CPLM-009957

CPLM 1.0 - Compendium of Protein Lysine Modification

Tag

Content

CPLM ID

CPLM-009957

UniProt Accession

ROCK1_MOUSE; P70335; Q8C3G4; Q8C7H0

Genbank Protein ID

U58512; AK050269; AK085974; BC057154

Genbank Nucleotide ID

AAC53132.1; BAC34154.1; BAC39581.1; AAH57154.1

Protein Name

Rho-associated protein kinase 1

Protein Synonyms/Alias

Rho-associated, coiled-coil-containing protein kinase 1; Rho-associated, coiled-coil-containing protein kinase I; ROCK-I; p160 ROCK-1; p160ROCK

Gene Name

Rock1

Gene Synonyms/Alias

Created Date

July 27, 2013

Organism

Mus musculus (Mouse)

NCBI Taxa ID

10090

Lysine Modification

Position	Peptide	Type	References
1093	DIEQLRAKLLDLSDS	ubiquitination	[1]

Reference

[1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]

Functional 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.

Sequence Annotation

DOMAIN 76 338 Protein kinase.
DOMAIN 341 409 AGC-kinase C-terminal.
REPEAT 458 542 REM.
DOMAIN 1118 1317 PH.
NP_BIND 82 90 ATP (By similarity).
ZN_FING 1228 1283 Phorbol-ester/DAG-type.
REGION 368 727 Interaction with FHOD1 (By similarity).
REGION 998 1010 RHOA binding (By similarity).
REGION 1115 1354 Auto-inhibitory (By similarity).
ACT_SITE 198 198 Proton acceptor (By similarity).
BINDING 105 105 ATP (By similarity).
MOD_RES 2 2 N-acetylserine (By similarity).
MOD_RES 1105 1105 Phosphoserine (By similarity).

Keyword

Acetylation; Alternative splicing; Apoptosis; ATP-binding; Cell membrane; Cell projection; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Golgi apparatus; Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.

Sequence Source

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

Protein Length

1354 AA

Protein Sequence

MSTGDSFETR FEKIDNLLRD PKSEVNSDCL LDGLDALVYD LDFPALRKNK NIDNFLSRYK 60
DTINKIRDLR MKAEDYEVVK VIGRGAFGEV QLVRHKSTRK VYAMKLLSKF EMIKRSDSAF 120
FWEERDIMAF ANSPWVVQLF YAFQDDRYLY MVMEYMPGGD LVNLMSNYDV PEKWARFYTA 180
EVVLALDAIH SMGFIHRDVK PDNMLLDKSG HLKLADFGTC MKMNKEGMVR CDTAVGTPDY 240
ISPEVLKSQG GDGYYGRECD WWSVGVFLYE MLVGDTPFYA DSLVGTYSKI MNHKNSLTFP 300
DDNDISKEAK NLICAFLTDR EVRLGRNGVE EIKRHLFFKN DQWAWETLRD TVAPVVPDLS 360
SDIDTSNFDD LEEDKGDEET FPIPKAFVGN QLPFVGFTYY SNRRYLPSAN ASENRSSSNV 420
DKSLQESLQK TIYKLEEQLH NEMQLKDEME QKCRTSNLKL DKIMKELDEE GNQRRNLESA 480
VSQIEKEKML LQHRINEYQR KVEQENEKRR NIENEVSTLK DQLEDLRKAS QTSQLANEKL 540
TQLQKQLEEA NDLLRTESDT AVRLRKSHTE MSKSISQLES LNRELQERNR ILENSKSQAD 600
KDYYQLQAVL EAERRDRGHD SEMIGDLQAR ITSLQEEVKH LKHNLERVEG ERKEAQDMLN 660
HSEKEKNNLE IDLNYKLKSI QQRLEQEVNE HKVTKARLTD KHQSIEEAKS VAMCEMEKKL 720
KEEREAREKA ENRVVETEKQ CSMLDVDLKQ SQQKLEHLTE NKERMEDEVK NLALQLEQES 780
NKRLLLQNEL KTQAFEADNL KGLEKQMKQE INTLLEAKRL LEFELAQLTK QYRGNEGQMR 840
ELQDQLEAEQ YFSTLYKTQV KELKEEIEEK NRENLRKIQE LQSEKETLST QLDLAETKAE 900
SEQLARGILE EQYFELTQES KKAASRNRQE ITDKDHTVSR LEETNSVLTK DIEMLRKENE 960
ELNERMRTAE EEYKLKKEEE INNLKAAFEK NISTERTLKT QAVNKLAEIM NRKDFKIDRK 1020
KANTQDLRKK EKENRKLQLE LNQEREKFNQ MVVKHQKELN DMQAQLVEEC THRNELQMQL 1080
ASKESDIEQL RAKLLDLSDS TSVASFPSAD ETDGNLPESR IEGWLSVPNR GNIKRYGWKK 1140
QYVVVSSKKI LFYNDEQDKE QSSPSMVLDI DKLFHVRPVT QGDVYRAETE EIPKIFQILY 1200
ANEGECRKDI EVEPVQQGEK TNFQNHKGHE FIPTLYHFPA NCEACAKPLW HVFKPPPALE 1260
CRRCHVKCHR DHLDKKEDLI SPCKVSYDVT SARDMLLLAC SQDEQKKWVT HLVKKIPKNP 1320
PSGFVRASPR TLSTRSTANQ SFRKVVKNTS GKTS 1354

Gene Ontology

GO:0032059; C:bleb; IEA:UniProtKB-SubCell.
GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
GO:0005856; C:cytoskeleton; IDA:UniProtKB.
GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO:0001726; C:ruffle; IDA:UniProtKB.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO:0005543; F:phospholipid binding; IEA:InterPro.
GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
GO:0003383; P:apical constriction; IGI:MGI.
GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO:0032060; P:bleb assembly; IMP:MGI.
GO:0050901; P:leukocyte tethering or rolling; IEA:Compara.
GO:0022614; P:membrane to membrane docking; IEA:Compara.
GO:0016525; P:negative regulation of angiogenesis; IEA:Compara.
GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
GO:0032970; P:regulation of actin filament-based process; IGI:MGI.
GO:0045616; P:regulation of keratinocyte differentiation; IEA:Compara.
GO:0007266; P:Rho protein signal transduction; ISO:MGI.

Interpro

IPR000961; AGC-kinase_C.
IPR011072; HR1_rho-bd.
IPR011009; Kinase-like_dom.
IPR011993; PH_like_dom.
IPR017892; Pkinase_C.
IPR001849; Pleckstrin_homology.
IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
IPR000719; Prot_kinase_cat_dom.
IPR017441; Protein_kinase_ATP_BS.
IPR020684; Rho-assoc_coiled-coil_kin.
IPR015008; Rho-bd_dom.
IPR002290; Ser/Thr_dual-sp_kinase_dom.
IPR008271; Ser/Thr_kinase_AS.

Pfam

PF02185; HR1
PF00169; PH
PF00069; Pkinase
PF00433; Pkinase_C
PF08912; Rho_Binding

SMART

SM00109; C1
SM00233; PH
SM00133; S_TK_X
SM00220; S_TKc

PROSITE

PS51285; AGC_KINASE_CTER
PS50003; PH_DOMAIN
PS00107; PROTEIN_KINASE_ATP
PS50011; PROTEIN_KINASE_DOM
PS00108; PROTEIN_KINASE_ST
PS00479; ZF_DAG_PE_1
PS50081; ZF_DAG_PE_2

PRINTS