dbPTM

DOCK1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DOCK1_HUMAN
UniProt AC	Q14185
Protein Name	Dedicator of cytokinesis protein 1
Gene Name	DOCK1
Organism	Homo sapiens (Human).
Sequence Length	1865
Subcellular Localization	Cytoplasm . Membrane . Recruited to membranes via its interaction with phosphatidylinositol 3,4,5-trisphosphate.
Protein Description	Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Along with DOCK1, mediates CRK/CRKL regulation of epithelial and endothelial cell spreading and migration on type IV collagen. [PubMed: 19004829 Functions as a guanine nucleotide exchange factor (GEF), which activates Rac Rho small GTPases by exchanging bound GDP for free GTP. Its GEF activity may be enhanced by ELMO1]
Protein Sequence	MTRWVPTKREEKYGVAFYNYDARGADELSLQIGDTVHILETYEGWYRGYTLRKKSKKGIFPASYIHLKEAIVEGKGQHETVIPGDLPLIQEVTTTLREWSTIWRQLYVQDNREMFRSVRHMIYDLIEWRSQILSGTLPQDELKELKKKVTAKIDYGNRILDLDLVVRDEDGNILDPELTSTISLFRAHEIASKQVEERLQEEKSQKQNIDINRQAKFAATPSLALFVNLKNVVCKIGEDAEVLMSLYDPVESKFISENYLVRWSSSGLPKDIDRLHNLRAVFTDLGSKDLKREKISFVCQIVRVGRMELRDNNTRKLTSGLRRPFGVAVMDVTDIINGKVDDEDKQHFIPFQPVAGENDFLQTVINKVIAAKEVNHKGQGLWVTLKLLPGDIHQIRKEFPHLVDRTTAVARKTGFPEIIMPGDVRNDIYVTLVQGDFDKGSKTTAKNVEVTVSVYDEDGKRLEHVIFPGAGDEAISEYKSVIYYQVKQPRWFETVKVAIPIEDVNRSHLRFTFRHRSSQDSKDKSEKIFALAFVKLMRYDGTTLRDGEHDLIVYKAEAKKLEDAATYLSLPSTKAELEEKGHSATGKSMQSLGSCTISKDSFQISTLVCSTKLTQNVDLLGLLKWRSNTSLLQQNLRQLMKVDGGEVVKFLQDTLDALFNIMMENSESETFDTLVFDALVFIIGLIADRKFQHFNPVLETYIKKHFSATLAYTKLTKVLKNYVDGAEKPGVNEQLYKAMKALESIFKFIVRSRILFNQLYENKGEADFVESLLQLFRSINDMMSSMSDQTVRVKGAALKYLPTIVNDVKLVFDPKELSKMFTEFILNVPMGLLTIQKLYCLIEIVHSDLFTQHDCREILLPMMTDQLKYHLERQEDLEACCQLLSHILEVLYRKDVGPTQRHVQIIMEKLLRTVNRTVISMGRDSELIGNFVACMTAILRQMEDYHYAHLIKTFGKMRTDVVDFLMETFIMFKNLIGKNVYPFDWVIMNMVQNKVFLRAINQYADMLNKKFLDQANFELQLWNNYFHLAVAFLTQESLQLENFSSAKRAKILNKYGDMRRQIGFEIRDMWYNLGQHKIKFIPEMVGPILEMTLIPETELRKATIPIFFDMMQCEFHSTRSFQMFENEIITKLDHEVEGGRGDEQYKVLFDKILLEHCRKHKYLAKTGETFVKLVVRLMERLLDYRTIMHDENKENRMSCTVNVLNFYKEIEREEMYIRYLYKLCDLHKECDNYTEAAYTLLLHAKLLKWSEDVCVAHLTQRDGYQATTQGQLKEQLYQEIIHYFDKGKMWEEAIALGKELAEQYENEMFDYEQLSELLKKQAQFYENIVKVIRPKPDYFAVGYYGQGFPTFLRGKVFIYRGKEYERREDFEARLLTQFPNAEKMKTTSPPGDDIKNSPGQYIQCFTVKPKLDLPPKFHRPVSEQIVSFYRVNEVQRFEYSRPIRKGEKNPDNEFANMWIERTIYTTAYKLPGILRWFEVKSVFMVEISPLENAIETMQLTNDKINSMVQQHLDDPSLPINPLSMLLNGIVDPAVMGGFANYEKAFFTDRYLQEHPEAHEKIEKLKDLIAWQIPFLAEGIRIHGDKVTEALRPFHERMEACFKQLKEKVEKEYGVRIMPSSLDDRRGSRPRSMVRSFTMPSSSRPLSVASVSSLSSDSTPSRPGSDGFALEPLLPKKMHSRSQDKLDKDDLEKEKKDKKKEKRNSKHQEIFEKEFKPTDISLQQSEAVILSETISPLRPQRPKSQVMNVIGSERRFSVSPSSPSSQQTPPPVTPRAKLSFSMQSSLELNGMTGADVADVPPPLPLKGSVADYGNLMENQDLLGSPTPPPPPPHQRHLPPPLPSKTPPPPPPKTTRKQASVDSGIVQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
18	Phosphorylation	EKYGVAFYNYDARGA HHCEEEEEEECCCCC	11.77	27642862
50	Phosphorylation	EGWYRGYTLRKKSKK CCHHCCCCCCCCCCC	23.94	24719451
100	Phosphorylation	TTTLREWSTIWRQLY HHHHHHHHHHHHHHH	12.78	-
101	Phosphorylation	TTLREWSTIWRQLYV HHHHHHHHHHHHHHC	26.15	-
107	Phosphorylation	STIWRQLYVQDNREM HHHHHHHHCCCCHHH	6.42	-
150	Phosphorylation	KELKKKVTAKIDYGN HHHHHHHEEEECCCC	30.98	-
152	Ubiquitination	LKKKVTAKIDYGNRI HHHHHEEEECCCCCE	27.09	-
155	Phosphorylation	KVTAKIDYGNRILDL HHEEEECCCCCEEEE	21.55	-
179	Phosphorylation	NILDPELTSTISLFR CCCCHHHHHHHHHHH	23.35	27135362
180	Phosphorylation	ILDPELTSTISLFRA CCCHHHHHHHHHHHH	36.05	27135362
181	Phosphorylation	LDPELTSTISLFRAH CCHHHHHHHHHHHHH	14.89	27135362
183	Phosphorylation	PELTSTISLFRAHEI HHHHHHHHHHHHHHH	22.88	27135362
193	Ubiquitination	RAHEIASKQVEERLQ HHHHHHHHHHHHHHH	49.71	-
204	Phosphorylation	ERLQEEKSQKQNIDI HHHHHHHHHHCCCCH	45.98	-
206	Ubiquitination	LQEEKSQKQNIDINR HHHHHHHHCCCCHHH	53.02	-
265	Phosphorylation	NYLVRWSSSGLPKDI CCEEEECCCCCCCCH	22.82	16674116
287	Phosphorylation	AVFTDLGSKDLKREK HHHHCCCCCCCCHHH	30.23	24945436
314	Phosphorylation	MELRDNNTRKLTSGL EEECCCCCCCCCCCC	35.12	-
319	Phosphorylation	NNTRKLTSGLRRPFG CCCCCCCCCCCCCCC	46.39	-
372	Ubiquitination	INKVIAAKEVNHKGQ HHHHHHHHHCCCCCC	53.85	-
405	Methylation	EFPHLVDRTTAVARK HCCHHHHHHHHHHHH	26.88	-
478	Phosphorylation	GDEAISEYKSVIYYQ CHHHHHHHHEEEEEE	11.19	-
483	Phosphorylation	SEYKSVIYYQVKQPR HHHHEEEEEEECCCC	5.91	-
512	Phosphorylation	NRSHLRFTFRHRSSQ CHHHEEEEEECCCCC	17.21	30576142
517	Phosphorylation	RFTFRHRSSQDSKDK EEEEECCCCCCCCCH	26.65	30576142
518	Phosphorylation	FTFRHRSSQDSKDKS EEEECCCCCCCCCHH	37.65	30576142
555	Ubiquitination	EHDLIVYKAEAKKLE CCEEEEEEEECCCHH	28.93	-
566	Phosphorylation	KKLEDAATYLSLPST CCHHHHHHHHCCCCC	27.07	22617229
567	Phosphorylation	KLEDAATYLSLPSTK CHHHHHHHHCCCCCH	6.92	22617229
572	Phosphorylation	ATYLSLPSTKAELEE HHHHCCCCCHHHHHH	48.08	22617229
574	Ubiquitination	YLSLPSTKAELEEKG HHCCCCCHHHHHHCC	44.17	-
583	Phosphorylation	ELEEKGHSATGKSMQ HHHHCCCCCCCCCHH	35.87	-
587	Ubiquitination	KGHSATGKSMQSLGS CCCCCCCCCHHHCCC	38.10	-
588	Phosphorylation	GHSATGKSMQSLGSC CCCCCCCCHHHCCCC	24.33	28348404
591	Phosphorylation	ATGKSMQSLGSCTIS CCCCCHHHCCCCEEC	26.51	-
728	Ubiquitination	NYVDGAEKPGVNEQL HHCCCCCCCCHHHHH	46.68	-
744	Phosphorylation	KAMKALESIFKFIVR HHHHHHHHHHHHHHH	33.89	24719451
760	Phosphorylation	RILFNQLYENKGEAD HHHHHHHHCCCCCHH	14.00	-
778	Phosphorylation	SLLQLFRSINDMMSS HHHHHHHHHHHHHHH	20.57	28270605
784	Phosphorylation	RSINDMMSSMSDQTV HHHHHHHHHCCCCEE	19.09	23401153
785	Phosphorylation	SINDMMSSMSDQTVR HHHHHHHHCCCCEEE	12.38	23401153
787	Phosphorylation	NDMMSSMSDQTVRVK HHHHHHCCCCEEEHH	28.63	23401153
790	Phosphorylation	MSSMSDQTVRVKGAA HHHCCCCEEEHHHHH	18.44	28270605
799	Ubiquitination	RVKGAALKYLPTIVN EHHHHHHHHHCCEEC	39.76	21890473
800	Phosphorylation	VKGAALKYLPTIVND HHHHHHHHHCCEECC	20.82	24719451
803	Phosphorylation	AALKYLPTIVNDVKL HHHHHHCCEECCEEE	34.66	24719451
815	Ubiquitination	VKLVFDPKELSKMFT EEEECCHHHHHHHHH	73.47	-
818	Phosphorylation	VFDPKELSKMFTEFI ECCHHHHHHHHHHHH	24.14	24719451
920	Phosphorylation	TVNRTVISMGRDSEL HHCHHHHHCCCCHHH	15.73	22210691
1054	Acetylation	KRAKILNKYGDMRRQ HHHHHHHHHHHHHHH	47.36	25953088
1054	Ubiquitination	KRAKILNKYGDMRRQ HHHHHHHHHHHHHHH	47.36	-
1146	Ubiquitination	GRGDEQYKVLFDKIL CCCHHHHHHHHHHHH	31.96	-
1162	Phosphorylation	EHCRKHKYLAKTGET HHHHHCCHHHHCCHH	16.18	19845377
1165	Ubiquitination	RKHKYLAKTGETFVK HHCCHHHHCCHHHHH	55.24	-
1186	Phosphorylation	ERLLDYRTIMHDENK HHHHCHHHHCCCCCC	19.20	30576142
1198	Phosphorylation	ENKENRMSCTVNVLN CCCCCCCCCEEEHHH	11.91	-
1200	Phosphorylation	KENRMSCTVNVLNFY CCCCCCCEEEHHHHH	14.07	-
1250	Phosphorylation	HAKLLKWSEDVCVAH HHHHHCCCCCCEEEH	23.49	-
1286	Ubiquitination	EIIHYFDKGKMWEEA HHHHHHHHCHHHHHH	51.00	-
1304	Phosphorylation	GKELAEQYENEMFDY CHHHHHHHHHCCCCH	16.54	25884760
1320	Ubiquitination	QLSELLKKQAQFYEN HHHHHHHHHHHHHHH	51.33	-
1330	Ubiquitination	QFYENIVKVIRPKPD HHHHHHHHHHCCCCC	28.31	-
1422	Phosphorylation	PKFHRPVSEQIVSFY CCCCCCHHHHHHEEE	26.85	28555341
1464	Phosphorylation	MWIERTIYTTAYKLP HHHHHHHHHHHHCCC	9.45	29759185
1560	Ubiquitination	EHPEAHEKIEKLKDL HCHHHHHHHHHHHHH	46.42	-
1602	Acetylation	ERMEACFKQLKEKVE HHHHHHHHHHHHHHH	55.39	130227
1605	Acetylation	EACFKQLKEKVEKEY HHHHHHHHHHHHHHH	53.66	130223
1610	Ubiquitination	QLKEKVEKEYGVRIM HHHHHHHHHHCCCCC	60.26	-
1612	Phosphorylation	KEKVEKEYGVRIMPS HHHHHHHHCCCCCCC	31.80	28270605
1619	Phosphorylation	YGVRIMPSSLDDRRG HCCCCCCCCCCCCCC	26.59	26270265
1620	Phosphorylation	GVRIMPSSLDDRRGS CCCCCCCCCCCCCCC	29.91	21815630
1627	Phosphorylation	SLDDRRGSRPRSMVR CCCCCCCCCCHHHHH	36.98	22798277
1635	Phosphorylation	RPRSMVRSFTMPSSS CCHHHHHEEECCCCC	17.41	28348404
1637	Phosphorylation	RSMVRSFTMPSSSRP HHHHHEEECCCCCCC	29.44	25884760
1640	Phosphorylation	VRSFTMPSSSRPLSV HHEEECCCCCCCCEE	30.08	28348404
1641	Phosphorylation	RSFTMPSSSRPLSVA HEEECCCCCCCCEEE	25.21	28348404
1642	Phosphorylation	SFTMPSSSRPLSVAS EEECCCCCCCCEEEE	42.10	27251275
1646	Phosphorylation	PSSSRPLSVASVSSL CCCCCCCEEEEHHHC	20.51	28348404
1649	Phosphorylation	SRPLSVASVSSLSSD CCCCEEEEHHHCCCC	22.00	28258704
1651	Phosphorylation	PLSVASVSSLSSDST CCEEEEHHHCCCCCC	24.06	28258704
1652	Phosphorylation	LSVASVSSLSSDSTP CEEEEHHHCCCCCCC	30.07	25850435
1654	Phosphorylation	VASVSSLSSDSTPSR EEEHHHCCCCCCCCC	33.76	25850435
1655	Phosphorylation	ASVSSLSSDSTPSRP EEHHHCCCCCCCCCC	40.65	25850435
1657	Phosphorylation	VSSLSSDSTPSRPGS HHHCCCCCCCCCCCC	44.13	25850435
1658	Phosphorylation	SSLSSDSTPSRPGSD HHCCCCCCCCCCCCC	30.21	28348404
1660	Phosphorylation	LSSDSTPSRPGSDGF CCCCCCCCCCCCCCC	51.72	27251275
1664	Phosphorylation	STPSRPGSDGFALEP CCCCCCCCCCCCCCC	36.92	25850435
1679	Phosphorylation	LLPKKMHSRSQDKLD CCCHHHCCCCCCCCC	30.08	29514088
1681	Phosphorylation	PKKMHSRSQDKLDKD CHHHCCCCCCCCCHH	45.83	23401153
1704	Phosphorylation	KKKEKRNSKHQEIFE HHHHHHHHHHHHHHH	35.23	26657352
1730	Phosphorylation	QSEAVILSETISPLR HHCEEHHHCCCCCCC	22.90	28348404
1732	Phosphorylation	EAVILSETISPLRPQ CEEHHHCCCCCCCCC	24.31	28348404
1734	Phosphorylation	VILSETISPLRPQRP EHHHCCCCCCCCCCC	25.87	24719451
1743	Phosphorylation	LRPQRPKSQVMNVIG CCCCCCHHHHHHHHC	30.59	25159151
1751	Phosphorylation	QVMNVIGSERRFSVS HHHHHHCCCCCEECC	19.46	25159151
1756	Phosphorylation	IGSERRFSVSPSSPS HCCCCCEECCCCCCC	21.63	27273156
1758	Phosphorylation	SERRFSVSPSSPSSQ CCCCEECCCCCCCCC	20.19	24670416
1760	Phosphorylation	RRFSVSPSSPSSQQT CCEECCCCCCCCCCC	47.58	26657352
1761	Phosphorylation	RFSVSPSSPSSQQTP CEECCCCCCCCCCCC	31.99	29978859
1763	Phosphorylation	SVSPSSPSSQQTPPP ECCCCCCCCCCCCCC	42.60	26657352
1764	Phosphorylation	VSPSSPSSQQTPPPV CCCCCCCCCCCCCCC	29.68	26657352
1767	Phosphorylation	SSPSSQQTPPPVTPR CCCCCCCCCCCCCCC	30.08	24670416
1772	Phosphorylation	QQTPPPVTPRAKLSF CCCCCCCCCCCEEEE	16.90	26657352
1807	Phosphorylation	PPLPLKGSVADYGNL CCCCCCCCHHHCCCC	16.73	30576142
1811	Phosphorylation	LKGSVADYGNLMENQ CCCCHHHCCCCCCCC	9.74	21082442
1823	Phosphorylation	ENQDLLGSPTPPPPP CCCCCCCCCCCCCCC	26.10	25159151
1825	Phosphorylation	QDLLGSPTPPPPPPH CCCCCCCCCCCCCCC	50.56	22199227
1842	Phosphorylation	HLPPPLPSKTPPPPP CCCCCCCCCCCCCCC	57.77	28188228
1844	Phosphorylation	PPPLPSKTPPPPPPK CCCCCCCCCCCCCCC	45.42	21815630
1857	Phosphorylation	PKTTRKQASVDSGIV CCCCCCCCCCCCCCC	17.98	-
1858	Phosphorylation	KTTRKQASVDSGIVQ CCCCCCCCCCCCCCC	24.78	24670416

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
1250	S	Phosphorylation	Kinase	PKACA	P17612	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DOCK1_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 DOCK1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CRK_HUMAN	CRK	physical	12615911
SRC_HUMAN	SRC	physical	12615911
BCAR1_HUMAN	BCAR1	physical	12615911
CRK_HUMAN	CRK	physical	26344197
RAC1_HUMAN	RAC1	physical	26344197
ARL4A_HUMAN	ARL4A	physical	21930703
RAC1_HUMAN	RAC1	physical	25468898

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 DOCK1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-1751, 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 SER-1858, AND MASSSPECTROMETRY.	16964243 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1811, AND MASSSPECTROMETRY.	19534553 [Abstract]