dbPTM

EXOC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EXOC1_HUMAN
UniProt AC	Q9NV70
Protein Name	Exocyst complex component 1
Gene Name	EXOC1
Organism	Homo sapiens (Human).
Sequence Length	894
Subcellular Localization	Midbody, Midbody ring . Cytoplasm . Cytoplasm, perinuclear region . Colocalizes with CNTRL/centriolin at the midbody ring.
Protein Description	Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.; (Microbial infection) Has an antiviral effect against flaviviruses by affecting viral RNA transcription and translation through the sequestration of elongation factor 1-alpha (EEF1A1). This results in decreased viral RNA synthesis and decreased viral protein translation..
Protein Sequence	MTAIKHALQRDIFTPNDERLLSIVNVCKAGKKKKNCFLCATVTTERPVQVKVVKVKKSDKGDFYKRQIAWALRDLAVVDAKDAIKENPEFDLHFEKIYKWVASSTAEKNAFISCIWKLNQRYLRKKIDFVNVSSQLLEESVPSGENQSVTGGDEEVVDEYQELNAREEQDIEIMMEGCEYAISNAEAFAEKLSRELQVLDGANIQSIMASEKQVNILMKLLDEALKEVDQIELKLSSYEEMLQSVKEQMDQISESNHLIHLSNTNNVKLLSEIEFLVNHMDLAKGHIKALQEGDLASSRGIEACTNAADALLQCMNVALRPGHDLLLAVKQQQQRFSDLRELFARRLASHLNNVFVQQGHDQSSTLAQHSVELTLPNHHPFHRDLLRYAKLMEWLKSTDYGKYEGLTKNYMDYLSRLYEREIKDFFEVAKIKMTGTTKESKKFATLPRKESAVKQETESLHGSSGKLTGSTSSLNKLSVQSSGNRRSQSSSLLDMGNMSASDLDVADRTKFDKIFEQVLSELEPLCLAEQDFISKFFKLQQHQSMPGTMAEAEDLDGGTLSRQHNCGTPLPVSSEKDMIRQMMIKIFRCIEPELNNLIALGDKIDSFNSLYMLVKMSHHVWTAQNVDPASFLSTTLGNVLVTVKRNFDKCISNQIRQMEEVKISKKSKVGILPFVAEFEEFAGLAESIFKNAERRGDLDKAYTKLIRGVFVNVEKVANESQKTPRDVVMMENFHHIFATLSRLKISCLEAEKKEAKQKYTDHLQSYVIYSLGQPLEKLNHFFEGVEARVAQGIREEEVSYQLAFNKQELRKVIKEYPGKEVKKGLDNLYKKVDKHLCEEENLLQVVWHSMQDEFIRQYKHFEGLIARCYPGSGVTMEFTIQDILDYCSSIAQSH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Acetylation	---MTAIKHALQRDI ---CCHHHHHHHCCC	21.99	19608861
5	Malonylation	---MTAIKHALQRDI ---CCHHHHHHHCCC	21.99	26320211
22	Phosphorylation	PNDERLLSIVNVCKA CCHHHHHHHHHHHHC	29.14	28122231
28	Acetylation	LSIVNVCKAGKKKKN HHHHHHHHCCCCCCC	56.76	25953088
28	Malonylation	LSIVNVCKAGKKKKN HHHHHHHHCCCCCCC	56.76	26320211
34	Malonylation	CKAGKKKKNCFLCAT HHCCCCCCCEEEEEE	68.76	26320211
41	Phosphorylation	KNCFLCATVTTERPV CCEEEEEEECCCCCE	19.86	20068231
43	Phosphorylation	CFLCATVTTERPVQV EEEEEEECCCCCEEE	20.70	20068231
44	Phosphorylation	FLCATVTTERPVQVK EEEEEECCCCCEEEE	26.17	20068231
85	Ubiquitination	VDAKDAIKENPEFDL ECHHHHHHHCCCCCC	53.83	-
117	Acetylation	AFISCIWKLNQRYLR HHHHHHHHHHHHHHH	20.04	25953088
160	Phosphorylation	DEEVVDEYQELNARE CHHHHHHHHHHCHHH	11.65	27642862
288 (in isoform 2)	Ubiquitination	-	37.05	21906983
288 (in isoform 1)	Ubiquitination	-	37.05	21906983
288	Malonylation	DLAKGHIKALQEGDL HHHHHHHHHHHHCCC	37.05	26320211
288	Ubiquitination	DLAKGHIKALQEGDL HHHHHHHHHHHHCCC	37.05	-
297	Phosphorylation	LQEGDLASSRGIEAC HHHCCCCHHHCHHHH	28.06	29255136
298	Phosphorylation	QEGDLASSRGIEACT HHCCCCHHHCHHHHH	28.99	29255136
337	Phosphorylation	KQQQQRFSDLRELFA HHHHHHHHHHHHHHH	37.61	24719451
397	Phosphorylation	KLMEWLKSTDYGKYE HHHHHHHCCCCCCCC	25.08	20068231
398	Phosphorylation	LMEWLKSTDYGKYEG HHHHHHCCCCCCCCC	31.49	20068231
400	Phosphorylation	EWLKSTDYGKYEGLT HHHHCCCCCCCCCCC	18.66	20068231
402	Ubiquitination	LKSTDYGKYEGLTKN HHCCCCCCCCCCCHH	33.62	-
441	Ubiquitination	TGTTKESKKFATLPR ECCCHHHHCCCCCCC	53.66	-
445	Phosphorylation	KESKKFATLPRKESA HHHHCCCCCCCCHHH	40.19	28348404
448 (in isoform 2)	Phosphorylation	-	59.49	30266825
449 (in isoform 2)	Phosphorylation	-	54.82	30266825
451	Phosphorylation	ATLPRKESAVKQETE CCCCCCHHHHHHHHH	41.20	29496963
453 (in isoform 2)	Phosphorylation	-	10.28	26434776
455 (in isoform 2)	Phosphorylation	-	57.13	25849741
456 (in isoform 2)	Phosphorylation	-	49.15	26434776
457 (in isoform 2)	Phosphorylation	-	28.51	25849741
457	Phosphorylation	ESAVKQETESLHGSS HHHHHHHHHHHCCCC	28.51	28985074
458 (in isoform 2)	Phosphorylation	-	51.02	25849741
459	Phosphorylation	AVKQETESLHGSSGK HHHHHHHHHCCCCCE	32.84	25849741
463	Phosphorylation	ETESLHGSSGKLTGS HHHHHCCCCCEECCC	25.77	25849741
464	Phosphorylation	TESLHGSSGKLTGST HHHHCCCCCEECCCC	44.53	25849741
468	Phosphorylation	HGSSGKLTGSTSSLN CCCCCEECCCCHHHC	32.35	30266825
470	Phosphorylation	SSGKLTGSTSSLNKL CCCEECCCCHHHCCE	21.63	29255136
471	Phosphorylation	SGKLTGSTSSLNKLS CCEECCCCHHHCCEE	24.55	29255136
472	Phosphorylation	GKLTGSTSSLNKLSV CEECCCCHHHCCEEE	34.23	29255136
473	Phosphorylation	KLTGSTSSLNKLSVQ EECCCCHHHCCEEEC	35.73	29255136
478	Phosphorylation	TSSLNKLSVQSSGNR CHHHCCEEECCCCCC	21.51	28152594
481	Phosphorylation	LNKLSVQSSGNRRSQ HCCEEECCCCCCCCC	37.75	30266825
482	Phosphorylation	NKLSVQSSGNRRSQS CCEEECCCCCCCCCC	24.01	30266825
487	Phosphorylation	QSSGNRRSQSSSLLD CCCCCCCCCCCCCHH	31.04	25159151
489	Phosphorylation	SGNRRSQSSSLLDMG CCCCCCCCCCCHHCC	24.12	23401153
490	Phosphorylation	GNRRSQSSSLLDMGN CCCCCCCCCCHHCCC	19.85	25159151
491	Phosphorylation	NRRSQSSSLLDMGNM CCCCCCCCCHHCCCC	37.89	25159151
499	Phosphorylation	LLDMGNMSASDLDVA CHHCCCCCHHHCCHH	28.72	30266825
501	Phosphorylation	DMGNMSASDLDVADR HCCCCCHHHCCHHCH	31.25	25159151
509	Phosphorylation	DLDVADRTKFDKIFE HCCHHCHHHHHHHHH	36.29	23403867
544	Phosphorylation	FKLQQHQSMPGTMAE HHHHHCCCCCCCCCE	25.48	29255136
548	Phosphorylation	QHQSMPGTMAEAEDL HCCCCCCCCCEEECC	13.82	29255136
559	Phosphorylation	AEDLDGGTLSRQHNC EECCCCCCCCCCCCC	27.39	29255136
561	Phosphorylation	DLDGGTLSRQHNCGT CCCCCCCCCCCCCCC	29.72	29255136
568	Phosphorylation	SRQHNCGTPLPVSSE CCCCCCCCCCCCCCH	24.69	26657352
609	Phosphorylation	DKIDSFNSLYMLVKM CHHHHHHHHHHHHHH	20.90	23663014
611	Phosphorylation	IDSFNSLYMLVKMSH HHHHHHHHHHHHHHC	6.55	23663014
635	Phosphorylation	PASFLSTTLGNVLVT HHHHHHHCCCCHHHE	29.32	24532841
642	Phosphorylation	TLGNVLVTVKRNFDK CCCCHHHEEECCHHH	19.02	24532841
649	Ubiquitination	TVKRNFDKCISNQIR EEECCHHHHHHHHHH	29.36	-
687	Phosphorylation	EFAGLAESIFKNAER HHHHHHHHHHHHHHH	27.93	24719451
700	Acetylation	ERRGDLDKAYTKLIR HHHCCHHHHHHHHHH	51.06	12432695
702	Phosphorylation	RGDLDKAYTKLIRGV HCCHHHHHHHHHHHH	15.33	22817900
703	Phosphorylation	GDLDKAYTKLIRGVF CCHHHHHHHHHHHHC	25.00	21955146
704	Acetylation	DLDKAYTKLIRGVFV CHHHHHHHHHHHHCC	29.28	25953088
704	Malonylation	DLDKAYTKLIRGVFV CHHHHHHHHHHHHCC	29.28	26320211
722	Acetylation	KVANESQKTPRDVVM HHCCCCCCCHHHEEH	70.54	25953088
769	Phosphorylation	HLQSYVIYSLGQPLE HHHHHHHHHCCCCHH	6.44	22817900
799	Phosphorylation	GIREEEVSYQLAFNK CCCHHHHHHHHHCCH	15.50	-
800	Phosphorylation	IREEEVSYQLAFNKQ CCHHHHHHHHHCCHH	16.84	28796482

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 EXOC1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EXOC1_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 EXOC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRIO_HUMAN	TRIO	physical	17043677
CDC5L_HUMAN	CDC5L	physical	17043677
DYST_HUMAN	DST	physical	17043677
LC7L2_HUMAN	LUC7L2	physical	17043677
EXOC4_HUMAN	EXOC4	physical	17043677
SYBU_HUMAN	SYBU	physical	17043677
SPTN1_HUMAN	SPTAN1	physical	17043677
SFR1_HUMAN	SFR1	physical	17043677
CCSE2_HUMAN	CCSER2	physical	17043677
CCD93_HUMAN	CCDC93	physical	17043677
GRDN_HUMAN	CCDC88A	physical	17043677
KDM1A_HUMAN	KDM1A	physical	17043677
NUF2_HUMAN	NUF2	physical	17043677
MACF1_HUMAN	MACF1	physical	17043677
SRGP2_HUMAN	SRGAP2	physical	17043677
GOGA4_HUMAN	GOLGA4	physical	17043677
3BP5_HUMAN	SH3BP5	physical	17043677
CE295_HUMAN	CEP295	physical	17043677
K1551_HUMAN	KIAA1551	physical	17043677
KIF5A_HUMAN	KIF5A	physical	17043677
TRIM9_HUMAN	TRIM9	physical	17043677
KANL1_HUMAN	KANSL1	physical	17043677
COL12_HUMAN	COLEC12	physical	17043677
EXOC4_HUMAN	EXOC4	physical	19889837
RUBIC_HUMAN	KIAA0226	physical	21241894
RBCC1_HUMAN	RB1CC1	physical	21241894
BAKOR_HUMAN	ATG14	physical	21241894
EXOC2_HUMAN	EXOC2	physical	26344197
EXOC3_HUMAN	EXOC3	physical	26344197
EXOC4_HUMAN	EXOC4	physical	26344197
NCK5L_HUMAN	NCKAP5L	physical	28514442
TUFT1_HUMAN	TUFT1	physical	28514442
GRAP1_HUMAN	GRIPAP1	physical	28514442
GOGA4_HUMAN	GOLGA4	physical	28514442
CLOCK_HUMAN	CLOCK	physical	28514442
EXOC2_HUMAN	EXOC2	physical	28514442
FKB15_HUMAN	FKBP15	physical	28514442
CAVN1_HUMAN	PTRF	physical	28514442
BL1S4_HUMAN	BLOC1S4	physical	28514442
EXOC4_HUMAN	EXOC4	physical	28514442
RABE2_HUMAN	RABEP2	physical	28514442
RBG10_HUMAN	RABGAP1L	physical	28514442
RBG1L_HUMAN	RABGAP1L	physical	28514442
NDC80_HUMAN	NDC80	physical	28514442
PF21A_HUMAN	PHF21A	physical	28514442
EXC6B_HUMAN	EXOC6B	physical	28514442
VPS53_HUMAN	VPS53	physical	28514442
RABX5_HUMAN	RABGEF1	physical	28514442
KIF5A_HUMAN	KIF5A	physical	28514442
CCDC6_HUMAN	CCDC6	physical	28514442
VPS50_HUMAN	CCDC132	physical	28514442
TRI32_HUMAN	TRIM32	physical	28514442
EXOC5_HUMAN	EXOC5	physical	28514442
KXDL1_HUMAN	KXD1	physical	28514442
GIT2_HUMAN	GIT2	physical	28514442
POTEE_HUMAN	POTEE	physical	28514442
ARHG7_HUMAN	ARHGEF7	physical	28514442
SNAPN_HUMAN	SNAPIN	physical	28514442
VPS51_HUMAN	VPS51	physical	28514442
BL1S2_HUMAN	BLOC1S2	physical	28514442
EXOC7_HUMAN	EXOC7	physical	28514442
UBP4_HUMAN	USP4	physical	28514442
THA11_HUMAN	THAP11	physical	28514442
JUN_HUMAN	JUN	physical	28514442
EIPR1_HUMAN	TSSC1	physical	28514442
CCHCR_HUMAN	CCHCR1	physical	28514442
SIKE1_HUMAN	SIKE1	physical	28514442
GIT1_HUMAN	GIT1	physical	28514442
NUF2_HUMAN	NUF2	physical	28514442
KINH_HUMAN	KIF5B	physical	28514442
RABE1_HUMAN	RABEP1	physical	28514442
TNIP1_HUMAN	TNIP1	physical	28514442
GOGA5_HUMAN	GOLGA5	physical	28514442
KIF5C_HUMAN	KIF5C	physical	28514442
STRN3_HUMAN	STRN3	physical	28514442
STRN_HUMAN	STRN	physical	28514442
PCNT_HUMAN	PCNT	physical	28514442
CC122_HUMAN	CCDC122	physical	28514442
ZWINT_HUMAN	ZWINT	physical	28514442
EXOC4_HUMAN	EXOC4	physical	27173435
EXOC5_HUMAN	EXOC5	physical	27173435
EIPR1_HUMAN	TSSC1	physical	27173435
TMED1_HUMAN	TMED1	physical	27173435
SNP29_HUMAN	SNAP29	physical	27173435
EXOC6_HUMAN	EXOC6	physical	27173435
EXOC7_HUMAN	EXOC7	physical	27173435
EXOC8_HUMAN	EXOC8	physical	27173435

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 EXOC1_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-5, 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-487 AND SER-501, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470 AND THR-471, ANDMASS SPECTROMETRY.	19369195 [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 THR-471 AND SER-473, ANDMASS 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-470 AND SER-473, ANDMASS SPECTROMETRY.	18669648 [Abstract]