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Protein

Serine/threonine-protein kinase MRCK alpha

Gene

Cdc42bpa

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12C and MYL9/MLC2. In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. Phosphorylates: PPP1R12A, LIMK1 and LIMK2. May play a role in TFRC-mediated iron uptake.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Mg2+1 Publication

Enzyme regulationi

Maintained in an inactive, closed conformation by an interaction between the kinase domain and the negative autoregulatory C-terminal coiled-coil region. Agonist binding to the phorbol ester binding site disrupts this, releasing the kinase domain to allow N-terminus-mediated dimerization and kinase activation by transautophosphorylation (By similarity). Inhibited by chelerythrine chloride.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061ATPPROSITE-ProRule annotation1 Publication
Active sitei201 – 2011Proton acceptorPROSITE-ProRule annotationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi83 – 919ATPPROSITE-ProRule annotationBy similarity
Zinc fingeri1012 – 106251Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • actomyosin structure organization Source: UniProtKB
  • cell migration Source: UniProtKB
  • cytoskeleton organization Source: RGD
  • intracellular signal transduction Source: InterPro
  • protein phosphorylation Source: UniProtKB
  • regulation of small GTPase mediated signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase MRCK alpha (EC:2.7.11.1)
Alternative name(s):
CDC42-binding protein kinase alpha
Myotonic dystrophy kinase-related CDC42-binding kinase alpha
Short name:
MRCK alpha
Short name:
Myotonic dystrophy protein kinase-like alpha
Gene namesi
Name:Cdc42bpaBy similarity
Synonyms:Pk428Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621406. Cdc42bpa.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: Displays a dispersed punctate distribution and concentrates along the cell periphery, especially at the leading edge and cell-cell junction. This concentration is PH-domain dependent.

GO - Cellular componenti

  • actomyosin Source: UniProtKB
  • cell-cell junction Source: UniProtKB
  • cell leading edge Source: UniProtKB
  • cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi106 – 1061K → A: Loss of kinase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17321732Serine/threonine-protein kinase MRCK alphaPRO_0000086393Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei222 – 2221Phosphoserine; by autocatalysisBy similarity
Modified residuei234 – 2341Phosphoserine; by autocatalysisBy similarity
Modified residuei240 – 2401Phosphothreonine; by autocatalysisBy similarity
Modified residuei1127 – 11271PhosphoserineCombined sources
Modified residuei1545 – 15451PhosphoserineBy similarity
Modified residuei1651 – 16511PhosphoserineCombined sources
Modified residuei1669 – 16691PhosphoserineBy similarity
Modified residuei1693 – 16931PhosphoserineBy similarity
Modified residuei1719 – 17191PhosphoserineBy similarity
Modified residuei1721 – 17211PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO54874.
PRIDEiO54874.

PTM databases

iPTMnetiO54874.
PhosphoSiteiO54874.

Expressioni

Tissue specificityi

Highly expressed in the brain and lung and present in lower levels in all other tissues tested.1 Publication

Interactioni

Subunit structurei

Homodimer and homotetramer via the coiled coil regions. Interacts tightly with GTP-bound but not GDP-bound CDC42. Forms a tripartite complex with MYO18A and LURAP1 with the latter acting as an adapter connecting CDC42BPA and MYO18A. LURAP1 binding results in activation of CDC42BPA by abolition of its negative autoregulation.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-689253,EBI-689253
Lurap1D4A8G38EBI-689253,EBI-2015467

GO - Molecular functioni

  • identical protein binding Source: UniProtKB

Protein-protein interaction databases

IntActiO54874. 7 interactions.
STRINGi10116.ENSRNOP00000003837.

Structurei

Secondary structure

1
1732
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1614Combined sources
Helixi18 – 203Combined sources
Turni21 – 233Combined sources
Helixi28 – 4316Combined sources
Turni46 – 494Combined sources
Helixi51 – 7020Combined sources
Helixi74 – 763Combined sources
Beta strandi77 – 859Combined sources
Beta strandi87 – 9610Combined sources
Turni97 – 993Combined sources
Beta strandi102 – 1098Combined sources
Helixi110 – 1156Combined sources
Turni116 – 1194Combined sources
Helixi122 – 13110Combined sources
Turni134 – 1363Combined sources
Beta strandi140 – 1456Combined sources
Beta strandi147 – 1548Combined sources
Helixi162 – 1676Combined sources
Turni168 – 1714Combined sources
Helixi175 – 19420Combined sources
Helixi204 – 2063Combined sources
Beta strandi207 – 2093Combined sources
Beta strandi215 – 2173Combined sources
Helixi241 – 2433Combined sources
Helixi246 – 2538Combined sources
Helixi262 – 27716Combined sources
Helixi287 – 2959Combined sources
Helixi297 – 3004Combined sources
Helixi312 – 3198Combined sources
Helixi325 – 3273Combined sources
Turni329 – 3346Combined sources
Helixi335 – 3384Combined sources
Helixi341 – 3433Combined sources
Turni348 – 3503Combined sources
Helixi351 – 3533Combined sources
Helixi397 – 3993Combined sources
Beta strandi404 – 4074Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AW2X-ray1.70A2-424[»]
ProteinModelPortaliO54874.
SMRiO54874. Positions 11-409.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini77 – 343267Protein kinasePROSITE-ProRule annotation1 PublicationAdd
BLAST
Domaini344 – 41471AGC-kinase C-terminalAdd
BLAST
Domaini1082 – 1201120PHPROSITE-ProRule annotationAdd
BLAST
Domaini1227 – 1499273CNHPROSITE-ProRule annotationAdd
BLAST
Domaini1571 – 158414CRIBPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili437 – 670234Sequence analysisAdd
BLAST
Coiled coili713 – 820108Sequence analysisAdd
BLAST
Coiled coili880 – 94364Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 CNH domain.PROSITE-ProRule annotation
Contains 1 CRIB domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1012 – 106251Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG0612. Eukaryota.
ENOG410XR1Q. LUCA.
HOGENOMiHOG000294133.
HOVERGENiHBG055933.
InParanoidiO54874.
KOiK16307.
PhylomeDBiO54874.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR001180. CNH_dom.
IPR000095. CRIB_dom.
IPR031597. KELK.
IPR011009. Kinase-like_dom.
IPR014930. Myotonic_dystrophy_kinase_coil.
IPR002219. PE/DAG-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR026611. Ser/Thr_kinase_MRCK_alpha.
[Graphical view]
PANTHERiPTHR22988:SF31. PTHR22988:SF31. 2 hits.
PfamiPF00130. C1_1. 1 hit.
PF00780. CNH. 1 hit.
PF08826. DMPK_coil. 1 hit.
PF15796. KELK. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
ProDomiPD011252. Myotonic_dystrophy_kinase_coil. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00109. C1. 1 hit.
SM00036. CNH. 1 hit.
SM00285. PBD. 1 hit.
SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50219. CNH. 1 hit.
PS50108. CRIB. 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.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O54874-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSGEVRLRQL EQFILDGPAQ TNGQCFSVET LLDILICLYD ECNNSPLRRE
60 70 80 90 100
KNILEYLEWA KPFTSKVKQM RLHREDFEIL KVIGRGAFGE VAVVKLKNAD
110 120 130 140 150
KVFAMKILNK WEMLKRAETA CFREERDVLV NGDSKWITTL HYAFQDDNNL
160 170 180 190 200
YLVMDYYVGG DLLTLLSKFE DRLPEEMARF YLAEMVIAID SVHQLHYVHR
210 220 230 240 250
DIKPDNILMD MNGHIRLADF GSCLKLMEDG TVQSSVAVGT PDYISPEILQ
260 270 280 290 300
AMEDGKGRYG PECDWWSLGV CMYEMLYGET PFYAESLVET YGKIMNHKER
310 320 330 340 350
FQFPTQVTDV SENAKDLIRR LICSREHRLG QNGIEDFKKH PFFSGIDWDN
360 370 380 390 400
IRNCEAPYIP EVSSPTDTSN FDVDDDCLKN SETMPPPTHT AFSGHHLPFV
410 420 430 440 450
GFTYTSSCVL SDRSCLRVTA GPTSLDLDVN VQRTLDNNLA TEAYERRIKR
460 470 480 490 500
LEQEKLELTR KLQESTQTVQ ALQYSTVDGP LTASKDLEIK SLKEEIEKLR
510 520 530 540 550
KQVAEVNHLE QQLEEANSVR RELDDAFRQI KAFEKQIKTL QQEREELNKE
560 570 580 590 600
LVQASERLKN QSKELKDAHC QRKLAMQEFM EINERLTELH TQKQKLARHV
610 620 630 640 650
RDKEEEVDLV MQKAESLRQE LRRAERAKKE LEVHTEALIA EASKDRKLRE
660 670 680 690 700
QSRHYSKQLE NELEGLKQKQ ISYSPGICSI EHQQEITKLK TDLEKKSIFY
710 720 730 740 750
EEEISKREGI HASEIKNLKK ELHDSEGQQL ALNKEIMVLK DKLEKTRRES
760 770 780 790 800
QSEREEFENE FKQQYEREKV LLTEENKKLT SELDKLTSLY ESLSLRNQHL
810 820 830 840 850
EEEVKDLADK KESVAHWEAQ ITEIIQWVSD EKDARGYLQA LASKMTEELE
860 870 880 890 900
ALRNSSLGTR ATDMPWKMRR FAKLDMSARL ELQSALDAEI RAKQAIQEEL
910 920 930 940 950
NKVKASNIIT ECKLKDSEKK NLELLSEIEQ LIKDTEELRS EKGVEHRDSQ
960 970 980 990 1000
HSFLAFLNTP TDALDQFERS PSCTPAGKGR RIADSAPLPV HTPTLRKKGC
1010 1020 1030 1040 1050
PASAGFPPKR KTHQFFVKSF TAPTKCHQCT SLMVGLIRQG CSCEVCGFSC
1060 1070 1080 1090 1100
HITCVNKAPT TCPVPPEQTK GPLGIDPQKG VGTAYEGHVR IPKPAGVKKG
1110 1120 1130 1140 1150
WQRALAVVCD FKLFLYDIAE GKASQPSSVI SQVIDMRDEE FSVSSVLASD
1160 1170 1180 1190 1200
VIHASRKDIP CIFRVTASQL SAPSDKCSIL MLADSETERS KWVGVLSELH
1210 1220 1230 1240 1250
KVLKKNKFRD RSVYVPKEAY DSTLPLIKTT QAAAIIDHER VALGNEEGLF
1260 1270 1280 1290 1300
VVHVTKDEII RVGDNKKIHQ IELIPSDQLV AVISGRNRHV RLFPMSALDG
1310 1320 1330 1340 1350
RETDFYKLAE TKGCQTIAAG KVRHGALSCL CVAMKRQVLC YELFQSKTRH
1360 1370 1380 1390 1400
RKFKEIQVPC NVQWMAIFSE HLCVGFQSGF LRYPLNGEGS PCNMLHSNDH
1410 1420 1430 1440 1450
TLAFITHQPM DAICAVEISN KEYLLCFSSI GIYTDCQGRR SRQQELMWPA
1460 1470 1480 1490 1500
NPSSCCYNAP YLSIYSENAV DIFDVNSMEW IQTLPLKKVR PLNTEGSLNL
1510 1520 1530 1540 1550
LGLETIRLIY FKNKMAEGDE LVVPETSDNS RKQMVRNINN KRRYSFRVPE
1560 1570 1580 1590 1600
EERMQQRREM LRDPEMRNKL ISNPTNFNHI AHMGPGDGIQ ILKDLPMNPR
1610 1620 1630 1640 1650
PQESRTVFSG SVSIPSITKS RPEPGRSMSA SSGLSARSSA QNGSALKREF
1660 1670 1680 1690 1700
SGGSYNTKRQ PMPSPSEGSL SSGGVDQGSD APVRDYDGED SDSPRHSTAS
1710 1720 1730
NSSNLSSPPS PVSPRKTKSL SLESTDRGSW DP
Length:1,732
Mass (Da):197,064
Last modified:June 1, 1998 - v1
Checksum:i65F62F7872ACCD3B
GO
Isoform 2 (identifier: O54874-2)

Sequence is not available
Length:
Mass (Da):
Isoform 3 (identifier: O54874-3)

Sequence is not available
Length:
Mass (Da):
Isoform 4 (identifier: O54874-4)

Sequence is not available
Length:
Mass (Da):
Isoform 5 (identifier: O54874-5)

Sequence is not available
Length:
Mass (Da):
Isoform 6 (identifier: O54874-6)

Sequence is not available
Length:
Mass (Da):

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF021935 mRNA. Translation: AAC02941.1.
PIRiT14039.
RefSeqiNP_446109.1. NM_053657.1. [O54874-1]
UniGeneiRn.10871.

Genome annotation databases

GeneIDi114116.
KEGGirno:114116.
UCSCiRGD:621406. rat. [O54874-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF021935 mRNA. Translation: AAC02941.1.
PIRiT14039.
RefSeqiNP_446109.1. NM_053657.1. [O54874-1]
UniGeneiRn.10871.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AW2X-ray1.70A2-424[»]
ProteinModelPortaliO54874.
SMRiO54874. Positions 11-409.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO54874. 7 interactions.
STRINGi10116.ENSRNOP00000003837.

PTM databases

iPTMnetiO54874.
PhosphoSiteiO54874.

Proteomic databases

PaxDbiO54874.
PRIDEiO54874.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi114116.
KEGGirno:114116.
UCSCiRGD:621406. rat. [O54874-1]

Organism-specific databases

CTDi8476.
RGDi621406. Cdc42bpa.

Phylogenomic databases

eggNOGiKOG0612. Eukaryota.
ENOG410XR1Q. LUCA.
HOGENOMiHOG000294133.
HOVERGENiHBG055933.
InParanoidiO54874.
KOiK16307.
PhylomeDBiO54874.

Miscellaneous databases

NextBioi618317.
PROiO54874.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR001180. CNH_dom.
IPR000095. CRIB_dom.
IPR031597. KELK.
IPR011009. Kinase-like_dom.
IPR014930. Myotonic_dystrophy_kinase_coil.
IPR002219. PE/DAG-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR026611. Ser/Thr_kinase_MRCK_alpha.
[Graphical view]
PANTHERiPTHR22988:SF31. PTHR22988:SF31. 2 hits.
PfamiPF00130. C1_1. 1 hit.
PF00780. CNH. 1 hit.
PF08826. DMPK_coil. 1 hit.
PF15796. KELK. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
ProDomiPD011252. Myotonic_dystrophy_kinase_coil. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00109. C1. 1 hit.
SM00036. CNH. 1 hit.
SM00285. PBD. 1 hit.
SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50219. CNH. 1 hit.
PS50108. CRIB. 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.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42 effector in promoting cytoskeletal reorganization."
    Leung T., Chen X.-Q., Tan I., Manser E., Lim L.
    Mol. Cell. Biol. 18:130-140(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-106.
    Tissue: BrainImported.
  2. "Intermolecular and intramolecular interactions regulate catalytic activity of myotonic dystrophy kinase-related Cdc42-binding kinase alpha."
    Tan I., Seow K.T., Lim L., Leung T.
    Mol. Cell. Biol. 21:2767-2778(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: OLIGOMERIZATION.
  3. "Genomic organization of human myotonic dystrophy kinase-related Cdc42-binding kinase alpha reveals multiple alternative splicing and functional diversity."
    Tan I., Cheong A., Lim L., Leung T.
    Gene 304:107-115(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  4. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "A tripartite complex containing MRCK modulates lamellar actomyosin retrograde flow."
    Tan I., Yong J., Dong J.M., Lim L., Leung T.
    Cell 135:123-136(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MYO18A AND LURAP1.
  6. "Chelerythrine perturbs lamellar actomyosin filaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase."
    Tan I., Lai J., Yong J., Li S.F., Leung T.
    FEBS Lett. 585:1260-1268(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF PPP1R12A AND MYL9/MLC2, ENZYME REGULATION.
  7. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1651 AND SER-1721, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMRCKA_RAT
AccessioniPrimary (citable) accession number: O54874
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: June 1, 1998
Last modified: May 11, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.