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Entry version 192 (17 Jun 2020)
Sequence version 2 (05 Dec 2001)
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Protein

C-Jun-amino-terminal kinase-interacting protein 1

Gene

Mapk8ip1

Organism
Mus musculus (Mouse)
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

The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. Required for JNK activation in response to excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK-regulated activity by retaining JNK in the cytoplasm and thus inhibiting the JNK phosphorylation of c-Jun. May also participate in ApoER2-specific reelin signaling. Directly, or indirectly, regulates GLUT2 gene expression and beta-cell function. Appears to have a role in cell signaling in mature and developing nerve terminals. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response (By similarity). Acts as a scaffold protein that coordinates with SH3RF1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the activation of MAPK8/JNK1 and differentiation of CD8+ T-cells (PubMed:23963642).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>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:
C-Jun-amino-terminal kinase-interacting protein 1
Short name:
JIP-1
Short name:
JNK-interacting protein 1
Alternative name(s):
Islet-brain-1
Short name:
IB-1
JNK MAP kinase scaffold protein 1
Mitogen-activated protein kinase 8-interacting protein 1
<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:Mapk8ip1
Synonyms:Ib1, Jip1, Mapk8ip, Prkm8ip
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 2

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1309464 Mapk8ip1

<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

<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>Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Nucleus

<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_00002206291 – 707C-Jun-amino-terminal kinase-interacting protein 1Add BLAST707

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 residuei14PhosphoserineCombined sources1
Modified residuei28PhosphoserineCombined sources1
Modified residuei39PhosphoserineBy similarity1
Modified residuei103Phosphothreonine; by MAPK8, MAPK9 and MAPK10By similarity1
Modified residuei148PhosphoserineBy similarity1
Modified residuei177PhosphoserineBy similarity1
Modified residuei183PhosphoserineBy similarity1
Modified residuei189PhosphoserineBy similarity1
Modified residuei191PhosphoserineBy similarity1
Modified residuei192PhosphoserineBy similarity1
Modified residuei201Phosphothreonine; by MAPK8, MAPK9 and MAPK10By similarity1
Modified residuei210PhosphoserineBy similarity1
Modified residuei307PhosphoserineBy similarity1
Modified residuei324PhosphoserineBy similarity1
Modified residuei326PhosphoserineBy similarity1
Modified residuei336PhosphoserineBy similarity1
Modified residuei351PhosphoserineBy similarity1
Modified residuei362PhosphoserineBy similarity1
Modified residuei365PhosphoserineBy similarity1
Modified residuei403PhosphoserineBy similarity1
Modified residuei405PhosphoserineBy similarity1
Modified residuei407PhosphothreonineBy similarity1
Modified residuei440PhosphoserineBy similarity1
Modified residuei443PhosphoserineBy similarity1
Modified residuei444PhosphothreonineBy similarity1
Modified residuei465PhosphoserineBy similarity1
Modified residuei467PhosphoserineBy similarity1
Modified residuei468PhosphoserineBy similarity1
Modified residuei469PhosphoserineBy 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

Phosphorylated by MAPK8, MAPK9 and MAPK10. Phosphorylation on Thr-103 is also necessary for the dissociation and activation of MAP3K12. Phosphorylated by VRK2. Hyperphosphorylated during mitosis following activation of stress-activated and MAP kinases (By similarity).By similarity
Ubiquitinated. Two preliminary events are required to prime for ubiquitination; phosphorylation and an increased in intracellular calcium concentration. Then, the calcium influx initiates ubiquitination and degradation by the ubiquitin-proteasome pathway.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
Q9WVI9

PeptideAtlas

More...
PeptideAtlasi
Q9WVI9

PRoteomics IDEntifications database

More...
PRIDEi
Q9WVI9

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9WVI9

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

More...
PhosphoSitePlusi
Q9WVI9

<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 predominantly in the brain and insulin-secreting cells. In the brain, high expression found in the cerebral cortex and hippocampus. Localizes in the synaptic regions of the olfactory bulb, retina, cerebral and cerebellar cortex and hippocampus. Also expressed in a restricted number of axons, including mossy fibers from the hippocampal dentate gyrus, soma, dendrites and axons of cerebellar Purkinje cells. Also expressed in kidney, testis and prostate. Low levels in heart, ovary and small intestine. Isoform JIP-1b is more predominant in the brain than isoform JIP-1a. Isoform Jip1-a is expressed both in the brain and kidney, isoform JIP-1c, isoform JIP-1d and isoform JIP-1e are brain specific.1 Publication

<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

Low levels at prenatal stage 15 dpc, increased levels during the first postnatal days, with a plateau at postnatal day 15.

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Upon neuron differentiation.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000027223 Expressed in cingulate cortex and 257 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9WVI9 MM

<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

Forms homo- or heterooligomeric complexes. Binds specific components of the JNK signaling pathway namely MAPK8/JNK1, MAPK9/JNK2, MAPK10/JNK3, MAP2K7/MKK7, MAP3K11/MLK3 and DLK1. Also binds the proline-rich domain-containing splice variant of apolipoprotein E receptor 2 (ApoER2) (By similarity). Binds the cytoplasmic tails of LRP1 and LRP2 (Megalin). Binds the TPR motif-containing C-terminal of kinesin light chain, KLC1. Pre-assembled MAPK8IP1 scaffolding complexes are then transported as a cargo of kinesin, to the required subcellular location.

Interacts with the cytoplasmic domain of APP (By similarity).

Interacts, via the PID domain, with ARHGEF28.

Interacts with MAP3K7/TAK1 and VRK2 (By similarity).

Interacts with DCLK2 (PubMed:16628014).

Found in a complex with SH3RF1, RAC1, MAP3K11/MLK3, MAP2K7/MKK7 and MAPK8/JNK1 (PubMed:23963642).

Found in a complex with SH3RF1, RAC2, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and MAPK9/JNK2 (PubMed:27084103).

Interacts with SH3RF2 (By similarity).

By similarity6 Publications

<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

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
202375, 8 interactors

Protein interaction database and analysis system

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IntActi
Q9WVI9, 18 interactors

Molecular INTeraction database

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MINTi
Q9WVI9

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000050773

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q9WVI9 protein

<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

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SMRi
Q9WVI9

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9WVI9

<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>Domaini484 – 545SH3PROSITE-ProRule annotationAdd BLAST62
Domaini557 – 696PIDPROSITE-ProRule annotationAdd BLAST140

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>Regioni127 – 281JNK-binding domain (JBD)Add BLAST155
Regioni153 – 172Minimal inhibitory domain (MID)Add BLAST20
Regioni279 – 467Interaction with MAP3K7By similarityAdd BLAST189
Regioni467 – 656Interaction with VRK2By similarityAdd BLAST190

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>Motifi349 – 356D-box 18
Motifi360 – 368D-box 29

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 biasi41 – 47Asp/Glu-rich (acidic)7
Compositional biasi107 – 116Asp/Glu-rich (acidic)10
Compositional biasi355 – 359Poly-Pro5

<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 SH3 domain mediates homodimerization.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 JIP scaffold family.Curated

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3775 Eukaryota
ENOG410ZFRJ LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157089

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_006711_1_1_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9WVI9

KEGG Orthology (KO)

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KOi
K04434

Identification of Orthologs from Complete Genome Data

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OMAi
QGNKCSH

Database of Orthologous Groups

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OrthoDBi
372907at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9WVI9

TreeFam database of animal gene trees

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TreeFami
TF325073

Family and domain databases

Conserved Domains Database

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CDDi
cd11943 SH3_JIP1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.30.29.30, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

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IDEALi
IID50056

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR035638 JIP1_SH3
IPR011993 PH-like_dom_sf
IPR006020 PTB/PI_dom
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00640 PID, 1 hit
PF14604 SH3_9, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00462 PTB, 1 hit
SM00326 SH3, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50044 SSF50044, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS01179 PID, 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>Sequences (5)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 describes 5 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform JIP-1b (identifier: Q9WVI9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAERESGLGG GAASPPAASP FLGLHIASPP NFRLTHDISL EEFEDEDLSE
60 70 80 90 100
ITDECGISLQ CKDTLSLRPP RAGLLSAGSS GSAGSRLQAE MLQMDLIDAA
110 120 130 140 150
GDTPGAEDDE EEEDDELAAQ RPGVGPPKAE SNQDPAPRSQ GQGPGTGSGD
160 170 180 190 200
TYRPKRPTTL NLFPQVPRSQ DTLNNNSLGK KHSWQDRVSR SSSPLKTGEQ
210 220 230 240 250
TPPHEHICLS DELPPQGSPV PTQDRGTSTD SPCRRSAATQ MAPPSGPPAT
260 270 280 290 300
APGGRGHSHR DRIHYQADVR LEATEEIYLT PVQRPPDPAE PTSTFMPPTE
310 320 330 340 350
SRMSVSSDPD PAAYSVTAGR PHPSISEEDE GFDCLSSPER AEPPGGGWRG
360 370 380 390 400
SLGEPPPPPR ASLSSDTSAL SYDSVKYTLV VDEHAQLELV SLRPCFGDYS
410 420 430 440 450
DESDSATVYD NCASASSPYE SAIGEEYEEA PQPRPPTCLS EDSTPDEPDV
460 470 480 490 500
HFSKKFLNVF MSGRSRSSSA ESFGLFSCVI NGEEHEQTHR AIFRFVPRHE
510 520 530 540 550
DELELEVDDP LLVELQAEDY WYEAYNMRTG ARGVFPAYYA IEVTKEPEHM
560 570 580 590 600
AALAKNSDWI DQFRVKFLGS VQVPYHKGND VLCAAMQKIA TTRRLTVHFN
610 620 630 640 650
PPSSCVLEIS VRGVKIGVKA DDALEAKGNK CSHFFQLKNI SFCGYHPKNN
660 670 680 690 700
KYFGFITKHP ADHRFACHVF VSEDSTKALA ESVGRAFQQF YKQFVEYTCP

TEDIYLE
Length:707
Mass (Da):77,282
Last modified:December 5, 2001 - v2
<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:i274013B12D91049D
GO
Isoform JIP-1a (identifier: Q9WVI9-2) [UniParc]FASTAAdd to basket
Also known as: 1

The sequence of this isoform differs from the canonical sequence as follows:
     558-604: Missing.

Show »
Length:660
Mass (Da):71,927
Checksum:iA303DB4A3C9A9775
GO
Isoform JIP-1c (identifier: Q9WVI9-3) [UniParc]FASTAAdd to basket
Also known as: 2a

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MAERESGLGGGAASPPAASPFLGLHIASPPNFR → MQLVLKMDSSPDNDSWLEDQWEHW

Show »
Length:698
Mass (Da):77,009
Checksum:i7451CE05C930E9F7
GO
Isoform JIP-1d (identifier: Q9WVI9-4) [UniParc]FASTAAdd to basket
Also known as: 2B

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MAERESGLGGGAASPPAASPFLGLHIASPPNFR → MQLVLKMDSSPDNDSWLEDQWEHW
     69-93: Missing.

Show »
Length:673
Mass (Da):74,585
Checksum:iCCB2C92E28D27E23
GO
Isoform JIP-1e (identifier: Q9WVI9-5) [UniParc]FASTAAdd to basket
Also known as: 3

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: Missing.

Show »
Length:617
Mass (Da):68,005
Checksum:iA22DC803C3DB62DF
GO

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 conflicti144 – 145PG → A in AAD38346 (PubMed:10098834).Curated2
Sequence conflicti144 – 145PG → A in AAD38347 (PubMed:10098834).Curated2
Sequence conflicti144 – 145PG → A in AAD38348 (PubMed:10098834).Curated2
Sequence conflicti593R → RP in AAD38346 (PubMed:10098834).Curated1
Sequence conflicti593R → RP in AAD38347 (PubMed:10098834).Curated1
Sequence conflicti593R → RP in AAD38348 (PubMed:10098834).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti10G → R in strain: ILS. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0027641 – 90Missing in isoform JIP-1e. 1 PublicationAdd BLAST90
Alternative sequenceiVSP_0027631 – 33MAERE…PPNFR → MQLVLKMDSSPDNDSWLEDQ WEHW in isoform JIP-1c and isoform JIP-1d. 1 PublicationAdd BLAST33
Alternative sequenceiVSP_00276569 – 93Missing in isoform JIP-1d. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_002766558 – 604Missing in isoform JIP-1a. 1 PublicationAdd BLAST47

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

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DDBJi
Links Updated
AF003115 mRNA Translation: AAB66317.1
AF109768 mRNA Translation: AAD38346.1
AF109769 mRNA Translation: AAD38347.1
AF109770 mRNA Translation: AAD38348.1
AF109771 mRNA Translation: AAD38349.1
AF054611 mRNA Translation: AAD22580.1
AF332075 mRNA Translation: AAK56103.1
AF332076 mRNA Translation: AAK56104.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS16446.1 [Q9WVI9-1]
CCDS57180.1 [Q9WVI9-3]

Protein sequence database of the Protein Information Resource

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PIRi
T03038

NCBI Reference Sequences

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RefSeqi
NP_035292.2, NM_011162.5 [Q9WVI9-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000050312; ENSMUSP00000050773; ENSMUSG00000027223 [Q9WVI9-1]
ENSMUST00000111279; ENSMUSP00000106910; ENSMUSG00000027223 [Q9WVI9-3]

Database of genes from NCBI RefSeq genomes

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GeneIDi
19099

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:19099

UCSC genome browser

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UCSCi
uc008kxv.2 mouse [Q9WVI9-3]
uc008kxw.2 mouse [Q9WVI9-4]
uc008kxx.2 mouse [Q9WVI9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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
AF003115 mRNA Translation: AAB66317.1
AF109768 mRNA Translation: AAD38346.1
AF109769 mRNA Translation: AAD38347.1
AF109770 mRNA Translation: AAD38348.1
AF109771 mRNA Translation: AAD38349.1
AF054611 mRNA Translation: AAD22580.1
AF332075 mRNA Translation: AAK56103.1
AF332076 mRNA Translation: AAK56104.1
CCDSiCCDS16446.1 [Q9WVI9-1]
CCDS57180.1 [Q9WVI9-3]
PIRiT03038
RefSeqiNP_035292.2, NM_011162.5 [Q9WVI9-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UKHX-ray2.35B153-163[»]
1UKIX-ray2.70B153-163[»]
3O17X-ray3.00F/G154-163[»]
3O2MX-ray2.70F/G154-163[»]
3V3VX-ray2.70B153-163[»]
6F5EX-ray2.70C153-163[»]
SMRiQ9WVI9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi202375, 8 interactors
IntActiQ9WVI9, 18 interactors
MINTiQ9WVI9
STRINGi10090.ENSMUSP00000050773

PTM databases

iPTMnetiQ9WVI9
PhosphoSitePlusiQ9WVI9

Proteomic databases

PaxDbiQ9WVI9
PeptideAtlasiQ9WVI9
PRIDEiQ9WVI9

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
26197 261 antibodies

Genome annotation databases

EnsembliENSMUST00000050312; ENSMUSP00000050773; ENSMUSG00000027223 [Q9WVI9-1]
ENSMUST00000111279; ENSMUSP00000106910; ENSMUSG00000027223 [Q9WVI9-3]
GeneIDi19099
KEGGimmu:19099
UCSCiuc008kxv.2 mouse [Q9WVI9-3]
uc008kxw.2 mouse [Q9WVI9-4]
uc008kxx.2 mouse [Q9WVI9-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
9479
MGIiMGI:1309464 Mapk8ip1

Phylogenomic databases

eggNOGiKOG3775 Eukaryota
ENOG410ZFRJ LUCA
GeneTreeiENSGT00940000157089
HOGENOMiCLU_006711_1_1_1
InParanoidiQ9WVI9
KOiK04434
OMAiQGNKCSH
OrthoDBi372907at2759
PhylomeDBiQ9WVI9
TreeFamiTF325073

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
19099 0 hits in 12 CRISPR screens
EvolutionaryTraceiQ9WVI9

Protein Ontology

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PROi
PR:Q9WVI9
RNActiQ9WVI9 protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000027223 Expressed in cingulate cortex and 257 other tissues
GenevisibleiQ9WVI9 MM

Family and domain databases

CDDicd11943 SH3_JIP1, 1 hit
Gene3Di2.30.29.30, 1 hit
IDEALiIID50056
InterProiView protein in InterPro
IPR035638 JIP1_SH3
IPR011993 PH-like_dom_sf
IPR006020 PTB/PI_dom
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
PfamiView protein in Pfam
PF00640 PID, 1 hit
PF14604 SH3_9, 1 hit
SMARTiView protein in SMART
SM00462 PTB, 1 hit
SM00326 SH3, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
PROSITEiView protein in PROSITE
PS01179 PID, 1 hit
PS50002 SH3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiJIP1_MOUSE
<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: Q9WVI9
Secondary accession number(s): O35145
, Q925J8, Q9R1H9, Q9R1Z1, Q9WVI7, Q9WVI8
<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: December 5, 2001
Last sequence update: December 5, 2001
Last modified: June 17, 2020
This is version 192 of the entry and version 2 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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