Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 114 (12 Aug 2020)
Sequence version 1 (23 Sep 2008)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

MAGUK p55 subfamily member 5

Gene

Mpp5

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

Plays a role in tight junction biogenesis and in the establishment of cell polarity in epithelial cells (By similarity). Also involved in adherens junction biogenesis by ensuring correct localization of the exocyst complex protein EXOC4/SEC8 which allows trafficking of adherens junction structural component CDH1 to the cell surface (By similarity). Plays a role through its interaction with CDH5 in vascular lumen formation and endothelial membrane polarity (By similarity). Required during embryonic and postnatal retinal development (By similarity). Required for the maintenance of cerebellar progenitor cells in an undifferentiated proliferative state, preventing premature differentiation, and is required for cerebellar histogenesis, fissure formation and cerebellar layer organization (By similarity). Plays a role in the radial and longitudinal extension of the myelin sheath in Schwann cells (By similarity). May modulate SC6A1/GAT1-mediated GABA uptake by stabilizing the transporter (By similarity). May play a role in the T-cell receptor-mediated activation of NF-kappa-B (By similarity). Required for localization of EZR to the apical membrane of parietal cells and may play a role in the dynamic remodeling of the apical cytoskeleton (By similarity). Required for the normal polarized localization of the vesicular marker STX4 (By similarity). Required for the correct trafficking of the myelin proteins PMP22 and MAG (PubMed:20237282).By similarity1 Publication

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 bindingi486 – 493ATPPROSITE-ProRule annotation8

<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, Transferase
LigandATP-binding, Nucleotide-binding

<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:
MAGUK p55 subfamily member 5Curated
<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:Mpp5By similarity
Synonyms:Pals11 Publication
<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)Imported
<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
  • UP000234681 Componentsi: Chromosome 6, Unassembled WGS sequence

Organism-specific databases

Rat genome database

More...
RGDi
1308071, Mpp5

<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, Golgi apparatus, Membrane, Tight junction

<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_00004475801 – 675MAGUK p55 subfamily member 5Add BLAST675

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 residuei14PhosphoserineBy similarity1
Modified residuei25PhosphoserineBy similarity1
Modified residuei83PhosphoserineBy similarity1
Modified residuei84PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
B4F7E7

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

More...
PaxDbi
B4F7E7

PeptideAtlas

More...
PeptideAtlasi
B4F7E7

PRoteomics IDEntifications database

More...
PRIDEi
B4F7E7

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
B4F7E7

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

More...
PhosphoSitePlusi
B4F7E7

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000008788, Expressed in lung and 20 other tissues

<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

Heterodimer with MPP1 (By similarity).

Component of a complex composed of MPP5, CRB1 and MPP4 (By similarity).

Component of a complex composed of MPP5, MPP3 and CRB1; MPP5 acts as a bridging protein between MPP3 (via guanylate kinase-like domain) and CRB1 (By similarity).

Interacts (via PDZ domain) with CRB1 (via C-terminal ERLI motif) (By similarity). While the PDZ domain is sufficient for interaction with CRB1, the adjacent SH3 and guanylate kinase-like domains are likely to contribute to a high affinity interaction (By similarity).

Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, PATJ and PARD3/PAR3 (By similarity).

Forms a heterotrimeric complex composed of MMP5, LIN7B and PATJ; the N-terminal L27 domain of MPP5 interacts with the L27 domain of PATJ and the C-terminal L27 domain of MPP5 interacts with the L27 domain of LIN7B (By similarity).

Interacts with MPP7 (By similarity).

Interacts with CRB3 (By similarity).

Interacts with EZR (By similarity).

Interacts with PATJ (By similarity).

Interacts with LIN7C (By similarity).

Interacts with MPDZ (By similarity).

Interacts with PARD6B (By similarity).

Interacts with SC6A1 (By similarity).

Interacts with CDH5; the interaction promotes MPP5 localization to cell junctions and is required for CDH5-mediated vascular lumen formation and endothelial cell (By similarity).

Interacts with NPHP1 (via coiled coil and SH3 domains) (By similarity).

Interacts with NPHP4 (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
B4F7E7, 3 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000012005

<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
B4F7E7

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>Domaini120 – 177L27 1PROSITE-ProRule annotationAdd BLAST58
Domaini179 – 235L27 2PROSITE-ProRule annotationAdd BLAST57
Domaini256 – 336PDZPROSITE-ProRule annotationAdd BLAST81
Domaini345 – 417SH3PROSITE-ProRule annotationAdd BLAST73
Domaini479 – 660Guanylate kinase-likePROSITE-ProRule annotationAdd BLAST182

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 345Required for the correct localization of MPP5 and PATJ at cell-cell contacts and the normal formation of tight junctions and adherens junctionsBy similarityAdd BLAST345
Regioni21 – 140Interaction with PARD6BBy similarityAdd BLAST120
Regioni181 – 243Interaction with LIN7CBy similarityAdd BLAST63

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The L27 domain 1 functions in targeting to the tight junctions by binding to and stabilizing PATJ.By similarity
The PDZ domain binds to the C-terminus of SC6A1.By similarity

<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

Belongs to the MAGUK family.Curated

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0609, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156087

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_001715_5_4_1

KEGG Orthology (KO)

More...
KOi
K06091

Identification of Orthologs from Complete Genome Data

More...
OMAi
MMPMRRS

Database of Orthologous Groups

More...
OrthoDBi
531106at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
B4F7E7

TreeFam database of animal gene trees

More...
TreeFami
TF314263

Family and domain databases

Conserved Domains Database

More...
CDDi
cd12036, SH3_MPP5, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.42.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008145, GK/Ca_channel_bsu
IPR008144, Guanylate_kin-like_dom
IPR020590, Guanylate_kinase_CS
IPR014775, L27_C
IPR004172, L27_dom
IPR036892, L27_dom_sf
IPR015145, L27_N
IPR031185, MPP5
IPR035601, MPP5_SH3
IPR027417, P-loop_NTPase
IPR001478, PDZ
IPR036034, PDZ_sf
IPR036028, SH3-like_dom_sf
IPR001452, SH3_domain

The PANTHER Classification System

More...
PANTHERi
PTHR23122:SF14, PTHR23122:SF14, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00625, Guanylate_kin, 1 hit
PF02828, L27, 1 hit
PF09060, L27_N, 1 hit
PF00595, PDZ, 1 hit
PF07653, SH3_2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00072, GuKc, 1 hit
SM00569, L27, 2 hits
SM00228, PDZ, 1 hit
SM00326, SH3, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF101288, SSF101288, 2 hits
SSF50044, SSF50044, 1 hit
SSF50156, SSF50156, 1 hit
SSF52540, SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00856, GUANYLATE_KINASE_1, 1 hit
PS50052, GUANYLATE_KINASE_2, 1 hit
PS51022, L27, 2 hits
PS50106, PDZ, 1 hit
PS50002, SH3, 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>Sequencei

<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.

B4F7E7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTTSYMNGHV TEESDSGIKN LGLASPEEHP KHREMAVDCP GDLGTRLMPV
60 70 80 90 100
RRSAQLERIR QQQEDMRRRR EEEGKKQELD LNSSMRLKKL AQIPPKTGID
110 120 130 140 150
NPIFDTEEGI VLESPHYAVK ILEVEDLFSS LKHIQHTLVD SQSQEDISLL
160 170 180 190 200
LQLVQNRDFQ NAFKIHNAVT VHMNKASPPF PLIANVQDLV QEVQTVLKPV
210 220 230 240 250
HQKEGQELTA LLNAPHIQAL LLAHDKVAEQ EMQLEPITDE RVYESIGHYG
260 270 280 290 300
GETVKIVRIE KARDIPLGAT VRNEMDSVII SRIVKGGAAE KSGLLHEGDE
310 320 330 340 350
VLEINGIEIR GKDVNEVFDL LSDMHGTLTF VLIPSQQIKP PPAKETVIHV
360 370 380 390 400
KAHFDYDPSD DPYVPCRELG LSFQKGDILH VISQEDPNWW QAYREGDEDN
410 420 430 440 450
QPLAGLVPGK SFQQQREAMK QTIEEDKEPE KSGKLWCAKK NKKKRKKVLY
460 470 480 490 500
NANKNDDYDN EEILTYEEMS LYHQPANRKR PIILIGPQNC GQNELRQRLM
510 520 530 540 550
NKEKDRFASA VPHTTRNRRD HEVAGRDYHF VSRQAFEADI AAGKFIEHGE
560 570 580 590 600
FEKNLYGTSI DSVRQVINSG KICLLSLRAQ SLKTLRNSDL KPYIIFIAPP
610 620 630 640 650
SQERLRALLA KEGKNPKPEE LREIIEKTRE MEQNNGHYFD TAIVNSDLDK
660 670
AYQELLRLIN KLDTEPQWVP STWLR
Length:675
Mass (Da):77,152
Last modified:September 23, 2008 - 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:i7F212741A8454B14
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AABR07073239 Genomic DNA No translation available.
AC120917 Genomic DNA No translation available.
AC139976 Genomic DNA No translation available.
CH473947 Genomic DNA Translation: EDM03700.1
BC168247 mRNA Translation: AAI68247.1

NCBI Reference Sequences

More...
RefSeqi
NP_001101504.1, NM_001108034.1
XP_006240320.1, XM_006240258.2
XP_008762995.1, XM_008764773.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000012005; ENSRNOP00000012005; ENSRNOG00000008788
ENSRNOT00000092157; ENSRNOP00000070368; ENSRNOG00000008788

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
314259

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:314259

UCSC genome browser

More...
UCSCi
RGD:1308071, 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
AABR07073239 Genomic DNA No translation available.
AC120917 Genomic DNA No translation available.
AC139976 Genomic DNA No translation available.
CH473947 Genomic DNA Translation: EDM03700.1
BC168247 mRNA Translation: AAI68247.1
RefSeqiNP_001101504.1, NM_001108034.1
XP_006240320.1, XM_006240258.2
XP_008762995.1, XM_008764773.2

3D structure databases

SMRiB4F7E7
ModBaseiSearch...

Protein-protein interaction databases

IntActiB4F7E7, 3 interactors
STRINGi10116.ENSRNOP00000012005

PTM databases

iPTMnetiB4F7E7
PhosphoSitePlusiB4F7E7

Proteomic databases

jPOSTiB4F7E7
PaxDbiB4F7E7
PeptideAtlasiB4F7E7
PRIDEiB4F7E7

Genome annotation databases

EnsembliENSRNOT00000012005; ENSRNOP00000012005; ENSRNOG00000008788
ENSRNOT00000092157; ENSRNOP00000070368; ENSRNOG00000008788
GeneIDi314259
KEGGirno:314259
UCSCiRGD:1308071, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
64398
RGDi1308071, Mpp5

Phylogenomic databases

eggNOGiKOG0609, Eukaryota
GeneTreeiENSGT00940000156087
HOGENOMiCLU_001715_5_4_1
KOiK06091
OMAiMMPMRRS
OrthoDBi531106at2759
PhylomeDBiB4F7E7
TreeFamiTF314263

Miscellaneous databases

Protein Ontology

More...
PROi
PR:B4F7E7

Gene expression databases

BgeeiENSRNOG00000008788, Expressed in lung and 20 other tissues

Family and domain databases

CDDicd12036, SH3_MPP5, 1 hit
Gene3Di2.30.42.10, 1 hit
InterProiView protein in InterPro
IPR008145, GK/Ca_channel_bsu
IPR008144, Guanylate_kin-like_dom
IPR020590, Guanylate_kinase_CS
IPR014775, L27_C
IPR004172, L27_dom
IPR036892, L27_dom_sf
IPR015145, L27_N
IPR031185, MPP5
IPR035601, MPP5_SH3
IPR027417, P-loop_NTPase
IPR001478, PDZ
IPR036034, PDZ_sf
IPR036028, SH3-like_dom_sf
IPR001452, SH3_domain
PANTHERiPTHR23122:SF14, PTHR23122:SF14, 1 hit
PfamiView protein in Pfam
PF00625, Guanylate_kin, 1 hit
PF02828, L27, 1 hit
PF09060, L27_N, 1 hit
PF00595, PDZ, 1 hit
PF07653, SH3_2, 1 hit
SMARTiView protein in SMART
SM00072, GuKc, 1 hit
SM00569, L27, 2 hits
SM00228, PDZ, 1 hit
SM00326, SH3, 1 hit
SUPFAMiSSF101288, SSF101288, 2 hits
SSF50044, SSF50044, 1 hit
SSF50156, SSF50156, 1 hit
SSF52540, SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00856, GUANYLATE_KINASE_1, 1 hit
PS50052, GUANYLATE_KINASE_2, 1 hit
PS51022, L27, 2 hits
PS50106, PDZ, 1 hit
PS50002, SH3, 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 nameiMPP5_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: B4F7E7
<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: July 3, 2019
Last sequence update: September 23, 2008
Last modified: August 12, 2020
This is version 114 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
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again