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Entry version 164 (22 Apr 2020)
Sequence version 1 (01 Jan 1998)
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Protein

Neurabin-2

Gene

Ppp1r9b

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

Seems to act as a scaffold protein in multiple signaling pathways. Modulates excitatory synaptic transmission and dendritic spine morphology. Binds to actin filaments (F-actin) and shows cross-linking activity. Binds along the sides of the F-actin. May play an important role in linking the actin cytoskeleton to the plasma membrane at the synaptic junction. Believed to target protein phosphatase 1/PP1 to dendritic spines, which are rich in F-actin, and regulates its specificity toward ion channels and other substrates, such as AMPA-type and NMDA-type glutamate receptors. Plays a role in regulation of G-protein coupled receptor signaling, including dopamine D2 receptors and alpha-adrenergic receptors. May establish a signaling complex for dopaminergic neurotransmission through D2 receptors by linking receptors downstream signaling molecules and the actin cytoskeleton. Binds to ADRA1B and RGS2 and mediates regulation of ADRA1B signaling. May confer to Rac signaling specificity by binding to both, RacGEFs and Rac effector proteins. Probably regulates p70 S6 kinase activity by forming a complex with TIAM1. Required for hepatocyte growth factor (HGF)-induced cell migration (By similarity).By similarity2 Publications

<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 functionActin-binding, Developmental protein
Biological processDifferentiation, Neurogenesis

<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:
Neurabin-2Curated
Alternative name(s):
Neurabin-II
Neural tissue-specific F-actin-binding protein II
PP1bp134
Protein phosphatase 1 regulatory subunit 9B
Spinophilin1 Publication
p130
<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:Ppp1r9bImported
Synonyms:Spino1 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)
<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 10

Organism-specific databases

Rat genome database

More...
RGDi
632281 Ppp1r9b

<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, Cytoskeleton, Membrane, Nucleus, Synapse

<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>Mutagenesisi17S → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi59S → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi87S → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi94S → A: Diminishes phosphorylation. 1 Publication1
Mutagenesisi99S → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi100S → A: Diminishes phosphorylation. 2 Publications1
Mutagenesisi116S → A: Diminishes phosphorylation. 1 Publication1
Mutagenesisi122S → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi126S → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi177S → A: Diminishes phosphorylation. 1 Publication1
Mutagenesisi447 – 451Missing : Abolishes protein phosphatase 1 binding. 1 Publication5
Mutagenesisi451F → A: Abolishes protein phosphatase 1 binding. 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_00000715091 – 817Neurabin-2Add BLAST817

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 residuei15PhosphoserineBy similarity1
Modified residuei17PhosphoserineBy similarity1
Modified residuei94Phosphoserine; by PKA1 Publication1
Modified residuei100Phosphoserine; by CaMK2Combined sources2 Publications1
Modified residuei116Phosphoserine; by CaMK21 Publication1
Modified residuei177Phosphoserine; by PKA1 Publication1
Modified residuei192PhosphoserineBy similarity1
Modified residuei193PhosphothreonineBy similarity1
Modified residuei205PhosphoserineCombined sources1
Modified residuei207PhosphothreonineBy similarity1
Modified residuei438PhosphoserineBy similarity1
Modified residuei658PhosphoserineBy similarity1

<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

Stimulation of D1 (but not D2) dopamine receptors induces Ser-94 and Ser-177 phosphorylation. Dephosphorylation of these residues is mediated by PP1 and possibly PP2A. Spinophilin unphosphorylated or phosphorylated at Ser-94 is concentrated in the postsynaptic density, whereas spinophilin phosphorylated at Ser-177 is absent from the postsynaptic density and enriched in the cytosol. Phosphorylation of spinophilin disrupts its association with F-actin, but does not affect its binding to PP1.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
O35274

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

More...
PaxDbi
O35274

PRoteomics IDEntifications database

More...
PRIDEi
O35274

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O35274

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

More...
PhosphoSitePlusi
O35274

<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

Ubiquitous. Abundantly expressed in the brain. Expressed at highest levels in hippocampus and at lower levels in the cortex, cerebellum and brainstem. Localizes to the dendritic spines of neurons. Also localizes to aspiny neurons, such as GABAergic interneurons.

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expression is low during embryogenesis and increases around postnatal day 21.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000052113 Expressed in brain and 9 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O35274 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

Interacts with DCLK2 (By similarity). Possibly exists as a homodimer, homotrimer or a homotetramer.

Interacts with F-actin, PPP1CA, neurabin-1, TGN38 and D2 dopamine receptor.

Interacts with RGS1, RGS2, RGS4, RGS19 and ADRA1B, ADRA2A, ADRA2B, ADRA2C, CDKN2A, PPP1R2, RASGFR1 and TIAM1.

Interacts (via C-terminus) with SPATA13 (via C-terminal tail) (By similarity).

Interacts with ADRA2B (By similarity).

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">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

Show more details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
250040, 2 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
O35274

Database of interacting proteins

More...
DIPi
DIP-30882N

Protein interaction database and analysis system

More...
IntActi
O35274, 8 interactors

Molecular INTeraction database

More...
MINTi
O35274

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000005498

<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

Secondary structure

1817
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
O35274

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O35274

<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>Domaini496 – 584PDZPROSITE-ProRule annotationAdd BLAST89

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 – 154Actin-bindingAdd BLAST154
Regioni100 – 371Interaction with D(2) dopamine receptorAdd BLAST272
Regioni164 – 282Actin-bindingAdd BLAST119
Regioni169 – 255Interaction with ADRA2A, ADRA2B and ADRA2C1 PublicationAdd BLAST87
Regioni417 – 494Interaction with protein phosphatase 1Add BLAST78
Regioni480 – 525Interaction with RGS21 PublicationAdd BLAST46
Regioni595 – 816Interaction with TGN381 PublicationAdd BLAST222

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 coili595 – 616Sequence analysisAdd BLAST22
Coiled coili665 – 816Sequence analysisAdd BLAST152

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi447 – 451PP1-binding motif1 Publication5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi253 – 260Poly-Pro8

<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 PP1 binding region is natively unstructured, upon PP1 binding, it acquires structure, blocks a substrate-binding site, and restricts PP1 phosphatase specificity to a subset of substrates.

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1945 Eukaryota
ENOG410Y7F2 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000158833

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_007401_1_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O35274

KEGG Orthology (KO)

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KOi
K17551

Identification of Orthologs from Complete Genome Data

More...
OMAi
AAHHKKY

Database of Orthologous Groups

More...
OrthoDBi
128743at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O35274

Family and domain databases

Database of protein disorder

More...
DisProti
DP00943

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029921 NEB2
IPR040645 Neurabin-1/2_PDZ
IPR001478 PDZ
IPR036034 PDZ_sf

The PANTHER Classification System

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PANTHERi
PTHR16154:SF24 PTHR16154:SF24, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00595 PDZ, 1 hit
PF17817 PDZ_5, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00228 PDZ, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50156 SSF50156, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50106 PDZ, 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.

O35274-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMKTEPRGPG GPLRSASPHR SAYEAGIQAL KPPDAPGPDE APKAAHHKKY
60 70 80 90 100
GSNVHRIKSM FLQMGTTTGP PGEAGGASGM AEAPRASDRG VRLSLPRASS
110 120 130 140 150
LNENVDHSAL LKLGTSVSER VSRFDSKPAP SAQPAPPPHP PSRLQETRKL
160 170 180 190 200
FERSVPAASG GDKEAVARRL LRQERASLQD RKLDVVVRFN GSTEALDKLD
210 220 230 240 250
ADAVSPTVSQ LSAVFEKADS RTGLHRAPGP PRAAGAPQVN SKLVTKRSRV
260 270 280 290 300
FQPPPPPPAP SGDAATEKDR GPGGQQPPQH RVAPARPPPK PREVRKIKPV
310 320 330 340 350
EVEESGESEA ESAPGEVIQA EVTVHAALEN GSTTATTASP APEEPKAEAV
360 370 380 390 400
PEEEASSSVA TLERGVDNGR APDMAPEEVD ESKKEDFSEA DLVDVSAYSG
410 420 430 440 450
LGEDSGGSAL EEDDEEDEED GEPPYEPESG CVEIPGLSEE EDPAPSRKIH
460 470 480 490 500
FSTAPIQVFS TYSNEDYDRR NEDVDPMAAS AEYELEKRVE RLELFPVELE
510 520 530 540 550
KDSEGLGISI IGMGAGADMG LEKLGIFVKT VTEGGAAHRD GRIQVNDLLV
560 570 580 590 600
EVDGTSLVGV TQSFAASVLR NTKGRVRFMI GRERPGEQSE VAQLIQQTLE
610 620 630 640 650
QERWQREMME QRYAQYGEDD EETGEYATDE DEELSPTFPG GEMAIEVFEL
660 670 680 690 700
AENEDALSPV EMEPEKLVHK FKELQIKHAV TEAEIQQLKR KLQSLEQEKG
710 720 730 740 750
RWRVEKAQLE QSVEENKERM EKLEGYWGEA QSLCQAVDEH LRETQAQYQA
760 770 780 790 800
LERKYSKAKR LIKDYQQKEI EFLKKETAQR RVLEESELAR KEEMDKLLDK
810
ISELEGNLQT LRNSNST
Length:817
Mass (Da):89,646
Last modified:January 1, 1998 - 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:iD31D3E94EE2FFB6A
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF016252 mRNA Translation: AAB72005.1
AF027181 Genomic DNA Translation: AAC05183.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T03852

NCBI Reference Sequences

More...
RefSeqi
NP_445926.1, NM_053474.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000089497; ENSRNOP00000074026; ENSRNOG00000052113

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
84686

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:84686

UCSC genome browser

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UCSCi
RGD:632281 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
AF016252 mRNA Translation: AAB72005.1
AF027181 Genomic DNA Translation: AAC05183.1
PIRiT03852
RefSeqiNP_445926.1, NM_053474.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2G5MNMR-B493-602[»]
3EGGX-ray1.85C/D417-583[»]
3EGHX-ray2.00C/D417-583[»]
SMRiO35274
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi250040, 2 interactors
CORUMiO35274
DIPiDIP-30882N
IntActiO35274, 8 interactors
MINTiO35274
STRINGi10116.ENSRNOP00000005498

PTM databases

iPTMnetiO35274
PhosphoSitePlusiO35274

Proteomic databases

jPOSTiO35274
PaxDbiO35274
PRIDEiO35274

Genome annotation databases

EnsembliENSRNOT00000089497; ENSRNOP00000074026; ENSRNOG00000052113
GeneIDi84686
KEGGirno:84686
UCSCiRGD:632281 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
84687
RGDi632281 Ppp1r9b

Phylogenomic databases

eggNOGiKOG1945 Eukaryota
ENOG410Y7F2 LUCA
GeneTreeiENSGT00940000158833
HOGENOMiCLU_007401_1_0_1
InParanoidiO35274
KOiK17551
OMAiAAHHKKY
OrthoDBi128743at2759
PhylomeDBiO35274

Miscellaneous databases

EvolutionaryTraceiO35274

Protein Ontology

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PROi
PR:O35274

Gene expression databases

BgeeiENSRNOG00000052113 Expressed in brain and 9 other tissues
GenevisibleiO35274 RN

Family and domain databases

DisProtiDP00943
InterProiView protein in InterPro
IPR029921 NEB2
IPR040645 Neurabin-1/2_PDZ
IPR001478 PDZ
IPR036034 PDZ_sf
PANTHERiPTHR16154:SF24 PTHR16154:SF24, 1 hit
PfamiView protein in Pfam
PF00595 PDZ, 1 hit
PF17817 PDZ_5, 1 hit
SMARTiView protein in SMART
SM00228 PDZ, 1 hit
SUPFAMiSSF50156 SSF50156, 1 hit
PROSITEiView protein in PROSITE
PS50106 PDZ, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiNEB2_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: O35274
<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: April 27, 2001
Last sequence update: January 1, 1998
Last modified: April 22, 2020
This is version 164 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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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