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Entry version 152 (12 Aug 2020)
Sequence version 1 (01 Oct 2003)
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Protein

Serine/threonine-protein kinase MRCK beta

Gene

Cdc42bpb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 (PubMed:21240187, PubMed:21457715). In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. Phosphorylates PPP1R12A (PubMed:18854160). In concert with FAM89B/LRAP25 mediates the targeting of LIMK1 to the lamellipodium resulting in its activation and subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation (By similarity).By similarity3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei105ATPPROSITE-ProRule annotationBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei200Proton acceptorPROSITE-ProRule annotationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi82 – 90ATPPROSITE-ProRule annotationBy similarity9
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri1026 – 1076Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST51

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Serine/threonine-protein kinase MRCK beta (EC:2.7.11.1)
Alternative name(s):
CDC42-binding protein kinase beta
DMPK-like beta
Myotonic dystrophy kinase-related CDC42-binding kinase beta
Short name:
MRCK beta
Short name:
Myotonic dystrophy protein kinase-like beta
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Cdc42bpbImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Rat genome database

More...
RGDi
621753, Cdc42bpb

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi952F → Q: Abolishes interaction with TJP1; when associated with Q-954. 1 Publication1
Mutagenesisi954Y → Q: Abolishes interaction with TJP1; when associated with Q-952. 1 Publication1
Mutagenesisi964L → Q: Abolishes interaction with TJP1; when associated with Q-966. 1 Publication1
Mutagenesisi966F → Q: Abolishes interaction with TJP1; when associated with Q-964. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000863961 – 1713Serine/threonine-protein kinase MRCK betaAdd BLAST1713

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei221Phosphoserine; by autocatalysisBy similarity1
Modified residuei233Phosphoserine; by autocatalysisBy similarity1
Modified residuei239Phosphothreonine; by autocatalysisBy similarity1
Modified residuei423PhosphothreonineBy similarity1
Modified residuei671Omega-N-methylarginineBy similarity1
Modified residuei927PhosphoserineBy similarity1
Modified residuei954PhosphotyrosineBy similarity1
Modified residuei1682PhosphoserineBy similarity1
Modified residuei1684PhosphoserineBy similarity1
Modified residuei1688PhosphoserineCombined sources1
Modified residuei1692PhosphoserineCombined sources1
Modified residuei1695PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Proteolytically cleaved by caspases upon apoptosis induction.By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q7TT49

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q7TT49

PRoteomics IDEntifications database

More...
PRIDEi
Q7TT49

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q7TT49

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q7TT49

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in all tissues examined with highest levels in lung and kidney.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000009675, Expressed in frontal cortex and 21 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q7TT49, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q7TT49, RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer and homotetramer via the coiled coil regions.

Interacts tightly with GTP-bound but not GDP-bound CDC42 (By similarity).

Interacts with TJP1; this interaction requires the presence of catalytically active CDC42 (PubMed:21240187).

Forms a tripartite complex with MYO18A and LURAP1 with the latter acting as an adapter connecting CDC42BPB and MYO18A. LURAP1 binding results in activation of CDC42BPB by abolition of its negative autoregulation (PubMed:18854160).

Interacts with STRIP1, STRN3 and SIKE1 (By similarity).

Interacts with CPNE4 (via VWFA domain) (By similarity).

Interacts with LURAP1 (PubMed:25107909).

Interacts (via AGC-kinase C-terminal domain) with FAM89B/LRAP25 (via LRR repeat) (PubMed:25107909).

Forms a tripartite complex with FAM89B/LRAP25 and LIMK1 (By similarity).

By similarity3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q7TT49, 15 interactors

Molecular INTeraction database

More...
MINTi
Q7TT49

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000036487

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q7TT49

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini76 – 342Protein kinasePROSITE-ProRule annotationBy similarityAdd BLAST267
Domaini343 – 413AGC-kinase C-terminalAdd BLAST71
Domaini1096 – 1215PHPROSITE-ProRule annotationAdd BLAST120
Domaini1241 – 1515CNHPROSITE-ProRule annotationAdd BLAST275
Domaini1585 – 1598CRIBPROSITE-ProRule annotationAdd BLAST14

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili434 – 649Sequence analysisAdd BLAST216
Coiled coili681 – 815Sequence analysisAdd BLAST135
Coiled coili882 – 939Sequence analysisAdd BLAST58

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1026 – 1076Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0612, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00990000203642

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000288_140_3_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q7TT49

KEGG Orthology (KO)

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KOi
K16307

Identification of Orthologs from Complete Genome Data

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OMAi
SYCEGYL

Database of Orthologous Groups

More...
OrthoDBi
759391at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q7TT49

TreeFam database of animal gene trees

More...
TreeFami
TF313551

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00029, C1, 1 hit
cd05624, STKc_MRCK_beta, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.30.29.30, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000961, AGC-kinase_C
IPR001180, CNH_dom
IPR000095, CRIB_dom
IPR020454, DAG/PE-bd
IPR031597, KELK
IPR011009, Kinase-like_dom_sf
IPR033232, MRCK_beta
IPR042718, MRCKB_STKc
IPR014930, Myotonic_dystrophy_kinase_coil
IPR002219, PE/DAG-bd
IPR011993, PH-like_dom_sf
IPR001849, PH_domain
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR008271, Ser/Thr_kinase_AS

The PANTHER Classification System

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PANTHERi
PTHR22988:SF34, PTHR22988:SF34, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00130, C1_1, 1 hit
PF00780, CNH, 1 hit
PF08826, DMPK_coil, 1 hit
PF15796, KELK, 1 hit
PF00069, Pkinase, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00008, DAGPEDOMAIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in 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

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112, SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in 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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q7TT49-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSAKVRLKKL EQLLLDGPWR NESSLSVETL LDVLVCLYTE CSHSALRRDK
60 70 80 90 100
YVAEFLEWAK PFTQLVKDMQ LHREDFEIIK VIGRGAFGEV AVVKMKNTER
110 120 130 140 150
IYAMKILNKW EMLKRAETAC FREERDVLVN GDCQWITALH YAFQDENYLY
160 170 180 190 200
LVMDYYVGGD LLTLLSKFED KLPEDMARFY IGEMVLAIDS IHQLHYVHRD
210 220 230 240 250
IKPDNVLLDV NGHIRLADFG SCLKMNDDGT VQSSVAVGTP DYISPEILQA
260 270 280 290 300
MEDGMGKYGP ECDWWSLGVC MYEMLYGETP FYAESLVETY GKIMNHEERF
310 320 330 340 350
QFPSHVTDVS EEAKDLIQRL ICSRERRLGQ NGIEDFKKHA FFEGLNWENI
360 370 380 390 400
RNLEAPYIPD VSSPSDTSNF DVDDDVLRNI EILPPGSHTG FSGLHLPFIG
410 420 430 440 450
FTFTTESCFS DRGSLKSMIQ SNTLTKDEDV QRDLENSLQI EAYERRIRRL
460 470 480 490 500
EQEKLELSRK LQESTQTVQS LHGSTRALGN SNRDKEIKRL NEELERMKSK
510 520 530 540 550
MADSNRLERQ LEDTVTLRQE HEDSTQRLKG LEKQYRLARQ EKEELHKQLV
560 570 580 590 600
EASERLKSQT KELKDAHQQR KRALQEFSEL NERMAELRSQ KQKVSRQLRD
610 620 630 640 650
KEEEMEVAMQ KIDSMRQDIR KSEKSRKELE ARLEDAVAEA SKERKLREHS
660 670 680 690 700
ESFSKQMERE LETLKVKQGG RGPGATLEHQ QEISKIRSEL EKKVLFYEEE
710 720 730 740 750
LVRREASHVL EVKNVKKEVH ESESHQLALQ KEVLMLKDKL EKSKRERHSE
760 770 780 790 800
MEEAIGAMKD KYERERAMLF DENKKLTAEN EKLCSFVDKL TAQNRQLEDE
810 820 830 840 850
LQDLASKKES VAHWEAQIAE IIQWVSDEKD ARGYLQALAS KMTEELETLR
860 870 880 890 900
SSSLGSRTLD PLWKVRRSQK LDMSARLELQ SALEAEIRAK QLVHEELRKV
910 920 930 940 950
KDTSLAFESK LKESEAKNRE LLEEMQSLKK RMEEKFRADT GLKLPDFQDP
960 970 980 990 1000
IFEYFNTAPL AHDLTFRTSS ASDQETQASK LDLSPSVSVA TSTEQQEDAA
1010 1020 1030 1040 1050
RSQQRPSTVP LPNTQALAMA GPKPKAHQFS IKSFPSPTQC SHCTSLMVGL
1060 1070 1080 1090 1100
IRQGYACEVC AFSCHVSCKD SAPQVCPIPP EQSKRPLGVD VQRGIGTAYK
1110 1120 1130 1140 1150
GYVKVPKPTG VKKGWQRAYA VVCDCKLFLY DLPEGKSTQP GVIASQVLDL
1160 1170 1180 1190 1200
RDDEFAVSSV LASDVIHATR RDIPCIFRVT ASLLGSPSKT SSLLILTENE
1210 1220 1230 1240 1250
NEKRKWVGIL EGLQAILHKN RLRSQVVHVA QEAYDSSLPL IKTVLAAAIV
1260 1270 1280 1290 1300
DGDRIAVGLE EGLYVIELTR DVIVRAADCK KVYQIELAPK EKLILLLCGR
1310 1320 1330 1340 1350
NHHVHLYPWT SFDGAEASNF DIKLPETKGC QLIATGTLRK SSSTCLFVAV
1360 1370 1380 1390 1400
KRLVLCYEIQ RTKPFHRKFN EIVAPGHVQW MAMFKDRLCV GYPSGFSLLS
1410 1420 1430 1440 1450
IQGDGQPLDL VNPADPSLAF LSQQSFDALC AVELKSEEYL LCFSHMGLYV
1460 1470 1480 1490 1500
DPQGRRSRTQ ELMWPAAPVA CSCSSSHVTV YSEYGVDVFD VRTMEWVQTI
1510 1520 1530 1540 1550
GLRRIRPLNS DGSLNLLGCE PPRLIYFKNK FSGTVLNVPD TSDNSKKQML
1560 1570 1580 1590 1600
RTRSKRRFVF KVPEEERLQQ RREMLRDPEL RSKMISNPTN FNHVAHMGPG
1610 1620 1630 1640 1650
DGMQVLMDLP LSAAPTAQEE KQGPAPTGLP RQLPSRNKPY VSWPSSGGSE
1660 1670 1680 1690 1700
PGVPVPLRSM SDPDQDFDKE PDSDSTKHST PSNSSNPSGP PSPNSPHRSQ
1710
LPLEGLDQPA CDA
Length:1,713
Mass (Da):194,888
Last modified:October 1, 2003 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i80C999262C96DAA6
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2KB58A0A0G2KB58_RAT
Non-specific serine/threonine prote...
Cdc42bpb
1,702Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAC02942 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti706A → R in AAC02942 (PubMed:9418861).Curated1
Sequence conflicti1523R → C in AAC02942 (PubMed:9418861).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF021936 mRNA Translation: AAC02942.1 Frameshift.
AY277590 mRNA Translation: AAP34403.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T14050

NCBI Reference Sequences

More...
RefSeqi
NP_446072.2, NM_053620.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000039059; ENSRNOP00000036487; ENSRNOG00000009675

Database of genes from NCBI RefSeq genomes

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GeneIDi
113960

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:113960

UCSC genome browser

More...
UCSCi
RGD:621753, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF021936 mRNA Translation: AAC02942.1 Frameshift.
AY277590 mRNA Translation: AAP34403.1
PIRiT14050
RefSeqiNP_446072.2, NM_053620.3

3D structure databases

SMRiQ7TT49
ModBaseiSearch...

Protein-protein interaction databases

IntActiQ7TT49, 15 interactors
MINTiQ7TT49
STRINGi10116.ENSRNOP00000036487

PTM databases

iPTMnetiQ7TT49
PhosphoSitePlusiQ7TT49

Proteomic databases

jPOSTiQ7TT49
PaxDbiQ7TT49
PRIDEiQ7TT49

Genome annotation databases

EnsembliENSRNOT00000039059; ENSRNOP00000036487; ENSRNOG00000009675
GeneIDi113960
KEGGirno:113960
UCSCiRGD:621753, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
9578
RGDi621753, Cdc42bpb

Phylogenomic databases

eggNOGiKOG0612, Eukaryota
GeneTreeiENSGT00990000203642
HOGENOMiCLU_000288_140_3_1
InParanoidiQ7TT49
KOiK16307
OMAiSYCEGYL
OrthoDBi759391at2759
PhylomeDBiQ7TT49
TreeFamiTF313551

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q7TT49

Gene expression databases

BgeeiENSRNOG00000009675, Expressed in frontal cortex and 21 other tissues
ExpressionAtlasiQ7TT49, baseline and differential
GenevisibleiQ7TT49, RN

Family and domain databases

CDDicd00029, C1, 1 hit
cd05624, STKc_MRCK_beta, 1 hit
Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR000961, AGC-kinase_C
IPR001180, CNH_dom
IPR000095, CRIB_dom
IPR020454, DAG/PE-bd
IPR031597, KELK
IPR011009, Kinase-like_dom_sf
IPR033232, MRCK_beta
IPR042718, MRCKB_STKc
IPR014930, Myotonic_dystrophy_kinase_coil
IPR002219, PE/DAG-bd
IPR011993, PH-like_dom_sf
IPR001849, PH_domain
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR008271, Ser/Thr_kinase_AS
PANTHERiPTHR22988:SF34, PTHR22988:SF34, 1 hit
PfamiView protein in Pfam
PF00130, C1_1, 1 hit
PF00780, CNH, 1 hit
PF08826, DMPK_coil, 1 hit
PF15796, KELK, 1 hit
PF00069, Pkinase, 1 hit
PRINTSiPR00008, DAGPEDOMAIN
SMARTiView protein in 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
SUPFAMiSSF56112, SSF56112, 1 hit
PROSITEiView protein in 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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMRCKB_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q7TT49
Secondary accession number(s): O54875
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: October 1, 2003
Last modified: August 12, 2020
This is version 152 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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