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P70335 (ROCK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho-associated protein kinase 1

EC=2.7.11.1
Alternative name(s):
Rho-associated, coiled-coil-containing protein kinase 1
Rho-associated, coiled-coil-containing protein kinase I
Short name=ROCK-I
p160 ROCK-1
Short name=p160ROCK
Gene names
Name:Rock1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.7 Ref.8 Ref.9 Ref.10

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by RHOA binding. Inhibited by Y-27632 By similarity.

Subunit structure

Homodimer By similarity. Interacts with RHOA (activated by GTP), RHOB, RHOC, GEM, MYLC2B, RHOE, PPP1R12A, LIMK1, LIMK2, TSG101, CHORDC1, DAPK3, PFN1 and JIP3 By similarity. Interacts with FHOD1 in a Src-dependent manner By similarity. Interacts with PTEN. Interacts with ITGB1BP1 (via N-terminus and PTB domain). Ref.5 Ref.6 Ref.9

Subcellular location

Cytoplasm. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole. Golgi apparatus membrane; Peripheral membrane protein By similarity. Cell projectionbleb By similarity. Cytoplasmcytoskeleton. Cell membrane. Cell projectionlamellipodium. Cell projectionruffle. Note: Associated with the mother centriole and an intercentriolar linker. A small proportion is associated with Golgi membranes By similarity. Colocalizes with ITGB1BP1 and ITGB1 at the cell membrane predominantly in lamellipodia and membrane ruffles, but also in retraction fibers. Localizes at the cell membrane in an ITGB1BP1-dependent manner. Ref.5

Tissue specificity

Highly expressed in brain, heart, lung, liver, stomach, spleen, kidney, testis, muscle, embryo and placenta. Ref.1

Domain

The C-terminal auto-inhibitory domain interferes with kinase activity. RHOA binding leads to a conformation change and activation of the kinase. Truncated ROCK1 is constitutively activated.

Post-translational modification

Autophosphorylated on serine and threonine residues.

Cleaved by caspase-3 during apoptosis. This leads to constitutive activation of the kinase and membrane blebbing By similarity.

Disruption phenotype

Mice exhibit both EOB (eyes open at birth) and omphalocele phenotypes as a result of disorganization of actomyosin cables in the eyelid epithelium and defective actin assembly in the umbilical ring. Ref.4

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 PH domain.

Contains 1 phorbol-ester/DAG-type zinc finger.

Contains 1 protein kinase domain.

Contains 1 REM (Hr1) repeat.

Sequence caution

The sequence AAH57154.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAC34154.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Zinc-finger
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRho protein signal transduction

Inferred from sequence orthology PubMed 18332105. Source: MGI

actin cytoskeleton organization

Inferred from genetic interaction PubMed 16249236. Source: MGI

apical constriction

Inferred from genetic interaction PubMed 21685893. Source: MGI

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

bleb assembly

Inferred from mutant phenotype PubMed 17135244. Source: MGI

leukocyte tethering or rolling

Inferred from electronic annotation. Source: Ensembl

membrane to membrane docking

Inferred from electronic annotation. Source: Ensembl

myoblast migration

Inferred from mutant phenotype Ref.6. Source: UniProtKB

negative regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 15071095. Source: MGI

positive regulation of focal adhesion assembly

Inferred from mutant phenotype Ref.6. Source: UniProtKB

regulation of actin filament-based process

Inferred from genetic interaction PubMed 21685893. Source: MGI

regulation of keratinocyte differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

bleb

Inferred from electronic annotation. Source: UniProtKB-SubCell

centriole

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from direct assay Ref.5. Source: UniProtKB

lamellipodium

Inferred from direct assay Ref.5. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.5. Source: UniProtKB

ruffle

Inferred from direct assay Ref.5. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Rnd3P615887EBI-989293,EBI-6930266

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P70335-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P70335-2)

The sequence of this isoform differs from the canonical sequence as follows:
     425-425: Missing.
Note: May be due to a competing donor splice site. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 13541353Rho-associated protein kinase 1
PRO_0000086620

Regions

Domain76 – 338263Protein kinase
Domain341 – 40969AGC-kinase C-terminal
Repeat458 – 54285REM
Domain1118 – 1317200PH
Nucleotide binding82 – 909ATP By similarity
Zinc finger1228 – 128356Phorbol-ester/DAG-type
Region368 – 727360Interaction with FHOD1 By similarity
Region998 – 101013RHOA binding By similarity
Region1115 – 1354240Auto-inhibitory By similarity
Coiled coil422 – 612191 Potential
Coiled coil1011 – 110292 Potential
Compositional bias636 – 980345Glu-rich

Sites

Active site1981Proton acceptor By similarity
Binding site1051ATP By similarity
Site1113 – 11142Cleavage; by caspase-3 By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue11051Phosphoserine By similarity

Natural variations

Alternative sequence4251Missing in isoform 2.
VSP_010448

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: A1CBD543B831CF96

FASTA1,354158,171
        10         20         30         40         50         60 
MSTGDSFETR FEKIDNLLRD PKSEVNSDCL LDGLDALVYD LDFPALRKNK NIDNFLSRYK 

        70         80         90        100        110        120 
DTINKIRDLR MKAEDYEVVK VIGRGAFGEV QLVRHKSTRK VYAMKLLSKF EMIKRSDSAF 

       130        140        150        160        170        180 
FWEERDIMAF ANSPWVVQLF YAFQDDRYLY MVMEYMPGGD LVNLMSNYDV PEKWARFYTA 

       190        200        210        220        230        240 
EVVLALDAIH SMGFIHRDVK PDNMLLDKSG HLKLADFGTC MKMNKEGMVR CDTAVGTPDY 

       250        260        270        280        290        300 
ISPEVLKSQG GDGYYGRECD WWSVGVFLYE MLVGDTPFYA DSLVGTYSKI MNHKNSLTFP 

       310        320        330        340        350        360 
DDNDISKEAK NLICAFLTDR EVRLGRNGVE EIKRHLFFKN DQWAWETLRD TVAPVVPDLS 

       370        380        390        400        410        420 
SDIDTSNFDD LEEDKGDEET FPIPKAFVGN QLPFVGFTYY SNRRYLPSAN ASENRSSSNV 

       430        440        450        460        470        480 
DKSLQESLQK TIYKLEEQLH NEMQLKDEME QKCRTSNLKL DKIMKELDEE GNQRRNLESA 

       490        500        510        520        530        540 
VSQIEKEKML LQHRINEYQR KVEQENEKRR NIENEVSTLK DQLEDLRKAS QTSQLANEKL 

       550        560        570        580        590        600 
TQLQKQLEEA NDLLRTESDT AVRLRKSHTE MSKSISQLES LNRELQERNR ILENSKSQAD 

       610        620        630        640        650        660 
KDYYQLQAVL EAERRDRGHD SEMIGDLQAR ITSLQEEVKH LKHNLERVEG ERKEAQDMLN 

       670        680        690        700        710        720 
HSEKEKNNLE IDLNYKLKSI QQRLEQEVNE HKVTKARLTD KHQSIEEAKS VAMCEMEKKL 

       730        740        750        760        770        780 
KEEREAREKA ENRVVETEKQ CSMLDVDLKQ SQQKLEHLTE NKERMEDEVK NLALQLEQES 

       790        800        810        820        830        840 
NKRLLLQNEL KTQAFEADNL KGLEKQMKQE INTLLEAKRL LEFELAQLTK QYRGNEGQMR 

       850        860        870        880        890        900 
ELQDQLEAEQ YFSTLYKTQV KELKEEIEEK NRENLRKIQE LQSEKETLST QLDLAETKAE 

       910        920        930        940        950        960 
SEQLARGILE EQYFELTQES KKAASRNRQE ITDKDHTVSR LEETNSVLTK DIEMLRKENE 

       970        980        990       1000       1010       1020 
ELNERMRTAE EEYKLKKEEE INNLKAAFEK NISTERTLKT QAVNKLAEIM NRKDFKIDRK 

      1030       1040       1050       1060       1070       1080 
KANTQDLRKK EKENRKLQLE LNQEREKFNQ MVVKHQKELN DMQAQLVEEC THRNELQMQL 

      1090       1100       1110       1120       1130       1140 
ASKESDIEQL RAKLLDLSDS TSVASFPSAD ETDGNLPESR IEGWLSVPNR GNIKRYGWKK 

      1150       1160       1170       1180       1190       1200 
QYVVVSSKKI LFYNDEQDKE QSSPSMVLDI DKLFHVRPVT QGDVYRAETE EIPKIFQILY 

      1210       1220       1230       1240       1250       1260 
ANEGECRKDI EVEPVQQGEK TNFQNHKGHE FIPTLYHFPA NCEACAKPLW HVFKPPPALE 

      1270       1280       1290       1300       1310       1320 
CRRCHVKCHR DHLDKKEDLI SPCKVSYDVT SARDMLLLAC SQDEQKKWVT HLVKKIPKNP 

      1330       1340       1350 
PSGFVRASPR TLSTRSTANQ SFRKVVKNTS GKTS 

« Hide

Isoform 2 [UniParc].

Checksum: 209CACFD07E756CF
Show »

FASTA1,353158,042

References

« Hide 'large scale' references
[1]"ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice."
Nakagawa O., Fujisawa K., Ishizaki T., Saito Y., Nakao K., Narumiya S.
FEBS Lett. 392:189-193(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Embryo and Heart.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-506 (ISOFORM 2).
Strain: FVB/N.
Tissue: Mammary gland.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 472-1354.
Strain: C57BL/6J.
Tissue: Heart and Liver.
[4]"ROCK-I regulates closure of the eyelids and ventral body wall by inducing assembly of actomyosin bundles."
Shimizu Y., Thumkeo D., Keel J., Ishizaki T., Oshima H., Oshima M., Noda Y., Matsumura F., Taketo M.M., Narumiya S.
J. Cell Biol. 168:941-953(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]"Integrin cytoplasmic domain-associated protein-1 (ICAP-1) interacts with the ROCK-I kinase at the plasma membrane."
Stroeken P.J., Alvarez B., Van Rheenen J., Wijnands Y.M., Geerts D., Jalink K., Roos E.
J. Cell. Physiol. 208:620-628(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITGB1BP1, SUBCELLULAR LOCATION.
[6]"Integrin Cytoplasmic domain-Associated Protein-1 (ICAP-1) promotes migration of myoblasts and affects focal adhesions."
Alvarez B., Stroeken P.J., Edel M.J., Roos E.
J. Cell. Physiol. 214:474-482(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITGB1BP1.
[7]"Identification of ROCK1 as an upstream activator of the JIP-3 to JNK signaling axis in response to UVB damage."
Ongusaha P.P., Qi H.H., Raj L., Kim Y.B., Aaronson S.A., Davis R.J., Shi Y., Liao J.K., Lee S.W.
Sci. Signal. 1:RA14-RA14(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Inhibition of Rho-dependent kinases ROCK I/II activates VEGF-driven retinal neovascularization and sprouting angiogenesis."
Kroll J., Epting D., Kern K., Dietz C.T., Feng Y., Hammes H.P., Wieland T., Augustin H.G.
Am. J. Physiol. 296:H893-H899(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"ROCK1 functions as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability."
Vemula S., Shi J., Hanneman P., Wei L., Kapur R.
Blood 115:1785-1796(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PTEN.
[10]"Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent fibronectin deposition."
Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.
J. Cell Biol. 194:307-322(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U58512 mRNA. Translation: AAC53132.1.
AK050269 mRNA. Translation: BAC34154.1. Different initiation.
AK085974 mRNA. Translation: BAC39581.1.
BC057154 mRNA. Translation: AAH57154.1. Sequence problems.
PIRS74244.
RefSeqNP_033097.1. NM_009071.2.
XP_006525788.1. XM_006525725.1.
UniGeneMm.6710.

3D structure databases

ProteinModelPortalP70335.
SMRP70335. Positions 6-402, 542-693, 946-1014, 1119-1288.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202950. 5 interactions.
IntActP70335. 4 interactions.
MINTMINT-4132852.

PTM databases

PhosphoSiteP70335.

Proteomic databases

PaxDbP70335.
PRIDEP70335.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000067947; ENSMUSP00000069549; ENSMUSG00000024290. [P70335-1]
GeneID19877.
KEGGmmu:19877.
UCSCuc008eaq.1. mouse. [P70335-1]

Organism-specific databases

CTD6093.
MGIMGI:107927. Rock1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117396.
HOGENOMHOG000017259.
HOVERGENHBG053111.
InParanoidP70335.
KOK04514.
OMAQIEKQCS.
OrthoDBEOG7DZ8J4.
PhylomeDBP70335.
TreeFamTF313551.

Gene expression databases

BgeeP70335.
GenevestigatorP70335.

Family and domain databases

Gene3D2.30.29.30. 2 hits.
InterProIPR000961. 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_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.
[Graphical view]
PANTHERPTHR22988:SF3. PTHR22988:SF3. 1 hit.
PfamPF02185. HR1. 1 hit.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
PF08912. Rho_Binding. 1 hit.
[Graphical view]
PIRSFPIRSF037568. Rho_kinase. 1 hit.
SMARTSM00109. C1. 1 hit.
SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSROCK1. mouse.
NextBio297366.
PROP70335.
SOURCESearch...

Entry information

Entry nameROCK1_MOUSE
AccessionPrimary (citable) accession number: P70335
Secondary accession number(s): Q8C3G4, Q8C7H0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot