ROCK1_MOUSE - dbPTM
ROCK1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ROCK1_MOUSE
UniProt AC P70335
Protein Name Rho-associated protein kinase 1
Gene Name Rock1
Organism Mus musculus (Mouse).
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 proje
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. Required for centrosome positioning and centrosome-dependent exit from mitosis. Plays a role in terminal erythroid differentiation. Promotes keratinocyte terminal differentiation (By similarity). 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. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles..
Protein Sequence MSTGDSFETRFEKIDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYKDTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGDEETFPIPKAFVGNQLPFVGFTYYSNRRYLPSANASENRSSSNVDKSLQESLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNLKLDKIMKELDEEGNQRRNLESAVSQIEKEKMLLQHRINEYQRKVEQENEKRRNIENEVSTLKDQLEDLRKASQTSQLANEKLTQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQERNRILENSKSQADKDYYQLQAVLEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLERVEGERKEAQDMLNHSEKEKNNLEIDLNYKLKSIQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEKKLKEEREAREKAENRVVETEKQCSMLDVDLKQSQQKLEHLTENKERMEDEVKNLALQLEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLRKIQELQSEKETLSTQLDLAETKAESEQLARGILEEQYFELTQESKKAASRNRQEITDKDHTVSRLEETNSVLTKDIEMLRKENEELNERMRTAEEEYKLKKEEEINNLKAAFEKNISTERTLKTQAVNKLAEIMNRKDFKIDRKKANTQDLRKKEKENRKLQLELNQEREKFNQMVVKHQKELNDMQAQLVEECTHRNELQMQLASKESDIEQLRAKLLDLSDSTSVASFPSADETDGNLPESRIEGWLSVPNRGNIKRYGWKKQYVVVSSKKILFYNDEQDKEQSSPSMVLDIDKLFHVRPVTQGDVYRAETEEIPKIFQILYANEGECRKDIEVEPVQQGEKTNFQNHKGHEFIPTLYHFPANCEACAKPLWHVFKPPPALECRRCHVKCHRDHLDKKEDLISPCKVSYDVTSARDMLLLACSQDEQKKWVTHLVKKIPKNPPSGFVRASPRTLSTRSTANQSFRKVVKNTSGKTS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MSTGDSFET
------CCCCCCHHH		53.02-
2Phosphorylation------MSTGDSFET
------CCCCCCHHH		53.0225338131
3Phosphorylation-----MSTGDSFETR
-----CCCCCCHHHH		57.7926824392
6Phosphorylation--MSTGDSFETRFEK
--CCCCCCHHHHHHH		26.7425338131
282PhosphorylationDTPFYADSLVGTYSK
CCCCHHCHHHHHHHH		19.45-
408PhosphorylationSNRRYLPSANASENR
CCCCCCCCCCCCCCC		31.4029472430
412PhosphorylationYLPSANASENRSSSN
CCCCCCCCCCCCCCC		34.9029899451
416PhosphorylationANASENRSSSNVDKS
CCCCCCCCCCCCCHH		50.1028285833
417PhosphorylationNASENRSSSNVDKSL
CCCCCCCCCCCCHHH		23.7729472430
418PhosphorylationASENRSSSNVDKSLQ
CCCCCCCCCCCHHHH		41.9625338131
517PhosphorylationRNIENEVSTLKDQLE
HHHHHHHHHHHHHHH		23.1127149854
639AcetylationTSLQEEVKHLKHNLE
HHHHHHHHHHHHHHH		46.6423954790
710PhosphorylationQSIEEAKSVAMCEME
HCHHHHHHHHHHHHH		23.3520469934
1005UbiquitinationLKTQAVNKLAEIMNR
HHHHHHHHHHHHHCC		42.34-
1093UbiquitinationDIEQLRAKLLDLSDS
HHHHHHHHHCCCCCC		43.0522790023
1098PhosphorylationRAKLLDLSDSTSVAS
HHHHCCCCCCCCCCC		29.2221082442
1100PhosphorylationKLLDLSDSTSVASFP
HHCCCCCCCCCCCCC		21.1421082442
1101PhosphorylationLLDLSDSTSVASFPS
HCCCCCCCCCCCCCC		32.0127087446
1102PhosphorylationLDLSDSTSVASFPSA
CCCCCCCCCCCCCCC		21.4527087446
1105PhosphorylationSDSTSVASFPSADET
CCCCCCCCCCCCCCC		35.2227087446
1108PhosphorylationTSVASFPSADETDGN
CCCCCCCCCCCCCCC		46.4721082442
1112PhosphorylationSFPSADETDGNLPES
CCCCCCCCCCCCCHH		50.1625619855
1126PhosphorylationSRIEGWLSVPNRGNI
HHEEEEECCCCCCCC		29.08-
1140MalonylationIKRYGWKKQYVVVSS
CCCCCCCEEEEEEEC		40.1126320211
1146PhosphorylationKKQYVVVSSKKILFY
CEEEEEEECCEEEEE		25.4929472430
1147PhosphorylationKQYVVVSSKKILFYN
EEEEEEECCEEEEEE		26.7629472430
1162PhosphorylationDEQDKEQSSPSMVLD
CCCCCCCCCCCEEEE		45.3625195567
1163PhosphorylationEQDKEQSSPSMVLDI
CCCCCCCCCCEEEEH		22.2325338131
1180PhosphorylationLFHVRPVTQGDVYRA
HHCCEECCCCCEEEE		29.53-
1189PhosphorylationGDVYRAETEEIPKIF
CCEEEECCCCCCHHH		37.6220469934
1322PhosphorylationKIPKNPPSGFVRASP
HCCCCCCCCCCCCCC		46.2323684622
1328PhosphorylationPSGFVRASPRTLSTR
CCCCCCCCCCCCCCC		12.3526824392
1333PhosphorylationRASPRTLSTRSTANQ
CCCCCCCCCCCCCCH		22.5925521595
1334PhosphorylationASPRTLSTRSTANQS
CCCCCCCCCCCCCHH		31.5825521595
1336PhosphorylationPRTLSTRSTANQSFR
CCCCCCCCCCCHHHH		31.7723737553
1337PhosphorylationRTLSTRSTANQSFRK
CCCCCCCCCCHHHHH		26.7423737553
1341PhosphorylationTRSTANQSFRKVVKN
CCCCCCHHHHHHHHC		27.1626824392
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

Oops, there are no upstream regulatory protein records of ROCK1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ROCK1_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHOA_HUMANRHOAphysical
9535835
CDC42_HUMANCDC42physical
9535835
CDK2_HUMANCDK2physical
26496610
RAD51_HUMANRAD51physical
26496610
SMCA4_HUMANSMARCA4physical
26496610
SMRC1_HUMANSMARCC1physical
26496610
SSRG_HUMANSSR3physical
26496610
IFT88_HUMANIFT88physical
26496610
GPAA1_HUMANGPAA1physical
26496610
UBC12_HUMANUBE2Mphysical
26496610
ROCK2_HUMANROCK2physical
26496610
HMGX4_HUMANHMGXB4physical
26496610
CEPT1_HUMANCEPT1physical
26496610
VPP2_HUMANATP6V0A2physical
26496610
SIR6_HUMANSIRT6physical
26496610
STX18_HUMANSTX18physical
26496610
ENY2_HUMANENY2physical
26496610
S39AA_HUMANSLC39A10physical
26496610
DOCK6_HUMANDOCK6physical
26496610
DOCK5_HUMANDOCK5physical
26496610
PSRC1_HUMANPSRC1physical
26496610
FBH1_HUMANFBXO18physical
26496610
RETR3_HUMANFAM134Cphysical
26496610
GA2L3_HUMANGAS2L3physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ROCK1_MOUSE

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Related Literatures of Post-Translational Modification

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