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Q5VT25

- MRCKA_HUMAN

UniProt

Q5VT25 - MRCKA_HUMAN

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Protein
Serine/threonine-protein kinase MRCK alpha
Gene
CDC42BPA, KIAA0451
Organism
Homo sapiens (Human)
Status
Reviewed - 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.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 Publication
Active sitei201 – 2011Proton acceptor By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi83 – 919ATP By similarityBy similarity
Zinc fingeri1012 – 106251Phorbol-ester/DAG-type
Add
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
Complete GO annotation...

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
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.

GO - Cellular componenti

  1. actomyosin Source: UniProtKB
  2. cell leading edge Source: UniProtKB
  3. cell-cell junction Source: UniProtKB
  4. cytoplasm Source: UniProtKB-SubCell
  5. extracellular vesicular exosome Source: UniProt
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
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 alpha
PRO_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 – 11271Phosphoserine By 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.3 Publications

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.3 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini77 – 343267Protein kinase1 Publication
Add
BLAST
Domaini344 – 41471AGC-kinase C-terminal
Add
BLAST
Domaini1082 – 1201120PH
Add
BLAST
Domaini1227 – 1499273CNH
Add
BLAST
Domaini1571 – 158414CRIB
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili437 – 820384 Reviewed prediction
Add
BLAST
Coiled coili880 – 94364 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Contains 1 CNH domain.
Contains 1 CRIB domain.
Contains 1 PH domain.

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 1 (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.

Length:1,732
Mass (Da):197,307
Last modified:December 7, 2004 - v1
Checksum:i48B10F81B5405A0A
GO
Isoform 2 (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.

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.

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.

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 Publication
VSP_051859Add
BLAST
Alternative sequencei969 – 100941Missing in isoform 4. 1 Publication
VSP_051862Add
BLAST
Alternative sequencei969 – 98113Missing in isoform 3, isoform 5 and isoform 6. 1 Publication
VSP_051860Add
BLAST
Alternative sequencei969 – 9691R → TDPVENTYVWNPSVKFHIQS RST in isoform 2.
VSP_051861
Alternative sequencei973 – 9819CTPASKGRR → TSSEAEPVK in isoform 2.
VSP_051863
Alternative sequencei1597 – 15971M → MPGFPYPSPHHHSGLISSPI NFEHIYHMTVNSAEKFLSPD SINPEYSPSLRSVPGTPSFM TLR in isoform 6.
VSP_035286

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251C → Y in AAB37126. 1 Publication
Sequence conflicti809 – 8091D → N in CAI46252. 1 Publication
Sequence conflicti1521 – 15211L → V1 Publication
Sequence conflicti1688 – 16881G → K in BAA32296. 1 Publication

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]
ENST00000366765; ENSP00000355727; ENSG00000143776. [Q5VT25-1]
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 ]
ENST00000366765 ; ENSP00000355727 ; ENSG00000143776 . [Q5VT25-1 ]
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

« Hide 'large scale' publications
  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. 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 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. 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: September 3, 2014
This is version 107 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

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