Q5VT25 (MRCKA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CDC42BPA
Synonyms:	KIAA0451

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1732 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Zinc-finger
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin 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: Compara nuclear migration Inferred from electronic annotation. Source: Compara
Cellular_component	actomyosin 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
Molecular_function	ATP binding Inferred from direct assay Ref.5. Source: UniProtKB magnesium ion binding Inferred from direct assay Ref.5. Source: UniProtKB phospholipid binding Inferred from electronic annotation. Source: InterPro 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
itself		9	EBI-689171,EBI-689171
CDC42	P60953	5	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1732	1732	Serine/threonine-protein kinase MRCK alpha		PRO_0000086392
Regions
	Domain	77 – 343	267	Protein kinase Ref.5
	Domain	344 – 414	71	AGC-kinase C-terminal
	Domain	1082 – 1201	120	PH
	Domain	1227 – 1499	273	CNH
	Domain	1571 – 1584	14	CRIB
	Nucleotide binding	83 – 91	9	ATP By similarity UniProtKB P54265
	Zinc finger	1012 – 1062	51	Phorbol-ester/DAG-type
	Coiled coil	437 – 820	384	Potential
	Coiled coil	880 – 943	64	Potential
Sites
	Active site	201	1	Proton acceptor By similarity UniProtKB P54265
	Binding site	106	1	ATP Ref.11
Amino acid modifications
	Modified residue	222	1	Phosphoserine; by autocatalysis Ref.11
	Modified residue	234	1	Phosphoserine; by autocatalysis Ref.11
	Modified residue	240	1	Phosphothreonine; by autocatalysis Ref.11
	Modified residue	1545	1	Phosphoserine Ref.14
	Modified residue	1651	1	Phosphoserine Ref.18
	Modified residue	1719	1	Phosphoserine Ref.14
	Modified residue	1721	1	Phosphoserine Ref.14
Natural variations
	Alternative sequence	550 – 630	81	Missing in isoform 3. Ref.1		VSP_051859
	Alternative sequence	969 – 1009	41	Missing in isoform 4. Ref.4		VSP_051862
	Alternative sequence	969 – 981	13	Missing in isoform 3, isoform 5 and isoform 6. Ref.1		VSP_051860
	Alternative sequence	969	1	R → TDPVENTYVWNPSVKFHIQS RST in isoform 2.		VSP_051861
	Alternative sequence	973 – 981	9	CTPASKGRR → TSSEAEPVK in isoform 2.		VSP_051863
	Alternative sequence	1597	1	M → MPGFPYPSPHHHSGLISSPI NFEHIYHMTVNSAEKFLSPD SINPEYSPSLRSVPGTPSFM TLR in isoform 6.		VSP_035286
	Natural variant	50	1	E → K in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.19		VAR_040830
	Natural variant	231	1	T → M. Ref.19 Corresponds to variant rs34614709 [ dbSNP | Ensembl ].		VAR_040831
	Natural variant	537	1	I → T. Ref.19 Corresponds to variant rs56364976 [ dbSNP | Ensembl ].		VAR_040832
	Natural variant	780	1	T → M. Ref.19 Corresponds to variant rs56119119 [ dbSNP | Ensembl ].		VAR_045583
	Natural variant	790	1	Y → C. Ref.19 Corresponds to variant rs34943764 [ dbSNP | Ensembl ].		VAR_045584
	Natural variant	1148	1	A → T. Ref.19		VAR_045585
	Natural variant	1211	1	R → H. Ref.19		VAR_045586
	Natural variant	1317	1	V → I. Ref.3 Ref.19		VAR_045587
	Natural variant	1418	1	I → K. Ref.19		VAR_040833
	Natural variant	1469	1	A → V. Ref.19 Corresponds to variant rs55687355 [ dbSNP | Ensembl ].		VAR_045588
	Natural variant	1618	1	T → A. Ref.19		VAR_045589
	Natural variant	1699	1	A → V. Corresponds to variant rs2802269 [ dbSNP | Ensembl ].		VAR_045590
	Natural variant	1712	1	A → V. Ref.2 Ref.3 Ref.6 Corresponds to variant rs2802269 [ dbSNP | Ensembl ].		VAR_057104
Experimental info
	Mutagenesis	106	1	K → A: Loss of kinase activity. Ref.11
	Mutagenesis	222	1	S → L: Increase in autophosphorylation but not kinase activity. Ref.11
	Mutagenesis	234	1	S → A: Loss of autophosphorylation and kinase activity. Ref.11
	Mutagenesis	240	1	T → A: Loss of autophosphorylation and kinase activity. Ref.11
	Mutagenesis	403	1	T → A: Loss of autophosphorylation and kinase activity. Ref.11
	Mutagenesis	1579	1	H → A: Loss of CDC42 binding; when associated with A-1582. Ref.8
	Mutagenesis	1582	1	H → A: Loss of CDC42 binding; when associated with A-1579. Ref.8
	Sequence conflict	25	1	C → Y in AAB37126. Ref.5
	Sequence conflict	809	1	D → N in CAI46252. Ref.3
	Sequence conflict	1521	1	L → V Ref.8
	Sequence conflict	1688	1	G → K in BAA32296. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 7, 2004. Version 1. Checksum: 48B10F81B5405A0A	FASTA	1,732	197,307
	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
	Isoform 2 [UniParc]. Checksum: F1CC5CC1ED23B388	FASTA	1,754	199,811
	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 TDALDQFETD PVENTYVWNP SVKFHIQSRS TSPSTSSEAE PVKTVDSTPL SVHTPTLRKK 1030 1040 1050 1060 1070 1080 GCPGSTGFPP KRKTHQFFVK SFTTPTKCHQ CTSLMVGLIR QGCSCEVCGF SCHITCVNKA 1090 1100 1110 1120 1130 1140 PTTCPVPPEQ TKGPLGIDPQ KGIGTAYEGH VRIPKPAGVK KGWQRALAIV CDFKLFLYDI 1150 1160 1170 1180 1190 1200 AEGKASQPSV VISQVIDMRD EEFSVSSVLA SDVIHASRKD IPCIFRVTAS QLSASNNKCS 1210 1220 1230 1240 1250 1260 ILMLADTENE KNKWVGVLSE LHKILKKNKF RDRSVYVPKE AYDSTLPLIK TTQAAAIIDH 1270 1280 1290 1300 1310 1320 ERIALGNEEG LFVVHVTKDE IIRVGDNKKI HQIELIPNDQ LVAVISGRNR HVRLFPMSAL 1330 1340 1350 1360 1370 1380 DGRETDFYKL SETKGCQTVT SGKVRHGALT CLCVAMKRQV LCYELFQSKT RHRKFKEIQV 1390 1400 1410 1420 1430 1440 PYNVQWMAIF SEQLCVGFQS GFLRYPLNGE GNPYSMLHSN DHTLSFIAHQ PMDAICAVEI 1450 1460 1470 1480 1490 1500 SSKEYLLCFN SIGIYTDCQG RRSRQQELMW PANPSSCCYN APYLSVYSEN AVDIFDVNSM 1510 1520 1530 1540 1550 1560 EWIQTLPLKK VRPLNNEGSL NLLGLETIRL IYFKNKMAEG DELVVPETSD NSRKQMVRNI 1570 1580 1590 1600 1610 1620 NNKRRYSFRV PEEERMQQRR EMLRDPEMRN KLISNPTNFN HIAHMGPGDG IQILKDLPMN 1630 1640 1650 1660 1670 1680 PRPQESRTVF SGSVSIPSIT KSRPEPGRSM SASSGLSARS SAQNGSALKR EFSGGSYSAK 1690 1700 1710 1720 1730 1740 RQPMPSPSEG SLSSGGMDQG SDAPARDFDG EDSDSPRHST ASNSSNLSSP PSPASPRKTK 1750 SLSLESTDRG SWDP
	Isoform 3 [UniParc]. Checksum: 7783E19090B345F7	FASTA	1,638	186,113
	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 QQEREDLNKL EVHTEALAAE ASKDRKLREQ SEHYSKQLEN ELEGLKQKQI SYSPGVCSIE 610 620 630 640 650 660 HQQEITKLKT DLEKKSIFYE EELSKREGIH ANEIKNLKKE LHDSEGQQLA LNKEIMILKD 670 680 690 700 710 720 KLEKTRRESQ SEREEFESEF KQQYEREKVL LTEENKKLTS ELDKLTTLYE NLSIHNQQLE 730 740 750 760 770 780 EEVKDLADKK ESVAHWEAQI TEIIQWVSDE KDARGYLQAL ASKMTEELEA LRNSSLGTRA 790 800 810 820 830 840 TDMPWKMRRF AKLDMSARLE LQSALDAEIR AKQAIQEELN KVKASNIITE CKLKDSEKKN 850 860 870 880 890 900 LELLSEIEQL IKDTEELRSE KGIEHQDSQH SFLAFLNTPT DALDQFETVD STPLSVHTPT 910 920 930 940 950 960 LRKKGCPGST GFPPKRKTHQ FFVKSFTTPT KCHQCTSLMV GLIRQGCSCE VCGFSCHITC 970 980 990 1000 1010 1020 VNKAPTTCPV PPEQTKGPLG IDPQKGIGTA YEGHVRIPKP AGVKKGWQRA LAIVCDFKLF 1030 1040 1050 1060 1070 1080 LYDIAEGKAS QPSVVISQVI DMRDEEFSVS SVLASDVIHA SRKDIPCIFR VTASQLSASN 1090 1100 1110 1120 1130 1140 NKCSILMLAD TENEKNKWVG VLSELHKILK KNKFRDRSVY VPKEAYDSTL PLIKTTQAAA 1150 1160 1170 1180 1190 1200 IIDHERIALG NEEGLFVVHV TKDEIIRVGD NKKIHQIELI PNDQLVAVIS GRNRHVRLFP 1210 1220 1230 1240 1250 1260 MSALDGRETD FYKLSETKGC QTVTSGKVRH GALTCLCVAM KRQVLCYELF QSKTRHRKFK 1270 1280 1290 1300 1310 1320 EIQVPYNVQW MAIFSEQLCV GFQSGFLRYP LNGEGNPYSM LHSNDHTLSF IAHQPMDAIC 1330 1340 1350 1360 1370 1380 AVEISSKEYL LCFNSIGIYT DCQGRRSRQQ ELMWPANPSS CCYNAPYLSV YSENAVDIFD 1390 1400 1410 1420 1430 1440 VNSMEWIQTL PLKKVRPLNN EGSLNLLGLE TIRLIYFKNK MAEGDELVVP ETSDNSRKQM 1450 1460 1470 1480 1490 1500 VRNINNKRRY SFRVPEEERM QQRREMLRDP EMRNKLISNP TNFNHIAHMG PGDGIQILKD 1510 1520 1530 1540 1550 1560 LPMNPRPQES RTVFSGSVSI PSITKSRPEP GRSMSASSGL SARSSAQNGS ALKREFSGGS 1570 1580 1590 1600 1610 1620 YSAKRQPMPS PSEGSLSSGG MDQGSDAPAR DFDGEDSDSP RHSTASNSSN LSSPPSPASP 1630 RKTKSLSLES TDRGSWDP
	Isoform 4 [UniParc]. Checksum: 28E904E222CFFEC5	FASTA	1,691	193,031
	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 TDALDQFERK THQFFVKSFT TPTKCHQCTS LMVGLIRQGC SCEVCGFSCH ITCVNKAPTT 1030 1040 1050 1060 1070 1080 CPVPPEQTKG PLGIDPQKGI GTAYEGHVRI PKPAGVKKGW QRALAIVCDF KLFLYDIAEG 1090 1100 1110 1120 1130 1140 KASQPSVVIS QVIDMRDEEF SVSSVLASDV IHASRKDIPC IFRVTASQLS ASNNKCSILM 1150 1160 1170 1180 1190 1200 LADTENEKNK WVGVLSELHK ILKKNKFRDR SVYVPKEAYD STLPLIKTTQ AAAIIDHERI 1210 1220 1230 1240 1250 1260 ALGNEEGLFV VHVTKDEIIR VGDNKKIHQI ELIPNDQLVA VISGRNRHVR LFPMSALDGR 1270 1280 1290 1300 1310 1320 ETDFYKLSET KGCQTVTSGK VRHGALTCLC VAMKRQVLCY ELFQSKTRHR KFKEIQVPYN 1330 1340 1350 1360 1370 1380 VQWMAIFSEQ LCVGFQSGFL RYPLNGEGNP YSMLHSNDHT LSFIAHQPMD AICAVEISSK 1390 1400 1410 1420 1430 1440 EYLLCFNSIG IYTDCQGRRS RQQELMWPAN PSSCCYNAPY LSVYSENAVD IFDVNSMEWI 1450 1460 1470 1480 1490 1500 QTLPLKKVRP LNNEGSLNLL GLETIRLIYF KNKMAEGDEL VVPETSDNSR KQMVRNINNK 1510 1520 1530 1540 1550 1560 RRYSFRVPEE ERMQQRREML RDPEMRNKLI SNPTNFNHIA HMGPGDGIQI LKDLPMNPRP 1570 1580 1590 1600 1610 1620 QESRTVFSGS VSIPSITKSR PEPGRSMSAS SGLSARSSAQ NGSALKREFS GGSYSAKRQP 1630 1640 1650 1660 1670 1680 MPSPSEGSLS SGGMDQGSDA PARDFDGEDS DSPRHSTASN SSNLSSPPSP ASPRKTKSLS 1690 LESTDRGSWD P
	Isoform 5 [UniParc]. Checksum: DBB15FA879AAC871	FASTA	1,719	195,922
	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 TDALDQFETV DSTPLSVHTP TLRKKGCPGS TGFPPKRKTH QFFVKSFTTP TKCHQCTSLM 1030 1040 1050 1060 1070 1080 VGLIRQGCSC EVCGFSCHIT CVNKAPTTCP VPPEQTKGPL GIDPQKGIGT AYEGHVRIPK 1090 1100 1110 1120 1130 1140 PAGVKKGWQR ALAIVCDFKL FLYDIAEGKA SQPSVVISQV IDMRDEEFSV SSVLASDVIH 1150 1160 1170 1180 1190 1200 ASRKDIPCIF RVTASQLSAS NNKCSILMLA DTENEKNKWV GVLSELHKIL KKNKFRDRSV 1210 1220 1230 1240 1250 1260 YVPKEAYDST LPLIKTTQAA AIIDHERIAL GNEEGLFVVH VTKDEIIRVG DNKKIHQIEL 1270 1280 1290 1300 1310 1320 IPNDQLVAVI SGRNRHVRLF PMSALDGRET DFYKLSETKG CQTVTSGKVR HGALTCLCVA 1330 1340 1350 1360 1370 1380 MKRQVLCYEL FQSKTRHRKF KEIQVPYNVQ WMAIFSEQLC VGFQSGFLRY PLNGEGNPYS 1390 1400 1410 1420 1430 1440 MLHSNDHTLS FIAHQPMDAI CAVEISSKEY LLCFNSIGIY TDCQGRRSRQ QELMWPANPS 1450 1460 1470 1480 1490 1500 SCCYNAPYLS VYSENAVDIF DVNSMEWIQT LPLKKVRPLN NEGSLNLLGL ETIRLIYFKN 1510 1520 1530 1540 1550 1560 KMAEGDELVV PETSDNSRKQ MVRNINNKRR YSFRVPEEER MQQRREMLRD PEMRNKLISN 1570 1580 1590 1600 1610 1620 PTNFNHIAHM GPGDGIQILK DLPMNPRPQE SRTVFSGSVS IPSITKSRPE PGRSMSASSG 1630 1640 1650 1660 1670 1680 LSARSSAQNG SALKREFSGG SYSAKRQPMP SPSEGSLSSG GMDQGSDAPA RDFDGEDSDS 1690 1700 1710 PRHSTASNSS NLSSPPSPAS PRKTKSLSLE STDRGSWDP
	Isoform 6 [UniParc]. Checksum: 979DA0EF4F17F9DF	FASTA	1,781	202,812
	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 TDALDQFETV DSTPLSVHTP TLRKKGCPGS TGFPPKRKTH QFFVKSFTTP TKCHQCTSLM 1030 1040 1050 1060 1070 1080 VGLIRQGCSC EVCGFSCHIT CVNKAPTTCP VPPEQTKGPL GIDPQKGIGT AYEGHVRIPK 1090 1100 1110 1120 1130 1140 PAGVKKGWQR ALAIVCDFKL FLYDIAEGKA SQPSVVISQV IDMRDEEFSV SSVLASDVIH 1150 1160 1170 1180 1190 1200 ASRKDIPCIF RVTASQLSAS NNKCSILMLA DTENEKNKWV GVLSELHKIL KKNKFRDRSV 1210 1220 1230 1240 1250 1260 YVPKEAYDST LPLIKTTQAA AIIDHERIAL GNEEGLFVVH VTKDEIIRVG DNKKIHQIEL 1270 1280 1290 1300 1310 1320 IPNDQLVAVI SGRNRHVRLF PMSALDGRET DFYKLSETKG CQTVTSGKVR HGALTCLCVA 1330 1340 1350 1360 1370 1380 MKRQVLCYEL FQSKTRHRKF KEIQVPYNVQ WMAIFSEQLC VGFQSGFLRY PLNGEGNPYS 1390 1400 1410 1420 1430 1440 MLHSNDHTLS FIAHQPMDAI CAVEISSKEY LLCFNSIGIY TDCQGRRSRQ QELMWPANPS 1450 1460 1470 1480 1490 1500 SCCYNAPYLS VYSENAVDIF DVNSMEWIQT LPLKKVRPLN NEGSLNLLGL ETIRLIYFKN 1510 1520 1530 1540 1550 1560 KMAEGDELVV PETSDNSRKQ MVRNINNKRR YSFRVPEEER MQQRREMLRD PEMRNKLISN 1570 1580 1590 1600 1610 1620 PTNFNHIAHM GPGDGIQILK DLPMPGFPYP SPHHHSGLIS SPINFEHIYH MTVNSAEKFL 1630 1640 1650 1660 1670 1680 SPDSINPEYS PSLRSVPGTP SFMTLRNPRP QESRTVFSGS VSIPSITKSR PEPGRSMSAS 1690 1700 1710 1720 1730 1740 SGLSARSSAQ NGSALKREFS GGSYSAKRQP MPSPSEGSLS SGGMDQGSDA PARDFDGEDS 1750 1760 1770 1780 DSPRHSTASN SSNLSSPPSP ASPRKTKSLS LESTDRGSWD P

References

	« Hide 'large scale' referencesShow 'large scale' references »
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[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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.
+	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.
IPI	IPI00550263. IPI00640468. IPI00640957. IPI00642165. IPI00654830. IPI00903296.
RefSeq	NP_003598.2. NM_003607.3. NP_055641.3. NM_014826.4.
UniGene	Hs.35433.
3D structure databases
ProteinModelPortal	Q5VT25.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q5VT25. 7 interactions.
PTM databases
PhosphoSite	Q5VT25.
Polymorphism databases
DMDM	74746874.
Proteomic databases
PaxDb	Q5VT25.
PRIDE	Q5VT25.
Protocols and materials databases
DNASU	8476.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000334218; ENSP00000335341; ENSG00000143776. ENST00000366764; ENSP00000355726; ENSG00000143776. ENST00000366765; ENSP00000355727; ENSG00000143776. ENST00000366766; ENSP00000355728; ENSG00000143776. ENST00000366767; ENSP00000355729; ENSG00000143776. ENST00000366769; ENSP00000355731; ENSG00000143776.
GeneID	8476.
KEGG	hsa:8476.
UCSC	uc001hqq.3. human. uc001hqr.3. human. uc001hqs.3. human. uc009xes.3. human.
Organism-specific databases
CTD	8476.
GeneCards	GC01M227177.
H-InvDB	HIX0001650.
HGNC	HGNC:1737. CDC42BPA.
MIM	603412. gene.
neXtProt	NX_Q5VT25.
PharmGKB	PA26267.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOVERGEN	HBG055933.
KO	K16307.
OMA	LRKKGCP.
Gene expression databases
ArrayExpress	Q5VT25.
Bgee	Q5VT25.
Genevestigator	Q5VT25.
GermOnline	ENSG00000143776. Homo sapiens.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR001180. Citron. IPR011009. Kinase-like_dom. IPR014930. Myotonic_dystrophy_kinase_coil. IPR000095. PAK_box_Rho-bd. IPR017892. Pkinase_C. IPR001849. Pleckstrin_homology. IPR002219. Prot_Kinase_C-like_PE/DAG-bd. IPR000719. Prot_kinase_cat_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]
PANTHER	PTHR22988:SF2. PTHR22988:SF2. 1 hit.
Pfam	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]
ProDom	PD011252. Myotonic_dystrophy_kinase_coil. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	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]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
BindingDB	Q5VT25.
ChEMBL	CHEMBL4516.
ChiTaRS	CDC42BPA. human.
GenomeRNAi	8476.
NextBio	31715.
SOURCE	Search...

Entry information

Entry name

MRCKA_HUMAN

Accession

Primary (citable) accession number: Q5VT25
Secondary accession number(s): O75039 , 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:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.