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Protein

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

Gene

Khdrbs1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.1 Publication

GO - Molecular functioni

  • poly(A) binding Source: Ensembl
  • poly(A) RNA binding Source: Ensembl
  • poly(U) RNA binding Source: Ensembl
  • protein complex binding Source: RGD
  • RNA binding Source: UniProtKB
  • SH3/SH2 adaptor activity Source: UniProtKB
  • SH3 domain binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

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
Gene namesi
Name:Khdrbs1Imported
Synonyms:Sam68Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi621459. Khdrbs1.

Subcellular locationi

  • Nucleus By similarity
  • Membrane By similarity

GO - Cellular componenti

  • cytoplasm Source: RGD
  • Grb2-Sos complex Source: RGD
  • membrane Source: UniProtKB
  • nucleoplasm Source: Ensembl
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443KH domain-containing, RNA-binding, signal transduction-associated protein 1PRO_0000050126Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181PhosphoserineBy similarity
Modified residuei20 – 201PhosphoserineBy similarity
Modified residuei21 – 211N6-acetyllysineBy similarity
Modified residuei29 – 291PhosphoserineBy similarity
Modified residuei45 – 451Asymmetric dimethylarginine; alternateBy similarity
Modified residuei45 – 451Omega-N-methylated arginine; by PRMT1; alternateBy similarity
Modified residuei52 – 521Asymmetric dimethylarginine; alternateBy similarity
Modified residuei52 – 521Omega-N-methylated arginine; by PRMT1; alternateBy similarity
Modified residuei58 – 581PhosphoserineBy similarity
Cross-linki102 – 102Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei113 – 1131PhosphoserineBy similarity
Modified residuei175 – 1751N6-acetyllysineBy similarity
Modified residuei291 – 2911Omega-N-methylated arginine; by PRMT1By similarity
Modified residuei304 – 3041Asymmetric dimethylarginine; alternateBy similarity
Modified residuei304 – 3041Omega-N-methylated arginine; by PRMT1; alternateBy similarity
Modified residuei310 – 3101Omega-N-methylarginine; alternateBy similarity
Modified residuei310 – 3101Omega-N-methylated arginine; by PRMT1; alternateBy similarity
Modified residuei315 – 3151Omega-N-methylarginine; alternateBy similarity
Modified residuei315 – 3151Omega-N-methylated arginine; by PRMT1; alternateBy similarity
Modified residuei320 – 3201Dimethylated arginine; alternateBy similarity
Modified residuei320 – 3201Omega-N-methylarginine; alternateBy similarity
Modified residuei320 – 3201Omega-N-methylated arginine; by PRMT1; alternateBy similarity
Modified residuei325 – 3251Omega-N-methylarginine; alternateBy similarity
Modified residuei325 – 3251Omega-N-methylated arginine; by PRMT1; alternateBy similarity
Modified residuei331 – 3311Dimethylated arginine; alternateBy similarity
Modified residuei331 – 3311Omega-N-methylated arginine; by PRMT1; alternateBy similarity
Modified residuei340 – 3401Dimethylated arginine; alternateBy similarity
Modified residuei340 – 3401Omega-N-methylarginine; alternateBy similarity
Modified residuei340 – 3401Omega-N-methylated arginine; by PRMT1; alternateBy similarity
Modified residuei346 – 3461Omega-N-methylated arginine; by PRMT1By similarity
Modified residuei390 – 3901PhosphoserineBy similarity
Modified residuei435 – 4351Phosphotyrosine; by PTK6By similarity
Modified residuei440 – 4401Phosphotyrosine; by PTK6By similarity
Modified residuei443 – 4431Phosphotyrosine; by PTK6By similarity

Post-translational modificationi

Tyrosine phosphorylated by several non-receptor tyrosine kinases, LCK, FYN and JAK3. Phosphorylation by PTK6 negatively regulates its RNA binding ability. Phosphorylation by PTK6 at Tyr-440 dictates the nulear localization of KHDRBS1 (By similarity).By similarity
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

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ91V33.
PRIDEiQ91V33.

PTM databases

iPTMnetiQ91V33.
PhosphoSiteiQ91V33.
SwissPalmiQ91V33.

Expressioni

Gene expression databases

GenevisibleiQ91V33. RN.

Interactioni

Subunit structurei

Self-associates to form homooligomers when bound to RNA, oligomerization appears to be limited when binding to proteins. Interacts with CBL, KHDRBS3, LCK, GRB2, JAK3, PIK3R1, PLCG1, PTPN6, RASA1, RBMY1A1 and STAT3. Interacts with PRMT1. Binds the WW domains of WBP4/FBP21, FNBP4/FBP30 and the SH3 domain of FYN through the Arg/Gly-rich-flanked Pro-rich regions. Forms a complex with ILF2, ILF3, YLPM1, RBMX, NCOA5 and PPP1CA (By similarity). Interacts with PTK6 (via SH3 and SH2 domains). Does not interact with TPR (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Pik3r1Q637872EBI-518436,EBI-518443

GO - Molecular functioni

  • protein complex binding Source: RGD
  • SH3/SH2 adaptor activity Source: UniProtKB
  • SH3 domain binding Source: RGD

Protein-protein interaction databases

BioGridi250715. 3 interactions.
IntActiQ91V33. 1 interaction.
STRINGi10116.ENSRNOP00000066894.

Structurei

3D structure databases

ProteinModelPortaliQ91V33.
SMRiQ91V33. Positions 155-278.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini171 – 19727KHPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi34 – 418Pro-richSequence analysis
Compositional biasi44 – 5512Arg/Gly-richSequence analysisAdd
BLAST
Compositional biasi59 – 8931Pro-richSequence analysisAdd
BLAST
Compositional biasi282 – 29211Arg/Gly-richSequence analysisAdd
BLAST
Compositional biasi295 – 3017Pro-richSequence analysis
Compositional biasi302 – 33231Arg/Gly-richSequence analysisAdd
BLAST
Compositional biasi334 – 36330Pro-richSequence analysisAdd
BLAST

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.

Sequence similaritiesi

Belongs to the KHDRBS family.Sequence analysis
Contains 1 KH domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiKOG1588. Eukaryota.
COG5176. LUCA.
GeneTreeiENSGT00550000074434.
HOGENOMiHOG000230771.
HOVERGENiHBG079164.
InParanoidiQ91V33.
KOiK13198.
OMAiFLFPDMM.
OrthoDBiEOG75MVX3.
PhylomeDBiQ91V33.

Family and domain databases

Gene3Di3.30.1370.10. 1 hit.
InterProiIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR032571. Qua1_dom.
IPR032335. Sam68-YY.
[Graphical view]
PfamiPF00013. KH_1. 1 hit.
PF16274. Qua1. 1 hit.
PF16568. Sam68-YY. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 1 hit.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 1 hit.
PROSITEiPS50084. KH_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91V33-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRRDDPAAR LTRSSGRSCS KDPSGAHPSV RLTPSRPSPL PHRSRGGGGG
60 70 80 90 100
PRGGARASPA TQPPPLLPPS NPGPDATVVG SAPTPLLPPS ATAAAKMEPE
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 YDDSYAEQSY EGYEGYYSQS QGESEYYDYG
410 420 430 440
HGELQDSYEA YGQDDWNGTR PSLKAPPARP VKGAYREHPY GRY
Length:443
Mass (Da):48,315
Last modified:December 1, 2001 - v1
Checksum:iC41A42831E7DCBC7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF305619 mRNA. Translation: AAL09361.1.
AF393783 mRNA. Translation: AAK77001.1.
BC061987 mRNA. Translation: AAH61987.1.
RefSeqiNP_569089.1. NM_130405.1.
UniGeneiRn.92906.

Genome annotation databases

EnsembliENSRNOT00000075270; ENSRNOP00000066894; ENSRNOG00000046794.
GeneIDi117268.
KEGGirno:117268.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF305619 mRNA. Translation: AAL09361.1.
AF393783 mRNA. Translation: AAK77001.1.
BC061987 mRNA. Translation: AAH61987.1.
RefSeqiNP_569089.1. NM_130405.1.
UniGeneiRn.92906.

3D structure databases

ProteinModelPortaliQ91V33.
SMRiQ91V33. Positions 155-278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250715. 3 interactions.
IntActiQ91V33. 1 interaction.
STRINGi10116.ENSRNOP00000066894.

PTM databases

iPTMnetiQ91V33.
PhosphoSiteiQ91V33.
SwissPalmiQ91V33.

Proteomic databases

PaxDbiQ91V33.
PRIDEiQ91V33.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000075270; ENSRNOP00000066894; ENSRNOG00000046794.
GeneIDi117268.
KEGGirno:117268.

Organism-specific databases

CTDi10657.
RGDi621459. Khdrbs1.

Phylogenomic databases

eggNOGiKOG1588. Eukaryota.
COG5176. LUCA.
GeneTreeiENSGT00550000074434.
HOGENOMiHOG000230771.
HOVERGENiHBG079164.
InParanoidiQ91V33.
KOiK13198.
OMAiFLFPDMM.
OrthoDBiEOG75MVX3.
PhylomeDBiQ91V33.

Miscellaneous databases

NextBioi620165.
PROiQ91V33.

Gene expression databases

GenevisibleiQ91V33. RN.

Family and domain databases

Gene3Di3.30.1370.10. 1 hit.
InterProiIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR032571. Qua1_dom.
IPR032335. Sam68-YY.
[Graphical view]
PfamiPF00013. KH_1. 1 hit.
PF16274. Qua1. 1 hit.
PF16568. Sam68-YY. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 1 hit.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 1 hit.
PROSITEiPS50084. KH_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "p59(fyn)-mediated phosphorylation regulates the activity of the tissue-specific splicing factor rSLM-1."
    Stoss O., Novoyatleva T., Gencheva M., Olbrich M., Benderska N., Stamm S.
    Mol. Cell. Neurosci. 27:8-21(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], HOMOOLIGOMERIZATION, INTERACTION WITH KHDRB2.
  2. "Characterization of Sam68 in skeletal muscle and brain of rat."
    Wang J.-M., Tseng C.-N., Yao Y., Wang Z.-Z.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-DawleyImported.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: ProstateImported.
  4. "p68 Sam is a substrate of the insulin receptor and associates with the SH2 domains of p85 PI3K."
    Sanchez-Margalet V., Najib S.
    FEBS Lett. 455:307-310(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH PIK3R1.
  5. "Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains."
    Bedford M.T., Frankel A., Yaffe M.B., Clarke S., Leder P., Richard S.
    J. Biol. Chem. 275:16030-16036(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FNBP4; WBP4; FYN AND PLCG1, METHYLATION.

Entry informationi

Entry nameiKHDR1_RAT
AccessioniPrimary (citable) accession number: Q91V33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.