dbPTM

ARHG6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ARHG6_HUMAN
UniProt AC	Q15052
Protein Name	Rho guanine nucleotide exchange factor 6
Gene Name	ARHGEF6
Organism	Homo sapiens (Human).
Sequence Length	776
Subcellular Localization	Cell projection, lamellipodium.
Protein Description	Acts as a RAC1 guanine nucleotide exchange factor (GEF)..
Protein Sequence	MNPEEQIVTWLISLGVLESPKKTICDPEEFLKSSLKNGVVLCKLINRLMPGSVEKFCLDPQTEADCINNINDFLKGCATLQVEIFDPDDLYSGVNFSKVLSTLLAVNKATEDQLSERPCGRSSSLSAANTSQTNPQGAVSSTVSGLQRQSKTVEMTENGSHQLIVKARFNFKQTNEDELSVCKGDIIYVTRVEEGGWWEGTLNGRTGWFPSNYVREIKSSERPLSPKAVKGFETAPLTKNYYTVVLQNILDTEKEYAKELQSLLVTYLRPLQSNNNLSTVEVTSLLGNFEEVCTFQQTLCQALEECSKFPENQHKVGGCLLSLMPHFKSMYLAYCANHPSAVNVLTQHSDELEQFMENQGASSPGILILTTNLSKPFMRLEKYVTLLQELERHMEDTHPDHQDILKAIVAFKTLMGQCQDLRKRKQLELQILSEPIQAWEGEDIKNLGNVIFMSQVMVQYGACEEKEERYLMLFSNVLIMLSASPRMSGFIYQGKIPIAGTVVTRLDEIEGNDCTFEITGNTVERIVVHCNNNQDFQEWLEQLNRLIRGPASCSSLSKTSSSSCSAHSSFSSTGQPRGPLEPPQIIKPWSLSCLRPAPPLRPSAALGYKERMSYILKESSKSPKTMKKFLHKRKTERKPSEEEYVIRKSTAALEEDAQILKVIEAYCTSANFQQGHGSSTRKDSIPQVLLPEEEKLIIEETRSNGQTIMEEKSLVDTVYALKDEVRELKQENKRMKQCLEEELKSRRDLEKLVRRLLKQTDECIRGESSSKTSILP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
19	Phosphorylation	ISLGVLESPKKTICD HHHCCCCCCCCCCCC	37.55	24719451
22	Ubiquitination	GVLESPKKTICDPEE CCCCCCCCCCCCHHH	46.65	-
32	Ubiquitination	CDPEEFLKSSLKNGV CCHHHHHHHHCCCCH	43.23	-
43	Ubiquitination	KNGVVLCKLINRLMP CCCHHHHHHHHHHCC	48.52	-
91	Phosphorylation	IFDPDDLYSGVNFSK ECCHHHCCCCCCHHH	15.46	22817900
101	Phosphorylation	VNFSKVLSTLLAVNK CCHHHHHHHHHHHCC	21.72	30576142
102	Phosphorylation	NFSKVLSTLLAVNKA CHHHHHHHHHHHCCC	22.94	26074081
108	Ubiquitination	STLLAVNKATEDQLS HHHHHHCCCCHHHHC	50.52	-
122	Phosphorylation	SERPCGRSSSLSAAN CCCCCCCCCCCCCCC	15.01	23401153
123	Phosphorylation	ERPCGRSSSLSAANT CCCCCCCCCCCCCCC	33.66	15570572
124	Phosphorylation	RPCGRSSSLSAANTS CCCCCCCCCCCCCCC	27.82	23911959
126	Phosphorylation	CGRSSSLSAANTSQT CCCCCCCCCCCCCCC	27.55	21082442
130	Phosphorylation	SSLSAANTSQTNPQG CCCCCCCCCCCCCCC	19.93	28450419
131	Phosphorylation	SLSAANTSQTNPQGA CCCCCCCCCCCCCCC	34.51	28450419
133	Phosphorylation	SAANTSQTNPQGAVS CCCCCCCCCCCCCHH	48.94	19690332
140	Phosphorylation	TNPQGAVSSTVSGLQ CCCCCCHHHHHHHHH	21.54	19690332
141	Phosphorylation	NPQGAVSSTVSGLQR CCCCCHHHHHHHHHH	26.65	28450419
142	Phosphorylation	PQGAVSSTVSGLQRQ CCCCHHHHHHHHHHC	15.93	19690332
144	Phosphorylation	GAVSSTVSGLQRQSK CCHHHHHHHHHHCCC	33.60	21082442
150	Phosphorylation	VSGLQRQSKTVEMTE HHHHHHCCCEEEECC	32.27	23401153
151	Ubiquitination	SGLQRQSKTVEMTEN HHHHHCCCEEEECCC	48.53	-
152	Phosphorylation	GLQRQSKTVEMTENG HHHHCCCEEEECCCC	27.26	28122231
166	Ubiquitination	GSHQLIVKARFNFKQ CCEEEEEEEEEEECC	27.18	-
188	Phosphorylation	VCKGDIIYVTRVEEG EECCCEEEEEEEEEC	8.97	29978859
190	Phosphorylation	KGDIIYVTRVEEGGW CCCEEEEEEEEECCE	16.42	29978859
201	Phosphorylation	EGGWWEGTLNGRTGW ECCEEEEEECCCCCE	12.92	24076635
219	Phosphorylation	NYVREIKSSERPLSP HHHHHHHCCCCCCCH	42.99	30266825
220	Phosphorylation	YVREIKSSERPLSPK HHHHHHCCCCCCCHH	32.40	26657352
225	Phosphorylation	KSSERPLSPKAVKGF HCCCCCCCHHHCCCC	27.34	23401153
227	Ubiquitination	SERPLSPKAVKGFET CCCCCCHHHCCCCCC	63.54	-
230	Ubiquitination	PLSPKAVKGFETAPL CCCHHHCCCCCCCCC	63.84	-
234	Phosphorylation	KAVKGFETAPLTKNY HHCCCCCCCCCCCCC	31.17	26074081
254	Ubiquitination	QNILDTEKEYAKELQ HHHHHCHHHHHHHHH	59.11	-
382	Ubiquitination	KPFMRLEKYVTLLQE CCHHHHHHHHHHHHH	50.00	-
406	Ubiquitination	PDHQDILKAIVAFKT CCHHHHHHHHHHHHH	36.08	-
412	Ubiquitination	LKAIVAFKTLMGQCQ HHHHHHHHHHHHHHH	30.89	-
454	Phosphorylation	LGNVIFMSQVMVQYG HHHEEHHEEEHHHHC	14.63	20068231
460	Phosphorylation	MSQVMVQYGACEEKE HEEEHHHHCCCCCHH	8.69	20068231
470	Phosphorylation	CEEKEERYLMLFSNV CCCHHHHHHHHHHCH	10.35	20068231
475	Phosphorylation	ERYLMLFSNVLIMLS HHHHHHHHCHHHHHC	23.28	24719451
482	Phosphorylation	SNVLIMLSASPRMSG HCHHHHHCCCCCCCC	14.88	20068231
484	Phosphorylation	VLIMLSASPRMSGFI HHHHHCCCCCCCCCE	15.06	20068231
488	Phosphorylation	LSASPRMSGFIYQGK HCCCCCCCCCEECCC	31.65	19664994
492	Phosphorylation	PRMSGFIYQGKIPIA CCCCCCEECCCCCCC	14.67	30266825
495	Ubiquitination	SGFIYQGKIPIAGTV CCCEECCCCCCCCEE	29.77	-
504	Phosphorylation	PIAGTVVTRLDEIEG CCCCEEEEEHHHCCC	22.60	-
552	Phosphorylation	RLIRGPASCSSLSKT HHHHCCCCCCCCCCC	20.05	26552605
554	Phosphorylation	IRGPASCSSLSKTSS HHCCCCCCCCCCCCC	31.64	26552605
555	Phosphorylation	RGPASCSSLSKTSSS HCCCCCCCCCCCCCC	40.78	26552605
557	Phosphorylation	PASCSSLSKTSSSSC CCCCCCCCCCCCCCC	35.52	26552605
558	Ubiquitination	ASCSSLSKTSSSSCS CCCCCCCCCCCCCCC	58.69	-
559	Phosphorylation	SCSSLSKTSSSSCSA CCCCCCCCCCCCCCC	30.39	28450419
560	Phosphorylation	CSSLSKTSSSSCSAH CCCCCCCCCCCCCCC	31.77	28450419
561	Phosphorylation	SSLSKTSSSSCSAHS CCCCCCCCCCCCCCC	31.35	28450419
562	Phosphorylation	SLSKTSSSSCSAHSS CCCCCCCCCCCCCCC	34.82	28450419
563	Phosphorylation	LSKTSSSSCSAHSSF CCCCCCCCCCCCCCC	17.65	28450419
565	Phosphorylation	KTSSSSCSAHSSFSS CCCCCCCCCCCCCCC	30.85	28450419
568	Phosphorylation	SSSCSAHSSFSSTGQ CCCCCCCCCCCCCCC	32.56	28450419
569	Phosphorylation	SSCSAHSSFSSTGQP CCCCCCCCCCCCCCC	21.20	28450419
571	Phosphorylation	CSAHSSFSSTGQPRG CCCCCCCCCCCCCCC	29.01	23312004
572	Phosphorylation	SAHSSFSSTGQPRGP CCCCCCCCCCCCCCC	34.25	27251275
573	Phosphorylation	AHSSFSSTGQPRGPL CCCCCCCCCCCCCCC	38.34	23312004
592	Phosphorylation	IIKPWSLSCLRPAPP CCCCCCCHHCCCCCC	12.94	18491316
608	Phosphorylation	RPSAALGYKERMSYI CCCHHCCHHHHHHHH	15.55	22210691
613	Phosphorylation	LGYKERMSYILKESS CCHHHHHHHHHHHCC	18.42	24275569
614	Phosphorylation	GYKERMSYILKESSK CHHHHHHHHHHHCCC	10.83	23312004
617	Ubiquitination	ERMSYILKESSKSPK HHHHHHHHHCCCCHH	46.09	-
619	Phosphorylation	MSYILKESSKSPKTM HHHHHHHCCCCHHHH	41.29	26074081
620	Phosphorylation	SYILKESSKSPKTMK HHHHHHCCCCHHHHH	37.94	26074081
622	Phosphorylation	ILKESSKSPKTMKKF HHHHCCCCHHHHHHH	33.31	26074081
625	Phosphorylation	ESSKSPKTMKKFLHK HCCCCHHHHHHHHHH	37.29	26074081
627	Acetylation	SKSPKTMKKFLHKRK CCCHHHHHHHHHHCC	45.68	30587013
635	Phosphorylation	KFLHKRKTERKPSEE HHHHHCCCCCCCCHH	45.09	26074081
638	Ubiquitination	HKRKTERKPSEEEYV HHCCCCCCCCHHHHH	46.81	-
640	Phosphorylation	RKTERKPSEEEYVIR CCCCCCCCHHHHHHH	61.75	22617229
644	Phosphorylation	RKPSEEEYVIRKSTA CCCCHHHHHHHHHHH	12.40	23927012
648	Ubiquitination	EEEYVIRKSTAALEE HHHHHHHHHHHHHHH	40.82	-
649	Phosphorylation	EEYVIRKSTAALEED HHHHHHHHHHHHHHH	17.27	29255136
650	Phosphorylation	EYVIRKSTAALEEDA HHHHHHHHHHHHHHH	20.98	30266825
661	Ubiquitination	EEDAQILKVIEAYCT HHHHHHHHHHHHHHH	42.68	-
666	Phosphorylation	ILKVIEAYCTSANFQ HHHHHHHHHHHCCCC	5.40	28796482
668	Phosphorylation	KVIEAYCTSANFQQG HHHHHHHHHCCCCCC	20.42	27080861
669	Phosphorylation	VIEAYCTSANFQQGH HHHHHHHHCCCCCCC	20.04	23882029
678	Phosphorylation	NFQQGHGSSTRKDSI CCCCCCCCCCCCCCC	23.90	29978859
679	Phosphorylation	FQQGHGSSTRKDSIP CCCCCCCCCCCCCCC	36.50	29978859
680	Phosphorylation	QQGHGSSTRKDSIPQ CCCCCCCCCCCCCCC	43.36	27080861
682	Ubiquitination	GHGSSTRKDSIPQVL CCCCCCCCCCCCCCC	56.78	-
684	Phosphorylation	GSSTRKDSIPQVLLP CCCCCCCCCCCCCCC	38.92	29255136
695	Ubiquitination	VLLPEEEKLIIEETR CCCCHHHHEEEEEHH	48.54	-
701	Phosphorylation	EKLIIEETRSNGQTI HHEEEEEHHHCCCEE	26.97	28450419
703	Phosphorylation	LIIEETRSNGQTIME EEEEEHHHCCCEEEE	53.37	19664995
712	Ubiquitination	GQTIMEEKSLVDTVY CCEEEEEHHHHHHHH	35.46	-
713	Phosphorylation	QTIMEEKSLVDTVYA CEEEEEHHHHHHHHH	36.58	28555341
717	Phosphorylation	EEKSLVDTVYALKDE EEHHHHHHHHHHHHH	14.13	29978859
719	Phosphorylation	KSLVDTVYALKDEVR HHHHHHHHHHHHHHH	14.33	29978859
722	Ubiquitination	VDTVYALKDEVRELK HHHHHHHHHHHHHHH	43.61	-
736	Ubiquitination	KQENKRMKQCLEEEL HHHHHHHHHHHHHHH	41.72	-
744	Acetylation	QCLEEELKSRRDLEK HHHHHHHHHHHHHHH	45.24	25953088
751	Acetylation	KSRRDLEKLVRRLLK HHHHHHHHHHHHHHH	60.63	19608861
758	Ubiquitination	KLVRRLLKQTDECIR HHHHHHHHHCCHHHC	56.60	-

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
225	S	Phosphorylation	Kinase	PRKCQ	Q04759	GPS
488	S	Phosphorylation	Kinase	PRKCQ	Q04759	GPS
684	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
684	S	Phosphorylation	Kinase	PRKG1	Q13976	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ARHG6_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 ARHG6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZN580_HUMAN	ZNF580	physical	21900206
PAK1_HUMAN	PAK1	physical	21900206
GIT1_HUMAN	GIT1	physical	21900206
GASP2_HUMAN	GPRASP2	physical	21900206
SH3G3_HUMAN	SH3GL3	physical	21900206
TM108_HUMAN	TMEM108	physical	21900206
PRKDC_HUMAN	PRKDC	physical	19918261
ARHG7_HUMAN	ARHGEF7	physical	15306850
ARHG6_HUMAN	ARHGEF6	physical	15306850
TGFR1_HUMAN	TGFBR1	physical	15761153
TGFR2_HUMAN	TGFBR2	physical	15761153
CBL_HUMAN	CBL	physical	26177020
GIT1_HUMAN	GIT1	physical	28514442
FBX28_HUMAN	FBXO28	physical	28514442
PAK1_HUMAN	PAK1	physical	28514442
PAK2_HUMAN	PAK2	physical	28514442
UBP7_HUMAN	USP7	physical	28514442
NHRF2_HUMAN	SLC9A3R2	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300436	Mental retardation, X-linked 46 (MRX46)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ARHG6_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-751, 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-126; SER-144; SER-150;TYR-188; SER-488; SER-640 AND SER-684, 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-488, 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-684, 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-488, AND MASSSPECTROMETRY.	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-488, AND MASSSPECTROMETRY.	18220336 [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 SER-488, AND MASSSPECTROMETRY.	16964243 [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-488, 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-225 AND SER-684, ANDMASS SPECTROMETRY.	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-488, AND MASSSPECTROMETRY.	15302935 [Abstract]