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Protein

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

Gene

KHDRBS1

Organism
Homo sapiens (Human)
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. According to some authors, is not involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species according to (PubMed:22253824). 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). Can regulate CD44 alternative splicing in a Ras pathway-dependent manner (By similarity). In cooperation with HNRNPA1 modulates alternative splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and of SMN1 (PubMed:17371836, PubMed:20186123). 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 (By similarity).By similarity6 Publications
Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase.1 Publication

<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

  • DNA binding Source: ProtInc
  • identical protein binding Source: UniProtKB
  • poly(A) binding Source: MGI
  • poly(U) RNA binding Source: MGI
  • protein-containing complex binding Source: Ensembl
  • protein domain specific binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • SH3/SH2 adaptor activity Source: UniProtKB
  • SH3 domain binding Source: UniProtKB-KW

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

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Reactomei
R-HSA-8849468 PTK6 Regulates Proteins Involved in RNA Processing

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q07666

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q07666

<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
Synonyms:SAM681 Publication
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000121774.17

Human Gene Nomenclature Database

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HGNCi
HGNC:18116 KHDRBS1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602489 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q07666

<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; 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>Mutagenesisi103Y → S: Impairs homodimerization. 1 Publication1
Mutagenesisi110E → A: Impairs homodimerization. 1 Publication1
Mutagenesisi118F → S: Disrupts homodimerization, impairs influence on alternative splicing. 1 Publication1
Mutagenesisi229V → F: Disrupts binding to poly(A). Decreased binding to the BCL2L1 mRNA. Loss of function in BCL2L1 splicing. Changed nuclear localization. 1 Publication1
Mutagenesisi241Y → E: Fails to influence alternative splicing of CD44, NRXN2 and NRXN3. 1 Publication1
Mutagenesisi381E → K: Disrupts interaction with APC. 1 Publication1
Mutagenesisi383Y → K: Impairs interaction with APC. 1 Publication1
Mutagenesisi384E → K: Disrupts interaction with APC. 1 Publication1
Mutagenesisi435Y → F: No effect on the nuclear localization. 1 Publication1
Mutagenesisi440Y → F: Completely blocks nuclear localization. 1 Publication1
Mutagenesisi443Y → F: No effect on the nuclear localization. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
10657

Open Targets

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OpenTargetsi
ENSG00000121774

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA30092

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
KHDRBS1

Domain mapping of disease mutations (DMDM)

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DMDMi
62511098

<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_00000501241 – 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 residuei18PhosphoserineCombined sources1
Modified residuei20PhosphoserineCombined sources1
Modified residuei29PhosphoserineCombined sources1
Modified residuei33PhosphothreonineCombined sources1
Modified residuei45Asymmetric dimethylarginine; by PRMT11 Publication1
Modified residuei52Asymmetric dimethylarginine; partial; by PRMT11 Publication1
Modified residuei58PhosphoserineCombined sources1
Modified residuei84Phosphothreonine; by MAPK1By similarity1
<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)Combined sources
Cross-linki102Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei113PhosphoserineBy similarity1
Cross-linki139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei150PhosphoserineCombined sources1
Modified residuei175N6-acetyllysine; alternateCombined sources1
Cross-linki175Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei183PhosphothreonineCombined sources1
Modified residuei282Omega-N-methylarginineCombined sources1
Modified residuei284Omega-N-methylarginineCombined sources1
Modified residuei291Omega-N-methylarginineBy similarity1
Modified residuei304Asymmetric dimethylarginine; by PRMT11 Publication1
Modified residuei310Omega-N-methylarginine; by PRMT11 Publication1
Modified residuei315Omega-N-methylarginine; by PRMT11 Publication1
Modified residuei320Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication1
Modified residuei320Omega-N-methylarginine; by PRMT11 Publication1
Modified residuei325Omega-N-methylarginine; by PRMT11 Publication1
Modified residuei331Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei331Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication1
Modified residuei331Omega-N-methylarginine; alternateCombined sources1
Modified residuei331Omega-N-methylated arginine; by PRMT1; alternate1 Publication1
Modified residuei340Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication1
Modified residuei340Omega-N-methylarginine; by PRMT1Combined sources1
Modified residuei387Phosphotyrosine1 Publication1
Modified residuei390PhosphoserineCombined sources1
Cross-linki432Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei435Phosphotyrosine; by PTK61 Publication1
Modified residuei440Phosphotyrosine; by PTK61 Publication1
Modified residuei443Phosphotyrosine; by PTK61 Publication1

<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 (PubMed:29496907). Negatively correlates with ability to bind RNA but required for many interactions with proteins. Phosphorylation by PTK6 negatively regulates its RNA binding ability. Phosphorylation by PTK6 at Tyr-440 dictates the nuclear localization of KHDRBS1. Phosphorylation at Tyr-387 disrupts interaction with APC. Phosphorylation at tyrosine residues by FYN inverts activity on modulation of BCL2L1 alternative splicing.6 Publications
Acetylated. Positively correlates with ability to bind RNA.1 Publication
Arginine methylation is required for nuclear localization. Also can affect interaction with other proteins. Inhibits interaction with Src-like SH3 domains, but not interaction with WW domains of WBP4/FBP21 AND FNBP4/FBP30.3 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q07666

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q07666

MaxQB - The MaxQuant DataBase

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MaxQBi
Q07666

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

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PaxDbi
Q07666

PeptideAtlas

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PeptideAtlasi
Q07666

PRoteomics IDEntifications database

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PRIDEi
Q07666

ProteomicsDB human proteome resource

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ProteomicsDBi
58523
58524 [Q07666-2]
58525 [Q07666-3]

Consortium for Top Down Proteomics

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TopDownProteomicsi
Q07666-1 [Q07666-1]
Q07666-3 [Q07666-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q07666

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

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PhosphoSitePlusi
Q07666

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q07666

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
Q07666

<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

Ubiquitously expressed in all tissue examined. Isoform 1 is expressed at lower levels in brain, skeletal muscle, and liver whereas isoform 3 is intensified in skeletal muscle and in liver.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

Isoform 3 is only expressed in growth-arrested cells.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000121774 Expressed in 237 organ(s), highest expression level in forebrain

CleanEx database of gene expression profiles

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CleanExi
HS_KHDRBS1

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q07666 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB005355
HPA051280
HPA056813

<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; dimerization increases RNA affinity (PubMed:26758068, PubMed:20610388). Interacts with KHDRBS3/SLIM-2 (PubMed:10332027). Interacts with KHDRBS2/SLIM-1; heterooligomer formation of KHDRBS family proteins may modulate RNA substrate specificity (By similarity). Interacts with RASA1, LCK, FYN, PTPN6, PLCG1, GRB2, CBL, JAK3, PIK3R, STAT3, APC, HNRNPA1 (PubMed:1374686, PubMed:9045636, PubMed:10332027, PubMed:11585385, PubMed:17371836, PubMed:22000517). Interacts with PTK6 (via SH3 and SH2 domains) (PubMed:10913193). Forms a complex with ILF2, ILF3, YLPM1, RBMX, NCOA5 and PPP1CA (PubMed:17890166). Does not interact with TPR (PubMed:22253824). Interacts with RBMY1A1, PRMT1 (By similarity). 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) (By similarity). Interacts with the non-receptor tyrosine kinase SRMS; the interaction leads to phosphorylation of KHDRBS1 (PubMed:29496907). Interacts with ZBTB7A; negatively regulates KHDRBS1 splicing activity toward BCL2L1 (PubMed:24514149).By similarity10 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
115900, 186 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q07666

Database of interacting proteins

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DIPi
DIP-29007N

Protein interaction database and analysis system

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IntActi
Q07666, 83 interactors

Molecular INTeraction database

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MINTi
Q07666

STRING: functional protein association networks

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STRINGi
9606.ENSP00000313829

<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

1443
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
2XA6NMR-A/B97-135[»]
3QHEX-ray2.40B/D365-419[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q07666

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

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SMRi
Q07666

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q07666

<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 homodimerization1 PublicationAdd BLAST161
Regioni351 – 443Interaction with HNRNPA11 PublicationAdd BLAST93
Regioni400 – 420Interaction with ZBTB7A1 PublicationAdd 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 – 55DMA/Gly-richSequence analysisAdd BLAST12
Compositional biasi59 – 89Pro-richSequence analysisAdd BLAST31
Compositional biasi282 – 292DMA/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.By similarity
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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000230771

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG079164

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q07666

KEGG Orthology (KO)

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KOi
K13198

Identification of Orthologs from Complete Genome Data

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OMAi
FLFPDMM

Database of Orthologous Groups

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OrthoDBi
1012406at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q07666

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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i

<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.

This entry describes 3 <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.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 11 Publication (identifier: Q07666-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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
MQRRDDPAAR MSRSSGRSGS MDPSGAHPSV RQTPSRQPPL PHRSRGGGGG
60 70 80 90 100
SRGGARASPA TQPPPLLPPS ATGPDATVGG PAPTPLLPPS ATASVKMEPE
110 120 130 140 150
NKYLPELMAE KDSLDPSFTH AMQLLTAEIE KIQKGDSKKD 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 SRGRGVPVRG RGAAPPPPPV
310 320 330 340 350
PRGRGVGPPR GALVRGTPVR GAITRGATVT RGVPPPPTVR GAPAPRARTA
360 370 380 390 400
GIQRIPLPPP PAPETYEEYG YDDTYAEQSY EGYEGYYSQS QGDSEYYDYG
410 420 430 440
HGEVQDSYEA YGQDDWNGTR PSLKAPPARP VKGAYREHPY GRY
Length:443
Mass (Da):48,227
Last modified:November 1, 1996 - 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:i59FB4DB6FB4DBE98
GO
Isoform 2Curated (identifier: Q07666-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     37-61: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:418
Mass (Da):45,861
Checksum:i36B5B877E35D9A2C
GO
Isoform 31 Publication (identifier: Q07666-3) [UniParc]FASTAAdd to basket
Also known as: DeltaKH1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     169-207: Missing.

Show »
Length:404
Mass (Da):44,027
Checksum:i0E6334E3447CCA5F
GO

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

The sequence AAH10132 differs from that shown. Intron retention.Curated

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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_05171937 – 61Missing in isoform 2. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_051720169 – 207Missing in isoform 3. 1 PublicationAdd BLAST39

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M88108 mRNA Translation: AAA59990.1
U78971 mRNA Translation: AAB47504.1
AK091346 mRNA Translation: BAC03643.1
AL139249 Genomic DNA No translation available.
AL445248 Genomic DNA No translation available.
CH471059 Genomic DNA Translation: EAX07576.1
CH471059 Genomic DNA Translation: EAX07577.1
BC000717 mRNA Translation: AAH00717.1
BC010132 mRNA Translation: AAH10132.1 Sequence problems.
BC019109 mRNA Translation: AAH19109.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS350.1 [Q07666-1]
CCDS60067.1 [Q07666-3]

Protein sequence database of the Protein Information Resource

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PIRi
A38219

NCBI Reference Sequences

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RefSeqi
NP_001258807.1, NM_001271878.1 [Q07666-3]
NP_006550.1, NM_006559.2 [Q07666-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.445893

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000327300; ENSP00000313829; ENSG00000121774 [Q07666-1]
ENST00000492989; ENSP00000417731; ENSG00000121774 [Q07666-3]

Database of genes from NCBI RefSeq genomes

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GeneIDi
10657

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:10657

UCSC genome browser

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UCSCi
uc001bua.3 human [Q07666-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
M88108 mRNA Translation: AAA59990.1
U78971 mRNA Translation: AAB47504.1
AK091346 mRNA Translation: BAC03643.1
AL139249 Genomic DNA No translation available.
AL445248 Genomic DNA No translation available.
CH471059 Genomic DNA Translation: EAX07576.1
CH471059 Genomic DNA Translation: EAX07577.1
BC000717 mRNA Translation: AAH00717.1
BC010132 mRNA Translation: AAH10132.1 Sequence problems.
BC019109 mRNA Translation: AAH19109.1
CCDSiCCDS350.1 [Q07666-1]
CCDS60067.1 [Q07666-3]
PIRiA38219
RefSeqiNP_001258807.1, NM_001271878.1 [Q07666-3]
NP_006550.1, NM_006559.2 [Q07666-1]
UniGeneiHs.445893

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XA6NMR-A/B97-135[»]
3QHEX-ray2.40B/D365-419[»]
ProteinModelPortaliQ07666
SMRiQ07666
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115900, 186 interactors
CORUMiQ07666
DIPiDIP-29007N
IntActiQ07666, 83 interactors
MINTiQ07666
STRINGi9606.ENSP00000313829

PTM databases

iPTMnetiQ07666
PhosphoSitePlusiQ07666
SwissPalmiQ07666

Polymorphism and mutation databases

BioMutaiKHDRBS1
DMDMi62511098

Proteomic databases

EPDiQ07666
jPOSTiQ07666
MaxQBiQ07666
PaxDbiQ07666
PeptideAtlasiQ07666
PRIDEiQ07666
ProteomicsDBi58523
58524 [Q07666-2]
58525 [Q07666-3]
TopDownProteomicsiQ07666-1 [Q07666-1]
Q07666-3 [Q07666-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
10657
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000327300; ENSP00000313829; ENSG00000121774 [Q07666-1]
ENST00000492989; ENSP00000417731; ENSG00000121774 [Q07666-3]
GeneIDi10657
KEGGihsa:10657
UCSCiuc001bua.3 human [Q07666-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10657
DisGeNETi10657
EuPathDBiHostDB:ENSG00000121774.17

GeneCards: human genes, protein and diseases

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GeneCardsi
KHDRBS1
HGNCiHGNC:18116 KHDRBS1
HPAiCAB005355
HPA051280
HPA056813
MIMi602489 gene
neXtProtiNX_Q07666
OpenTargetsiENSG00000121774
PharmGKBiPA30092

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1588 Eukaryota
COG5176 LUCA
GeneTreeiENSGT00940000155718
HOGENOMiHOG000230771
HOVERGENiHBG079164
InParanoidiQ07666
KOiK13198
OMAiFLFPDMM
OrthoDBi1012406at2759
PhylomeDBiQ07666
TreeFamiTF314878

Enzyme and pathway databases

ReactomeiR-HSA-8849468 PTK6 Regulates Proteins Involved in RNA Processing
SignaLinkiQ07666
SIGNORiQ07666

Miscellaneous databases

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

More...
ChiTaRSi
KHDRBS1 human
EvolutionaryTraceiQ07666

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
KHDRBS1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
10657
PMAP-CutDBiQ07666

Protein Ontology

More...
PROi
PR:Q07666

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000121774 Expressed in 237 organ(s), highest expression level in forebrain
CleanExiHS_KHDRBS1
GenevisibleiQ07666 HS

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

More...
ProtoNeti
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_HUMAN
<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: Q07666
Secondary accession number(s): D3DPP3
, Q6PJX7, Q8NB97, Q99760
<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: November 1, 1996
Last modified: January 16, 2019
This is version 191 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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