dbPTM

GBF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GBF1_HUMAN
UniProt AC	Q92538
Protein Name	Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
Gene Name	GBF1
Organism	Homo sapiens (Human).
Sequence Length	1859
Subcellular Localization	Golgi apparatus, cis-Golgi network . Endoplasmic reticulum-Golgi intermediate compartment . Golgi apparatus, trans-Golgi network . Cytoplasm . Lipid droplet . Membrane Peripheral membrane protein . Cycles rapidly on and off early Golgi membranes (Pu
Protein Description	Guanine-nucleotide exchange factor (GEF) for members of the Arf family of small GTPases involved in trafficking in the early secretory pathway; its GEF activity initiates the coating of nascent vesicles via the localized generation of activated ARFs through replacement of GDP with GTP. Recruitment to cis-Golgi membranes requires membrane association of Arf-GDP and can be regulated by ARF1, ARF3, ARF4 and ARF5. Involved in the recruitment of the COPI coat complex to the endoplasmic reticulum exit sites (ERES), and the endoplasmic reticulum-Golgi intermediate (ERGIC) and cis-Golgi compartments which implicates ARF1 activation. Involved in COPI vesicle-dependent retrograde transport from the ERGIC and cis-Golgi compartments to the endoplasmic reticulum (ER). [PubMed: 16926190]
Protein Sequence	MVDKNIYIIQGEINIVVGAIKRNARWSTHTPLDEERDPLLHSFGHLKEVLNSITELSEIEPNVFLRPFLEVIRSEDTTGPITGLALTSVNKFLSYALIDPTHEGTAEGMENMADAVTHARFVGTDPASDEVVLMKILQVLRTLLLTPVGAHLTNESVCEIMQSCFRICFEMRLSELLRKSAEHTLVDMVQLLFTRLPQFKEEPKNYVGTNMKKLKMRAGGMSDSSKWKKQKRSPRPPRHMTKVTPGSELPTPNGTTLSSNLTGGMPFIDVPTPISSASSEAASAVVSPSTDSGLEFSSQTTSKEDLTDLEQPGSPGYSTATEPGSSELGVPEQPDLQEGTHVEKSQSASVESIPEVLEECTSPADHSDSASVHDMDYVNPRGVRFTQSSQKEGTALVPYGLPCIRELFRFLISLTNPHDRHNSEVMIHMGLHLLTVALESAPVAQCQTLLGLIKDEMCRHLFQLLSIERLNLYAASLRVCFLLFESMREHLKFQMEMYIKKLMEIITVENPKMPYEMKEMALEAIVQLWRIPSFVTELYINYDCDYYCSNLFEELTKLLSKNAFPVSGQLYTTHLLSLDALLTVIDSTEAHCQAKVLNSLTQQEKKETARPSCEIVDGTREASNTERTASDGKAVGMASDIPGLHLPGGGRLPPEHGKSGCSDLEEAVDSGADKKFARKPPRFSCLLPDPRELIEIKNKKKLLITGTEQFNQKPKKGIQFLQEKGLLTIPMDNTEVAQWLRENPRLDKKMIGEFVSDRKNIDLLESFVSTFSFQGLRLDEALRLYLEAFRLPGEAPVIQRLLEAFTERWMNCNGSPFANSDACFSLAYAVIMLNTDQHNHNVRKQNAPMTLEEFRKNLKGVNGGKDFEQDILEDMYHAIKNEEIVMPEEQTGLVRENYVWNVLLHRGATPEGIFLRVPTASYDLDLFTMTWGPTIAALSYVFDKSLEETIIQKAISGFRKCAMISAHYGLSDVFDNLIISLCKFTALSSESIENLPSVFGSNPKAHIAAKTVFHLAHRHGDILREGWKNIMEAMLQLFRAQLLPKAMIEVEDFVDPNGKISLQREETPSNRGESTVLSFVSWLTLSGPEQSSVRGPSTENQEAKRVALECIKQCDPEKMITESKFLQLESLQELMKALVSVTPDEETYDEEDAAFCLEMLLRIVLENRDRVGCVWQTVRDHLYHLCVQAQDFCFLVERAVVGLLRLAIRLLRREEISAQVLLSLRILLLMKPSVLSRVSHQVAYGLHELLKTNAANIHSGDDWATLFTLLECIGSGVKPPAALQATARADAPDAGAQSDSELPSYHQNDVSLDRGYTSDSEVYTDHGRPGKIHRSATDADVVNSGWLVVGKDDVDNSKPGPSRPGPSPLINQYSLTVGLDLGPHDTKSLLKCVESLSFIVRDAAHITPDNFELCVKTLRIFVEASLNGGCKSQEKRGKSHKYDSKGNRFKKKSKEGSMLRRPRTSSQHASRGGQSDDDEDEGVPASYHTVSLQVSQDLLDLMHTLHTRAASIYSSWAEEQRHLETGGQKIEADSRTLWAHCWCPLLQGIACLCCDARRQVRMQALTYLQRALLVHDLQKLDALEWESCFNKVLFPLLTKLLENISPADVGGMEETRMRASTLLSKVFLQHLSPLLSLSTFAALWLTILDFMDKYMHAGSSDLLSEAIPESLKNMLLVMDTAEIFHSADARGGGPSALWEITWERIDCFLPHLRDELFKQTVIQDPMPMEPQGQKPLASAHLTSAAGDTRTPGHPPPPEIPSELGACDFEKPESPRAASSSSPGSPVASSPSRLSPTPDGPPPLAQPPLILQPLASPLQVGVPPMTLPIILNPALIEATSPVPLLATPRPTDPIPTSEVN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
74	Phosphorylation	PFLEVIRSEDTTGPI HHHHHHHCCCCCCCC	28.80	20068231
77	Phosphorylation	EVIRSEDTTGPITGL HHHHCCCCCCCCCCE	29.60	20068231
78	Phosphorylation	VIRSEDTTGPITGLA HHHCCCCCCCCCCEE	53.97	20068231
82	Phosphorylation	EDTTGPITGLALTSV CCCCCCCCCEEHHHH	29.31	20068231
87	Phosphorylation	PITGLALTSVNKFLS CCCCEEHHHHHHHHH	25.64	20068231
88	Phosphorylation	ITGLALTSVNKFLSY CCCEEHHHHHHHHHH	25.25	20068231
134	Sulfoxidation	ASDEVVLMKILQVLR CCCHHHHHHHHHHHH	1.39	21406390
174	Phosphorylation	ICFEMRLSELLRKSA HHHHHHHHHHHHHHH	18.81	28355574
200	Acetylation	FTRLPQFKEEPKNYV HHCCHHHCCCCCCCC	56.79	25953088
212	Ubiquitination	NYVGTNMKKLKMRAG CCCCCCHHHHHHHCC	57.96	21890473
222	Phosphorylation	KMRAGGMSDSSKWKK HHHCCCCCCHHHHHH	37.30	21406692
224	Phosphorylation	RAGGMSDSSKWKKQK HCCCCCCHHHHHHHC	26.89	23401153
225	Phosphorylation	AGGMSDSSKWKKQKR CCCCCCHHHHHHHCC	47.75	21406692
233	Phosphorylation	KWKKQKRSPRPPRHM HHHHHCCCCCCCCCC	32.09	30576142
283	O-linked_Glycosylation	SASSEAASAVVSPST CCCHHHHHHCCCCCC	28.75	32119511
292	Phosphorylation	VVSPSTDSGLEFSSQ CCCCCCCCCCCCCCC	45.42	-
297	Phosphorylation	TDSGLEFSSQTTSKE CCCCCCCCCCCCCHH	16.50	26074081
298	Phosphorylation	DSGLEFSSQTTSKED CCCCCCCCCCCCHHH	36.55	26074081
300	Phosphorylation	GLEFSSQTTSKEDLT CCCCCCCCCCHHHCC	34.68	26074081
301	Phosphorylation	LEFSSQTTSKEDLTD CCCCCCCCCHHHCCC	30.11	26074081
302	Phosphorylation	EFSSQTTSKEDLTDL CCCCCCCCHHHCCCC	37.12	26074081
307	Phosphorylation	TTSKEDLTDLEQPGS CCCHHHCCCCCCCCC	51.35	23663014
314	Phosphorylation	TDLEQPGSPGYSTAT CCCCCCCCCCCCCCC	23.10	25159151
317	Phosphorylation	EQPGSPGYSTATEPG CCCCCCCCCCCCCCC	13.26	25159151
318	Phosphorylation	QPGSPGYSTATEPGS CCCCCCCCCCCCCCC	19.92	23663014
319	Phosphorylation	PGSPGYSTATEPGSS CCCCCCCCCCCCCCC	29.16	23663014
321	Phosphorylation	SPGYSTATEPGSSEL CCCCCCCCCCCCCCC	42.68	23663014
325	Phosphorylation	STATEPGSSELGVPE CCCCCCCCCCCCCCC	31.21	23663014
326	Phosphorylation	TATEPGSSELGVPEQ CCCCCCCCCCCCCCC	42.63	23663014
340	Phosphorylation	QPDLQEGTHVEKSQS CCCCCCCCCCCHHCC	23.23	26074081
345	Phosphorylation	EGTHVEKSQSASVES CCCCCCHHCCCCCCC	18.83	23927012
347	Phosphorylation	THVEKSQSASVESIP CCCCHHCCCCCCCHH	29.60	23927012
349	Phosphorylation	VEKSQSASVESIPEV CCHHCCCCCCCHHHH	31.50	23927012
352	Phosphorylation	SQSASVESIPEVLEE HCCCCCCCHHHHHHH	41.09	23927012
361	Phosphorylation	PEVLEECTSPADHSD HHHHHHCCCCCCCCC	40.81	25159151
362	Phosphorylation	EVLEECTSPADHSDS HHHHHCCCCCCCCCC	29.74	23927012
367	Phosphorylation	CTSPADHSDSASVHD CCCCCCCCCCCCCCC	33.53	23927012
369	Phosphorylation	SPADHSDSASVHDMD CCCCCCCCCCCCCCC	26.00	23927012
371	Phosphorylation	ADHSDSASVHDMDYV CCCCCCCCCCCCCCC	24.76	23927012
377	Phosphorylation	ASVHDMDYVNPRGVR CCCCCCCCCCCCCCE	8.76	23927012
473	Phosphorylation	SIERLNLYAASLRVC CHHHHHHHHHHHHHH	10.07	-
476	Phosphorylation	RLNLYAASLRVCFLL HHHHHHHHHHHHHHH	14.45	-
486	Phosphorylation	VCFLLFESMREHLKF HHHHHHHHHHHHHHH	18.79	-
507	Phosphorylation	KKLMEIITVENPKMP HHHHHHHHCCCCCCC	27.68	21955146
515	Phosphorylation	VENPKMPYEMKEMAL CCCCCCCHHHHHHHH	25.75	-
599	Phosphorylation	CQAKVLNSLTQQEKK HHHHHHHHHCHHHHH	28.74	25159151
601	Phosphorylation	AKVLNSLTQQEKKET HHHHHHHCHHHHHHH	28.20	19691289
605	Ubiquitination	NSLTQQEKKETARPS HHHCHHHHHHHCCCC	52.12	-
606	Ubiquitination	SLTQQEKKETARPSC HHCHHHHHHHCCCCC	60.59	-
608	Phosphorylation	TQQEKKETARPSCEI CHHHHHHHCCCCCEE	36.52	23312004
612	Phosphorylation	KKETARPSCEIVDGT HHHHCCCCCEEECCC	20.87	27050516
619	Phosphorylation	SCEIVDGTREASNTE CCEEECCCCCCCCCE	22.37	23312004
637	Sulfoxidation	SDGKAVGMASDIPGL CCCCEEEECCCCCCC	2.31	30846556
659	Phosphorylation	LPPEHGKSGCSDLEE CCCCCCCCCCCCHHH	50.01	30266825
662	Phosphorylation	EHGKSGCSDLEEAVD CCCCCCCCCHHHHHH	49.07	25159151
663	Phosphorylation	HGKSGCSDLEEAVDS CCCCCCCCHHHHHHC	63.28	24719451
670	Phosphorylation	DLEEAVDSGADKKFA CHHHHHHCCCCHHHC	29.31	23403867
674	Ubiquitination	AVDSGADKKFARKPP HHHCCCCHHHCCCCC	49.62	-
684	Phosphorylation	ARKPPRFSCLLPDPR CCCCCCCCCCCCCHH	12.72	28555341
697	Ubiquitination	PRELIEIKNKKKLLI HHHHHHCCCCCEEEE	50.34	-
713	Acetylation	GTEQFNQKPKKGIQF CHHHHCCCCCCCCHH	60.97	25953088
713	Malonylation	GTEQFNQKPKKGIQF CHHHHCCCCCCCCHH	60.97	26320211
713	Ubiquitination	GTEQFNQKPKKGIQF CHHHHCCCCCCCCHH	60.97	-
715	Malonylation	EQFNQKPKKGIQFLQ HHHCCCCCCCCHHHH	71.33	26320211
715	Ubiquitination	EQFNQKPKKGIQFLQ HHHCCCCCCCCHHHH	71.33	-
716	Malonylation	QFNQKPKKGIQFLQE HHCCCCCCCCHHHHH	70.54	26320211
716	Ubiquitination	QFNQKPKKGIQFLQE HHCCCCCCCCHHHHH	70.54	-
731	Sulfoxidation	KGLLTIPMDNTEVAQ CCCEEECCCCHHHHH	5.69	30846556
750	Sulfoxidation	NPRLDKKMIGEFVSD CCCCCHHHHHHHHCC	6.15	21406390
756	Phosphorylation	KMIGEFVSDRKNIDL HHHHHHHCCCCCHHH	36.70	-
844	Ubiquitination	QHNHNVRKQNAPMTL CCCCCHHHCCCCCCH	43.55	-
859	Acetylation	EEFRKNLKGVNGGKD HHHHHHCCCCCCCCC	70.92	7935095
859	Ubiquitination	EEFRKNLKGVNGGKD HHHHHHCCCCCCCCC	70.92	-
865	Ubiquitination	LKGVNGGKDFEQDIL CCCCCCCCCHHHHHH	61.72	-
898	Phosphorylation	TGLVRENYVWNVLLH HCCCHHHHHHHHHHC	11.33	-
953	Ubiquitination	LEETIIQKAISGFRK HHHHHHHHHHHHHHH	36.96	21890473
953	Ubiquitination	LEETIIQKAISGFRK HHHHHHHHHHHHHHH	36.96	21890473
953	Ubiquitination	LEETIIQKAISGFRK HHHHHHHHHHHHHHH	36.96	21890473
965	Phosphorylation	FRKCAMISAHYGLSD HHHHHHHHHHCCCHH	8.91	22210691
971	Phosphorylation	ISAHYGLSDVFDNLI HHHHCCCHHHHHHHH	27.62	22210691
985	Phosphorylation	IISLCKFTALSSESI HHHHHHHHHCCHHHH	16.51	27050516
991	Phosphorylation	FTALSSESIENLPSV HHHCCHHHHHCCHHH	36.83	24719451
992	Phosphorylation	TALSSESIENLPSVF HHCCHHHHHCCHHHH	3.41	24719451
1004	Ubiquitination	SVFGSNPKAHIAAKT HHHCCCHHHHHHHHH	57.77	-
1059	Ubiquitination	DFVDPNGKISLQREE HHCCCCCCEEEEEEC	35.44	-
1061	Phosphorylation	VDPNGKISLQREETP CCCCCCEEEEEECCC	23.18	24719451
1062	Phosphorylation	DPNGKISLQREETPS CCCCCEEEEEECCCC	6.74	24719451
1112	Acetylation	RVALECIKQCDPEKM HHHHHHHHHCCHHHH	57.44	26051181
1112	Ubiquitination	RVALECIKQCDPEKM HHHHHHHHHCCHHHH	57.44	-
1124	Ubiquitination	EKMITESKFLQLESL HHHHCHHHHHCHHHH	43.81	-
1244	Phosphorylation	RVSHQVAYGLHELLK HHHHHHHHHHHHHHH	22.74	28152594
1298	Phosphorylation	APDAGAQSDSELPSY CCCCCCCCCCCCCCC	42.44	29255136
1299	Phosphorylation	PDAGAQSDSELPSYH CCCCCCCCCCCCCCC	33.77	24719451
1300	Phosphorylation	DAGAQSDSELPSYHQ CCCCCCCCCCCCCCC	46.40	29255136
1304	Phosphorylation	QSDSELPSYHQNDVS CCCCCCCCCCCCCCC	48.12	30278072
1305	Phosphorylation	SDSELPSYHQNDVSL CCCCCCCCCCCCCCC	12.89	30278072
1311	Phosphorylation	SYHQNDVSLDRGYTS CCCCCCCCCCCCCCC	27.67	30278072
1316	Phosphorylation	DVSLDRGYTSDSEVY CCCCCCCCCCCCCEE	12.17	30278072
1317	Phosphorylation	VSLDRGYTSDSEVYT CCCCCCCCCCCCEEC	28.96	22167270
1318	Phosphorylation	SLDRGYTSDSEVYTD CCCCCCCCCCCEECC	30.56	22167270
1319	Phosphorylation	LDRGYTSDSEVYTDH CCCCCCCCCCEECCC	40.80	24719451
1320	Phosphorylation	DRGYTSDSEVYTDHG CCCCCCCCCEECCCC	28.82	22167270
1323	Phosphorylation	YTSDSEVYTDHGRPG CCCCCCEECCCCCCC	11.46	22167270
1324	Phosphorylation	TSDSEVYTDHGRPGK CCCCCEECCCCCCCC	27.05	22167270
1335	Phosphorylation	RPGKIHRSATDADVV CCCCCCCCCCCCCCC	22.74	30266825
1337	Phosphorylation	GKIHRSATDADVVNS CCCCCCCCCCCCCCC	32.73	30266825
1338	Phosphorylation	KIHRSATDADVVNSG CCCCCCCCCCCCCCC	40.25	24719451
1344	Phosphorylation	TDADVVNSGWLVVGK CCCCCCCCCEEEEEC	21.53	30266825
1351	Ubiquitination	SGWLVVGKDDVDNSK CCEEEEECCCCCCCC	38.86	-
1357	Phosphorylation	GKDDVDNSKPGPSRP ECCCCCCCCCCCCCC	35.45	26074081
1362	Phosphorylation	DNSKPGPSRPGPSPL CCCCCCCCCCCCCCC	57.95	26074081
1367	Phosphorylation	GPSRPGPSPLINQYS CCCCCCCCCCCCEEE	37.95	22199227
1373	Phosphorylation	PSPLINQYSLTVGLD CCCCCCEEEEEEECC	10.93	26074081
1374	Phosphorylation	SPLINQYSLTVGLDL CCCCCEEEEEEECCC	14.06	25159151
1388	Phosphorylation	LGPHDTKSLLKCVES CCCCCHHHHHHHHHH	40.81	24719451
1416	Ubiquitination	DNFELCVKTLRIFVE CCHHHHHHHHHHHHH	40.62	-
1444	Phosphorylation	GKSHKYDSKGNRFKK CCCCCCCCCCCCCCC	39.10	28258704
1453	Phosphorylation	GNRFKKKSKEGSMLR CCCCCCCCCCCCCCC	44.83	27251275
1454	Acetylation	NRFKKKSKEGSMLRR CCCCCCCCCCCCCCC	74.99	7824197
1457	Phosphorylation	KKKSKEGSMLRRPRT CCCCCCCCCCCCCCC	18.74	28857561
1458	Phosphorylation	KKSKEGSMLRRPRTS CCCCCCCCCCCCCCC	5.05	24719451
1464	Phosphorylation	SMLRRPRTSSQHASR CCCCCCCCCCCCHHC	35.10	23312004
1465	Phosphorylation	MLRRPRTSSQHASRG CCCCCCCCCCCHHCC	29.31	23312004
1466	Phosphorylation	LRRPRTSSQHASRGG CCCCCCCCCCHHCCC	25.93	23312004
1475	Phosphorylation	HASRGGQSDDDEDEG CHHCCCCCCCCCCCC	46.40	22617229
1475 (in isoform 3)	Phosphorylation	-	46.40	22777824
1476	Phosphorylation	ASRGGQSDDDEDEGV HHCCCCCCCCCCCCC	60.54	24719451
1476 (in isoform 2)	Phosphorylation	-	60.54	22777824
1486	Phosphorylation	EDEGVPASYHTVSLQ CCCCCCCCCEEEEEE	16.04	27251275
1486 (in isoform 3)	Phosphorylation	-	16.04	26330541
1487	Phosphorylation	DEGVPASYHTVSLQV CCCCCCCCEEEEEEE	12.01	27251275
1487 (in isoform 2)	Phosphorylation	-	12.01	26330541
1487 (in isoform 3)	Phosphorylation	-	12.01	26330541
1488 (in isoform 2)	Phosphorylation	-	19.80	26330541
1489	Phosphorylation	GVPASYHTVSLQVSQ CCCCCCEEEEEEECH	11.98	27251275
1489 (in isoform 3)	Phosphorylation	-	11.98	26330541
1490 (in isoform 2)	Phosphorylation	-	3.24	26330541
1491	Phosphorylation	PASYHTVSLQVSQDL CCCCEEEEEEECHHH	17.78	28464451
1495	Phosphorylation	HTVSLQVSQDLLDLM EEEEEEECHHHHHHH	12.67	27251275
1529	Ubiquitination	HLETGGQKIEADSRT HHHHCCCCCCCCHHH	45.87	21890473
1567	Phosphorylation	VRMQALTYLQRALLV HHHHHHHHHHHHHHH	11.16	-
1579	Ubiquitination	LLVHDLQKLDALEWE HHHHCHHHCCCCCHH	56.48	-
1587	Phosphorylation	LDALEWESCFNKVLF CCCCCHHHHHHHHHH	25.69	20068231
1591	Ubiquitination	EWESCFNKVLFPLLT CHHHHHHHHHHHHHH	21.77	2190698
1598	Phosphorylation	KVLFPLLTKLLENIS HHHHHHHHHHHHCCC	27.59	20068231
1605	Phosphorylation	TKLLENISPADVGGM HHHHHCCCHHHCCCH	26.14	20068231
1615	Phosphorylation	DVGGMEETRMRASTL HCCCHHHHHHHHHHH	19.23	20068231
1624	Phosphorylation	MRASTLLSKVFLQHL HHHHHHHHHHHHHHH	29.86	24719451
1654	Phosphorylation	ILDFMDKYMHAGSSD HHHHHHHHHCCCCHH	7.00	29759185
1680	Phosphorylation	NMLLVMDTAEIFHSA HCHHHEEHHHHHHCC	14.22	-
1686	Phosphorylation	DTAEIFHSADARGGG EHHHHHHCCCCCCCC	19.66	-
1718	Ubiquitination	HLRDELFKQTVIQDP HHHHHHHHHCCCCCC	58.65	-
1750	Phosphorylation	SAAGDTRTPGHPPPP CCCCCCCCCCCCCCC	35.40	23927012
1761	Phosphorylation	PPPPEIPSELGACDF CCCCCCCCCCCCCCC	51.63	30266825
1770	Acetylation	LGACDFEKPESPRAA CCCCCCCCCCCCCCC	54.82	26051181
1770	Phosphorylation	LGACDFEKPESPRAA CCCCCCCCCCCCCCC	54.82	24719451
1773	Phosphorylation	CDFEKPESPRAASSS CCCCCCCCCCCCCCC	28.36	29255136
1776	Phosphorylation	EKPESPRAASSSSPG CCCCCCCCCCCCCCC	18.32	24719451
1778	Phosphorylation	PESPRAASSSSPGSP CCCCCCCCCCCCCCC	29.75	30266825
1779	Phosphorylation	ESPRAASSSSPGSPV CCCCCCCCCCCCCCC	30.06	29255136
1780	Phosphorylation	SPRAASSSSPGSPVA CCCCCCCCCCCCCCC	37.75	29255136
1781	Phosphorylation	PRAASSSSPGSPVAS CCCCCCCCCCCCCCC	34.92	29255136
1784	Phosphorylation	ASSSSPGSPVASSPS CCCCCCCCCCCCCCC	21.42	29255136
1785	Phosphorylation	SSSSPGSPVASSPSR CCCCCCCCCCCCCCC	31.44	24719451
1786	Phosphorylation	SSSPGSPVASSPSRL CCCCCCCCCCCCCCC	9.63	24719451
1788	Phosphorylation	SPGSPVASSPSRLSP CCCCCCCCCCCCCCC	42.91	30266825
1789	Phosphorylation	PGSPVASSPSRLSPT CCCCCCCCCCCCCCC	19.70	30266825
1791	Phosphorylation	SPVASSPSRLSPTPD CCCCCCCCCCCCCCC	48.04	30278072
1794	Phosphorylation	ASSPSRLSPTPDGPP CCCCCCCCCCCCCCC	26.14	26074081
1796	Phosphorylation	SPSRLSPTPDGPPPL CCCCCCCCCCCCCCC	30.54	26074081
1838	Phosphorylation	NPALIEATSPVPLLA CHHHHHCCCCCCCCC	22.30	26074081
1839	Phosphorylation	PALIEATSPVPLLAT HHHHHCCCCCCCCCC	30.83	26074081

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
174	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
292	S	Phosphorylation	Kinase	CK2A1	P68400	PSP
297	S	Phosphorylation	Kinase	CK2A1	P68400	PSP
1337	T	Phosphorylation	Kinase	AMPK	Q9Y478	Uniprot
1337	T	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
1337	T	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
1337	T	Phosphorylation		18063581
AMPK-mediated phosphorylation at Thr-1337 is induced by 2-deoxyglucose (2-DG) and AICA ribonucleotide, and occurs during mitosis leading to membrane disassociation and inactivation of ARF1 during mitosis.

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 GBF1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
COPG1_BOVIN	COPG1	physical	19039328
COPG1_HUMAN	COPG1	physical	19039328
PLPL2_HUMAN	PNPLA2	physical	21789191
BIRC6_HUMAN	BIRC6	physical	22863883
EP15R_HUMAN	EPS15L1	physical	22863883
CCAR2_HUMAN	CCAR2	physical	22863883
CND2_HUMAN	NCAPH	physical	22863883
RABL6_HUMAN	RABL6	physical	22863883
PUS7_HUMAN	PUS7	physical	26344197
RBM26_HUMAN	RBM26	physical	26344197
SYVC_HUMAN	VARS	physical	26344197

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 GBF1_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 SER-1298; TYR-1316;SER-1335; SER-1475; SER-1773 AND SER-1784, AND MASS 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-1298, AND MASSSPECTROMETRY.	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 SER-1781; SER-1784; SER-1788AND SER-1789, 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-662 AND SER-1298, ANDMASS SPECTROMETRY.	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-599 AND SER-1318, ANDMASS SPECTROMETRY.	18691976 [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 THR-507 AND SER-1318, ANDMASS SPECTROMETRY.	18088087 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1773, AND MASSSPECTROMETRY.	16565220 [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-1784, AND MASSSPECTROMETRY.	15302935 [Abstract]

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