CCCCCCCCCCCCCCC	17.05	27259358
12	Phosphorylation	AAGGKYRSTVSKSKD CCCCCCCCCCCCCCC	30.03	26699800
13	Phosphorylation	AGGKYRSTVSKSKDP CCCCCCCCCCCCCCC	21.57	26699800
15	Phosphorylation	GKYRSTVSKSKDPSG CCCCCCCCCCCCCCC	31.16	26699800
17	Phosphorylation	YRSTVSKSKDPSGLL CCCCCCCCCCCCCCH	34.48	28464451
18	Acetylation	RSTVSKSKDPSGLLI CCCCCCCCCCCCCHH	76.91	26051181
18	Ubiquitination	RSTVSKSKDPSGLLI CCCCCCCCCCCCCHH	76.91	-
21	Phosphorylation	VSKSKDPSGLLISVI CCCCCCCCCCHHEHH	52.81	26699800
26	Phosphorylation	DPSGLLISVIRTLST CCCCCHHEHHHHCCC	16.09	20860994
30	Phosphorylation	LLISVIRTLSTSDDV CHHEHHHHCCCCCCC	17.59	27273156
32	Phosphorylation	ISVIRTLSTSDDVED HEHHHHCCCCCCCCH	25.83	23401153
33	Phosphorylation	SVIRTLSTSDDVEDR EHHHHCCCCCCCCHH	39.01	27273156
34	Phosphorylation	VIRTLSTSDDVEDRE HHHHCCCCCCCCHHH	28.56	27273156
40	Methylation	TSDDVEDRENEKGRL CCCCCCHHHHHCCHH	34.82	-
44	Ubiquitination	VEDRENEKGRLEEAY CCHHHHHCCHHHHHH	62.00	-
51	Phosphorylation	KGRLEEAYEKCDRDL CCHHHHHHHHCCCCH	21.14	28796482
53	Ubiquitination	RLEEAYEKCDRDLDE HHHHHHHHCCCCHHH	28.85	-
66	Phosphorylation	DELIVQHYTELTTAI HHHHHHHHHHHHHHH	5.70	27642862
75	Phosphorylation	ELTTAIRTYQSITER HHHHHHHHHHHHHHH	21.57	28796482
76	Phosphorylation	LTTAIRTYQSITERI HHHHHHHHHHHHHHH	7.16	28796482
94	Ubiquitination	RNKIKQVKENLLSCK HHHHHHHHHHHHHHH	38.09	-
101	Ubiquitination	KENLLSCKMLLHCKR HHHHHHHHHHHHCCH	29.25	-
113	Ubiquitination	CKRDELRKLWIEGIE CCHHHHHHHHHHCCC	61.88	-
122	Ubiquitination	WIEGIEHKHVLNLLD HHHCCCHHHHHHHHH	23.71	-
135	Ubiquitination	LDEIENIKQVPQKLE HHHHHHHHHHCHHHH	57.75	-
140	Ubiquitination	NIKQVPQKLEQCMAS HHHHHCHHHHHHHHC	48.17	-
175	Phosphorylation	LLQVEGLSDLRLELH EEEEECCCHHHHHHH	45.51	24719451
203	Ubiquitination	LHRHLYIKSTSRVVQ HHHHHHHCCCCHHHH	33.84	-
213	Acetylation	SRVVQRNKEKGKISS CHHHHHHHHCCCHHH	64.09	7265069
215	Acetylation	VVQRNKEKGKISSLV HHHHHHHCCCHHHHH	68.09	7265079
217	Acetylation	QRNKEKGKISSLVKD HHHHHCCCHHHHHCC	50.94	7265089
217	Ubiquitination	QRNKEKGKISSLVKD HHHHHCCCHHHHHCC	50.94	-
219	Phosphorylation	NKEKGKISSLVKDAS HHHCCCHHHHHCCCC	22.55	28464451
220	Phosphorylation	KEKGKISSLVKDASV HHCCCHHHHHCCCCC	40.43	28464451
223	Ubiquitination	GKISSLVKDASVPLI CCHHHHHCCCCCCEE	53.52	21890473
223	Ubiquitination	GKISSLVKDASVPLI CCHHHHHCCCCCCEE	53.52	21890473
226	Phosphorylation	SSLVKDASVPLIDVT HHHHCCCCCCEEECC	34.11	30266825
233	Phosphorylation	SVPLIDVTNLPTPRK CCCEEECCCCCCCCH	27.56	30266825
237	Phosphorylation	IDVTNLPTPRKFLDT EECCCCCCCCHHCCC	38.60	23401153
240	Ubiquitination	TNLPTPRKFLDTSHY CCCCCCCHHCCCCCC	52.03	21890473
240	Acetylation	TNLPTPRKFLDTSHY CCCCCCCHHCCCCCC	52.03	25953088
240	Ubiquitination	TNLPTPRKFLDTSHY CCCCCCCHHCCCCCC	52.03	21890473
244	Phosphorylation	TPRKFLDTSHYSTAG CCCHHCCCCCCCCCC	21.39	21945579
245	Phosphorylation	PRKFLDTSHYSTAGS CCHHCCCCCCCCCCC	21.79	21945579
247	Phosphorylation	KFLDTSHYSTAGSSS HHCCCCCCCCCCCCC	13.90	21945579
248	Phosphorylation	FLDTSHYSTAGSSSV HCCCCCCCCCCCCCC	13.32	21945579
249	Phosphorylation	LDTSHYSTAGSSSVR CCCCCCCCCCCCCCE	28.07	21945579
252	Phosphorylation	SHYSTAGSSSVREIN CCCCCCCCCCCEEEE	19.58	21945579
253	Phosphorylation	HYSTAGSSSVREINL CCCCCCCCCCEEEEH	31.75	21945579
254	Phosphorylation	YSTAGSSSVREINLQ CCCCCCCCCEEEEHH	27.22	21945579
315	Phosphorylation	KQIVKRSTTQVADSG HHHHHHHCCCCCCCC	25.86	23403867
316	Phosphorylation	QIVKRSTTQVADSGY HHHHHHCCCCCCCCC	23.46	23403867
323	Phosphorylation	TQVADSGYQRGENVT CCCCCCCCCCCCCCC	10.05	23403867
366	Phosphorylation	VLGYLQDTVVTPLTQ HHHHCCCCCCCCCCC	12.15	22798277
380	Phosphorylation	QQEDIKLYDMADVWV CHHHCCCCCHHHHHH	9.93	22817900
400	Phosphorylation	LQMLLTEYLDMKNTR HHHHHHHHHCCCCCC	11.63	22817900
406	Phosphorylation	EYLDMKNTRTASEPS HHHCCCCCCCCCCCC	24.71	-
408	Phosphorylation	LDMKNTRTASEPSAQ HCCCCCCCCCCCCHH	32.28	23186163
410	Phosphorylation	MKNTRTASEPSAQLS CCCCCCCCCCCHHCE	49.80	23186163
413	Phosphorylation	TRTASEPSAQLSYAS CCCCCCCCHHCEEHH	25.29	-
418	Phosphorylation	EPSAQLSYASTGREF CCCHHCEEHHCCHHH	17.11	27642862
432	Ubiquitination	FAAFFAKKKPQRPKN HHHHHHCCCCCCCCC	67.28	-
440	Phosphorylation	KPQRPKNSLFKFESS CCCCCCCCCEEEECC	41.11	24719451
446	Phosphorylation	NSLFKFESSSHAISM CCCEEEECCHHHHHH	40.03	25072903
447	Phosphorylation	SLFKFESSSHAISMS CCEEEECCHHHHHHH	20.95	25072903
448	Phosphorylation	LFKFESSSHAISMSA CEEEECCHHHHHHHH	26.64	28857561
452	Phosphorylation	ESSSHAISMSAYLRE ECCHHHHHHHHHHHH	13.89	25072903
454	Phosphorylation	SSHAISMSAYLREQR CHHHHHHHHHHHHHH	13.63	25072903
456	Phosphorylation	HAISMSAYLREQRRE HHHHHHHHHHHHHHH	10.05	20860994
465	Phosphorylation	REQRRELYSRSGELQ HHHHHHHHHHCCCCC	9.40	-
466	Phosphorylation	EQRRELYSRSGELQG HHHHHHHHHCCCCCC	32.37	24719451
468	Phosphorylation	RRELYSRSGELQGGP HHHHHHHCCCCCCCC	30.58	23927012
486	Ubiquitination	LIEGGGTKFVCKPGA CCCCCCCEEEECCCC	38.79	-
490	Ubiquitination	GGTKFVCKPGARNIT CCCEEEECCCCCCEE	40.98	-
554	Phosphorylation	EIEGVTKTSDPLKIL HCCCCCCCCCHHHHH	29.06	20068231
555	Phosphorylation	IEGVTKTSDPLKILA CCCCCCCCCHHHHHH	38.49	20068231
559	Ubiquitination	TKTSDPLKILANADT CCCCCHHHHHHCCCH	40.85	-
566	Phosphorylation	KILANADTMKVLGVQ HHHHCCCHHHHHCCC	19.24	20068231
568	2-Hydroxyisobutyrylation	LANADTMKVLGVQRP HHCCCHHHHHCCCCC	36.08	-
616	Ubiquitination	CVKLQEYKDTCTAAY HHHHHHHHHHCHHHH	45.89	-
623	Phosphorylation	KDTCTAAYRGIVQSE HHHCHHHHHCCCCCC	13.60	22817900
662	Ubiquitination	WMNMAQPKQLRPKRE HHHHCCCCCCCCCHH	50.30	-
667	Ubiquitination	QPKQLRPKREEEEDF CCCCCCCCHHHHHHH	67.04	-
681	Ubiquitination	FIRAAFGKESEVLIG HHHHHHCCCCEEEEE	52.17	-
693	Ubiquitination	LIGNLGDKLIPPQDI EEECCCCCCCCHHHH	46.66	-
705	Phosphorylation	QDILRDVSDLKALAN HHHHCCHHHHHHHHH	41.33	29759185
716	Phosphorylation	ALANMHESLEWLASR HHHHHHHHHHHHHHC	19.53	29759185
722	Phosphorylation	ESLEWLASRTKSAFS HHHHHHHHCCHHHHH	38.01	29759185
724	Phosphorylation	LEWLASRTKSAFSNL HHHHHHCCHHHHHCC	27.19	29759185
729	Phosphorylation	SRTKSAFSNLSTSQM HCCHHHHHCCCHHHC	36.26	30576142
732	Phosphorylation	KSAFSNLSTSQMLSP HHHHHCCCHHHCCCC	30.20	25627689
733	Phosphorylation	SAFSNLSTSQMLSPA HHHHCCCHHHCCCCC	26.58	30576142
734	Phosphorylation	AFSNLSTSQMLSPAQ HHHCCCHHHCCCCCC	15.37	25159151
738	Phosphorylation	LSTSQMLSPAQDSHT CCHHHCCCCCCCCCC	16.91	25159151
743	Phosphorylation	MLSPAQDSHTNTDLP CCCCCCCCCCCCCCC	21.82	25627689
745	Phosphorylation	SPAQDSHTNTDLPPV CCCCCCCCCCCCCCH	43.71	25627689
747	Phosphorylation	AQDSHTNTDLPPVSE CCCCCCCCCCCCHHH	39.82	24173317
799	Phosphorylation	PLAKEGNYAIVANVE HHHHCCCEEEEECCC	14.46	27642862
819	Ubiquitination	PLVVKLNKDISAIEE CEEEECCCCHHHHHH	67.86	-
822	Phosphorylation	VKLNKDISAIEEAMS EECCCCHHHHHHHHH	33.07	24173317
863	Phosphorylation	AQYFRRISESGIKKM HHHHHHHCHHHHHHH	24.73	22985185
868	2-Hydroxyisobutyrylation	RISESGIKKMCRNIF HHCHHHHHHHHHHHH	37.67	-
885	Phosphorylation	QQNLTNITMSREADL ECCCCCCCCCCHHCH	15.91	24719451
887	Phosphorylation	NLTNITMSREADLDF CCCCCCCCCHHCHHH	20.51	24719451
898	Phosphorylation	DLDFARQYYEMLYNT CHHHHHHHHHHHHHC	8.88	-
899	Phosphorylation	LDFARQYYEMLYNTA HHHHHHHHHHHHHCH	6.11	-
903	Phosphorylation	RQYYEMLYNTADELL HHHHHHHHHCHHHHH	14.79	-
935	Phosphorylation	ALTLLHRSQTGVGEL HHHHHHHHCCCCCCC	22.73	25072903
937	Phosphorylation	TLLHRSQTGVGELTT HHHHHHCCCCCCCCC	34.77	30242111
943	Phosphorylation	QTGVGELTTQNTRLQ CCCCCCCCCCCHHHH	23.25	27251275
953	Ubiquitination	NTRLQRLKEIICEQA CHHHHHHHHHHHHHH	49.40	-
963	Ubiquitination	ICEQAAIKQATKDKK HHHHHHHHHHHCCCC	29.20	-

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 EXOC4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EXOC4_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 EXOC4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DLG3_HUMAN	DLG3	physical	12738960
EXOC3_HUMAN	EXOC3	physical	12738960
DLG4_HUMAN	DLG4	physical	12738960
NMDE2_HUMAN	GRIN2B	physical	12738960
EXOC3_HUMAN	EXOC3	physical	12687004
EXOC7_HUMAN	EXOC7	physical	12687004
DLG4_HUMAN	DLG4	physical	12675619
EXOC7_HUMAN	EXOC7	physical	22939629
EXOC8_HUMAN	EXOC8	physical	22939629
EXOC5_HUMAN	EXOC5	physical	22939629
EXOC1_HUMAN	EXOC1	physical	19889837
EXOC3_HUMAN	EXOC3	physical	19889837
ATG5_HUMAN	ATG5	physical	21241894
ATG12_HUMAN	ATG12	physical	21241894
EXOC2_HUMAN	EXOC2	physical	21241894
EXOC7_HUMAN	EXOC7	physical	21241894
BECN1_HUMAN	BECN1	physical	21241894
EXOC6_HUMAN	EXOC6	physical	26344197
EXOC7_HUMAN	EXOC7	physical	26344197
MTMR4_HUMAN	MTMR4	physical	27432908
EXOC5_HUMAN	EXOC5	physical	27173435
EXOC8_HUMAN	EXOC8	physical	27173435
EIPR1_HUMAN	TSSC1	physical	27173435
SNP29_HUMAN	SNAP29	physical	27173435

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of EXOC4_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-9, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-226; THR-233 ANDTHR-237, AND MASS 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 THR-237, AND MASSSPECTROMETRY.	18669648 [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-237, AND MASSSPECTROMETRY.	16964243 [Abstract]