dbPTM

BIG1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BIG1_HUMAN
UniProt AC	Q9Y6D6
Protein Name	Brefeldin A-inhibited guanine nucleotide-exchange protein 1
Gene Name	ARFGEF1
Organism	Homo sapiens (Human).
Sequence Length	1849
Subcellular Localization	Cytoplasm. Cytoplasm, perinuclear region. Golgi apparatus. Golgi apparatus, trans-Golgi network. Nucleus. Nucleus, nucleolus. Nucleus matrix. Membrane. Translocates from cytoplasm to membranes and nucleus upon cAMP treatment.
Protein Description	Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturaion of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competetive RhoA binding. The function in the nucleus remains to be determined..
Protein Sequence	MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKAETEKQSPPHGEAKAGSSTLPPVKSKTNFIEADKYFLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGNAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVTSQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMEKERHRQHHHLLQSPVSHHEPESPQLRYLPPQTVDHISQEHEGDLDLHTNDVDKSLQDDTEPENGSDISSAENEQTEADQATAAETLSKNEVLYDGENHDCEEKPQDIVQNIVEEMVNIVVGDMGEGTTINASADGNIGTIEDGSDSENIQANGIPGTPISVAYTPSLPDDRLSVSSNDTQESGNSSGPSPGAKFSHILQKDAFLVFRSLCKLSMKPLSDGPPDPKSHELRSKILSLQLLLSILQNAGPIFRTNEMFINAIKQYLCVALSKNGVSSVPEVFELSLSIFLTLLSNFKTHLKMQIEVFFKEIFLYILETSTSSFDHKWMVIQTLTRICADAQSVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRGSQELGMSNVQELSLRKKGLECLVSILKCMVEWSKDQYVNPNSQTTLGQEKPSEQEMSEIKHPETINRYGSLNSLESTSSSGIGSYSTQMSGTDNPEQFEVLKQQKEIIEQGIDLFNKKPKRGIQYLQEQGMLGTTPEDIAQFLHQEERLDSTQVGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRMFLEGFRLPGEAQKIDRLMEKFAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSAIYNEIAGKKISMKETKELTIPTKSSKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHVQAPFTSATHLEHVRPMFKLAWTPFLAAFSVGLQDCDDTEVASLCLEGIRCAIRIACIFSIQLERDAYVQALARFTLLTVSSGITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKPRYISGTVRGREGSLTGTKDQAPDEFVGLGLVGGNVDWKQIASIQESIGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELLSTTHPRMFSLQKIVEISYYNMGRIRLQWSRIWEVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKRNRSPTIRDMVVRCIAQMVNSQAANIRSGWKNIFSVFHLAASDQDESIVELAFQTTGHIVTLVFEKHFPATIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRHCAKYVSDRPQAFKEYTSDDMNVAPEDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKTYGHTYEKHWWQDLFRIVFRIFDNMKLPEQQTEKAEWMTTTCNHALYAICDVFTQYLEVLSDVLLDDIFAQLYWCVQQDNEQLARSGTNCLENVVILNGEKFTLEIWDKTCNCTLDIFKTTIPHALLTWRPNSGETAPPPPSPVSEKPLDTISQKSVDIHDSIQPRSVDNRPQAPLVSASAVNEEVSKIKSTAKFPEQKLFAALLIKCVVQLELIQTIDNIVFFPATSKKEDAENLAAAQRDAVDFDVRVDTQDQGMYRFLTSQQLFKLLDCLLESHRFAKAFNSNNEQRTALWKAGFKGKSKPNLLKQETSSLACGLRILFRMYMDESRVSAWEEVQQRLLNVCSEALSYFLTLTSESHREAWTNLLLLFLTKVLKISDNRFKAHASFYYPLLCEIMQFDLIPELRAVLRRFFLRIGVVFQISQPPEQELGINKQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MYEGKKTKN ------CCCCHHHHC	44.70	26074081
7	Phosphorylation	-MYEGKKTKNMFLTR -CCCCHHHHCHHHHH	31.01	26074081
13	Phosphorylation	KTKNMFLTRALEKIL HHHCHHHHHHHHHHH	11.57	26074081
23	Ubiquitination	LEKILADKEVKKAHH HHHHHCCHHHHHHHH	59.82	-
48	Phosphorylation	LEEIKAETEKQSPPH HHHHHHHHHCCCCCC	54.03	23401153
52	Phosphorylation	KAETEKQSPPHGEAK HHHHHCCCCCCCCCC	52.01	25159151
63	Phosphorylation	GEAKAGSSTLPPVKS CCCCCCCCCCCCCCC	32.80	-
70	Phosphorylation	STLPPVKSKTNFIEA CCCCCCCCCCCCEEC	44.97	24719451
109	Phosphorylation	CLQKLIAYGHLTGNA HHHHHHHCCHHHCCC	9.70	-
234	Phosphorylation	QHHHLLQSPVSHHEP HHHHHHCCCCCCCCC	27.52	29255136
237	Phosphorylation	HLLQSPVSHHEPESP HHHCCCCCCCCCCCC	23.63	29255136
243	Phosphorylation	VSHHEPESPQLRYLP CCCCCCCCCCCCCCC	28.76	29255136
248	Phosphorylation	PESPQLRYLPPQTVD CCCCCCCCCCHHHHC	31.95	27642862
258	Phosphorylation	PQTVDHISQEHEGDL HHHHCCCHHHCCCCC	26.54	24719451
269	Phosphorylation	EGDLDLHTNDVDKSL CCCCCCCCCCCCHHH	40.17	-
275	Phosphorylation	HTNDVDKSLQDDTEP CCCCCCHHHCCCCCC	27.14	22199227
280	Phosphorylation	DKSLQDDTEPENGSD CHHHCCCCCCCCCCC	62.82	28450419
286	Phosphorylation	DTEPENGSDISSAEN CCCCCCCCCCCHHHH	43.27	30278072
289	Phosphorylation	PENGSDISSAENEQT CCCCCCCCHHHHHHC	28.61	30278072
290	Phosphorylation	ENGSDISSAENEQTE CCCCCCCHHHHHHCH	39.68	26657352
296	Phosphorylation	SSAENEQTEADQATA CHHHHHHCHHHHHHH	27.28	26657352
302	Phosphorylation	QTEADQATAAETLSK HCHHHHHHHHHHHCC	22.29	28450419
306	Phosphorylation	DQATAAETLSKNEVL HHHHHHHHHCCCCCE	31.44	27251275
308	Phosphorylation	ATAAETLSKNEVLYD HHHHHHHCCCCCEEC	40.63	22115753
378	Phosphorylation	QANGIPGTPISVAYT CCCCCCCCCEEEEEC	16.46	26657352
385	Phosphorylation	TPISVAYTPSLPDDR CCEEEEECCCCCCCC	9.18	26074081
387	Phosphorylation	ISVAYTPSLPDDRLS EEEEECCCCCCCCEE	44.74	26074081
394	Phosphorylation	SLPDDRLSVSSNDTQ CCCCCCEECCCCCCC	22.35	19664994
396	Phosphorylation	PDDRLSVSSNDTQES CCCCEECCCCCCCCC	21.76	23401153
397	Phosphorylation	DDRLSVSSNDTQESG CCCEECCCCCCCCCC	36.25	29255136
400	Phosphorylation	LSVSSNDTQESGNSS EECCCCCCCCCCCCC	38.19	29255136
403	Phosphorylation	SSNDTQESGNSSGPS CCCCCCCCCCCCCCC	33.19	23927012
406	Phosphorylation	DTQESGNSSGPSPGA CCCCCCCCCCCCCCC	39.95	23403867
407	Phosphorylation	TQESGNSSGPSPGAK CCCCCCCCCCCCCCC	59.74	25627689
410	Phosphorylation	SGNSSGPSPGAKFSH CCCCCCCCCCCCHHH	39.22	23927012
432	Acetylation	LVFRSLCKLSMKPLS HHHHHHHHHCCCCCC	49.22	7823421
452	Phosphorylation	PKSHELRSKILSLQL CCCHHHHHHHHHHHH	36.35	26546556
504	Phosphorylation	VPEVFELSLSIFLTL CHHHHHHHHHHHHHH	16.93	26074081
506	Phosphorylation	EVFELSLSIFLTLLS HHHHHHHHHHHHHHH	14.12	26074081
510	Phosphorylation	LSLSIFLTLLSNFKT HHHHHHHHHHHCHHH	18.20	26074081
513	Phosphorylation	SIFLTLLSNFKTHLK HHHHHHHHCHHHHHH	43.25	26074081
539	Phosphorylation	LYILETSTSSFDHKW HHHHHHCCCCCCCHH	35.49	20860994
540	Phosphorylation	YILETSTSSFDHKWM HHHHHCCCCCCCHHH	28.86	20860994
541	Phosphorylation	ILETSTSSFDHKWMV HHHHCCCCCCCHHHH	34.48	20860994
553	Phosphorylation	WMVIQTLTRICADAQ HHHHHHHHHHHCCCH	22.75	20860994
595	Phosphorylation	KIAQGRGSQELGMSN HHHCCCCCHHHCCCC	21.08	-
607	Phosphorylation	MSNVQELSLRKKGLE CCCHHHHHHHHHHHH	25.94	24719451
618	Phosphorylation	KGLECLVSILKCMVE HHHHHHHHHHHHHHH	14.84	24719451
631	Phosphorylation	VEWSKDQYVNPNSQT HHHCCCCCCCCCCCC	16.60	27642862
636	Phosphorylation	DQYVNPNSQTTLGQE CCCCCCCCCCCCCCC	30.11	23312004
638	Phosphorylation	YVNPNSQTTLGQEKP CCCCCCCCCCCCCCC	24.65	23312004
639	Phosphorylation	VNPNSQTTLGQEKPS CCCCCCCCCCCCCCC	22.66	23312004
646	Phosphorylation	TLGQEKPSEQEMSEI CCCCCCCCHHHHHHC	64.08	29255136
651	Phosphorylation	KPSEQEMSEIKHPET CCCHHHHHHCCCHHH	35.10	30001349
658	Phosphorylation	SEIKHPETINRYGSL HHCCCHHHHHCCCCC	28.18	30576142
662	Phosphorylation	HPETINRYGSLNSLE CHHHHHCCCCCCCCC	13.43	21082442
664	Phosphorylation	ETINRYGSLNSLEST HHHHCCCCCCCCCCC	18.55	21082442
667	Phosphorylation	NRYGSLNSLESTSSS HCCCCCCCCCCCCCC	38.51	23898821
670	Phosphorylation	GSLNSLESTSSSGIG CCCCCCCCCCCCCCC	38.59	28464451
671	Phosphorylation	SLNSLESTSSSGIGS CCCCCCCCCCCCCCC	24.21	19690332
672	Phosphorylation	LNSLESTSSSGIGSY CCCCCCCCCCCCCCC	31.61	28450419
673	Phosphorylation	NSLESTSSSGIGSYS CCCCCCCCCCCCCCC	32.45	28450419
674	Phosphorylation	SLESTSSSGIGSYST CCCCCCCCCCCCCCC	33.91	28450419
678	Phosphorylation	TSSSGIGSYSTQMSG CCCCCCCCCCCCCCC	17.62	28450419
679	Phosphorylation	SSSGIGSYSTQMSGT CCCCCCCCCCCCCCC	15.55	28450419
680	Phosphorylation	SSGIGSYSTQMSGTD CCCCCCCCCCCCCCC	17.54	28450419
681	Phosphorylation	SGIGSYSTQMSGTDN CCCCCCCCCCCCCCC	21.76	28450419
684	Phosphorylation	GSYSTQMSGTDNPEQ CCCCCCCCCCCCHHH	28.82	26657352
686	Phosphorylation	YSTQMSGTDNPEQFE CCCCCCCCCCHHHHH	25.87	28450419
757	Ubiquitination	EFLGDNDKFNKEVMY HHHCCCCCCCCHHHH	58.03	-
796	Ubiquitination	RLPGEAQKIDRLMEK CCCCHHHHHHHHHHH	54.33	-
849	Acetylation	QVKNKMTKEQYIKMN HHHCCCCHHHHHHHH	39.04	7363985
852	Phosphorylation	NKMTKEQYIKMNRGI CCCCHHHHHHHHCCC	12.00	-
863	Ubiquitination	NRGINDSKDLPEEYL HCCCCCCCCCCHHHH	67.17	-
869	Phosphorylation	SKDLPEEYLSAIYNE CCCCCHHHHHHHHHH	12.32	-
871	Phosphorylation	DLPEEYLSAIYNEIA CCCHHHHHHHHHHHC	16.24	-
874	Phosphorylation	EEYLSAIYNEIAGKK HHHHHHHHHHHCCCC	13.37	-
880	Ubiquitination	IYNEIAGKKISMKET HHHHHCCCCCCCCHH	37.60	-
883	Phosphorylation	EIAGKKISMKETKEL HHCCCCCCCCHHHCC	32.45	16467138
891	Phosphorylation	MKETKELTIPTKSSK CCHHHCCCCCCCCCC	26.46	22673903
894	Phosphorylation	TKELTIPTKSSKQNV HHCCCCCCCCCCCCC	39.44	30576142
896	Phosphorylation	ELTIPTKSSKQNVAS CCCCCCCCCCCCCCC	45.29	22673903
897	Phosphorylation	LTIPTKSSKQNVASE CCCCCCCCCCCCCCH	39.55	22673903
921	Phosphorylation	EMEQMAKTAKALMEA HHHHHHHHHHHHHHH	24.69	-
1062	Phosphorylation	ELAQLIGTGVKPRYI HHHHHHCCCCCCCEE	31.63	-
1068	Phosphorylation	GTGVKPRYISGTVRG CCCCCCCEEECEECC	14.15	-
1072	Phosphorylation	KPRYISGTVRGREGS CCCEEECEECCCCCC	10.55	-
1079	Phosphorylation	TVRGREGSLTGTKDQ EECCCCCCCCCCCCC	20.29	23401153
1081	Phosphorylation	RGREGSLTGTKDQAP CCCCCCCCCCCCCCC	44.49	23927012
1083	Phosphorylation	REGSLTGTKDQAPDE CCCCCCCCCCCCCCC	26.64	28450419
1130	Phosphorylation	VAVDRIFTGSTRLDG EEEEEEECCCCCCCC	28.05	24275569
1132	Phosphorylation	VDRIFTGSTRLDGNA EEEEECCCCCCCCCH	13.80	24275569
1133	Phosphorylation	DRIFTGSTRLDGNAI EEEECCCCCCCCCHH	36.27	24275569
1220	Ubiquitination	SLRQLSMKFLEKGEL HHHHHHHHHHHCCCC	43.34	-
1224	2-Hydroxyisobutyrylation	LSMKFLEKGELANFR HHHHHHHCCCCCCEE	60.89	-
1224	Ubiquitination	LSMKFLEKGELANFR HHHHHHHCCCCCCEE	60.89	21890473
1234	Ubiquitination	LANFRFQKDFLRPFE CCCEECCHHHHHHHH	47.97	-
1249	Phosphorylation	HIMKRNRSPTIRDMV HHHHHCCCHHHHHHH	29.91	24719451
1352	Ubiquitination	RLIRHCAKYVSDRPQ HHHHHHHHHHCCCCH	52.13	-
1415	Phosphorylation	MFEIMKTYGHTYEKH HHHHHHHHCCCCHHH	11.03	25599653
1418	Phosphorylation	IMKTYGHTYEKHWWQ HHHHHCCCCHHHHHH	29.07	25599653
1419	Phosphorylation	MKTYGHTYEKHWWQD HHHHCCCCHHHHHHH	19.80	25599653
1533	Phosphorylation	CTLDIFKTTIPHALL CEEEEHHHCCCCCCE	21.14	27080861
1534	Phosphorylation	TLDIFKTTIPHALLT EEEEHHHCCCCCCEE	32.85	27080861
1541	Phosphorylation	TIPHALLTWRPNSGE CCCCCCEEECCCCCC	21.93	29523821
1546	Phosphorylation	LLTWRPNSGETAPPP CEEECCCCCCCCCCC	40.46	26657352
1549	Phosphorylation	WRPNSGETAPPPPSP ECCCCCCCCCCCCCC	48.25	29523821
1555	Phosphorylation	ETAPPPPSPVSEKPL CCCCCCCCCCCCCCC	43.65	29255136
1558	Phosphorylation	PPPPSPVSEKPLDTI CCCCCCCCCCCCCCC	43.20	22115753
1564	Phosphorylation	VSEKPLDTISQKSVD CCCCCCCCCCCCCCC	30.15	29255136
1566	Phosphorylation	EKPLDTISQKSVDIH CCCCCCCCCCCCCCH	33.38	29255136
1569	Phosphorylation	LDTISQKSVDIHDSI CCCCCCCCCCCHHCC	19.86	29255136
1575	Phosphorylation	KSVDIHDSIQPRSVD CCCCCHHCCCCCCCC	14.68	23927012
1580	Phosphorylation	HDSIQPRSVDNRPQA HHCCCCCCCCCCCCC	40.27	25159151
1591	Phosphorylation	RPQAPLVSASAVNEE CCCCCCCCHHHCCHH	24.96	24850871
1593	Phosphorylation	QAPLVSASAVNEEVS CCCCCCHHHCCHHHH	25.83	21406692
1600	Phosphorylation	SAVNEEVSKIKSTAK HHCCHHHHHHHHCCC	31.76	24850871
1601	Ubiquitination	AVNEEVSKIKSTAKF HCCHHHHHHHHCCCC	60.37	-
1641	Phosphorylation	IVFFPATSKKEDAEN EEEEECCCCHHHHHH	43.78	-
1694	Ubiquitination	LESHRFAKAFNSNNE HHHHHHHHHHCCCHH	51.29	-
1704	Phosphorylation	NSNNEQRTALWKAGF CCCHHHHHHHHHCCC	26.29	-
1708	Acetylation	EQRTALWKAGFKGKS HHHHHHHHCCCCCCC	39.21	19608861
1708	Ubiquitination	EQRTALWKAGFKGKS HHHHHHHHCCCCCCC	39.21	19608861
1715	Phosphorylation	KAGFKGKSKPNLLKQ HCCCCCCCCCCHHHH	63.11	-
1721	Malonylation	KSKPNLLKQETSSLA CCCCCHHHHHHHHHH	49.61	26320211
1725	Phosphorylation	NLLKQETSSLACGLR CHHHHHHHHHHHHHH	23.70	24732914
1726	Phosphorylation	LLKQETSSLACGLRI HHHHHHHHHHHHHHH	27.66	24732914

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
883	S	Phosphorylation	Kinase	PRKACA	P17612	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BIG1_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 BIG1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KAP0_HUMAN	PRKAR1A	physical	12571360
BIG2_HUMAN	ARFGEF2	physical	10716990
RSP5_YEAST	RSP5	physical	18832381
NUCL_HUMAN	NCL	physical	18292223
FBRL_HUMAN	FBL	physical	18292223
NUP62_HUMAN	NUP62	physical	18292223
LA_HUMAN	SSB	physical	18292223
NUCL_HUMAN	NCL	physical	14973189
NUP62_HUMAN	NUP62	physical	14973189

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 BIG1_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-1708, AND MASS SPECTROMETRY.	19608861 [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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, 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 SER-1569, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-397 ANDSER-1569, AND MASS SPECTROMETRY.	18691976 [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-1569, AND MASSSPECTROMETRY.	17081983 [Abstract]