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Q5VT25

- MRCKA_HUMAN

UniProt

Q5VT25 - MRCKA_HUMAN

Protein

Serine/threonine-protein kinase MRCK alpha

Gene

CDC42BPA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (07 Dec 2004)
      Previous versions | rss
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    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.8 Publications

    Catalytic activityi

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

    Cofactori

    Magnesium.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. Inhibited by chelerythrine chloride.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei106 – 1061ATP1 PublicationPROSITE-ProRule annotation
    Active sitei201 – 2011Proton acceptorBy similarityPROSITE-ProRule annotation

    Regions

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. identical protein binding Source: IntAct
    3. magnesium ion binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. protein serine/threonine kinase activity Source: UniProtKB
    6. small GTPase regulator activity Source: InterPro

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: UniProtKB
    2. actomyosin structure organization Source: UniProtKB
    3. cell migration Source: UniProtKB
    4. intracellular signal transduction Source: InterPro
    5. microtubule cytoskeleton organization Source: Ensembl
    6. nuclear migration Source: Ensembl
    7. protein phosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    SignaLinkiQ5VT25.

    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
    DMPK-like alpha
    Myotonic dystrophy kinase-related CDC42-binding kinase alpha
    Short name:
    MRCK alpha
    Short name:
    Myotonic dystrophy protein kinase-like alpha
    Gene namesi
    Name:CDC42BPAImported
    Synonyms:KIAA0451
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1737. CDC42BPA.

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. actomyosin Source: UniProtKB
    2. cell-cell junction Source: UniProtKB
    3. cell leading edge Source: UniProtKB
    4. cytoplasm Source: UniProtKB-SubCell
    5. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi106 – 1061K → A: Loss of kinase activity. 1 Publication
    Mutagenesisi222 – 2221S → L: Increase in autophosphorylation but not kinase activity. 1 Publication
    Mutagenesisi234 – 2341S → A: Loss of autophosphorylation and kinase activity. 1 Publication
    Mutagenesisi240 – 2401T → A: Loss of autophosphorylation and kinase activity. 1 Publication
    Mutagenesisi403 – 4031T → A: Loss of autophosphorylation and kinase activity. 1 Publication
    Mutagenesisi1579 – 15791H → A: Loss of CDC42 binding; when associated with A-1582. 1 Publication
    Mutagenesisi1582 – 15821H → A: Loss of CDC42 binding; when associated with A-1579. 1 Publication

    Organism-specific databases

    PharmGKBiPA26267.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17321732Serine/threonine-protein kinase MRCK alphaPRO_0000086392Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei222 – 2221Phosphoserine; by autocatalysis1 Publication
    Modified residuei234 – 2341Phosphoserine; by autocatalysis1 Publication
    Modified residuei240 – 2401Phosphothreonine; by autocatalysis1 Publication
    Modified residuei1127 – 11271PhosphoserineBy similarity
    Modified residuei1545 – 15451Phosphoserine1 Publication
    Modified residuei1651 – 16511Phosphoserine1 Publication
    Modified residuei1719 – 17191Phosphoserine1 Publication
    Modified residuei1721 – 17211Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ5VT25.
    PaxDbiQ5VT25.
    PRIDEiQ5VT25.

    PTM databases

    PhosphoSiteiQ5VT25.

    Expressioni

    Tissue specificityi

    Abundant in the heart, brain, skeletal muscle, kidney, and pancreas, with little or no expression in the lung and liver.1 Publication

    Inductioni

    Regulated by cellular iron levels.1 Publication

    Gene expression databases

    ArrayExpressiQ5VT25.
    BgeeiQ5VT25.
    GenevestigatoriQ5VT25.

    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.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself9EBI-689171,EBI-689171
    CDC42P609535EBI-689171,EBI-81752

    Protein-protein interaction databases

    BioGridi114051. 5 interactions.
    IntActiQ5VT25. 8 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5VT25.
    SMRiQ5VT25. Positions 2-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini77 – 343267Protein kinase1 PublicationPROSITE-ProRule annotationAdd
    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 – 820384Sequence 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

    eggNOGiCOG0515.
    HOVERGENiHBG055933.
    KOiK16307.
    OMAiKKGCPGS.
    OrthoDBiEOG7F511X.
    PhylomeDBiQ5VT25.
    TreeFamiTF313551.

    Family and domain databases

    InterProiIPR000961. AGC-kinase_C.
    IPR001180. Citron.
    IPR000095. CRIB_dom.
    IPR011009. Kinase-like_dom.
    IPR014930. Myotonic_dystrophy_kinase_coil.
    IPR001849. PH_domain.
    IPR017892. Pkinase_C.
    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_alpha.
    [Graphical view]
    PANTHERiPTHR22988:SF31. PTHR22988:SF31. 1 hit.
    PfamiPF00130. C1_1. 1 hit.
    PF00780. CNH. 1 hit.
    PF08826. DMPK_coil. 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]
    SUPFAMiSSF56112. 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. Align

    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 1Curated (identifier: Q5VT25-1) [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

    MSGEVRLRQL EQFILDGPAQ TNGQCFSVET LLDILICLYD ECNNSPLRRE     50
    KNILEYLEWA KPFTSKVKQM RLHREDFEIL KVIGRGAFGE VAVVKLKNAD 100
    KVFAMKILNK WEMLKRAETA CFREERDVLV NGDNKWITTL HYAFQDDNNL 150
    YLVMDYYVGG DLLTLLSKFE DRLPEDMARF YLAEMVIAID SVHQLHYVHR 200
    DIKPDNILMD MNGHIRLADF GSCLKLMEDG TVQSSVAVGT PDYISPEILQ 250
    AMEDGKGRYG PECDWWSLGV CMYEMLYGET PFYAESLVET YGKIMNHKER 300
    FQFPAQVTDV SENAKDLIRR LICSREHRLG QNGIEDFKKH PFFSGIDWDN 350
    IRNCEAPYIP EVSSPTDTSN FDVDDDCLKN SETMPPPTHT AFSGHHLPFV 400
    GFTYTSSCVL SDRSCLRVTA GPTSLDLDVN VQRTLDNNLA TEAYERRIKR 450
    LEQEKLELSR KLQESTQTVQ ALQYSTVDGP LTASKDLEIK NLKEEIEKLR 500
    KQVTESSHLE QQLEEANAVR QELDDAFRQI KAYEKQIKTL QQEREDLNKE 550
    LVQASERLKN QSKELKDAHC QRKLAMQEFM EINERLTELH TQKQKLARHV 600
    RDKEEEVDLV MQKVESLRQE LRRTERAKKE LEVHTEALAA EASKDRKLRE 650
    QSEHYSKQLE NELEGLKQKQ ISYSPGVCSI EHQQEITKLK TDLEKKSIFY 700
    EEELSKREGI HANEIKNLKK ELHDSEGQQL ALNKEIMILK DKLEKTRRES 750
    QSEREEFESE FKQQYEREKV LLTEENKKLT SELDKLTTLY ENLSIHNQQL 800
    EEEVKDLADK KESVAHWEAQ ITEIIQWVSD EKDARGYLQA LASKMTEELE 850
    ALRNSSLGTR ATDMPWKMRR FAKLDMSARL ELQSALDAEI RAKQAIQEEL 900
    NKVKASNIIT ECKLKDSEKK NLELLSEIEQ LIKDTEELRS EKGIEHQDSQ 950
    HSFLAFLNTP TDALDQFERS PSCTPASKGR RTVDSTPLSV HTPTLRKKGC 1000
    PGSTGFPPKR KTHQFFVKSF TTPTKCHQCT SLMVGLIRQG CSCEVCGFSC 1050
    HITCVNKAPT TCPVPPEQTK GPLGIDPQKG IGTAYEGHVR IPKPAGVKKG 1100
    WQRALAIVCD FKLFLYDIAE GKASQPSVVI SQVIDMRDEE FSVSSVLASD 1150
    VIHASRKDIP CIFRVTASQL SASNNKCSIL MLADTENEKN KWVGVLSELH 1200
    KILKKNKFRD RSVYVPKEAY DSTLPLIKTT QAAAIIDHER IALGNEEGLF 1250
    VVHVTKDEII RVGDNKKIHQ IELIPNDQLV AVISGRNRHV RLFPMSALDG 1300
    RETDFYKLSE TKGCQTVTSG KVRHGALTCL CVAMKRQVLC YELFQSKTRH 1350
    RKFKEIQVPY NVQWMAIFSE QLCVGFQSGF LRYPLNGEGN PYSMLHSNDH 1400
    TLSFIAHQPM DAICAVEISS KEYLLCFNSI GIYTDCQGRR SRQQELMWPA 1450
    NPSSCCYNAP YLSVYSENAV DIFDVNSMEW IQTLPLKKVR PLNNEGSLNL 1500
    LGLETIRLIY FKNKMAEGDE LVVPETSDNS RKQMVRNINN KRRYSFRVPE 1550
    EERMQQRREM LRDPEMRNKL ISNPTNFNHI AHMGPGDGIQ ILKDLPMNPR 1600
    PQESRTVFSG SVSIPSITKS RPEPGRSMSA SSGLSARSSA QNGSALKREF 1650
    SGGSYSAKRQ PMPSPSEGSL SSGGMDQGSD APARDFDGED SDSPRHSTAS 1700
    NSSNLSSPPS PASPRKTKSL SLESTDRGSW DP 1732

    Note: No experimental confirmation available.Curated

    Length:1,732
    Mass (Da):197,307
    Last modified:December 7, 2004 - v1
    Checksum:i48B10F81B5405A0A
    GO
    Isoform 2Curated (identifier: Q5VT25-2) [UniParc]FASTAAdd to Basket

    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.Curated

    Show »
    Length:1,754
    Mass (Da):199,811
    Checksum:iF1CC5CC1ED23B388
    GO
    Isoform 31 Publication (identifier: Q5VT25-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         550-630: Missing.
         969-981: Missing.

    Show »
    Length:1,638
    Mass (Da):186,113
    Checksum:i7783E19090B345F7
    GO
    Isoform 41 Publication (identifier: Q5VT25-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         969-1009: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:1,691
    Mass (Da):193,031
    Checksum:i28E904E222CFFEC5
    GO
    Isoform 51 Publication (identifier: Q5VT25-5) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,719
    Mass (Da):195,922
    Checksum:iDBB15FA879AAC871
    GO
    Isoform 6 (identifier: Q5VT25-6) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,781
    Mass (Da):202,812
    Checksum:i979DA0EF4F17F9DF
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251C → Y in AAB37126. (PubMed:9092543)Curated
    Sequence conflicti809 – 8091D → N in CAI46252. (PubMed:17974005)Curated
    Sequence conflicti1521 – 15211L → V(PubMed:9418861)Curated
    Sequence conflicti1688 – 16881G → K in BAA32296. (PubMed:9455484)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti50 – 501E → K in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
    VAR_040830
    Natural varianti231 – 2311T → M.1 Publication
    Corresponds to variant rs34614709 [ dbSNP | Ensembl ].
    VAR_040831
    Natural varianti537 – 5371I → T.1 Publication
    Corresponds to variant rs56364976 [ dbSNP | Ensembl ].
    VAR_040832
    Natural varianti780 – 7801T → M.1 Publication
    Corresponds to variant rs56119119 [ dbSNP | Ensembl ].
    VAR_045583
    Natural varianti790 – 7901Y → C.1 Publication
    Corresponds to variant rs34943764 [ dbSNP | Ensembl ].
    VAR_045584
    Natural varianti1148 – 11481A → T.1 Publication
    VAR_045585
    Natural varianti1211 – 12111R → H.1 Publication
    VAR_045586
    Natural varianti1317 – 13171V → I.2 Publications
    Corresponds to variant rs1929860 [ dbSNP | Ensembl ].
    VAR_045587
    Natural varianti1418 – 14181I → K.1 Publication
    VAR_040833
    Natural varianti1469 – 14691A → V.1 Publication
    Corresponds to variant rs55687355 [ dbSNP | Ensembl ].
    VAR_045588
    Natural varianti1618 – 16181T → A.1 Publication
    Corresponds to variant rs2297417 [ dbSNP | Ensembl ].
    VAR_045589
    Natural varianti1699 – 16991A → V.
    Corresponds to variant rs2802269 [ dbSNP | Ensembl ].
    VAR_045590
    Natural varianti1712 – 17121A → V.3 Publications
    Corresponds to variant rs2802269 [ dbSNP | Ensembl ].
    VAR_057104

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei550 – 63081Missing in isoform 3. 1 PublicationVSP_051859Add
    BLAST
    Alternative sequencei969 – 100941Missing in isoform 4. 2 PublicationsVSP_051862Add
    BLAST
    Alternative sequencei969 – 98113Missing in isoform 3, isoform 5 and isoform 6. 2 PublicationsVSP_051860Add
    BLAST
    Alternative sequencei969 – 9691R → TDPVENTYVWNPSVKFHIQS RST in isoform 2. 1 PublicationVSP_051861
    Alternative sequencei973 – 9819CTPASKGRR → TSSEAEPVK in isoform 2. 1 PublicationVSP_051863
    Alternative sequencei1597 – 15971M → MPGFPYPSPHHHSGLISSPI NFEHIYHMTVNSAEKFLSPD SINPEYSPSLRSVPGTPSFM TLR in isoform 6. 1 PublicationVSP_035286

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS1558.1. [Q5VT25-5]
    CCDS1559.1. [Q5VT25-3]
    RefSeqiNP_003598.2. NM_003607.3. [Q5VT25-5]
    NP_055641.3. NM_014826.4. [Q5VT25-3]
    XP_005273378.1. XM_005273321.1. [Q5VT25-6]
    XP_005273379.1. XM_005273322.1. [Q5VT25-2]
    XP_005273381.1. XM_005273324.1. [Q5VT25-1]
    UniGeneiHs.35433.

    Genome annotation databases

    EnsembliENST00000334218; ENSP00000335341; ENSG00000143776. [Q5VT25-6]
    ENST00000366764; ENSP00000355726; ENSG00000143776. [Q5VT25-4]
    ENST00000366766; ENSP00000355728; ENSG00000143776. [Q5VT25-2]
    ENST00000366767; ENSP00000355729; ENSG00000143776. [Q5VT25-3]
    ENST00000366769; ENSP00000355731; ENSG00000143776. [Q5VT25-5]
    GeneIDi8476.
    KEGGihsa:8476.
    UCSCiuc001hqr.3. human. [Q5VT25-5]
    uc001hqs.3. human. [Q5VT25-3]
    uc009xes.3. human. [Q5VT25-4]

    Polymorphism databases

    DMDMi74746874.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS1558.1. [Q5VT25-5 ]
    CCDS1559.1. [Q5VT25-3 ]
    RefSeqi NP_003598.2. NM_003607.3. [Q5VT25-5 ]
    NP_055641.3. NM_014826.4. [Q5VT25-3 ]
    XP_005273378.1. XM_005273321.1. [Q5VT25-6 ]
    XP_005273379.1. XM_005273322.1. [Q5VT25-2 ]
    XP_005273381.1. XM_005273324.1. [Q5VT25-1 ]
    UniGenei Hs.35433.

    3D structure databases

    ProteinModelPortali Q5VT25.
    SMRi Q5VT25. Positions 2-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114051. 5 interactions.
    IntActi Q5VT25. 8 interactions.

    Chemistry

    BindingDBi Q5VT25.
    ChEMBLi CHEMBL4516.
    GuidetoPHARMACOLOGYi 1507.

    PTM databases

    PhosphoSitei Q5VT25.

    Polymorphism databases

    DMDMi 74746874.

    Proteomic databases

    MaxQBi Q5VT25.
    PaxDbi Q5VT25.
    PRIDEi Q5VT25.

    Protocols and materials databases

    DNASUi 8476.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334218 ; ENSP00000335341 ; ENSG00000143776 . [Q5VT25-6 ]
    ENST00000366764 ; ENSP00000355726 ; ENSG00000143776 . [Q5VT25-4 ]
    ENST00000366766 ; ENSP00000355728 ; ENSG00000143776 . [Q5VT25-2 ]
    ENST00000366767 ; ENSP00000355729 ; ENSG00000143776 . [Q5VT25-3 ]
    ENST00000366769 ; ENSP00000355731 ; ENSG00000143776 . [Q5VT25-5 ]
    GeneIDi 8476.
    KEGGi hsa:8476.
    UCSCi uc001hqr.3. human. [Q5VT25-5 ]
    uc001hqs.3. human. [Q5VT25-3 ]
    uc009xes.3. human. [Q5VT25-4 ]

    Organism-specific databases

    CTDi 8476.
    GeneCardsi GC01M227177.
    H-InvDB HIX0001650.
    HGNCi HGNC:1737. CDC42BPA.
    MIMi 603412. gene.
    neXtProti NX_Q5VT25.
    PharmGKBi PA26267.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG055933.
    KOi K16307.
    OMAi KKGCPGS.
    OrthoDBi EOG7F511X.
    PhylomeDBi Q5VT25.
    TreeFami TF313551.

    Enzyme and pathway databases

    SignaLinki Q5VT25.

    Miscellaneous databases

    ChiTaRSi CDC42BPA. human.
    GeneWikii CDC42BPA.
    GenomeRNAii 8476.
    NextBioi 31715.
    PROi Q5VT25.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5VT25.
    Bgeei Q5VT25.
    Genevestigatori Q5VT25.

    Family and domain databases

    InterProi IPR000961. AGC-kinase_C.
    IPR001180. Citron.
    IPR000095. CRIB_dom.
    IPR011009. Kinase-like_dom.
    IPR014930. Myotonic_dystrophy_kinase_coil.
    IPR001849. PH_domain.
    IPR017892. Pkinase_C.
    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_alpha.
    [Graphical view ]
    PANTHERi PTHR22988:SF31. PTHR22988:SF31. 1 hit.
    Pfami PF00130. C1_1. 1 hit.
    PF00780. CNH. 1 hit.
    PF08826. DMPK_coil. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    ProDomi PD011252. Myotonic_dystrophy_kinase_coil. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00109. 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 ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. 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 ]
    ProtoNeti Search...

    Publicationsi

    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: ColonImported.
    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: BrainImported.
    3. 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.
      , 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 gland1 Publication.
    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: Brain1 Publication.
    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. 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. 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.
      , 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.

    Entry informationi

    Entry nameiMRCKA_HUMAN
    AccessioniPrimary (citable) accession number: Q5VT25
    Secondary accession number(s): O75039
    , Q59GZ1, Q5H9N9, Q5T797, Q5VT26, Q5VT27, Q86XX2, Q86XX3, Q99646
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3