dbPTM

ROCK1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ROCK1_HUMAN
UniProt AC	Q13464
Protein Name	Rho-associated protein kinase 1
Gene Name	ROCK1
Organism	Homo sapiens (Human).
Sequence Length	1354
Subcellular Localization	Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Golgi apparatus membrane Peripheral membrane protein. Cell projection, bleb. Cytoplasm, cytoskeleton. Cell membrane. Cell projection, lamellipodium. Cell projection
Protein Description	Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, PFN1 and PPP1R12A. Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing. Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress. Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Required for centrosome positioning and centrosome-dependent exit from mitosis. Plays a role in terminal erythroid differentiation. May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles. Promotes keratinocyte terminal differentiation. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization..
Protein Sequence	MSTGDSFETRFEKMDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYKDTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPKAFVGNQLPFVGFTYYSNRRYLSSANPNDNRTSSNADKSLQESLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQERNRILENSKSQTDKDYYQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLNHSEKEKNNLEIDLNYKLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEKKLKEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLKKIQELQNEKETLATQLDLAETKAESEQLARGLLEEQYFELTQESKKAASRNRQEITDKDHTVSRLEEANSMLTKDIEILRRENEELTEKMKKAEEEYKLEKEEEISNLKAAFEKNINTERTLKTQAVNKLAEIMNRKDFKIDRKKANTQDLRKKEKENRKLQLELNQEREKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQLASKESDIEQLRAKLLDLSDSTSVASFPSADETDGNLPESRIEGWLSVPNRGNIKRYGWKKQYVVVSSKKILFYNDEQDKEQSNPSMVLDIDKLFHVRPVTQGDVYRAETEEIPKIFQILYANEGECRKDVEMEPVQQAEKTNFQNHKGHEFIPTLYHFPANCDACAKPLWHVFKPPPALECRRCHVKCHRDHLDKKEDLICPCKVSYDVTSARDMLLLACSQDEQKKWVTHLVKKIPKNPPSGFVRASPRTLSTRSTANQSFRKVVKNTSGKTS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSTGDSFET ------CCCCCCHHH	53.02	22814378
2	Phosphorylation	------MSTGDSFET ------CCCCCCHHH	53.02	28450419
3	Phosphorylation	-----MSTGDSFETR -----CCCCCCHHHH	57.79	28450419
6	Phosphorylation	--MSTGDSFETRFEK --CCCCCCHHHHHHH	26.74	28450419
9	Phosphorylation	STGDSFETRFEKMDN CCCCCHHHHHHHHHH	38.35	28450419
13	Ubiquitination	SFETRFEKMDNLLRD CHHHHHHHHHHHHCC	49.17	29967540
65	Ubiquitination	RYKDTINKIRDLRMK HHHHHHHHHHHHHHH	34.96	24816145
80	Ubiquitination	AEDYEVVKVIGRGAF HHHCEEEEEEECCCC	33.05	29967540
108	Phosphorylation	VYAMKLLSKFEMIKR HHHHHHHHHHHHHHC	45.81	29083192
109	Ubiquitination	YAMKLLSKFEMIKRS HHHHHHHHHHHHHCC	45.36	-
155	Phosphorylation	YLYMVMEYMPGGDLV EEEEEEECCCCCCHH	7.18	24275569
200	Ubiquitination	GFIHRDVKPDNMLLD CCCCCCCCCCCCEEC	51.44	2190698
225	Ubiquitination	GTCMKMNKEGMVRCD HHCCCCCCCCCEECC	52.74	29967540
229	Ubiquitination	KMNKEGMVRCDTAVG CCCCCCCEECCCCCC	8.95	24816145
237	Phosphorylation	RCDTAVGTPDYISPE ECCCCCCCCCCCCHH	13.34	28348404
240	Phosphorylation	TAVGTPDYISPEVLK CCCCCCCCCCHHHHH	12.42	27642862
247	Ubiquitination	YISPEVLKSQGGDGY CCCHHHHHCCCCCCC	46.00	22817900
255	Phosphorylation	SQGGDGYYGRECDWW CCCCCCCCCCCCCHH	18.42	22817900
276	Phosphorylation	YEMLVGDTPFYADSL HHHHHCCCCCHHCHH	14.90	26074081
279	Phosphorylation	LVGDTPFYADSLVGT HHCCCCCHHCHHHHH	15.65	26074081
282	Phosphorylation	DTPFYADSLVGTYSK CCCCHHCHHHHHHHH	19.45	26074081
286	Phosphorylation	YADSLVGTYSKIMNH HHCHHHHHHHHHHCC	19.69	26074081
287	Phosphorylation	ADSLVGTYSKIMNHK HCHHHHHHHHHHCCC	11.31	26074081
288	Phosphorylation	DSLVGTYSKIMNHKN CHHHHHHHHHHCCCC	18.62	26074081
294	Ubiquitination	YSKIMNHKNSLTFPD HHHHHCCCCCCCCCC	43.13	29967540
296	Phosphorylation	KIMNHKNSLTFPDDN HHHCCCCCCCCCCCC	33.32	26074081
298	Phosphorylation	MNHKNSLTFPDDNDI HCCCCCCCCCCCCCC	32.70	26074081
306	Phosphorylation	FPDDNDISKEAKNLI CCCCCCCCHHHHHHH	27.57	26074081
307	Ubiquitination	PDDNDISKEAKNLIC CCCCCCCHHHHHHHH	63.12	29967540
339	Ubiquitination	IKRHLFFKNDQWAWE HHHHHHCCCCHHHHH	52.89	29967540
398	Phosphorylation	QLPFVGFTYYSNRRY CCCCEEEEEECCCCC	18.67	28348404
401	Phosphorylation	FVGFTYYSNRRYLSS CEEEEEECCCCCCCC	17.28	28348404
405	Phosphorylation	TYYSNRRYLSSANPN EEECCCCCCCCCCCC	14.01	22817900
407	Phosphorylation	YSNRRYLSSANPNDN ECCCCCCCCCCCCCC	20.62	22817900
416	Phosphorylation	ANPNDNRTSSNADKS CCCCCCCCCCCCCHH	42.64	28348404
417	Phosphorylation	NPNDNRTSSNADKSL CCCCCCCCCCCCHHH	20.54	30576142
418	Phosphorylation	PNDNRTSSNADKSLQ CCCCCCCCCCCHHHH	35.11	30576142
430	Ubiquitination	SLQESLQKTIYKLEE HHHHHHHHHHHHHHH	42.03	29967540
452	Acetylation	LKDEMEQKCRTSNIK CHHHHHHHHHHCCCC	16.63	25953088
455	Phosphorylation	EMEQKCRTSNIKLDK HHHHHHHHCCCCHHH	35.28	22817900
456	Phosphorylation	MEQKCRTSNIKLDKI HHHHHHHCCCCHHHH	19.73	22817900
527	Ubiquitination	KDQLEDLKKVSQNSQ HHHHHHHHHHHHHHH	64.55	32015554
533	Phosphorylation	LKKVSQNSQLANEKL HHHHHHHHHHHHHHH	20.95	-
539	Ubiquitination	NSQLANEKLSQLQKQ HHHHHHHHHHHHHHH	53.93	32015554
567	Phosphorylation	TAVRLRKSHTEMSKS HHHHHHHHHHHHHHH	29.25	-
569	Phosphorylation	VRLRKSHTEMSKSIS HHHHHHHHHHHHHHH	40.24	-
572	Phosphorylation	RKSHTEMSKSISQLE HHHHHHHHHHHHHHH	19.61	-
574	Phosphorylation	SHTEMSKSISQLESL HHHHHHHHHHHHHHH	21.84	-
576	Phosphorylation	TEMSKSISQLESLNR HHHHHHHHHHHHHHH	35.49	-
603	Phosphorylation	KSQTDKDYYQLQAIL CCCCCCCHHHHHHHH	10.00	24043423
604	Phosphorylation	SQTDKDYYQLQAILE CCCCCCHHHHHHHHH	16.93	24043423
621	Phosphorylation	RRDRGHDSEMIGDLQ HHHCCCCHHHHHHHH	24.32	24719451
633	Phosphorylation	DLQARITSLQEEVKH HHHHHHHHHHHHHHH	26.19	24719451
639	Acetylation	TSLQEEVKHLKHNLE HHHHHHHHHHHHHHH	46.64	25953088
647	Acetylation	HLKHNLEKVEGERKE HHHHHHHHHHHHHHH	49.07	19608861
658	Sulfoxidation	ERKEAQDMLNHSEKE HHHHHHHHHHCCHHH	2.41	30846556
679	Phosphorylation	DLNYKLKSLQQRLEQ HHHHHHHHHHHHHHH	41.67	21722762
692	Ubiquitination	EQEVNEHKVTKARLT HHHHHHHHCHHHHCC	45.48	24816145
709	Acetylation	HQSIEEAKSVAMCEM HHCHHHHHHHHHHHH	49.06	25953088
710	Phosphorylation	QSIEEAKSVAMCEME HCHHHHHHHHHHHHH	23.35	-
713	Sulfoxidation	EEAKSVAMCEMEKKL HHHHHHHHHHHHHHH	1.54	30846556
716	Sulfoxidation	KSVAMCEMEKKLKEE HHHHHHHHHHHHHHH	8.56	30846556
718	Acetylation	VAMCEMEKKLKEERE HHHHHHHHHHHHHHH	63.19	23749302
742	Phosphorylation	VQIEKQCSMLDVDLK HHHHHHHHCCCCCHH	21.64	24532841
782	Ubiquitination	QLEQESNKRLLLQNE HHHHHHHHHHHHHHH	54.42	29967540
791	Acetylation	LLLQNELKTQAFEAD HHHHHHHHHHHHHHH	32.20	25953088
830	Ubiquitination	FELAQLTKQYRGNEG HHHHHHHHHHCCCHH	54.66	32015554
857	Ubiquitination	QYFSTLYKTQVKELK HHHHHHHHHHHHHHH	35.28	29967540
887	Phosphorylation	ELQNEKETLATQLDL HHHHHHHHHHHHHHH	32.53	-
889	Ubiquitination	QNEKETLATQLDLAE HHHHHHHHHHHHHHH	10.75	24816145
890	Phosphorylation	NEKETLATQLDLAET HHHHHHHHHHHHHHH	32.55	-
897	Phosphorylation	TQLDLAETKAESEQL HHHHHHHHHHHHHHH	29.91	-
898	Ubiquitination	QLDLAETKAESEQLA HHHHHHHHHHHHHHH	41.48	29967540
913	Phosphorylation	RGLLEEQYFELTQES HHHHHHHHHHHCHHH	11.42	29978859
917	Phosphorylation	EEQYFELTQESKKAA HHHHHHHCHHHHHHH	24.08	29978859
920	Phosphorylation	YFELTQESKKAASRN HHHHCHHHHHHHHCC	29.64	29978859
921	Ubiquitination	FELTQESKKAASRNR HHHCHHHHHHHHCCH	45.75	32015554
939	Phosphorylation	TDKDHTVSRLEEANS CCCHHHHHHHHHHHH	32.10	29116813
947	Sulfoxidation	RLEEANSMLTKDIEI HHHHHHHHHHHHHHH	5.74	30846556
950	Ubiquitination	EANSMLTKDIEILRR HHHHHHHHHHHHHHH	53.39	32015554
985	Ubiquitination	EEEISNLKAAFEKNI HHHHHHHHHHHHCCC	41.75	32015554
990	Malonylation	NLKAAFEKNINTERT HHHHHHHCCCCHHHH	57.59	26320211
1024	Phosphorylation	IDRKKANTQDLRKKE CCHHHCCHHHHHHHH	28.46	21685893
1036	Malonylation	KKEKENRKLQLELNQ HHHHHHHHHHHHHHH	52.76	26320211
1057	Ubiquitination	QMVVKHQKELNDMQA HHHHHHHHHHHHHHH	64.98	29967540
1078	Sulfoxidation	AHRNELQMQLASKES HHHHHHHHHHHCCCC	5.72	21406390
1093	Ubiquitination	DIEQLRAKLLDLSDS HHHHHHHHHCCCCCC	43.05	29967540
1098	Phosphorylation	RAKLLDLSDSTSVAS HHHHCCCCCCCCCCC	29.22	30266825
1100	Phosphorylation	KLLDLSDSTSVASFP HHCCCCCCCCCCCCC	21.14	30266825
1101	Phosphorylation	LLDLSDSTSVASFPS HCCCCCCCCCCCCCC	32.01	30266825
1102	Phosphorylation	LDLSDSTSVASFPSA CCCCCCCCCCCCCCC	21.45	26503892
1105	Phosphorylation	SDSTSVASFPSADET CCCCCCCCCCCCCCC	35.22	29255136
1108	Phosphorylation	TSVASFPSADETDGN CCCCCCCCCCCCCCC	46.47	30266825
1112	Phosphorylation	SFPSADETDGNLPES CCCCCCCCCCCCCHH	50.16	30278072
1119	Phosphorylation	TDGNLPESRIEGWLS CCCCCCHHHEEEEEC	36.30	22199227
1126	Phosphorylation	SRIEGWLSVPNRGNI HHEEEEECCCCCCCC	29.08	28857561
1140	Malonylation	IKRYGWKKQYVVVSS CCCCCCCEEEEEEEC	40.11	26320211
1142	Phosphorylation	RYGWKKQYVVVSSKK CCCCCEEEEEEECCE	12.23	28060719
1146	Phosphorylation	KKQYVVVSSKKILFY CEEEEEEECCEEEEE	25.49	28060719
1147	Phosphorylation	KQYVVVSSKKILFYN EEEEEEECCEEEEEE	26.76	28060719
1148	Acetylation	QYVVVSSKKILFYND EEEEEECCEEEEEEC	36.01	25953088
1153	Phosphorylation	SSKKILFYNDEQDKE ECCEEEEEECCCCHH	20.47	-
1180	Phosphorylation	LFHVRPVTQGDVYRA HHEEEECCCCCEEEE	29.53	17525332
1185	Phosphorylation	PVTQGDVYRAETEEI ECCCCCEEEECCCCC	14.62	28060719
1189	Phosphorylation	GDVYRAETEEIPKIF CCEEEECCCCCCCHH	37.62	26657352
1194	Acetylation	AETEEIPKIFQILYA ECCCCCCCHHHHHHC	62.91	18530499
1212	Sulfoxidation	ECRKDVEMEPVQQAE CCCCCCCCCCCCHHH	7.68	21406390
1254	Acetylation	KPLWHVFKPPPALEC CCHHHHCCCCCCHHC	56.37	25953088
1284	Acetylation	EDLICPCKVSYDVTS CCCEECCCCEEECCC	21.25	25953088
1284	Malonylation	EDLICPCKVSYDVTS CCCEECCCCEEECCC	21.25	26320211
1286	Phosphorylation	LICPCKVSYDVTSAR CEECCCCEEECCCHH	10.91	28796482
1287	Phosphorylation	ICPCKVSYDVTSARD EECCCCEEECCCHHH	19.88	28796482
1290	Phosphorylation	CKVSYDVTSARDMLL CCCEEECCCHHHHHH	17.48	28796482
1291	Phosphorylation	KVSYDVTSARDMLLL CCEEECCCHHHHHHH	22.58	28796482
1310	Phosphorylation	DEQKKWVTHLVKKIP HHHHHHHHHHHHHCC	14.37	28857561
1322	Phosphorylation	KIPKNPPSGFVRASP HCCCCCCCCCCCCCC	46.23	23403867
1328	Phosphorylation	PSGFVRASPRTLSTR CCCCCCCCCCCCCCC	12.35	23401153
1331	Phosphorylation	FVRASPRTLSTRSTA CCCCCCCCCCCCCCC	28.57	23403867
1333	Phosphorylation	RASPRTLSTRSTANQ CCCCCCCCCCCCCCH	22.59	23403867
1334	Phosphorylation	ASPRTLSTRSTANQS CCCCCCCCCCCCCHH	31.58	23403867
1336	O-linked_Glycosylation	PRTLSTRSTANQSFR CCCCCCCCCCCHHHH	31.77	28510447
1336	Phosphorylation	PRTLSTRSTANQSFR CCCCCCCCCCCHHHH	31.77	29255136
1337	Phosphorylation	RTLSTRSTANQSFRK CCCCCCCCCCHHHHH	26.74	29255136
1341	Phosphorylation	TRSTANQSFRKVVKN CCCCCCHHHHHHHHC	27.16	21685893
1352	Ubiquitination	VVKNTSGKTS----- HHHCCCCCCC-----	45.41	24816145

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
1024	T	Phosphorylation	Kinase	PKCI	P41743	PSP
1333	S	Phosphorylation	Kinase	PKCI	P41743	PSP
1334	T	Phosphorylation	Kinase	PKCI	P41743	PSP
1337	T	Phosphorylation	Kinase	PKCI	P41743	PSP
1341	S	Phosphorylation	Kinase	PKCI	P41743	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ROCK1_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 ROCK1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MPIP1_HUMAN	CDC25A	physical	14657354
PROF2_HUMAN	PFN2	physical	14517206
GAB1_HUMAN	GAB1	physical	12748184
RHOA_HUMAN	RHOA	physical	8816443
RHOA_HUMAN	RHOA	physical	8798490
LIMK2_HUMAN	LIMK2	physical	10436159
ANFY1_HUMAN	ANKFY1	physical	22863883
MON2_HUMAN	MON2	physical	22863883
IKKB_HUMAN	IKBKB	physical	24240172
RPC3_HUMAN	POLR3C	physical	25416956
CF206_HUMAN	C6orf165	physical	25416956
F124A_HUMAN	FAM124A	physical	25416956
HGS_HUMAN	HGS	physical	26819309
SL9A1_HUMAN	SLC9A1	physical	26819309
UBE2T_HUMAN	UBE2T	physical	28162934

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
D01840	Fasudil hydrochloride (JAN)
D03115	Fasudil hydrochloride hydrate (JAN); Eril-S (TN)
D07941	Fasudil (INN)
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ROCK1_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-647, 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-1105, AND MASSSPECTROMETRY.	19690332 [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-1105, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455 AND SER-456, ANDMASS SPECTROMETRY.	18187866 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1180, AND MASSSPECTROMETRY.	17525332 [Abstract]