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Entry version 166 (16 Oct 2019)
Sequence version 2 (12 Apr 2005)
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Protein

KH domain-containing, RNA-binding, signal transduction-associated protein 1

Gene

Khdrbs1

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

Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. May not be involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species. RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). In cooperation with HNRNPA1 modulates alternative splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and of SMN1 (By similarity). Can regulate CD44 alternative splicing in a Ras pathway-dependent manner. Can regulate alternative splicing of NRXN1 and NRXN3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. In a neuronal activity-dependent manner cooperates synergistically with KHDRBS2/SLIM-1 in regulation of NRXN1 exon skipping at AS4. The cooperation with KHDRBS2/SLIM-1 is antagonistic for regulation of NXRN3 alternative splicing at AS4 (PubMed:12478298, PubMed:22196734, PubMed:24469635).By similarity6 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 functionRNA-binding
Biological processCell cycle, mRNA processing, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-8849468 PTK6 Regulates Proteins Involved in RNA Processing

<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_and_taxonomy_section">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:
KH domain-containing, RNA-binding, signal transduction-associated protein 1
Alternative name(s):
GAP-associated tyrosine phosphoprotein p62
Src-associated in mitosis 68 kDa protein
Short name:
Sam68
p21 Ras GTPase-activating protein-associated p62
p68
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:Khdrbs1Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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 4

Organism-specific databases

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

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MGIi
MGI:893579 Khdrbs1

<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

Cytoplasm, Membrane, Nucleus

<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_and_biotech_section">'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>Mutagenesisi58S → A: Abolishes phosphorylation, abolishes CD44 splicing regulation; when associated with A-71 and A-84. 1 Publication1
Mutagenesisi71T → A: Abolishes phosphorylation, abolishes CD44 splicing regulation; when associated with A-58 and A-84. 1 Publication1
Mutagenesisi84T → A: Abolishes phosphorylation, abolishes CD44 splicing regulation; when associated with A-58 and A-71. 1 Publication1
Mutagenesisi229V → F: Abolishes splicing regulation. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000501251 – 443KH domain-containing, RNA-binding, signal transduction-associated protein 1Add BLAST443

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 residuei18PhosphoserineBy similarity1
Modified residuei20PhosphoserineBy similarity1
Modified residuei21N6-acetyllysineCombined sources1
Modified residuei29PhosphoserineBy similarity1
Modified residuei33PhosphothreonineBy similarity1
Modified residuei45Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei45Omega-N-methylated arginine; by PRMT1; alternateBy similarity1
Modified residuei52Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei52Omega-N-methylated arginine; by PRMT1; alternateBy similarity1
Modified residuei58Phosphoserine; by MAPK11 Publication1
Modified residuei71Phosphothreonine; by MAPK11 Publication1
Modified residuei84Phosphothreonine; by MAPK11 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki96Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki102Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei113Phosphoserine1 Publication1
Cross-linki139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei150PhosphoserineBy similarity1
Modified residuei175N6-acetyllysine; alternateBy similarity1
Cross-linki175Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei183PhosphothreonineBy similarity1
Modified residuei282Omega-N-methylarginineCombined sources1
Modified residuei284Omega-N-methylarginineCombined sources1
Modified residuei291Omega-N-methylarginine; alternateCombined sources1
Modified residuei291Omega-N-methylated arginine; by PRMT1; alternateBy similarity1
Modified residuei304Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei304Omega-N-methylated arginine; by PRMT1; alternateBy similarity1
Modified residuei310Omega-N-methylarginine; alternateBy similarity1
Modified residuei310Omega-N-methylated arginine; by PRMT1; alternateBy similarity1
Modified residuei315Omega-N-methylarginine; alternateBy similarity1
Modified residuei315Omega-N-methylated arginine; by PRMT1; alternateBy similarity1
Modified residuei320Dimethylated arginine; alternateBy similarity1
Modified residuei320Omega-N-methylarginine; alternateBy similarity1
Modified residuei320Omega-N-methylated arginine; by PRMT1; alternateBy similarity1
Modified residuei325Omega-N-methylarginine; alternateBy similarity1
Modified residuei325Omega-N-methylated arginine; by PRMT1; alternateBy similarity1
Modified residuei331Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei331Dimethylated arginine; alternateBy similarity1
Modified residuei331Omega-N-methylarginine; alternateBy similarity1
Modified residuei331Omega-N-methylated arginine; by PRMT1; alternateBy similarity1
Modified residuei340Dimethylated arginine; alternateBy similarity1
Modified residuei340Omega-N-methylarginine; alternateBy similarity1
Modified residuei340Omega-N-methylated arginine; by PRMT1; alternateBy similarity1
Modified residuei346Omega-N-methylated arginine; by PRMT1By similarity1
Modified residuei387PhosphotyrosineBy similarity1
Modified residuei390PhosphoserineBy similarity1
Cross-linki432Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei435Phosphotyrosine; by PTK6By similarity1
Modified residuei440Phosphotyrosine; by PTK6By similarity1
Modified residuei443Phosphotyrosine; by PTK6By similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

Tyrosine phosphorylated by several non-receptor tyrosine kinases including LCK, FYN and JAK3. Also tyrosine phosphorylated by the non-receptor tyrosine kinase SRMS in an EGF-dependent manner (By similarity). Phosphorylation by PTK6 negatively regulates its RNA binding ability. Phosphorylation by PTK6 at Tyr-440 dictates the nuclear localization of KHDRBS1. Phosphorylation by MAPK1 at Ser-58, Thr-71 and Thr-84 regulates CD44 alternative splicing by promoting CD44 exon v5 inclusion.By similarity2 Publications
Acetylated. Positively correlates with ability to bind RNA (By similarity).By similarity
Arginine methylation is required for nuclear localization. Inhibits interaction with Src-like SH3 domains, but not interaction with WW domains of WBP4/FBP21 AND FNBP4/FBP30 (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q60749

MaxQB - The MaxQuant DataBase

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MaxQBi
Q60749

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

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PaxDbi
Q60749

PeptideAtlas

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PeptideAtlasi
Q60749

PRoteomics IDEntifications database

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PRIDEi
Q60749

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q60749

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

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PhosphoSitePlusi
Q60749

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q60749

<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

In adult cerebellum expressed in most neuronal cell populations, specifically in cerebellar granule cells of the internal granular layer, ROR(alpha)-positive Purkinje cells, internal granular layer and molecuar layer interneurons (at protein level).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

In the developping cerebellum expression is high at birth and declines over the first 3 weeks. At P7 highly expressed in granule cell precursor cells in the external granular layer and mature granule cells of the internal granule layer.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000028790 Expressed in 306 organ(s), highest expression level in ureter

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q60749 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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Self-associates to form homooligomers when bound to RNA, oligomerization appears to be limited when binding to proteins (PubMed:9315629).

Interacts with KHDRBS3/SLIM-2 and KHDRBS2/SLIM-1; heterooligomer formation of KHDRBS family proteins may modulate RNA substrate specificity (PubMed:10077576, PubMed:24469635).

Interacts with RASA1, FYN, GRB2, PLCG1, SRC, RBMY1A1, CBP, PRMT1 (PubMed:7799925, PubMed:7512695, PubMed:10077576, PubMed:10823932, PubMed:12496368, PubMed:12529443).

Interacts with PTK6 (via SH3 and SH2 domains).

Forms a complex with ILF2, ILF3, YLPM1, RBMX, NCOA5 and PPP1CA. Binds WBP4/FBP21 (via WW domains), FNBP4/FBP30 (via WW domains).

Interacts (via Arg/Gly-rich-flanked Pro-rich regions) with FYN (via the SH3 domain).

Interacts with APC, HNRNPA1 (By similarity).

Interacts with the non-receptor tyrosine kinase SRMS; the interaction leads to phosphorylation of KHDRBS1 (By similarity).

Interacts with ZBTB7A; negatively regulates KHDRBS1 splicing activity toward BCL2L1 (By similarity).

By similarity7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
203068, 17 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q60749

Database of interacting proteins

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DIPi
DIP-2861N

Protein interaction database and analysis system

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IntActi
Q60749, 21 interactors

Molecular INTeraction database

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MINTi
Q60749

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000066516

<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
Q60749

Database of comparative protein structure models

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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_and_domains_section">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>Domaini171 – 197KHPROSITE-ProRule annotationAdd BLAST27

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>Regioni100 – 260Involved in homodimerizationBy similarityAdd BLAST161
Regioni351 – 443Interaction with HNRNPA1By similarityAdd BLAST93
Regioni400 – 420Interaction with ZBTB7ABy similarityAdd BLAST21

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 biasi34 – 41Pro-richSequence analysis8
Compositional biasi44 – 55Arg/Gly-richSequence analysisAdd BLAST12
Compositional biasi59 – 89Pro-richSequence analysisAdd BLAST31
Compositional biasi282 – 292Arg/Gly-richSequence analysisAdd BLAST11
Compositional biasi295 – 301Pro-richSequence analysis7
Compositional biasi302 – 332Arg/Gly-richSequence analysisAdd BLAST31
Compositional biasi334 – 363Pro-richSequence analysisAdd BLAST30

<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 KH domain is required for binding to RNA.1 Publication
The Pro-rich domains are flanked by Arg/Gly-rich motifs which can be asymmetric dimethylated on arginine residues to give the DMA/Gly-rich regions. Selective methylation on these motifs can modulate protein-protein interactions (By similarity).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 KHDRBS family.Sequence analysis

Keywords - Domaini

SH3-binding

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1588 Eukaryota
COG5176 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155718

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q60749

KEGG Orthology (KO)

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KOi
K13198

Identification of Orthologs from Complete Genome Data

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OMAi
YESYGQD

Database of Orthologous Groups

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OrthoDBi
1012406at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q60749

TreeFam database of animal gene trees

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TreeFami
TF314878

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.1370.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR004087 KH_dom
IPR004088 KH_dom_type_1
IPR036612 KH_dom_type_1_sf
IPR032571 Qua1_dom
IPR032335 Sam68-YY

Pfam protein domain database

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Pfami
View protein in Pfam
PF00013 KH_1, 1 hit
PF16274 Qua1, 1 hit
PF16568 Sam68-YY, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00322 KH, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54791 SSF54791, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50084 KH_TYPE_1, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

Q60749-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQRRDDPASR LTRSSGRSCS KDPSGAHPSV RLTPSRPSPL PHRPRGGGGG
60 70 80 90 100
PRGGARASPA TQPPPLLPPS TPGPDATVVG SAPTPLLPPS ATAAVKMEPE
110 120 130 140 150
NKYLPELMAE KDSLDPSFTH AMQLLSVEIE KIQKGESKKD DEENYLDLFS
160 170 180 190 200
HKNMKLKERV LIPVKQYPKF NFVGKILGPQ GNTIKRLQEE TGAKISVLGK
210 220 230 240 250
GSMRDKAKEE ELRKGGDPKY AHLNMDLHVF IEVFGPPCEA YALMAHAMEE
260 270 280 290 300
VKKFLVPDMM DDICQEQFLE LSYLNGVPEP SRGRGVSVRG RGAAPPPPPV
310 320 330 340 350
PRGRGVGPPR GALVRGTPVR GSITRGATVT RGVPPPPTVR GAPTPRARTA
360 370 380 390 400
GIQRIPLPPT PAPETYEDYG YDDTYAEQSY EGYEGYYSQS QGESEYYDYG
410 420 430 440
HGELQDSYEA YGQDDWNGTR PSLKAPPARP VKGAYREHPY GRY
Length:443
Mass (Da):48,371
Last modified:April 12, 2005 - 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:iD33DE960BEA9E5AA
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 conflicti104L → P in AAA64997 (PubMed:7799925).Curated1
Sequence conflicti147D → N AA sequence (PubMed:7512695).Curated1
Sequence conflicti174G → R in AAA86693 (PubMed:7541765).Curated1
Sequence conflicti197V → VS in AAA86693 (PubMed:7541765).Curated1
Sequence conflicti225 – 230MDLHVF → LGENGL AA sequence (PubMed:7512695).Curated6
Sequence conflicti327A → S in AAA86693 (PubMed:7541765).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U17961 mRNA Translation: AAA86693.1
U17046 mRNA Translation: AAA64997.1
AK050520 mRNA Translation: BAC34303.1
AK152084 mRNA Translation: BAE30934.1
AL669834 Genomic DNA No translation available.
CU210913 Genomic DNA No translation available.
BC002051 mRNA Translation: AAH02051.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS18703.1

Protein sequence database of the Protein Information Resource

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PIRi
I49140
S43974

NCBI Reference Sequences

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RefSeqi
NP_035447.3, NM_011317.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000066257; ENSMUSP00000066516; ENSMUSG00000028790
ENSMUST00000129342; ENSMUSP00000115402; ENSMUSG00000028790

Database of genes from NCBI RefSeq genomes

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GeneIDi
20218

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:20218

UCSC genome browser

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UCSCi
uc008uyd.2 mouse

<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
U17961 mRNA Translation: AAA86693.1
U17046 mRNA Translation: AAA64997.1
AK050520 mRNA Translation: BAC34303.1
AK152084 mRNA Translation: BAE30934.1
AL669834 Genomic DNA No translation available.
CU210913 Genomic DNA No translation available.
BC002051 mRNA Translation: AAH02051.1
CCDSiCCDS18703.1
PIRiI49140
S43974
RefSeqiNP_035447.3, NM_011317.4

3D structure databases

SMRiQ60749
ModBaseiSearch...

Protein-protein interaction databases

BioGridi203068, 17 interactors
CORUMiQ60749
DIPiDIP-2861N
IntActiQ60749, 21 interactors
MINTiQ60749
STRINGi10090.ENSMUSP00000066516

PTM databases

iPTMnetiQ60749
PhosphoSitePlusiQ60749
SwissPalmiQ60749

Proteomic databases

EPDiQ60749
MaxQBiQ60749
PaxDbiQ60749
PeptideAtlasiQ60749
PRIDEiQ60749

Genome annotation databases

EnsembliENSMUST00000066257; ENSMUSP00000066516; ENSMUSG00000028790
ENSMUST00000129342; ENSMUSP00000115402; ENSMUSG00000028790
GeneIDi20218
KEGGimmu:20218
UCSCiuc008uyd.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
10657
MGIiMGI:893579 Khdrbs1

Phylogenomic databases

eggNOGiKOG1588 Eukaryota
COG5176 LUCA
GeneTreeiENSGT00940000155718
InParanoidiQ60749
KOiK13198
OMAiYESYGQD
OrthoDBi1012406at2759
PhylomeDBiQ60749
TreeFamiTF314878

Enzyme and pathway databases

ReactomeiR-MMU-8849468 PTK6 Regulates Proteins Involved in RNA Processing

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Khdrbs1 mouse

Protein Ontology

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PROi
PR:Q60749

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000028790 Expressed in 306 organ(s), highest expression level in ureter
GenevisibleiQ60749 MM

Family and domain databases

Gene3Di3.30.1370.10, 1 hit
InterProiView protein in InterPro
IPR004087 KH_dom
IPR004088 KH_dom_type_1
IPR036612 KH_dom_type_1_sf
IPR032571 Qua1_dom
IPR032335 Sam68-YY
PfamiView protein in Pfam
PF00013 KH_1, 1 hit
PF16274 Qua1, 1 hit
PF16568 Sam68-YY, 1 hit
SMARTiView protein in SMART
SM00322 KH, 1 hit
SUPFAMiSSF54791 SSF54791, 1 hit
PROSITEiView protein in PROSITE
PS50084 KH_TYPE_1, 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 nameiKHDR1_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: Q60749
Secondary accession number(s): A2ACH3
, B2KG38, Q3U8T3, Q60735, Q7M4N5, Q99M33
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: April 12, 2005
Last modified: October 16, 2019
This is version 166 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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