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Q5VT25 (MRCKA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Serine/threonine-protein kinase MRCK alpha

EC=2.7.11.1
Alternative name(s):
CDC42-binding protein kinase alpha
DMPK-like alpha
Myotonic dystrophy kinase-related CDC42-binding kinase alpha
Short name=MRCK alpha
Short name=Myotonic dystrophy protein kinase-like alpha
Gene names
Name:CDC42BPA
Synonyms:KIAA0451
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1732 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5 Ref.8 Ref.9 Ref.10 Ref.13 Ref.15 Ref.17

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.5

Cofactor

Magnesium. Ref.5

Enzyme regulation

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. Inhibited by chelerythrine chloride. Ref.11 Ref.17

Subunit structure

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. Ref.8 Ref.11 Ref.13

Subcellular location

Cytoplasm By similarity. 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 By similarity.

Tissue specificity

Abundant in the heart, brain, skeletal muscle, kidney, and pancreas, with little or no expression in the lung and liver. Ref.5

Induction

Regulated by cellular iron levels. Ref.11 Ref.15 Ref.17

Sequence similarities

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

Contains 1 AGC-kinase C-terminal domain.

Contains 1 CNH domain.

Contains 1 CRIB domain.

Contains 1 PH domain.

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

Contains 1 protein kinase domain.

Sequence caution

The sequence BAD92205.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Zinc-finger
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton reorganization

Inferred from direct assay Ref.8. Source: UniProtKB

actomyosin structure organization

Inferred from mutant phenotype Ref.13. Source: UniProtKB

cell migration

Inferred from mutant phenotype Ref.13. Source: UniProtKB

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

microtubule cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

nuclear migration

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay Ref.5. Source: UniProtKB

   Cellular_componentactomyosin

Inferred from direct assay Ref.13. Source: UniProtKB

cell leading edge

Inferred from sequence or structural similarity. Source: UniProtKB

cell-cell junction

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

   Molecular_functionATP binding

Inferred from direct assay Ref.5. Source: UniProtKB

identical protein binding

Inferred from physical interaction Ref.11PubMed 23414517. Source: IntAct

magnesium ion binding

Inferred from direct assay Ref.5. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.10Ref.9Ref.17Ref.5. Source: UniProtKB

small GTPase regulator activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself9EBI-689171,EBI-689171
CDC42P609535EBI-689171,EBI-81752

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist. They arise due to a two alternate splice sites, the first site involves splicing of exons 21-24 while the second site involves exons 36-40.
Isoform 1 (identifier: Q5VT25-1)

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.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q5VT25-2)

The sequence of this isoform differs from the canonical sequence as follows:
     969-969: R → TDPVENTYVWNPSVKFHIQSRST
     973-981: CTPASKGRR → TSSEAEPVK
Note: No experimental confirmation available.
Isoform 3 Ref.1 (identifier: Q5VT25-3)

The sequence of this isoform differs from the canonical sequence as follows:
     550-630: Missing.
     969-981: Missing.
Isoform 4 Ref.4 (identifier: Q5VT25-4)

The sequence of this isoform differs from the canonical sequence as follows:
     969-1009: Missing.
Note: No experimental confirmation available.
Isoform 5 Ref.1 (identifier: Q5VT25-5)

The sequence of this isoform differs from the canonical sequence as follows:
     969-981: Missing.
Isoform 6 (identifier: Q5VT25-6)

The sequence of this isoform differs from the canonical sequence as follows:
     969-981: Missing.
     1597-1597: M → MPGFPYPSPHHHSGLISSPINFEHIYHMTVNSAEKFLSPDSINPEYSPSLRSVPGTPSFMTLR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17321732Serine/threonine-protein kinase MRCK alpha
PRO_0000086392

Regions

Domain77 – 343267Protein kinase Ref.5
Domain344 – 41471AGC-kinase C-terminal
Domain1082 – 1201120PH
Domain1227 – 1499273CNH
Domain1571 – 158414CRIB
Nucleotide binding83 – 919ATP By similarity UniProtKB P54265
Zinc finger1012 – 106251Phorbol-ester/DAG-type
Coiled coil437 – 820384 Potential
Coiled coil880 – 94364 Potential

Sites

Active site2011Proton acceptor By similarity UniProtKB P54265
Binding site1061ATP Ref.11

Amino acid modifications

Modified residue2221Phosphoserine; by autocatalysis Ref.11
Modified residue2341Phosphoserine; by autocatalysis Ref.11
Modified residue2401Phosphothreonine; by autocatalysis Ref.11
Modified residue11271Phosphoserine By similarity
Modified residue15451Phosphoserine Ref.14
Modified residue16511Phosphoserine Ref.18
Modified residue17191Phosphoserine Ref.14
Modified residue17211Phosphoserine Ref.14

Natural variations

Alternative sequence550 – 63081Missing in isoform 3. Ref.1
VSP_051859
Alternative sequence969 – 100941Missing in isoform 4. Ref.4
VSP_051862
Alternative sequence969 – 98113Missing in isoform 3, isoform 5 and isoform 6. Ref.1
VSP_051860
Alternative sequence9691R → TDPVENTYVWNPSVKFHIQS RST in isoform 2.
VSP_051861
Alternative sequence973 – 9819CTPASKGRR → TSSEAEPVK in isoform 2.
VSP_051863
Alternative sequence15971M → MPGFPYPSPHHHSGLISSPI NFEHIYHMTVNSAEKFLSPD SINPEYSPSLRSVPGTPSFM TLR in isoform 6.
VSP_035286
Natural variant501E → K in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.19
VAR_040830
Natural variant2311T → M. Ref.19
Corresponds to variant rs34614709 [ dbSNP | Ensembl ].
VAR_040831
Natural variant5371I → T. Ref.19
Corresponds to variant rs56364976 [ dbSNP | Ensembl ].
VAR_040832
Natural variant7801T → M. Ref.19
Corresponds to variant rs56119119 [ dbSNP | Ensembl ].
VAR_045583
Natural variant7901Y → C. Ref.19
Corresponds to variant rs34943764 [ dbSNP | Ensembl ].
VAR_045584
Natural variant11481A → T. Ref.19
VAR_045585
Natural variant12111R → H. Ref.19
VAR_045586
Natural variant13171V → I. Ref.3 Ref.19
Corresponds to variant rs1929860 [ dbSNP | Ensembl ].
VAR_045587
Natural variant14181I → K. Ref.19
VAR_040833
Natural variant14691A → V. Ref.19
Corresponds to variant rs55687355 [ dbSNP | Ensembl ].
VAR_045588
Natural variant16181T → A. Ref.19
Corresponds to variant rs2297417 [ dbSNP | Ensembl ].
VAR_045589
Natural variant16991A → V.
Corresponds to variant rs2802269 [ dbSNP | Ensembl ].
VAR_045590
Natural variant17121A → V. Ref.2 Ref.3 Ref.6
Corresponds to variant rs2802269 [ dbSNP | Ensembl ].
VAR_057104

Experimental info

Mutagenesis1061K → A: Loss of kinase activity. Ref.11
Mutagenesis2221S → L: Increase in autophosphorylation but not kinase activity. Ref.11
Mutagenesis2341S → A: Loss of autophosphorylation and kinase activity. Ref.11
Mutagenesis2401T → A: Loss of autophosphorylation and kinase activity. Ref.11
Mutagenesis4031T → A: Loss of autophosphorylation and kinase activity. Ref.11
Mutagenesis15791H → A: Loss of CDC42 binding; when associated with A-1582. Ref.8
Mutagenesis15821H → A: Loss of CDC42 binding; when associated with A-1579. Ref.8
Sequence conflict251C → Y in AAB37126. Ref.5
Sequence conflict8091D → N in CAI46252. Ref.3
Sequence conflict15211L → V Ref.8
Sequence conflict16881G → K in BAA32296. Ref.6

Sequences

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

Last modified December 7, 2004. Version 1.
Checksum: 48B10F81B5405A0A

FASTA1,732197,307
        10         20         30         40         50         60 
MSGEVRLRQL EQFILDGPAQ TNGQCFSVET LLDILICLYD ECNNSPLRRE KNILEYLEWA 

        70         80         90        100        110        120 
KPFTSKVKQM RLHREDFEIL KVIGRGAFGE VAVVKLKNAD KVFAMKILNK WEMLKRAETA 

       130        140        150        160        170        180 
CFREERDVLV NGDNKWITTL HYAFQDDNNL YLVMDYYVGG DLLTLLSKFE DRLPEDMARF 

       190        200        210        220        230        240 
YLAEMVIAID SVHQLHYVHR DIKPDNILMD MNGHIRLADF GSCLKLMEDG TVQSSVAVGT 

       250        260        270        280        290        300 
PDYISPEILQ AMEDGKGRYG PECDWWSLGV CMYEMLYGET PFYAESLVET YGKIMNHKER 

       310        320        330        340        350        360 
FQFPAQVTDV SENAKDLIRR LICSREHRLG QNGIEDFKKH PFFSGIDWDN IRNCEAPYIP 

       370        380        390        400        410        420 
EVSSPTDTSN FDVDDDCLKN SETMPPPTHT AFSGHHLPFV GFTYTSSCVL SDRSCLRVTA 

       430        440        450        460        470        480 
GPTSLDLDVN VQRTLDNNLA TEAYERRIKR LEQEKLELSR KLQESTQTVQ ALQYSTVDGP 

       490        500        510        520        530        540 
LTASKDLEIK NLKEEIEKLR KQVTESSHLE QQLEEANAVR QELDDAFRQI KAYEKQIKTL 

       550        560        570        580        590        600 
QQEREDLNKE LVQASERLKN QSKELKDAHC QRKLAMQEFM EINERLTELH TQKQKLARHV 

       610        620        630        640        650        660 
RDKEEEVDLV MQKVESLRQE LRRTERAKKE LEVHTEALAA EASKDRKLRE QSEHYSKQLE 

       670        680        690        700        710        720 
NELEGLKQKQ ISYSPGVCSI EHQQEITKLK TDLEKKSIFY EEELSKREGI HANEIKNLKK 

       730        740        750        760        770        780 
ELHDSEGQQL ALNKEIMILK DKLEKTRRES QSEREEFESE FKQQYEREKV LLTEENKKLT 

       790        800        810        820        830        840 
SELDKLTTLY ENLSIHNQQL EEEVKDLADK KESVAHWEAQ ITEIIQWVSD EKDARGYLQA 

       850        860        870        880        890        900 
LASKMTEELE ALRNSSLGTR ATDMPWKMRR FAKLDMSARL ELQSALDAEI RAKQAIQEEL 

       910        920        930        940        950        960 
NKVKASNIIT ECKLKDSEKK NLELLSEIEQ LIKDTEELRS EKGIEHQDSQ HSFLAFLNTP 

       970        980        990       1000       1010       1020 
TDALDQFERS PSCTPASKGR RTVDSTPLSV HTPTLRKKGC PGSTGFPPKR KTHQFFVKSF 

      1030       1040       1050       1060       1070       1080 
TTPTKCHQCT SLMVGLIRQG CSCEVCGFSC HITCVNKAPT TCPVPPEQTK GPLGIDPQKG 

      1090       1100       1110       1120       1130       1140 
IGTAYEGHVR IPKPAGVKKG WQRALAIVCD FKLFLYDIAE GKASQPSVVI SQVIDMRDEE 

      1150       1160       1170       1180       1190       1200 
FSVSSVLASD VIHASRKDIP CIFRVTASQL SASNNKCSIL MLADTENEKN KWVGVLSELH 

      1210       1220       1230       1240       1250       1260 
KILKKNKFRD RSVYVPKEAY DSTLPLIKTT QAAAIIDHER IALGNEEGLF VVHVTKDEII 

      1270       1280       1290       1300       1310       1320 
RVGDNKKIHQ IELIPNDQLV AVISGRNRHV RLFPMSALDG RETDFYKLSE TKGCQTVTSG 

      1330       1340       1350       1360       1370       1380 
KVRHGALTCL CVAMKRQVLC YELFQSKTRH RKFKEIQVPY NVQWMAIFSE QLCVGFQSGF 

      1390       1400       1410       1420       1430       1440 
LRYPLNGEGN PYSMLHSNDH TLSFIAHQPM DAICAVEISS KEYLLCFNSI GIYTDCQGRR 

      1450       1460       1470       1480       1490       1500 
SRQQELMWPA NPSSCCYNAP YLSVYSENAV DIFDVNSMEW IQTLPLKKVR PLNNEGSLNL 

      1510       1520       1530       1540       1550       1560 
LGLETIRLIY FKNKMAEGDE LVVPETSDNS RKQMVRNINN KRRYSFRVPE EERMQQRREM 

      1570       1580       1590       1600       1610       1620 
LRDPEMRNKL ISNPTNFNHI AHMGPGDGIQ ILKDLPMNPR PQESRTVFSG SVSIPSITKS 

      1630       1640       1650       1660       1670       1680 
RPEPGRSMSA SSGLSARSSA QNGSALKREF SGGSYSAKRQ PMPSPSEGSL SSGGMDQGSD 

      1690       1700       1710       1720       1730 
APARDFDGED SDSPRHSTAS NSSNLSSPPS PASPRKTKSL SLESTDRGSW DP 

« Hide

Isoform 2 [UniParc].

Checksum: F1CC5CC1ED23B388
Show »

FASTA1,754199,811
Isoform 3 [UniParc].

Checksum: 7783E19090B345F7
Show »

FASTA1,638186,113
Isoform 4 [UniParc].

Checksum: 28E904E222CFFEC5
Show »

FASTA1,691193,031
Isoform 5 [UniParc].

Checksum: DBB15FA879AAC871
Show »

FASTA1,719195,922
Isoform 6 [UniParc].

Checksum: 979DA0EF4F17F9DF
Show »

FASTA1,781202,812

References

« Hide 'large scale' references
[1]"Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and cell invasion."
Wilkinson S., Paterson H.F., Marshall C.J.
Nat. Cell Biol. 7:255-261(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 5), FUNCTION.
Tissue: Colon.
[2]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT VAL-1712.
Tissue: Brain.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS ILE-1317 AND VAL-1712.
Tissue: Testis.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Cloning and chromosomal location of a novel member of the myotonic dystrophy family of protein kinases."
Zhao Y., Loyer P., Li H., Valentine V., Kidd V., Kraft A.S.
J. Biol. Chem. 272:10013-10020(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-496, FUNCTION, TISSUE SPECIFICITY.
Tissue: Mammary gland.
[6]"Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 799-1732 (ISOFORM 6), VARIANT VAL-1712.
Tissue: Brain.
[7]Ohara O.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[8]"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] OF 1521-1644, FUNCTION, INTERACTION WITH CDC42, MUTAGENESIS OF HIS-1579 AND HIS-1582.
Tissue: Brain.
[9]"Phosphorylation of a novel myosin binding subunit of protein phosphatase 1 reveals a conserved mechanism in the regulation of actin cytoskeleton."
Tan I., Ng C.H., Lim L., Leung T.
J. Biol. Chem. 276:21209-21216(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF PPP1R12C.
[10]"Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase alpha."
Sumi T., Matsumoto K., Shibuya A., Nakamura T.
J. Biol. Chem. 276:23092-23096(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF LIMK1 AND LIMK2.
[11]"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: ENZYME REGULATION, OLIGOMERIZATION, PHOSPHORYLATION AT SER-222; SER-234 AND THR-240, MUTAGENESIS OF LYS-106; SER-222; SER-234; THR-240 AND THR-403.
[12]"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.
[13]"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 LURAP1 AND MYO18A.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1545; SER-1719 AND SER-1721, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Human MRCKalpha is regulated by cellular iron levels and interferes with transferrin iron uptake."
Cmejla R., Ptackova P., Petrak J., Savvulidi F., Cerny J., Sebesta O., Vyoral D.
Biochem. Biophys. Res. Commun. 395:163-167(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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.
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1651, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-50; MET-231; THR-537; MET-780; CYS-790; THR-1148; HIS-1211; ILE-1317; LYS-1418; VAL-1469 AND ALA-1618.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ518975 mRNA. Translation: CAD57745.1.
AJ518976 mRNA. Translation: CAD57746.1.
AB208968 mRNA. Translation: BAD92205.1. Different initiation.
CR933723 mRNA. Translation: CAI46252.1.
AL353689 Genomic DNA. Translation: CAI19113.1.
AL451047, AL353689, AL627308 Genomic DNA. Translation: CAH71184.1.
AL451047, AL627308, AL353689 Genomic DNA. Translation: CAH71185.1.
AL627308, AL353689, AL451047 Genomic DNA. Translation: CAH71336.1.
AL627308, AL353689, AL451047 Genomic DNA. Translation: CAH71337.1.
AL353689, AL451047, AL627308 Genomic DNA. Translation: CAI19108.1.
AL451047, AL353689, AL627308 Genomic DNA. Translation: CAH71183.1.
AL627308, AL353689, AL451047 Genomic DNA. Translation: CAH71338.1.
AL353689, AL627308, AL451047 Genomic DNA. Translation: CAI19109.1.
AL353689, AL451047, AL627308 Genomic DNA. Translation: CAI19110.1.
AB007920 mRNA. Translation: BAA32296.2.
U59305 mRNA. Translation: AAB37126.1.
RefSeqNP_003598.2. NM_003607.3.
NP_055641.3. NM_014826.4.
XP_005273378.1. XM_005273321.1.
XP_005273379.1. XM_005273322.1.
XP_005273381.1. XM_005273324.1.
UniGeneHs.35433.

3D structure databases

ProteinModelPortalQ5VT25.
SMRQ5VT25. Positions 2-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114051. 4 interactions.
IntActQ5VT25. 7 interactions.

Chemistry

BindingDBQ5VT25.
ChEMBLCHEMBL4516.
GuidetoPHARMACOLOGY1507.

PTM databases

PhosphoSiteQ5VT25.

Polymorphism databases

DMDM74746874.

Proteomic databases

PaxDbQ5VT25.
PRIDEQ5VT25.

Protocols and materials databases

DNASU8476.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000334218; ENSP00000335341; ENSG00000143776. [Q5VT25-6]
ENST00000366764; ENSP00000355726; ENSG00000143776. [Q5VT25-4]
ENST00000366765; ENSP00000355727; ENSG00000143776. [Q5VT25-1]
ENST00000366766; ENSP00000355728; ENSG00000143776. [Q5VT25-2]
ENST00000366767; ENSP00000355729; ENSG00000143776. [Q5VT25-3]
ENST00000366769; ENSP00000355731; ENSG00000143776. [Q5VT25-5]
GeneID8476.
KEGGhsa:8476.
UCSCuc001hqr.3. human. [Q5VT25-5]
uc001hqs.3. human. [Q5VT25-3]
uc009xes.3. human. [Q5VT25-4]

Organism-specific databases

CTD8476.
GeneCardsGC01M227177.
H-InvDBHIX0001650.
HGNCHGNC:1737. CDC42BPA.
MIM603412. gene.
neXtProtNX_Q5VT25.
PharmGKBPA26267.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG055933.
KOK16307.
OMAKKGCPGS.
OrthoDBEOG7F511X.
PhylomeDBQ5VT25.
TreeFamTF313551.

Enzyme and pathway databases

SignaLinkQ5VT25.

Gene expression databases

ArrayExpressQ5VT25.
BgeeQ5VT25.
GenevestigatorQ5VT25.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR001180. Citron.
IPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR014930. Myotonic_dystrophy_kinase_coil.
IPR017892. Pkinase_C.
IPR001849. Pleckstrin_homology.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR026611. Ser/Thr_kinase_MRCK.
[Graphical view]
PANTHERPTHR22988:SF2. PTHR22988:SF2. 1 hit.
PfamPF00130. C1_1. 1 hit.
PF00780. CNH. 1 hit.
PF08826. DMPK_coil. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
ProDomPD011252. Myotonic_dystrophy_kinase_coil. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00109. 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]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51285. 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]
ProtoNetSearch...

Other

ChiTaRSCDC42BPA. human.
GeneWikiCDC42BPA.
GenomeRNAi8476.
NextBio31715.
PROQ5VT25.
SOURCESearch...

Entry information

Entry nameMRCKA_HUMAN
AccessionPrimary (citable) accession number: Q5VT25
Secondary accession number(s): O75039 expand/collapse secondary AC list , Q59GZ1, Q5H9N9, Q5T797, Q5VT26, Q5VT27, Q86XX2, Q86XX3, Q99646
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: December 7, 2004
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM